AU2008212020B2 - Nucleic acids and corresponding proteins entitled 109P1D4 useful in treatment and detection of cancer - Google Patents

Abstract

A novel gene 109P1D4 and its encoded protein, and variants thereof, are described wherein 109P1D4 exhibits tissue specific expression in normal adult tissue, and is aberrantly expressed in the cancers listed in Table i. Consequently, 109P1D4 provides a diagnostic, prognostic, prophylactic and/or therapeutic target for cancer. The 109P1D4 gene or fragment thereof, or its encoded protein, or variants thereof, or a fragment thereof, can be used to elicit a humoral or cellular immune response; antibodies or T cells reactive with 109P1 D4 can be used in active or passive immunization.

Description

1 AUSTRALIA Patents Act 1990 FB RICE & CO Patent and Trade Mark Attorneys AGENSYS, INC. COMPLETE SPECIFICATION STANDARD PATENT Invention Title: Nucleic acids and corresponding proteins entitled 109P1D4 useful in treatment and detection of cancer The following statement is a full description of this invention including the best method of performing it known to us:- 1A NUCLEIC ACIDS AND CORRESPONDING PROTEINS ENTITLED 109P1 D4 USEFUL IN TREATMENT AND DETECTION OF CANCER RELATED APPLICATIONS This application is a divisional application under S.79B of the Patents Act 1990 of Australian Patent Application No. 5 2004235755 filed 30 April 2004 which corresponds to International Application No. PCT/US2004/013568 in the Australian national phase, and claims priority from United States Patent Application No. 60/467,002 filed on 30 April 2003. The contents of each of the foregoing applications is hereby incorporated in its entirety by way of reference into this divisional application. 10 FIELD OF THE INVENTION The invention described herein relates to genes and their encoded proteins, termed 109P1D4 and variants thereof, expressed in certain cancers, and to diagnostic and therapeutic methods and compositions useful in the management of cancers that express 109P1D4. 15 BACKGROUND OF THE INVENTION Cancer is the second leading cause of human death next to coronary disease. Worldwide, millions of people die from cancer every year. In the United States alone, as reported by the American Cancer Society, cancer causes the death of well over a half-million people annually, with over 1. 2 million new cases diagnosed per year. While deaths from heart disease have been declining significantly, those resulting from cancer generally are on the rise. In the early part of the next 20 century, cancer is predicted to become the leading cause of death. Worldwide, several cancers stand out as the leading killers. In particular, carcinomas of the lung, prostate, breast, colon, pancreas, and ovary represent the primary causes of cancer death. These and virtually all other carcinomas share a common lethal feature. With very few exceptions, metastatic disease from a carcinoma is fatal. Moreover, even for those 25 cancer patients who initially survive their primary cancers, common experience has shown that their lives are dramatically altered. Many cancer patients experience strong anxieties driven by the awareness of the potential for recurrence or treatment failure. Many cancer patients experience physical debilitations following treatment. Furthermore, many cancer patients experience a recurrence. 30 Worldwide, prostate cancer is the fourth most prevalent cancer in men. In North America and Northem Europe, it is by far the most common cancer in males and is the second leading cause of cancer death in men. In the United States alone, well over 30, 000 men die annually of this disease-second only to lung cancer. Despite the magnitude of these figures, there is still no effective treatment for metastatic prostate cancer. Surgical prostatectomy, radiation therapy, hormone ablation therapy, surgical castration and chemotherapy continue to be the main treatment modalities. 35 Unfortunately, these treatments are ineffective for many and are often associated with undesirable consequences. On the diagnostic front, the lack of a prostate tumor marker that can accurately detect early-stage, localized tumors remains a significant limitation in the diagnosis and management of this disease. Although the serum prostate specific 40 antigen (PSA) assay has been a very useful tool, however its specificity and general utility is widely regarded as lacking in several important respects.

2 Progress in identifying additional specific markers for prostate cancer has been improved by the generation of prostate cancer xenografts that can recapitulate different stages of the disease in mice. The LAPC (Los Angeles Erostate .Cancer) xenografts are prostate cancer xenografts that have survived passage in severe combined immune deficient (SCID) mice and have exhibited the capacity to mimic the transition from androgen dependence to androgen Independence (Klein et at., 1997, Nat. Med. 3:402). More recently identified prostate cancer markers indude PCTA-1 (Su et al., 1996, Proc. Nati. Acad. Sci. USA 93: 7252), prostate-specific membrane (PSM) antigen (Pinto et aL., Clin Cancer Res 1996 Sep 2 (9): 1445 51), STEAP (Hubert, et al., Proc Nail Acad Sci U S A 1999 Dec 7; 96(25): 14523-8) and prostate stem cell antigen (PSCA) (Reiter et al., 1998, Proc. Nall. Acad. Sci. USA 95: 1735). While previously identified markers such as PSA, PSM, PCTA and PSCA have facilitated efforts to diagnose and treat prostate cancer, there Is need for the identification of additional markers and therapeutic targets for prostate and related cancers in order to further improve diagnosis and therapy. Renal cell carcinoma (RCC) accounts for approximately 3 percent of adult malignancies. Once adenomas reach a diameter of 2 to 3 cm, malignant potential exists. In the adult, the two principal malignant renal tumors are renal cell adenocarcinoma and transitional cell carcinoma of the renal pelvis or ureter. The Incidence of renal cell adenocarcinoma Is estimated at more than 29,000 cases in the United States, and more than 11,600 patients died of this disease in 1998. Transitional cell carcinoma Is less frequent, with an Incidence of approximately 500 cases per year In the United States. Surgery has been the primary therapy for renal cell adenocarcinoma for many decades. Until recently, metastatic disease has been refractory to any systemic therapy. With recent developments in systemic therapies, particularly immunotheraples, metastatic renal cell carcinoma may be approached aggressively in appropriate patients with a possibility of durable responses. Nevertheless, there Is a remaining need for effective therapies for these patients. Of all new cases of cancer in the United States, bladder cancer represents approximately 5 percent in men (fifth most common neoplasm) and 3 percent in women (eighth most common neoplasm). The Incidence Is increasing slowly, concurrent with an increasing older population. In 1998, there was an estimated 54,500 cases, including 39,500 In men and 15,000 in women. The age-adjusted incidence in the United States is 32 per 100,000 for men and eight per 100,000 in women. The historic male/female ratio of 3:1 may be decreasing related to smoking patterns in women. There were an estimated 11,000 deaths from bladder cancer in 1998 (7,800 in men and 3,900 in women). Bladder cancer Incidence and mortality strongly increase with age and will be an increasing problem as the population becomes more elderly. Most bladder cancers recur In the bladder. Bladder cancer Is managed with a combination of transurethral resection of the bladder (TUR) and intravesical chemotherapy or immunotherapy. The multifocal and recurrent nature of bladder cancer points out the limitations of TUR. Most muscle-Invasive cancers are not cured by TUR alone. Radical cystectomy and urinary diversion is the most effective means to eliminate the cancer but carry an undeniable Impact on urinary and sexual function. There continues to be a significant need for treatment modalities that are beneficial for bladder cancer patients. An estimated 130,200 cases of colorectal cancer occurred In 2000 in the United States, Including 93,800 cases of colon cancer and 36,400 of rectal cancer. Colorectal cancers are the third most common cancers in men and women. Incidence rates declined significantly during 1992-1996 (-2.1% per year). Research suggests that these declines have been due to increased screening and polyp removal, preventing progression of polyps to invasive cancers. There were an estimated 56,300 deaths (47,700 from colon cancer, 8,600 from rectal cancer) in 2000, accounting for about 11% of all U.S. cancer deaths. Al present, surgery is the most common form of therapy for colorectal cancer, and for cancers that have not spread, It Is frequently curative. Chemotherapy, or chemotherapy plus radiation, is given before or after surgery to most 3 patients whose cancer has deeply perforated the bowel wall or has spread to the lymph nodes. A permanent colostomy (creation of an abdominal opening for elimination of body wastes) is occasionally needed for colon cancer and is infrequently required for rectal cancer. There continues to be a need for effective diagnostic and treatment modalities for colorectal cancer. There were an estimated 164,100 new cases of lung and bronchial cancer in 2000, accounting for 14% of all U.S. cancer diagnoses. The Incidence rate of lung and bronchial cancer is declining significantly in men, from a high of 86.5 per 100,000 in 1984 to 70.0 in 1996. In the 1990s, the rate of increase among women began to slow. In 1996, the incidence rate In women was 42.3 per 100,000. Lung and bronchial cancer caused an estimated 156,900 deaths in 2000, accounting for 28% of all cancer deaths. During 1992-1996, mortality from lung cancer declined significantly among men (-1.7% per year) while rates for women were still significantly increasing (0.9% per year). Since 1987, more women have died each year of lung cancer than breast cancer, which, for over 40 years, was the major cause of cancer death in women. Decreasing lung cancer incidence and mortality rates most likely resulted from decreased smoking rates over the previous 30 years; however, decreasing smoking patterns among women lag behind those of men. Of concern, although the declines in adult tobacco use have slowed, tobacco use in youth is increasing again. Treatment options for lung and bronchial cancer are determined by the type and stage of the cancer and include surgery, radiation therapy, and chemotherapy. For many localized cancers, surgery is usually the treatment of choice. Because the disease has usually spread by the time it is discovered, radiation therapy and chemotherapy are often needed in combination with surgery. Chemotherapy alone or combined with radiation is the treatment of choice for small cell lung cancer; on this regimen, a large percentage of patients experience remission, which in some cases is long lasting. There Is however, an ongoing need for effective treatment and diagnostic approaches for lung and bronchial cancers. An estimated 182,800 new invasive cases of breast cancer were expected to occur among women In the United States during 2000. Additionally, about 1,400 neW cases of breast cancer were expected to be diagnosed in men in 2000. After increasing about 4% per year In the 1 980s, breast cancer incidence rates in women have leveled off In the 1990s to about 110.6 cases per 100,000. In the U.S. alone, there were an estimated 41,200 deaths (40,800 women, 400 men) in 2000 due to breast cancer. Breast cancer ranks second among cancer deaths in women. According to the most recent data, mortality rates declined significantly during 1992-1996 with the largest decreases In younger women, both white and black. These decreases were probably the result of earlier detection and improved treatment. Taking into account the medical circumstances and the patient's preferences, treatment of breast cancer may Involve lumpectomy (local removal of the tumor) and removal of the lymph nodes under the arm; mastectomy (surgical removal of the breast) and removal of the lymph nodes under the arm; radiation therapy; chemotherapy; or hormone therapy. Often, two or more methods are used in combination. Numerous studies have shown that, for early stage disease, long-term survival rates after lumpectomy plus radiotherapy are similar to survival rates after modified radical mastectomy. Significant advances in reconstruction techniques provide several options for breast reconstruction after mastectomy. Recently, such reconstruction has been done at the same time as the mastectomy. Local excision of ductal carcinoma In situ (DCIS) with adequate amounts of surrounding normal breast tissue may prevent the local recurrence of the DCIS. Radiation to the breast and/or tamoxifen may reduce the chance of OCIS occurring in the remaining breast tissue. This is important because DCIS, If left untreated, may develop Into invasive breast cancer. Nevertheless, there are serious side effects or sequelae to these treatments. There is, therefore, a need for efficacious breast cancer treatments. 3 4 There were an estimated 28,300 new cases of pancreatic cancer in the United States in 2000. Over the past 20 years, rates of pancreatic cancer have declined in men. Rates among women have remained approximately constant but may be beginning to decline. Pancreatic cancer caused an estimated 28, 200 deaths in 2000 in the United States. Over the past 20 years, there has been a slight but significant decrease in mortality rates among men (about-0. 9% per year) while rates have increased slightly among women. Surgery, radiation therapy, and chemotherapy are treatment options for pancreatic cancer. These treatment options can extend survival and/or relieve symptoms in many patients but are not likely to produce a cure for most. There is a significant need for additional therapeutic and diagnostic options for pancreatic cancer. SUMMARY OF THE INVENTION The present invention relates to a gene, designated 109P1D4, that has now been found to be over-expressed in the cancer(s) listed in Table 1. Northem blot expression analysis of 109P1D4 gene expression in normal tissues shows a restricted expression patten in adult tissues. The nucleotide (Figure 2) and amino acid (Figure 2, and Figure 3) sequences of 109P1D4 are provided. The tissue-related profile of 109P1D4 in normal adult tissues, combined with the over-expression observed in the tissues listed in Table 1, shows that 109P1D4 is aberrant over-expressed in at least some cancers, and thus serves as a useful diagnostic, prophylactic, prognostic, and/or therapeutic target for cancers of the tissue(s) such as those listed in Table 1. The invention provides polynucleotides corresponding or complementary to all or part of the 109P1D4 genes, mRNAs, and/or coding sequences, preferably in isolated form, including polynucleotides encoding 109P1D4-related proteins and fragments of 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, or more than 25 contiguous amino acids ; at least 30, 35, 40, 45, 50, 55, 60, 65, 70, 80, 85, 90, 95, 100 or more than 100 contiguous amino acids of a 109P1D4-related protein, as well as the peptides/proteins themselves; DNA, RNA, DNAIRNA hybrids, and related molecules, polynucleotides or oligonucleotides complementary or having at least a 90% homology to the 109P1D4 genes or mRNA sequences or parts thereof, and polynucleotides or oligonucleotides that hybridize to the 109P1 D4 genes, mRNAs, or to 109P1 D4-encoding polynucleotides. Also provided are means for isolating cDNAs and the genes encoding 109P1 D4. Recombinant DNA molecules containing 109P1D4 polynucleotides, cells transformed or transduced with such molecules, and host-vector systems for the expression of 109P1D4 gene products are also provided. The invention further provides antibodies that bind to 109P1 D4 proteins and polypeptide fragments thereof, including polyclonal and monoclonal antibodies, murine and other mammalian antibodies, chimeric antibodies, humanized and fully human antibodies, and antibodies labeled with a detectable marker or therapeutic agent. in certain embodiments, there is a proviso that the entire nucleic acid sequence of Figure 2 is not encoded and/or the entire amino acid sequence of Figure 2 is not prepared. In certain embodiments, the entire nucleic acid sequence of Figure 2 is encoded and/or the entire amino acid sequence of Figure 2 is prepared, either of which are in respective human unit dose forms. One embodiment of the invention comprises an isolated polynucleotide that encodes a 109P1 D4 protein, wherein the polynucleotide is selected from the group consisting of: (a) a polynucleotide comprising the sequence of SEQ ID NO:2, from nucleotide residue numbers 846 through 3911; (b) a polynucleotide comprising the sequence of SEQ ID NO:4, from nucleotide residue numbers 503 through 3667; 4A (c) a polynucleotide comprising the sequence of SEQ ID NO:6, from nucleotide residue numbers 846 through 4889; (d) a polynucleotide comprising the sequence of SEQ ID NO:8, from nucleotide residue numbers 846 through 4778; (e) a polynucleotide comprising the sequence of SEQ ID NO:10, from nucleotide residue numbers 846 through 4778; (f) a polynucleotide comprising the sequence of SEQ ID NO:12, from nucleotide residue numbers 614 through 3727; (g) a polynucleotide comprising the sequence of SEQ ID NO:14, from nucleotide residue numbers 735 through 3881; (h) a polynucleotide comprising the sequence of SEQ ID NO:16, from nucleotide residue numbers 735 through 4757; (i) a polynucleotide comprising the sequence of SEQ ID NO:18, from nucleotide residue numbers 514 through 3627; and (j) a polynucleotide of any one of (a)-(i), wherein T can also be U.

5 The invention further provides methods for detecting the presence and status of 109P1D4 polynucleotides and proteins in various biological samples, as well as methods for identifying cells that express 109P1 D4. A typical embodiment of this invention provides methods for monitoring 109P1D4 gene products in a tissue or hematology sample having or suspected of having some form of growth dysregulation such as cancer. The invention further provides various immunogenic or therapeutic compositions and strategies for treating cancers that express 109P1D4 such as cancers of tissues listed in Table 1, including therapies aimed at inhibiting the transcription, translation, processing or function of 109P1D4 as well as cancer vaccines. In one aspect, the invention provides compositions, and methods comprising them, for treating a cancer that expresses 109P1D4 in a human subject wherein the composition comprises a carrier suitable for human use and a human unit dose of one or more than one agent that inhibits the production or function of 109P1 D4. Preferably, the carrier is a uniquely human carrier. In another aspect of the invention, the agent is a moiety that is immunoreactive with 109P1D4 protein. Non-limiting examples of such moieties include, but are not limited to, antibodies (such as single chain, monoclonal, polyclonal, humanized, chimeric, or human antibodies), functional equivalents thereof (whether naturally occurring or synthetic), and combinations thereof. The antibodies can be conjugated to a diagnostic or therapeutic moiety. In another aspect, the agent is a small molecule as defined herein. In another aspect, the agent comprises one or more than one peptide which comprises a cytotoxic T lymphocyte (CTL) epitope that binds an HLA class I molecule in a human to elicit a CTL response to 109P1 D4 and/or one or more than one peptide which comprises a helper T lymphocyte (HTL) epitope which binds an HLA class 11 molecule in a human to elicit an HTL response. The peptides of the invention may be on the same or on one or more separate polypeptide molecules. In a further aspect of the invention, the agent comprises one or more than one nucleic acid molecule that expresses one or more than one of the CTL or HTL response stimulating peptides as described above. In yet another aspect of the invention, the one or more than one nucleic acid molecule may express a moiety that is immunologically reactive with 109P1D4 as described above. The one or more than one nucleic acid molecule may also be, or encodes, a molecule that inhibits production of 109P1D4. Non-limiting examples of such molecules include, but are not limited to, those complementary to a nucleotide sequence essential for production of 109P1D4 (e.g. antisense sequences or molecules that form a triple helix with a nucleotide double helix essential for 109P1D4 production) or a ribozyme effective to lyse 109P1D4 mRNA. Note that to determine the starting position of any peptide set forth in Tables VIII-XXI and XXII to XLIX (collectively HLA Peptide Tables) respective to its parental protein, e.g., variant 1, variant 2, etc., reference is made to three factors: the particular variant, the length of the peptide in an HLA Peptide Table, and the Search Peptides in Table VII. Generally, a unique Search Peptide is used to obtain HLA peptides of a particular for a particular variant. The position of each Search Peptide relative to its respective parent molecule is listed in Table Vil. Accordingly, if a Search Peptide begins at position "X", one must add the value"X-1"to each position in Tables VIII-XXI and XXII to XLIX to obtain the actual position of the HLA peptides in their parental molecule. For example, if a particular Search Peptide begins at position 150 of its parental molecule, one must add 150-1, i. e., 149 to each HLA peptide amino acid position to calculate the position of that amino acid in the parent molecule. One embodiment of the invention comprises an HLA peptide, that occurs at least twice in Tables VIII-XXI and XXII to XLIX collectively, or an oligonucleotide that encodes the HLA peptide. Another embodiment of the invention comprises an HLA peptide that occurs at least once in Tables VIII-XXI and at least once in tables XXII to XLIX, or an oligonucleotide that encodes the HLA peptide.

5A Another embodiment of the invention comprises an isolated 109P1D4 protein, wherein the 109P1D4 protein comprises a polypeptide sequence as set forth in any one of SEQ ID NOs: 3, 5, 7, 9,11, 13,15,17 or 19. Another embodiment of the invention comprises an isolated antibody or fragment thereof that immunospecifically binds to an epitope on a 109P1D4 protein, wherein the 109P1D4 protein comprises a polypeptide sequence as set forth in any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17 or 19. Another embodiment of the invention is antibody epitopes, which comprise a peptide regions, or an oligonucleotide encoding the peptide region, that has one two, three, four, or five of the following characteristics: 6 i) a peptide region of at least 5 amino acids of a particular peptide of Figure 3, in any whole number increment up to the full length of that protein in Figure 3, that indudes an amino acid position having a value equal to or greater than 0.5, 0.6, 0.7. 0.8, 0.9, or having a value equal to 1.0, in the Hydrophilicity profile of Figure 5; li) a peptide region of at least 5 amino acids of a particular peptide of Figure 3, In any whole number increment up to the full length of that protein in Figure 3, that Includes an amino acid position having a value equal to or less than 0.5, 0.4, 0.3, 0.2, 0.1, or having a value equal to 0.0, in the Hydropathicity profile of Figure 6; iii) a peptide region of at least 5 amino acids of a particular peptide of Figure 3, In any whole number increment up to the full length of that protein in Figure 3, that includes an amino acid position having a value equal to or greater than 0.5, 0.6, 0.7, 0.8, 0.9, or having a value equal to 1.0, in the Percent Accessible Residues profile of Figure 7; Iv) a peptide region of at least 5 amino acids of a particular peptide of Figure 3, In any whole number Increment up to the full length of that protein In Figure 3, that includes an amino acid position having a value equal to or greater than 0.5, 0.6, 0.7, 0.8, 0.9, or having a value equal to 1.0, in the Average Flexibility profile of Figure 8; or v) a peptide region of at least 5 amino acids of a particular peptide of Figure 3, in any whole number Increment up to the full length of that protein in Figure 3, that includes an amino acid position having a value equal to or greater than 0.5, 0.6, 0.7,0.8, 0.9, or having a value equal to 1.0, in the Beta-turn profile of Figure 9. BRIEF DESCRIPTION OF THE FIGURES Figure 1. The 109P1D4 SSH sequence of 192 nudeotides. Figure 2. A) The cDNA and amino acid sequence of 109P1 D4 variant 1 (also caed "109P1D4 v.1" or 109P1D4 variant 1") is shown in Figure 2A. The start methionine is underlined. The open reading frame extends from nudeic acid 846-3911 including the stop codon. B) The cDNA and amino acid sequence of 109P1D4 variant 2 (also called '109P1D4 v.2") is shown in Figure 2B. The codon for the start methionine Is underlined. The open reading frame extends from nucleic acid 503-3667 including the stop codon. C) The cDNA and amino acid sequence of 109P1D4 variant 3 (also called "109P1D4 v.3") is shown in Figure 2C. The codon for the start methionine is undefined. The open reading frame extends from nucleic acid 846-4889 including the stop codon. D) The cDNA and amino acid sequence of 109P1D4 variant 4 (also called "109P1D4 v.4") Is shown in Figure 2D. The codon for the start methionine Is underlined. The open reading frame extends from nucleic add 846-4859 Including the stop codon. E) The cDNA and amino acid sequence of 109P1 D4 variant 5 (also called I 09P1 D4 v.5") is shown In Figure 2E. The codon for the start methlonine Is underlined. The open reading frame extends from nucleic acid 846-4778 including the stop codon. F) The cDNA and amino acid sequence of 109P1D4 variant 6 (also called "109P1D4 v.6") Is shown In Figure 2F. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 614-3727 including the stop codon. G) The cDNA and amino acid sequence of 109P1 D4 variant 7 (also called "109P1 D4 v.7") Is shown in Figure 2G. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 735-3881 including the stop codon. H) The cDNA and amino acid sequence of 109P1D4 variant 8 (also called "109P1D4 v.8") Is shown in Figure 2H. The codon for the start methionine Is underlined. The open reading frame extends from nucleic acid 735-4757 including the stop codon.

7 I) The cDNA and amino acid sequence of 109P1D4 variant 9 (also called "109P1D4 v.9") is shown in Figure 21. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 514-3627 including the stop codon. J) 109PID4 v.1, v.2 and v.3 SNP variants. Though these SNP variants are shown separately, they can also occur In any combinations and In any of the transcript variants listed above. K) 109PID4 v.6, v.7 and v.8 SNP variants. Though these SNP variants are shown separately, they can also occur in at combinations and in any of the transcript variants listed above. Figure 3. A) The amino acid sequence of 109P1D4 v.1 Is shown in FIgure 3A; it has 1021 amino acids. B) The amino acid sequence of 109P1 D4 v.2 Is shown In Figure 38; it has 1054 amino acids. C) The amino acid sequence of 109P1D4 v.3 Is shown In Figure 3C; It has 1347 amino acids. 0) The amino acid sequence of 109P1D4 v.4 is shown in Figure 3D; It has 1337 amino acids. E) The amino acid sequence of 109P1D4 v.6 is shown in Figure 3E; it has 1310 amino acids. F) The amino acid sequence of 109P1 D4 v.6 is shown in Figure 3F; it has 1037 amino acids. G) The amino acid sequence of 109P1D4 v.7 is shown in Figure 3G; it has 1048 amino acids. H) The amino acid sequence of 109P1 D4 v.8 is shown in Figure 3H; it has 1340 amino acids. 1) The amino acid sequence of 109PI1D4 v.9 is shown In Figure 31; it has 1037 amino acids. As used herein, a reference to 109P1D4 Includes all variants thereof, Including those shown in Figures 2, 3, 10, 11, and 12 unless the context clearly indicates otherwise. Figure 4. Alignment of 109P1 D4 v.1 Protein with protocadherin-1 1. Figure . Hydrophilicity amino acid profile of 109P1D4 v.1-v.9 determined by computer algorithm sequence analysis using the method of Hopp and Woods (Hopp T.P., Woods KR., 1981. Proc. Nall. Aced. Sci. U.S.A. 78:3824-3828) accessed on the Protscale website located on the World Wide Web at (expasy.ch/cgi-bin/protscale.pl) through the ExPasy molecular biology server. Figure 6. Hydropathicity amino acid profile of 109P1D4 v.1-v.9 determined by computer algorithm sequence analysis using the method of Kyte and Doolittle (Kyle J., Doolittle R.F., 1982. J. Mol. Biol. 157:105-132) accessed on the ProtScale website located on the World Wide Web at (.expasy.ch/cgi-bin/protscale.pl) through the ExPasy molecular biology server. Figure 7. Percent accessible residues amino acid profile of 109P1D4 v.1-v.9 determined by computer algorithm sequence analysis using the method of Janin (Janin J., 1979 Nature 277:491-492) accessed on the ProtScale website located on the World Wide Web at (.expasy.ch/cgi-bin/protscale.pl) through the ExPasy molecular biology server. Figure 8. Average flexibility amino acid profile of 109P1D4 v.1-v.9 determined by computer algorithm sequence analysis using the method of Bhaskaran and Ponnuswamy (Bhaskaran R., and Ponnuswamy P.K., 1988. Int. J. Pept Protein Res. 32:242-255) accessed on the ProtScale website located on the World Wide Web at (.expasy.ch/cgi-bin/protscale.pl) through the ExPasy molecular biology server. * Figure 9. Beta-tum amino acid profile of 109P1D4 v.1-v.9 determined by computer algorithm sequence analysis using the method of Deleage and Roux (Deleage, G., Roux B. 1987 Protein Engineering 1:289-294) accessed on the ProtScale website located on the World Wide Web at (.expasy.ch/cgi-bIn/protscale.pl) through the ExPasy molecular biology server. Figure 10. Structure of transcript variants of 109P1D4. Variants 109P1D4 v.2 through v.9 were transcript variants of v.1. Variant v.2 shared mIddle portion of v.1 sequence (the 3' portion of exon I and 5' portion of exon 2). Variant 8 v.6 was similar to v.2 but added an extra exon between exons 1 and 2 of v.2. V.3 shared exon 1 and 5' portion of exon 2 with v.1 with five additional exons downstream. Compared with v.3, v.4 deleted exon 4 of v.3 while v.5 deleted exons 3 and 4 of v.3. Variant v.5 lacked exons 3 and 4. This gene (called PCD1 1) is located in sex chromosomes X and Y. Ends of exons in the transcripts are marked above the boxes. Potential exons of this gene are shown in order as on the human genome. Poly A tails and single nucleotide differences are not shown in the figure. Lengths of introns and exons are not proportional. Figure 1i. Schematic alignment of protein variants of 109P1D4. Variants 109P1D4 v.2 through v.9 were proteins translated from the corresponding transcript variants. All these protein variants shared a common portion of the sequence, I.e., 3-1011 of v.1, except for a few amino acids different in this segment resulted from SNP in the transcripts. Variant v.6 and v.9 were the same except for two amino acids at 906 and 1001. Variant v.8 was almost the same as v.5, except for the N-terminal end, and a 2-aa deletion at 1117-8. Single amino acid difference was not shown. Numbers in parentheses corresponded to positions in variant v.3. Figure 12. Intentionally Omitted. Figure 13. Figures 13(a)-(l): Secondary structure and transmembrane domains prediction for 109P1D4 protein variants 1-9 (v.1 - (SEQ ID NO: a1); v.2 - (SEQ ID NO 32); v.3 - (SEQ ID NO: 33); v.4 - (SEQ ID NO: 34); v.5 - (SEQ ID NO: 35); v.6 - (SEQ ID NO 36); v.7 - (SEQ ID NO: 37); v.8 - (SEQ ID NO: 38); v.9 - (SEQ ID NO: 39)). The secondary structures of 109P1 D4 protein variants were predicted using the HNN - Hierarchical Neural Network method (NPS@: Network Protein Sequence Analysis TIBS 2000 March Vol. 25, No 3 [291]:147-150 Combet C., Blanchet C., Geouron C. and Deleage G., httpJ/pbi.ibcp.fr/cgi-binlnpsa-automat.p?page=npsa-nn.html), accessed from the ExPasy molecular biology server located on the World Wide Web at (.expasy.chltools). This method predicts the presence and location of alpha helices, extended strands, and random coils from the primary protein sequence. The percent of the protein variant in a given secondary structure is also listed. Figures 13(J)-(R) top panels: Schematic representation of the probability of existence of transmembrane regions of 109P1 D4 variants based on the TMpred algorithm of Hofmann and Stoffel which utilizes TMBASE (K. Hofmann, W. Stoffel. TMBASE - A database of membrane spanning protein segments Blol. Chem. Hoppe-Seyler 374:166, 1993). Figures 13(J)-R) bottom panels: Schematic representation of the probability of the existence of transmembrane regions of 109P1 D4 variants based on the TMHMM algorithm of Sonnhammer, von Heijne, and Krogh (Erik L.L Sonnhammer, Gunnar von Heijne, and Anders Krogh: A hidden Markov model for predicting transmembrane helices in protein sequences. In Proc. of Sixth Int. Conf. on Intelligent Systems for Molecular Biology, p 175-182 Ed J. Glasgow, T. Littlejohn, F. Major, R. Lathrop, D. Sankoff, and C. Sensen Menlo Park, CA' AAA[ Press, 1998). The TMpred and TMHMM algorithms are accessed from the ExPasy molecular biology server located on the World Wide Web at (.expasy.ch/tools). Figure 14. Expression of 109P1D41n Lymphoma Cancer Patient Specimens. RNA was extracted from peripheral blood lymphocytes, cord blood Isolated from normal individuals, and from lymphoma patient cancer specimens. Northern blots with 1Opg of total RNA were probed with the 109P1 D4 sequence. Size standards in kilobases are on the side. Results show expression of 109P1 D4 In lymphoma patient specimens but not In the normal blood cells tested. Figure 15. Expression of 109P1D4 by RT-PCR. First strand cDNA was prepared from vital pool I (liver, lung and kidney), vital pool 2 (pancreas, colon and stomach), prostate cancer pool, bladder cancer pool, kidney cancer pool, colon cancer pool, lung cancer pool, ovary cancer pool, breast cancer pool, cancer metastasis pool, and pancreas cancer pool. Normalization was performed by PCR using primers to acting and GAPDH. Semi-quantitative PCR, using primers to S109P1D04, was performed at 30 cycles of amplification. Results show strong expression of 109P1D4 in all cancer pools tested. Very low expression was detected In the vital pools. Figure 16. Expression of 109PID4 In normal tissues. Two multiple tissue northem blots (Clontech), both with 2 pg of mRNAJane, were probed with the 109P1 D4 SSH fragment Size standards In kilobases (kb) are indicated on the side.

9 Results show expression of approximately 10 kb 109P1D4 transcript in ovary. Weak expression was also detected in placenta and brain, but not in the other normal tissues tested. Figure 17. Expression of 109P1 D4 In human cancer cell lines. RNA was extracted from a number of human prostate and bone cancer cell lines. Northern blots with 10 pg of total RNAlane were probed with the 109P1 D4 SSH fragment Size standards in kilobases (kb) are indicated on the side. Results show expression of 109P1D4 in LAPC-9AD, LAPC-9Al, LNCaP prostate cancer cell lines, and in the bone cancer cell lines, SK-ES-1 and RD-ES. Figure 18. Figure 18A: 109P1D4 Expression In Human Normal Tissues. An cDNA dot blot containing 76 different samples from human tissues was analyzed using a 109P1D4 SSH probe. Expression was only detected in multiple areas of the brain, placenta, ovary, and fetal brain, amongst all tissues tested. Figure 18B: Expression of 109P1D4 In patient cancer specimens. Expression of 109P1D4 was assayed In a panel of human cancers (T) and their respective matched normal tissues (N) on RNA dot blots. Upregulated expression of 109P1 D4 in tumors compared to normal tissues was observed In uterus, lung and stomach. The expression detected In normal adjacent tissues (isolated from diseased tissues) but not in normal tissues (isolated from healthy donors) may Indicate that these tissues are not fully normal and that 109P1D4 may be expressed in early stage tumors. Figure 19. 10P1 D4 Expression In Lung Cancer Patient Specimens. RNA was extracted from normal lung, prostate cancer xenograft LAPC-9AD, bone cancer cell line RD-ES, and lung cancer patient tumors. Northern blots with 10 pg of total RNA were probed with 109P1 D4. Size standards in kilobases are on the side. Results show strong expression of 109P1 D4 in lung tumor tissues as well as the RD-ES cell line, but not In normal lung. Figure 20. Expression of soluble secreted Tag5 109P1 D4 in 293T cells. 293T cells were transfected with either an empty vector or with the Tag5 secretion vector encoding the extracellular domain (ECD; amino acids 24-812) of 109P1D4 vacant I fused to a Myc/His epitope Tag. 2 days later, cells and media harvested and analyzed for expression of the recombinant Tag5 109P1D4 protein by SDS-PAGE followed by anti-His epitope tag Western blotting. An arrow Indicates the immunoreactive band corresponding to the 109P1D4 ECD present in the media and the lysate from Tag5 109P1D4 transfected cells. Figure 21. Expression of 109P1 D4 protein In 293T cells. 293T cells were transfected with either an empty vector or with pCDNA3.1 vector encoding the full length cDNA of 109P1D4 variant I fused to a Myc/His epitope Tag. 2 days later, cells were harvested and analyzed for expression of 109P1D4 variant I protein by SDS-PAGE followed by anti-His epitope tag Western blotting. An arrow Indicates the immunoreactive band corresponding to the full length 109PID4 variant I protein expressed in cells transfected with the 109P1 D4 vector but not In control cells. Figure 22. Tyrosine phosphorylation of 109P1 D4 after pervanadate treatment 293T cells were transfected with the neomycin resistance gene alone or with 109P1D4 In pSRp vector. Twenty four hours after transfection, the cells were either left In 10% serum or grown In 0.1% serum overnight. The cells were then left untreated or were treated with 200 pM pervanadate (1:1 mixture of Na3VO4 and H202) for 30 minutes. The cells were lysed In Triton X-1 00, and the 109P1 D4 protein was Immunoprecipitated with anti-His monoclonal antibody. The lmmunoprecipitates were run on SDS-PAGE and then Western blotted with either anti-hosphotyrosine (upper panel) or anti-His (lower panel). The 109P1D4 protein Is phosphorylated on tyrosine In response to pervanadate treatment, and a large amount of the protein moves to the Insoluble fraction following pervanadate-Induced activation. Figure 23. Effect of 109PID4 RNA on cell proliferation. LNCaP cells were transfected with Upofectamine 2000 alone or with siRNA oligonudeotides. The sIRNA oigonucleotides Included a negative control, Luc4, specific for Luciferase, a positive control, Eg5, specific for the mitotic spindle protein Eg5, or three siRNAs specific for the 109P1D4 protein, 109P1D4.a, 109P1D4.c and 109P1D4.d at 20 nM concentration. Twenty four hours after transfection, the cells were pulsed 10 with 3 H-thymidine and incorporation was measured after 72 hours. All three siRNAs to 109P1 D4 inhibited the proliferation of LNCaP cells, indicating that 109P1D4 expression is important for the cell growth pathway of these cancer cells. DETAILED DESCRIPTION OF THE INVENTION Outline of Sections I.) Definitions I1.) 109P1D4 Polynudeotides llA) Uses of 109P1D4 Polynucleotides IIA1.) Monitoring of Genetic Abnormalities Il.A2.) Antisense Embodiments ILA.3.) Primers and Primer Pairs IIA4.) Lolation of 109PID4-Encoding Nucleic Acid Molecules A.A.5.) Recombinant Nucleic Acid Molecules and Host-Vector Systems I.) 109P1D4-related Proteins IA) Motif-bearing Protein Embodiments ilI.B.) Expression of 109P1D4-related Proteins IIlC.) Modifications of I09P1 D4-related Proteins i1.D.) Uses of 109P1 D4-related Proteins IV.) 109P1D4 Antibodles V.) 109P1D4 Cellular immune Responses VI.) 109P1D4 Transgenlc Animals VII.) Methods for the Detection of 109PiD4 VIll.) Methods for Monitoring the Status of 109P1D04-related Genes and Their Products IX) Identification of Molecules That Interact With 109PI D4 X) Therapeutic Methods and Compositions XA) Anti-Cancer Vaccines X.B.) 109P1D4 as a Target for Antibody-Based Therapy X.C.) 109P1D4 as a Target for Cellular immune Responses X.C.1. Minigene Vaccines X.C.2. Combinations of CTL Peptides with Helper Peptides X.C.3. Combinations of CTL Peptides with T Cell Priming Agents X.C.4. Vaccine Compositions Comprising DC Pulsed with CTL and/or HTL Peptildes X.D.) Adoptive Immunotherapy X.E.) Administration of Vaccines for Therapeutic or Prophylactic Purposes XI.) Diagnostic and Prognostic Embodiments of 109P1 D4. X11.) Inhibition of 109PID4 Protein Function XIIA) Inhibition of 109PID4 With Intracellular Antibodies XHI.B.) Inhibition of 109P1D4 with Recombinant Proteins X1I.C.) Inhibition of 109P1D4 Transcription or Translation XIl.D.) General Considerations for Therapeutic Strategies XIl) Identification, Characterization and Use of Modulators of 109P1D4 XIV.) KITSIArticies of Manufacture 11 1.)-Definitions: Unless otherwise defined, all terms of art, notations and other scientific terms or terminology used herein are intended to have the meanings commonly understood by those of skill in the art to which this invention pertains. In some cases, terms with commonly understood meanings are defined herein for clarity and/or for ready reference, and the inclusion of such definitions herein should not necessarily be construed to represent a substantial difference over what is generally understood in the art. Many of the techniques and procedures described or referenced herein are well understood and commonly employed using conventional methodology by those skilled in the art, such as, for example, the widely utilized molecular cloning methodologies described in Sambrook et al., Molecular Cloning : A Laboratory Manual 2nd. edition (1989) Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N. Y. As appropriate, procedures involving the use of commercially available kits and reagents are generally carried out in accordance with manufacturer defined protocols and/or parameters unless otherwise noted. Any discussion of documents, acts, materials, devices, articles or the like which has been included in the present specification is solely for the purpose of providing a context for the present invention. It is not to be taken as an admission that any or all of these matters form part of the prior art base or were common general knowledge in the field relevant to the present invention as it existed before the priority date of each claim of this application. Throughout this specification the word "comprise", or variations such as "comprises" or "comprising", will be understood to imply the infusion of a stated element, integer or step, or group of elements, integers or steps, but not the exclusion of any other element, integer or step, or group of elements, integers or steps. The terms "advanced prostate cancer", "locally advanced prostate cancer", "advanced disease" and "locally advanced disease" mean prostate cancers that have extended through the prostate capsule, and are meant to include stage C disease under the American Urological Association (AUA) system, stage CI-C2 disease under the Whitmore-Jewett system, and stage T3-T4 and N+ disease under the TNM (tumor, node, metastasis) system. In general, surgery is not recommended for patients with locally advanced disease, and these patients have substantially less favorable outcomes compared to patients having clinically localized (organ-confined) prostate cancer. Locally advanced disease is clinically identified by palpable evidence of induration beyond the lateral border of the prostate, or asymmetry or induration above the prostate base. Locally advanced prostate cancer is presently diagnosed pathologically following radical prostatectomy if the tumor invades or penetrates the prostatic capsule, extends into the surgical margin, or invades the seminal vesicles. "Altering the native glycosylation patten" is intended for purposes herein to mean deleting one or more carbohydrate moieties found in native sequence 109P1 D4 (either by removing the underlying glycosylation site or by deleting the glycosylation by chemical and/or enzymatic means), and/or adding one or more glycosylation sites that are not present in the native sequence 109P1D4. In addition, the phrase includes qualitative changes in the glycosylation of the native proteins, involving a change in the nature and proportions of the various carbohydrate moieties present. The term "analog" refers to a molecule which is structurally similar or shares similar or corresponding attributes with another molecule (e. g. a 109P1 4-related protein). For example, an analog of a 109P1 D4 protein can be specifically bound by an antibody or T cell that specifically binds to 109P1 D4. The term "antibody" is used in the broadest sense. Therefore, an "antibody" can be naturally occurring or man made such as monoclonal antibodies produced by conventional hybridoma technology. Anti-109P1D4 antibodies comprise monoclonal and polyclonal antibodies as well as fragments containing the antigen-binding domain and/or one or more complementarity determining regions of these antibodies.

11A An "antibody fragment" is defined as at least a portion of the variable region of the immunoglobulin molecule that binds to its target, i.e., the antigen-binding region. In one embodiment, it specifically covers single anti-109P1D4 antibodies and clones thereof (including agonist, antagonist and neutralizing antibodies) and anti-109P1D4 antibody compositions with polyepitopic specificity. The term "codon optimized sequences" refers to nucleotide sequences that have been optimized for a particular host species by replacing any codons having a usage frequency of less than about 20%. Nucleotide sequences that have been optimized for expression in a given host species by elimination of spurious polyadenylation sequences, elimination of exonfintron splicing signals, elimination of transposon-like repeats and/or optimization of GC content in addition to codon 12 optimization are referred to herein as an "expression enhanced sequences." A combinatonal library" is a collection of diverse chemical compounds generated by either chemical synthesis or biological synthesis by combining a number of chemical 'building blocks" such as reagents. For example, a linear combinatorial chemical library, such as a polypeptide (e.g., mutein) library, is formed by combining a set of chemical building blocks called amino acids in every possible way for a given compound length (i.e., the number of amino acids in a polypeptide compound). Numerous chemical compounds are synthesized through such combinatorial mixing of chemical building blocks (Gallop et al., J. Med. Chem. 37(9):1233-1251 (1994)). Preparation and screening of combinatorial libraries Is well known to those of skill in the art. Such combinatorial chemical libraries Include, but are not limited to, peptide libraries (see, e.g., U.S. Patent No. 5,010,175, Furka, Pept. Prot. Res. 37:487-493 (1991), Houghton et al., Nature, 354:84-88 (1991)), peptolds (PCT Publication No WO 91/19735), encoded peptides (PCT Publication WO 93/20242), random blo- oligomers (PCT Publication WO 92/00091), benzodiazepines (U.S. Pat. No. 5,288,514), diversomers such as hydantoins, benzodiazepines and dipeptides (Hobbs et al., Proc. Nat Acad. Sci. USA 90:6909-6913 (1993)), vinylogous polypeptides (Hagihara et al., J. Amer. Chem. Soc. 114:6568 (1992)), nonpeptidal peptidomimetics with a Beta-D-Glucose scaffolding (Hirschmann et al., J. Amer. Chem. Soc. 114:9217-9218 (1992)), analogous organic syntheses of small compound libraries (Chen et al., J. Amer. Chem. Soc. 116:2661 (1994)), oligocarbamates (Cho, et al., Science 261:1303 (1993)), and/or peptidyl phosphonates (Campbell et al., J. Org. Chem. 59-658 (1994)). See, generally, Gordon et al., J. Med. Chem. 37:1385 (1994), nucleic acid libraries (see, e.g., Stratagene, Corp.), peptide nucleic acid libraries (see, e.g., U.S. Patent 5,539,083), antibody libraries (see, e.g., Vaughn et al., Nature Biotechnology 14(3): 309-314 (1996), and PCTAJS96/10287), carbohydrate libraries (see, e.g., Uang et al., Science 274:1520-1522 (1996), and U.S. Patent No. 5,593,853), and small organic molecule libraries (see, e.g., benzodiazepines, Baum, C&EN, Jan 18, page 33 (1993); isoprenoids, U.S. Patent No. 5,569,588; thiazolidinones and metathlazanones, U.S. Patent No. 5,549,974; pyrrolidines, U.S. Patent Nos. 5,525,735 and 5,519,134; morpholino compounds, U.S. Patent No. 5,506, 337; benzodiazepines, U.S. Patent No. 5,288,514; and the like). Devices for the preparation of combinatorial libraries are commercially available (see, e.g., 357 NIPS, 390 NIPS, Advanced Chem Tech, Louisville KY; Symphony, Rainin, Wobum, MA; 433A, Applied Biosystems, Foster City, CA; 9050, Plus, Millipore, Bedford, NIA). A number of well-known robotic systems have also been developed for solution phase chemistries. These systems include automated workstations such as the automated synthesis apparatus developed by Takeda Chemical Industries, LTD. (Osaka, Japan) and many robotic systems utilizing robotic arms (Zymate H, Zymark Corporation, Hopkinton, Mass.; Orca, Hewlett-Packard, Palo Alto, Calif.), which mimic the manual synthetic operations performed by a chemist Any of the above devices are suitable for use with the present invention. The nature and Implementation of modifications to these devices (if any) so that they can operate as discussed herein will be apparent to persons skilled in the relevant art. In addition, numerous combinatorial libraries are themselves commercially available (see, e.g., ComGenex, Princeton, NJ; Asinex, Moscow, RU; Tripos, Inc., St. Louis, MO; ChemStar, Ltd, Moscow, RU; 3D Pharmaceuticals, Exton, PA; Martek Biosciences, Columbia, MD; etc.). The term "cytotoxic agent' refers to a substance that inhibits or prevents the expression activity of cells, function of cells and/or causes destruction of cells. The term is intended to include radioactive isotopes chemotherapeutic agents, and toxins such as small molecule toxins or enzymatically active toxins of bacterial, fungal, plant or animal origin, including fragments and/or variants thereof. Examples of cytotoxic agents include, but are not limited to auristatins, auromycins, maytansinoids, yttrium, bismuth, ricin, ricin A-chain, combrestatin, duocarmycins, dolostatins, doxorubicin, daunorubicin, taxol, cisplatin, cc1065, ethidium bromide, mitomycln, etoposIde, tenoposide, vincristine, vinblastine, colchicine, dihydroxy anthracin dione, actinomycin, diphtheria toxin, Pseudomonas exotoxin (PE) A, PE4O, abrin, abrin A chain, modeccin A chain, 13 alpha-sarcin, gelonin, mitogellin, retstrictocin, phenomycin, enomycin, curicin, crotin, calicheamicin, Sapaonaria officinalis inhibitor, and glucocorticoid and other chemotherapeutic agents, as well as radioisotopes such as At 21 1, 1131, 1125, Y9D, Rel8, Re 1 , Sm 1 sa, Bi212or213, Pa2 and radioactive isotopes of Lu induding Lu'n'. Antibodies may also be conjugated to an anti cancer pro-drug activating enzyme capable of converting the pro-drug to Its active form. The "gene product" Is sometimes referred to herein as a protein or mRNA. For example, a "gene product of the invention' Is sometimes referred to herein as a 'cancer amino acid sequence", 'cancer protein", 'protein of a cancer listed in Table I', a "cancer mRNA", 'mRNA of a cancer listed in Table I", etc. In one embodiment, the cancer protein Is encoded by a nucleic acid of Figure 2. The cancer protein can be a fragment, or alternatively, be the full-length protein to the fragment encoded by the nucleic acids of Figure 2. In one embodiment, a cancer amino acid sequence is used to determine sequence Identity or similarity. In another embodiment, the sequences are naturally occurring allelic variants of a protein encoded by a nucleic acid of Figure 2. In another embodiment, the sequences are sequence variants as further described herein. 'High throughput screening" assays for the presence, absence, quantification, or other properties of particular nudeic acids or protein products are well known to those of skill in the art. Similarly, binding assays and reporter gene assays are similarly well known. Thus, e.g., U.S. Patent No. 5,559,410 discloses high throughput screening methods for proteins; U.S. Patent No. 5,585,639 discloses high throughput screening methods for nudeic acid binding (i.e., In arrays); while U.S. Patent Nos. 5,576,220 and 5,541,061 disclose high throughput methods of screening for ligand/antibody binding. In addition, high throughput screening systems are commercially available (see, e.g., Amersham Biosciences, Piscataway, NJ; Zymark Corp., Hopkinton, MA; Air Technical Industries, Mentor, OH; Beckman Instruments, Inc. Fullerton, CA; Precision Systems, Inc., Natick, MA; etc.). These systems typically automate entire procedures, including all sample and reagent pipetting, liquid dispensing, timed Incubations, and final readings of the microplate in detector(s) appropriate for the assay. These configurable systems provide high throughput and rapid start up as well as a high degree of flexibility and customization. The manufacturers of such systems provide detailed protocols for various high throughput systems. Thus, e.g., Zymark Corp. provides technical bulletins describing screening systems for detecting the modulation of gene transcription, ligand binding, and the like. The term 'homolog" refers to a molecule which exhibits homology to another molecule, by for example, having sequences of chemical residues that are the same or similar at corresponding positions. "Human Leukocyte Antigen' or 'HLA Is a human class I or class II Major Histocompatibility Complex (MHC) protein (see, e.g., Stites, et al., IMMUNOLOGY, 8TH ED., Lange Publishing, Los Altos, CA (1994). The terms 'hybridize", 'hybridizing', 'hybridizes' and the like, used In the context of polynucleotides, are meant to refer to conventional hybridization conditions, preferably such as hybridization In 50% formamide/6XSSC/0.1 % SDS1 00 pg/ml ssDNA, in which temperatures for hybridization are above 37 degrees C and temperatures for washing in 0.1XSSC/0.1% SDS are above 55 degrees C. The phrases "isolated' or "biologically pure' refer to material which is substantially or essentially free from components which normally accompany the material as it Is found in its native state. Thus, isolated peptides In accordance with the invention preferably do not contain materials normally associated with the peptides in their in situ environment For example, a polynudeotide is said to be "Isolated" when it is substantially separated from contaminant polynudeotides that correspond or are complementary to genes other than the 109P1 D4 genes or that encode polypeptides other than 109P1 D4 gene product or fragments thereof. A skilled arisan can readily employ nudeic acid isolation procedures to obtain an isolated 109P1 D4 polynudeotide. A protein is said to be Isolated," for example, when physical, mechanical or chemical methods are employed to remove the 109P1 D4 proteins from celular constituents that are normally associated with the protein. A skilled artisan can readily 14 employ standard purification methods to obtain an isolated 109P1D4 protein. Alternatively, an isolated protein can be prepared by chemical means. The term "mammar refers to any organism dassitied as a mammal, Including mice, rats, rabbits, dogs, cats, cows, horses and humans. In one embodiment of the invention, the mammal is a mouse. In another embodiment of the invention, the mammal is a human. The terms "metastatic prostate cancer" and "metastatic disease mean prostate cancers that have spread to regional lymph nodes or to distant sites, and are meant to Include stage D disease under the AUA system and stage TxNxM+ under the TNM system. As is the case with locally advanced prostate cancer, surgery is generally not indicated for patients with metastatic disease, and hormonal (androgen ablation) therapy is a preferred treatment modality. Patients with metastatic prostate cancer eventually develop an androgen-refractory state within 12 to 18 months of treatment initiation. Approximately half of these androgen-refractory patients die within 6 months after developing that status. The most common site for prostate cancer metastasis is bone. Prostate cancer bone metastases are often osteoblastic rather than osteolytic (i.e., resulting in net bone formation). Bone metastases are found most frequently in the spine, followed by the femur, pelvis, rib cage, skull and humerus. Other common sites for metastasis Indude lymph nodes, lung, liver and brain. Metastatic prostate cancer is typically diagnosed by open or laparoscopic pelvic lymphadenectomy, whole body radionuclide scans, skeletal radiography, and/or bone lesion biopsy. The term "modulator" or test compound" or "drug candidate' or grammatical equivalents as used herein describe any molecule, e.g., protein, oligopeptide, small organic molecule, polysaccharide, polynucleotide, etc., to be tested for the capacity to directly or indirectly alter the cancer phenotype or the expression of a cancer sequence, e.g., a nucleic acid or protein sequences, or effects of cancer sequences (e.g., signaling, gene expression, protein interaction, etc.) In one aspect, a modulator will neutralize the effect of a cancer protein of the invention. By "neutralize" Is meant that an activity of a protein is inhibited or blocked, along with the consequent effect on the cell. In another aspect, a modulator will neutralize the effect of a gene, and its corresponding protein, of the invention by normalizing levels of said protein. In preferred embodiments, modulators alter expression profiles, or expression profile nucleic acids or proteins provided herein, or downstream effector pathways. In one embodiment, the modulator suppresses a cancer phenotype, e.g. to a normal tissue fingerprint In another embodiment, a modulator induced a cancer phenotype. Generally, a plurality of assay mixtures Is run in parallel with different agent concentrations to obtain a differential response to the various concentrations. Typically, one of these concentrations serves as a negative control, i.e., at zero concentration or below the level of detection. Modulators, drug candidates or test compounds encompass numerous chemical classes, though typically they are organic molecules, preferably small organic compounds having a molecular weight of more than 100 and less than about 2,500 Daltons. Preferred small molecules are less than 2000, or less than 1500 or less than 1000 or less than 500 D. Candidate agents comprise functional groups necessary for structural Interaction with proteins, particularly hydrogen bonding, and typically Include at least an amine, carbonyl, hydroxyl or carboxyl group, preferably at least two of the functional chemical groups. The candidate agents often comprise cyclical carbon or heterocyclic structures and/or aromatic or polyaromatic structures substituted with one or more of the above functional groups. Modulators also comprise blomolecules such as peptides, saccharides, fatty acids, steroids, purines, pyrimidines, derivatives, structural analogs or combinations thereof. Particularly preferred are peptides. One class of modulators are peptides, for example of from about five to about 35 amino acids, with from about five to about 20 amino acids being preferred, and from about 7 to about 15 being particularly preferred. Preferably, the cancer modulatory protein is soluble, Includes a non-transmembrane region, and/or, has an N terminal Cys to aId in solubility. In one embodiment, the C-terminus of the fragment Is kept as a free acid and the N-tenninus Is a free amine to aid in coupling, i.e., to cysteine. In one embodiment, a cancer protein of the invention Is conjugated to an I5 immunogenic agent as discussed herein. In one embodiment, the cancer protein is conjugated to BSA. The peptides of the invention, e.g., of preferred lengths, can be linked to each other or to other amino acids to create a longer peptide/protein. The modulatory peptides can be digests of naturally occurring proteins as Is outlined above, random peptides, or 'biased" random peptides. In a preferred embodiment peptide/protein-based modulators are antibodies, and fragments thereof, as defined herein. Modulators of cancer can also be nucleic acids. Nucleic acid modulating agents can be naturally occurring nucleic acids, random nudeic acids, or 'biased" random nucleic acids. For example, digests of prokaryotic or eukaryotic genomes can be used in an approach analogous to that outlined above for proteins. The term monoclonall antibody" refers to an antibody obtained from a population of substantially homogeneous antibodies, i.e., the antibodies comprising the population are identical except for possible naturally occurring mutations that are present in minor amounts. A "motif", as In biological motif of a 109P1 D4-related protein, refers to any patten of amino acids forming part of the primary sequence of a protein, that Is associated with a particular function (e.g. protein-protein interaction, protein-DNA interaction, etc) or modification (e.g. that is phosphorylated, glycosylated or amidated), or localization (e.g. secretory sequence, nuclear localization sequence, etc.) or a sequence that is correlated with being immunogenic, either humorally or cellularly. A motif can be either contiguous or capable of being aligned to certain positions that are generally correlated with a certain function or property. In the context of HLA motifs, "motif" refers to the pattern of residues in a peptide of defined length, usually a peptide of from about 8 to about 13 amino acids for a class I HLA motif and from about 6 to about 25 amino acids for a dass I HLA motif, which is recognized by a particular HLA molecule. Peptide motifs for HLA binding are typically different for each protein encoded by each human HLA allele and differ In the pattern of the primary and secondary anchor residues. A "pharmaceutical excipient" comprises a material such as an adjuvant, a carrier, pH-adjusting and buffering agents, tonicity adjusting agents, wetting agents, preservative, and the like. "Pharmaceutically acceptable" refers to a non-toxic, inert, and/or composition that is physiologically compatible with humans or other mammals. The term "polynucleotide' means a polymeric form of nucleotides of at least 10 bases or base pairs in length, either ribonucleotides or deoxynudeotides or a modified form of either type of nucleotide, and is meant to include single and double stranded forms of DNA and/or RNA. In the art, this term If often used interchangeably with "oligonudeoide". A polynudeotide can comprise a nucleotide sequence disclosed herein wherein thymldlne (T), as shown for example in Figure 2, can also be uracil (U); this definition pertains to the differences between the chemical structures of DNA and RNA, in particular the observation that one of the four major bases In RNA is uracil (U) instead of thymidine (T). The term "polypeptide" means a polymer of at least about 4, 5, 6, 7, or 8 amino acids. Throughout the specification, standard three letter or single letter designations for amino acids are used. In the art, this term Is often used interchangeably with "peptide" or "protein". An HLA *primary anchor residue" is an amino acid at a specific position along a peptide sequence which is understood to provide a contact point between the Immunogenic peptide and the HLA molecule. One to three, usually two, primary anchor residues within a peptide of defined length generally defines a "motif" for an immunogenic peptide. These residues are understood to fit in close contact with peptide binding groove of an HLA molecule, with their side chains buried In specific pockets of the binding groove. In one embodiment, for example, the primary anchor residues for an HLA class I molecule are located at position 2 (from the amino terminal position) and at the carboxyl terminal position of a 8, 9, 10, 11, or 12 residue peptide epitope in accordance with the invention. Alternatively, In another embodiment, the primary anchor 16 residues of a peptide binds an HLA class Il molecule are spaced relative to each other, rather than to the termini of a peptide, where the peptide is generally of at least 9 amino acids in length. The primary anchor positions for each motif and supermotif are set forth in Table IV. For example, analog peptides can be created by altering the presence or absence of particular residues In the primary and/or secondary anchor positions shown in Table IV. Such analogs are used to modulate the binding affinity and/or population coverage of a peptide comprising a particular HLA motif or supermotif. 'Radioisotopes" include, but are not limited to the following (non-limiting exemplary uses are also set forth): Examples of Medical Isotopes: Isotope Description of use Actinium-225 See Thorium-229 (Th-229) (AC-225) Actinium-227 Parent of Radium-223 (Ra-223) which is an alpha emitter used to treat metastases in the skeleton (AC-227) resulting from cancer (i.e., breast and prostate cancers), and cancer radioimmunotherapy Bismuth-212 See Thorum-228 (Th-228) (Bi-212) Bismuth-213 See Thorium-229 (Th-229) (Ni-21 3) Cadmium-109 Cancer detection (Cd-109) Cobalt-60 Radiation source for radiotherapy of cancer, for food irradiators, and for sterilization of medical (Co-60) supplies Copper-64 A positron emitter used for cancer therapy and SPECT Imaging (Cu-64) Copper-67 Beta/gamma emitter used in cancer radioimmunotherapy and diagnostic studies (i.e., breast and (Cu-67) colon cancers, and lymphoma} Dysprosium-166 Cancer radioimmunotherapy (Dy-i 66) Erblum-169 Rheumatoid arthritis treatment, particularly for the small joints associated with fingers and toes (Er-1 69) Europium- 152 Radiation source for food irradiation and for sterilization of medical supplies (Eu-I52) Euroium-154 Radiation source for food Irradiation and for sterilization of medical supplies (Eu-I 54) Gad m-153 Osteoporosis detection and nuclear medical quality assurance devices Gold-I 98 Implant and Intracavity therapy of ovarian, prostate, and brain cancers (Au-I 98) Holmium-166 Multiple myeloma treatment in targeted skeletal therapy, cancer radioimmunotherapy, bone (Ho-166) marrow ablation, and rheumatoid arthritis treatment Osteoporosis detection, diagnostic imaging, tracer drugs, brain cancer treatment, radiolabefing, Iodine-125 tumor Imaging, mapping of receptors in the brain, interstitial radiation therapy, brachytherapy for (I-125) treatment of prostate cancer, determination of glomerular filtration rate (GFR), determination of plasma volume, detection of deep vein thrombosis of the legs Iodine-131 Thyroid function evaluation, thyroid disease detection, treatment of thyroid cancer as wel as other (1-131) non-malignant thyroid diseases (i.e., Graves disease, goiters, and hyperthyroidism), treatment of leukemia, lymphoma, and other forms of cancer (e.g., breast cancer) using radioimmunotherapy IrIdium-192 Brachytherapy, brain and spinal cord tumor treatment, treatment of blocked arteries (i.e., (Ir-192) arteriosclerosis and restenosis), and Implants for breast and prostate tumors Lutetium-177 Cancer radioimmunotherapy and treatment of blocked arteries (i.e., arteriosclerosis and (Lu-177) restenosis) Parent of Technetium-99m (Tc-99m) which Is used for imaging the brain, liver, lungs, heart, and Molybdenum-99 other organs. Currently, To-99m Is the most widely used radioisotope used for diagnostic imaging (Mo-99) of various cancers and diseases Involving the brain, heart, liver, lungs; also used in detection of deep vein thrombosis of the legs Osmium-194 Cancer radioimmunotherapy (Os-I 94) Palladium-103 Prostate cancer treatment 17 (Pd- 103) Platinum-i 95m Studies on biodistribution and metabolism of cisplatin, a chemotherapeutic drug (Pt-195m) Polycythemia rubra vera (blood cell disease) and leukemia treatment, bone cancer Phosphorus-32 diagnosisitreatment; colon, pancreatic, and river cancer treatment; radiolabeling nucleic acids for (P-32) in vitro research, diagnosis of superficial tumors, treatment of blocked arteries (i.e., arteriosclerosis and restenosis), and intracavity therapy Phosphorus-33 Leukemia treatment, bone disease diagnosisitreatment, radiolabeling, and treatment of blocked (P-33) arteries (i.e., arteriosclerosis and restenosis) Radium-223 See Actinium-227 (Ac-227) (Ra-223) Rhenium-186 Bone cancer pain relief, rheumatoid arthritis treatment, and diagnosis and treatment of lymphoma (Re-186) and bone, breast, colon, and liver cancers using radioimmunotherapy Rhenium-188 Cancer diagnosis and treatment using radioimmunotherapy, bone cancer pain relief, treatment of (Re-188) rheumatoid arthritis, and treatment of prostate cancer Rhium-105 Cancer radioimmunotherapy Samanum-145 Ocular cancer treatment (Sm- 1 45) Samarium-I53 Cancer radioimmunotherapy and bone cancer pain relief (Sm-i 53) Scandium-47 Cancer radioimmunotherapy and bone cancer pain relief (Sc-47) Selenlum-75 Radliotracer used in brain studies, Imaging of adrenal cortex by gamma-scintigraphy, lateral Seenm-75 locations of steroid secreting tumors, pancreatic scanning, detection of hyperactive parathyroid (Se-75) glands, measure rate of bile acid loss from the endogenous pool Strontium-85 Bone cancer detection and brain scans (Sr-85). Strontium-89 Bone cancer pain relief, multiple myeloma treatment, and osteoblastic therapy (Sr-8) Technetum-99m See Molybdenum-99 (Mo-99) (To-99m) Thorum-228 Parent of Bismuth-212 (Bi-212) which is an alpha emitter used in cancer radioimmunotherapy (Th-228) Thorium-229 Parent of Actinium-225 (Ao-225) and grandparent of Bismuth-213 (Bi-213) which are alpha (Th-229) emitters used in cancer radiolmmunotherapy Thulium-170 Gamma source for blood irradiators, energy source for implanted medical devices ( Tm-1 7) (Sn-i17m) Cancer immunotherapy and bone cancer pain relief Parent for Rhenium-188 (Re-188) which is used for cancer diagnostics/treatment, bone cancer Tungsten-188 pain relief, rheumatoid arthritis treatment, and treatment of blocked arteries (i.e., arteriosclerosis (W-188) and restenosis) Xenon-127 Neuroimaging of brain disorders, high resolution SPECT studies, pulmonary function tests, and (Xe-127) cerebral blood flow studies Yterbium-175 Cancer radioimmunotherapy (YbI75) Ytbium-90 Microseeds obtained from Irradiating Yttrium-89 (Y-89) for liver cancer treatment (Y-90) Yttrium-91 A gamma-emitting label for Yttrium-90 (Y-90) which is used for cancer radioimmunotherapy (i.e., (Y-91) lymphoma, breast, colon, kidney, lung, ovarian, prostate, pancreatic, and inoperable liver cancers) 1R By 'randomized' or grammatical equivalents as herein applied to nuclelc acids and proteins is meant that each nucleic acid and peptide consists of essentially random nudeotides and amino acids, respectively. These random peptides (or nuclelc acids, discussed herein) can incorporate any nucleotide or amino add at any position. The synthetic process can be designed to generate randomized proteins or nucleic adds, to allow the formation of all or most of the possible combinations over the length of the sequence, thus forming a library of randomized candidate bioactive proteinaceous agents. In one embodiment, a library is 'fully randomized,' with no sequence preferences or constants at any position. In another embodiment, the library is a 'biased random' library. That is, some positions within the sequence either are held constant, or are selected from a limited number of possibilities. For example, the nucleotides or amino acid residues are randomized within a defined class, e.g., of hydrophobic amino adds, hydrophific residues, sterically biased (either small or large) residues, towards the creation of nudlec add binding domains, the creation of cysteines, for cross-linking, prolines for SH-3 domains, serines, threonines, tyrosines or histidines for phosphoryation sites, etc., or to purnes, etc. A 'recombinant' DNA or RNA molecule is a DNA or RNA molecule that has been subjected to molecular manipulation in vif. Non-limiting examples of small molecules indude compounds that bind or interact with 109P1 D4, ligands including hormones, neuropeptides, chemokines, odorants, phospholipids, and functional equivalents thereof that bind and preferably inhibit 109P1D4 protein function. Such non-limiting small molecules preferably have a molecular weight of less than about 10 kDa, more preferably below about 9, about 8, about 7, about 6, about 5 or about 4 kDa. In certain embodiments, small molecules physically associate with, or bind, 109P1 D4 protein; are not found in naturally occurring metabolic pathways; and/or are more soluble In aqueous than non-aqueous solutions 'Stringency' of hybridization reactions Is readily determinable by one of ordinary skill in the art, and generally is an empirical calculation dependent upon probe length, washing temperature, and salt concentration. In general, longer probes require higher temperatures for proper annealing, while shorter probes need lower temperatures. Hybridization generally depends on the ability of denatured nucleic acid sequences to reanneal when complementary strands are present in an environment below their melting temperature. The higher the degree of desired homology between the probe and hybridizable sequence, the higher the relative temperature that can be used. As a result, it follows that higher relative temperatures would tend to make the reaction conditions more stringent, while lower temperatures less so. For additional details and explanation of stringency of hybridization reactions, see Ausubel et al., Current Protocols in Molecular Biology, Wiley Interscience Publishers, (1995). 'Stringent conditions' or 'high stringency conditions", as defined herein, are Identified by, but not limited to, those that (1) employ low ionic strength and high temperature for washing, for example 0.015 M sodium chloride/0.0015 M sodium citrate/0.1% sodium dodecyl sulfate at 500C; (2) employ during hybridization a denaturing agent, such as formamide, for example, 50% (v/v) formamide with 0.1% bovine serum albumin/0.1 % Ficoll/0.1 % polyvinylpyrrolidone/50 mM sodium phosphate buffer at pH 6.5 with 750 mM sodium chloride, 75 mM sodium citrate at 42 oC; or (3) employ 50% formamide, 5 x SSC (0.75 M NaCl, 0.075 M sodium citrate), 50 mM sodium phosphate (pH 6.8), 0.1% sodium pyrophosphate, 5 x Denhardfs solution, sonicated salmon sperm DNA (50 lpg/ml), 0.1% SDS, and 10% dextran sulfate at 42 OC, with washes at 420C In 0.2 x SSC (sodium chloride/sodium. citrate) and 50% formamide at 55 oC, followed by a high-stringency wash consisting of 0.1 x SSC containing EDTA at 55 OC. 'Moderately stringent conditions' are described by, but not limited to, those In Sambrook et al., Molecular Cloning: A Laboratory Manual, New York: Cold Spring Harbor Press, 1989, and Include 19 the use of washing solution and hybridization conditions (e.g., temperature, ionic strength and %SDS) less stringent than those described above. An example of moderately stringent conditions is overnight incubation at 370C in a solution comprising: 20% formamide, 5 x SSC (150 mM NaCl, 15 mM trisodium citrate), 50 mM sodium phosphate (pH 7.6), 5 x Denhardts solution, 10% dextran sulfate, and 20 mg/mL denatured sheared salmon sperm DNA, followed by washing the filters in 1 x SSC at about 37-500C. The skilled artisan will recognize how to adjust the temperature, ionic strength, etc. as necessary to accommodate factors such as probe length and the like. An HLA "supermotif is a peptide binding specificity shared by HLA molecules encoded by two or more HLA alleles. Overall phenotypic frequencies of HLA-supertypes in different ethnic populations are set forth in Table IV (F). The non limiting constituents of various supetypes are as follows: It A*0201, A*0202, A*0203, A*0204, A* 0205, A*0206, A*6802, A*6901, A*0207 A3, A3, All, A31, A*3301, A*6801, A*0301, A*1101, A*3101 Bl: 87, B*3501-03, B*51, B*5301, B*5401, B*5501, 8*5502, B*5601, B*6701, B*7801, B*0702, B*5101, B*5602 M B*3701, B*4402, B*4403, B*60 (B*4001), 861 (B*4006) At A*01 02, A*2604, A*3601, A*4301, A*8001 A24 A*24, A*30, A*2403, A*2404, A*3002, A*3003 B27 B*1401-02, B*1503, B*1509, B*1510, B*1518, B*3801-02, 8*3901, B*3902, B*3903-04, B*4801-02, 87301, B*2701-08 B5; 8*1516, B*1517, 8*5701, B*5702, B58 1ji2;_B*4601, B52, B*1501 (B62), B*1502 (B75), B*1513 (877) Calculated population coverage afforded by different HLA-supertype combinations are set forth in Table IV (G). As used herein "to treat or "therapeutic" and grammatically related terms, refer to any improvement of any consequence of disease, such as prolonged survival, less morbidity, and/or a lessening of side effects which are the byproducts of an alternative therapeutic modality; full eradication of disease Is not required. A 'transgenic animal" (e.g., a mouse or rat) Is an animal having cells that contain a transgene, which transgene was introduced into the animal or an ancestor of the animal at a prenatal, e.g., an embryonic stage. A "transgene" is a DNA that is integrated into the genome of a cell from which a transgenic animal develops. As used herein, an HLA or cellular immune response "vaccine" Is a composition that contains or encodes one or more peptides of the invention. There are numerous embodiments of such vaccines, such as a cocktail of one or more individual peptides; one or more peptides of the invention comprised by a polyepitopic peptide; or nucleic acids that encode such individual peptides or polypeptides, e.g., a minIgene that encodes a polyepitopic peptide. The "one or more peptides" can Include any whole unit Integer from 1-150 or more, e.g., at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20,21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31,32, 33, 34, 35, 36, 37, 38, 39,40,41, 42,43, 44, 45, 46,47,48, 49, 50, 55, 60, 65,70, 75, 80, 85, 90, 95, 100, 105, 110,115, 120,125,130,135,140,145, or 150 or more peptides of the Invention. The peptides or polypeptides can optionally be modified, such as by lipidation, addition of targeting or other sequences. HLA class I peptides of the invention can be admixed with, or linked to, HLA class 11 peptides, to facilitate activation of both cytotoxic T lymphocytes and helper T lymphocytes. HLA vaccines can also comprise peptide-pulsed antigen presenting cells, e.g., dendritic cells. The term "variant refers to a molecule that exhibits a variation from a described type or norm, such as a protein that has one or more different amino acid residues in the corresponding positions) of a specifically described protein (e.g. the 109P1D4 protein shown In Figure 2 or Figure 3. An analog Is an example of a variant protein. Splice Isoforms and single nucleotides polymorphisms (SNPs) are further examples of variants.

20 The "109P104-related proteins" of the invention indude those specifically identified herein, as well as allelic variants, conservative substitution variants, analogs and homologs that can be isolated/generated and characterized without undue experimentation following the methods outlined herein or readily available in the art Fusion proteins that combine parts of different 109P1D4 proteins or fragments thereof, as well as fusion proteins of a 109P1D4 protein and a heterologous polypeptide are also induded. Such 109P1D4 proteins are collectively referred to as the 109P1D4-related proteins, the proteins of the invention, or 109P1D4. The term "109P1 D4-related protein" refers to a polypeptide fragment or a 109P1 4 protein sequence of 4, 5,6,7, 8,9,10,11,12,13,14,15,16,17,18,19, 20, 21, 22, 23, 24, 25, or more than 25 amino adds; or, at least 30, 35, 40, 45, 50, 55, 60, 65, 70, 80, 85, 90, 95, 100, 105, 110,115,120,125,130,135,140,145,150,155, 160, 165,170,175,180,185, 190,195, 200, 225,250, 275, 300, 325, 350, 375, 400, 425,450, 475, 500, 525, 550, 575, or 576 or more amino acids. II.) 109P1D4 Polynucleotides One aspect of the invention provides polynudeotides corresponding or complementary to all or part of a 109P1 D4 gene, mRNA, and/or coding sequence, preferably in Isolated form, including polynucleotides encoding a 109P1 D4-related protein and fragments thereof, DNA, RNA, DNAJRNA hybrid, and related molecules, polynucleotides or oligonudeotides complementary to a 109P1 D4 gene or mRNA sequence or a part thereof, and polynucleotides or oligonucleotides that hybridize to a 109P1D4 gene, mRNA, or to a 109P1D4 encoding polynuceotide (collectively, "109P1D4 polynucleotides"). In all Instances when refenred to in this section, T can also be U in Figure 2. Embodiments of a 109P1 D4 polynucleotide Include: a 109P1 D4 polynucleotide having the sequence shown in Figure 2, the nucleotide sequence of 109P1D4 as shown in Figure 2 wherein T is U; at least 10 contiguous nucleotides of a polynudeotide having the sequence as shown in Figure 2; or, at least 10 contiguous nucleotides of a polynucleotide having the sequence as shown in Figure 2 where T is U. For example, embodiments of 1091P1D4 nucleotides comprise, without limitation: (I) a polynudeotide comprising, consisting essentially of, or consisting of a sequence as shown in Figure 2, wherein T can also be U; (II) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2A, from nucleotide residue number 846 through nucleotide residue number 3911, induding the stop codon, wherein T can also be U; (1ll) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2B, from nucleotide residue number 503 through nucleotide residue number 3667, Including the stop codon, wherein T can also be U; (IV) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2C, from nudeotide residue number 846 through nucleotide residue number 4889, Including the a stop codon, wherein T can also be U; (V) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2D, from nucleotide residue number 846 through nucleotide residue number 4859, Including the stop codon, wherein T can also be U; (VI) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2E, from nucleotide residue number 846 through nucleotide residue number 4778, Including the stop codon, wherein T can also be U; 21 (VII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2F, from nucleotide residue number 614 through nucleotide residue number 3727, including the stop codon, wherein T can also be U; (Vill) a polynudeoide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2G, from nucleotide residue number 735 through nucleotide residue number 3881, including the stop codon, wherein T can also be U; (IX) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2H, from nudeotide residue number 735 through nucleotide residue number 4757, induding the stop codon, wherein T can also be U; (X) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 21, from nucleotide residue number 514 through nucleotide residue number 3627, including the stop codon, wherein T can also be U; (Xi) a polynucleotide that encodes a 1091P1 D4-related protein that is at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99 or 100% homologous to an entire amino acid sequence shown in Figure 2A-1; (XII) a polynucleotide that encodes a 109P1 D4-related protein that is at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99 or 100% Identical to an entire amino acid sequence shown in Figure 2A-1; (XIII) a polynucleotide that encodes at least one peptide set forth in Tables Vill-XXI and XXIl-XLIX (XIV) a polynudeotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16,17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figures 3A in any whole number increment up to 1021 that Includes at least 1, 2, 3,4, 5, 6, 7, 8, 9, 10, 11, 12,13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Hydrophilicity profile of Figure 5; (XV) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 12,13,14, 15, 16,17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30,31, 32, 33, 34, 35 amino adds of a peptide of Figure 3A in any whole number increment up to 1021 that indudes 1, 2, 3,4, 5, 6, 7, 8, 9,10,11, 12, 13,14, 15, 16,17, 18,19, 20,21, 22, 23, 24, 25,26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid positioi(s) having a value less than 0.5 in the Hydropathilcity profile of Figure 6; (XVI) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9,10, 11, 12,13, 14,15, 16,17,18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino adds of a peptide of Figure 3A in any whole number increment up to 1021 that includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25,26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Percent Accessible Residues profile of Figure 7; (XVII) a polynudeotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino adds of a peptide of Figure 3A in any whole number increment up to 1021 that includes 1, 2, 3, 4, 5, 6, 7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Average Flexibility profile of Figure 8; (XVIII) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 12, 13,14,15,16, 17, 22 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3A in any whole number increment up to 1021 that includes 1, 2, 3, 4, 5, 6, 7, 8, 9,10,11,12,13,14, 15,16, 17, 18,19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 In the Beta-turn profile of Figure 9; (XIX) a polynudeotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10,11, 12, 13,14, 15,16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3B, 3C, and/or 3D in any whole number increment up to 1054, 1347, and/or 1337 respectively that includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Hydrophilicity profile of Figure 5; (XX) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino adds of a peptide of Figure 3B, 3C, and/or 3D In any whole number Increment up to 1054,1347, and/or 1337 respectively that Includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15,16,17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value less than 0.5 In the Hydropathicity profile of Figure 6; (XXI) a polynucleotide that encodes a peptide region of at least 5, 6,7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17,18, 19, 20, 21, 22, 23, 24, 25, 26,27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3B, 3C, and or 3D in any whole number increment up to 1054, 1347, and/or 1337 respectively that includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12,13, 14,15,16, 17,18,19, 20, 21, 22, 23, 24,25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Percent Accessible Residues profile of Figure 7; (XXII) a polynucleoide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3B, 3C, and/or 3D in any whole number Increment up to 1054, 1347, and/or 1337 respectively that includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 In the Average Flexibility profile of Figure 8; (XXIll) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3B, 3C, and/or 3D in any whole number increment up to 1054, 1347, and/or 1337 respectively that Indudes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12,13,14, 15,16, 17,18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Beta-tum profile of Figure 9; (XXIV) a polynucleotide that encodes a peptide region of at least 5,6, 7, 8, 9, 10, 11, 12, 13,14,15, 16,17,18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32 33, 34, 35 amino acids of a peptide of Figure 3E, 3F, 3G, 3H and/or 31 in any whole number increment up to 1310, 1037, 1048, 1340, and/or 1037 respectively that includes 1, 2, 3,4, 5, 6, 7, 8,9,10,11,12,13,14,15,16,17,18,19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29,30, 31, 32, 33,34, 35 amino acid positions) having a value greater than 0.6 in the Hydrophilicity profile of Figure 5; (XXV) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10,11, 12,13,14,15, 16, 17,18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3E, 3F, 3G, 3H and/or 31 In any whole number increment up to 1310, 1037, 1048, 1340, and/or 1037 respectively that includes 1, 2,3, 4, 5,6, 7,8,9, 10, 11, 12,13, 14, 15,16, 17,18,19,20, 21, 22,23, 24,25, 26,27,28, 29, 30, 31,32, 33,34, 35 amino acid position(s) having a value less than 0.5 In the Hydropathicity profile of Figure 6; 23 (XXVI) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9,10, 11, 12,13,14,15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30,31, 32, 33, 34, 35 amino acids of a peptide of Figure 3E, 3F, 3G, 3H and/or 31 in any whole number increment up to 1310, 1037, 1048, 1340, and/or 1037 respectively that includes 1, 2, 3, 4, 5,6, 7, 8, 9, 10,11,12,13,14,15,16,17, 18, 19, 20, 21, 22, 23, 24,25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Percent Accessible Residues profile of Figure 7; (XXVII) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9,10,11,12,13,14,15,16, 17,18, 19, 20,21,22, 23, 24,25, 26, 27, 28,29, 30,31,32, 33,34, 35 amino acids of a peptide of Figure 3E, 3F, 3G, 3H and/or 31 in any whole number increment up to 1310, 1037, 1048, 1340, and/or 1037 respectively that includes 1, 2, 3,4, 5, 6, 7, 8, 9,10, 11, 12,13,14,15,16,17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29,30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Average Flexibility profile of Figure 8; (XVI) a polynudeoide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 12 13,14,15,16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3E, 3F, 3G, 3H, and/or 31 In any whole number Increment up to 1310, 1037,1048, 1340, and/or 1037 respectively that includes 1, 2, 3,4, 5, 6, 7, 8, 9,10,11,12,13,14,15,16,17,18, 19,20, 21, 22, 23, 24,25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Beta-tum profile of Figure 9; (XXIX) a polynudeotide that Is fully complementary to a polynucleotide of any one of (I)-(XXVIlI); () a polynudeotide that is fully complementary to a polynucleotide of any one of (1)-(XXIX); (XXXI) a peptide that is encoded by any of (1) to (XXX); and; (XXXII) a composition comprising a polynucleotide of any of (IHXXX) or peptide of (XXXI) together with a pharmaceutical excipient and/or In a human unit dose form; (Xill) a method of using a polynucleotide of any (I)-(XXX) or peptide of (XXXI) or a composition of (XXXII) In a method to modulate a cell expressing 1 09P1 D4; (XXXIV) a method of using a polynudeotide of any (l)-(XX) or peptide of (XXXI) or a composition of (XXXII) in a method to diagnose, prophylax, prognose, or treat an individual who bears a cell expressing 109P1D4; (XXXV) a method of using a polynucleotide of any (1)-(XXX) or peptide of (XXXI) or a composition of (X)XlI) in a method to diagnose, prophylax, prognose, or treat an Individual who bears a cell expressing 109P1D4, said cell from a cancer of a tissue listed In Table I; (XXXVI) a method of using a polynudeotide of any (I)-(XXX) or peptide of (XXXI) or a composition of (XXXIl) in a method to diagnose, prophylax, prognose, or treat a a cancer; (X)VII) a method of using a polynucleotide of any (IHXXX) or peptide of (XXXI) or a composition of (XXXII) in a method to diagnose, prophylax, prognose, or treat a a cancer of a tissue listed in Table I; and; (X)Vlll) a method of using a polynucleotide of any (I)-(XX) or peptide of (XXXI) or a composition of (XXMVl) In a method to identify or characterize a modulator of a cell expressing 1 09P1 D4. As used herein, a range Is understood to disclose specifically all whole unit positions thereof. Typical embodiments of the Invention disclosed herein Include 109P1 D4 polynucleotides that encode specific portions of 109P1D4 mRNA sequences (and those which are complementary to such sequences) such as those that encode the proteins and/or fragments thereof, for example: .

24 (a) 4, 5, 6, 7, 8, 9, 10,11, 12, 13,14,15,16,17,18,19, 20, 21, 22, 23, 24, 25, 30, 35, 40, 45,50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 225, 250, 275, 300, 325, 350, 375, 400, 425, 450, 475, 500, 525, 550, 575, 600, 625, 650, 675, 700, 725, 750, 775, 800, 825, 850, 875, 900, 925, 950, 975, 1000, 1010, 1020, and 1021 or more contiguous amino acids of 109P1D4 variant 1; the maximal lengths relevant for other variants are: variant 2, 1054 amino acids; variant 3, 1347 amino acids, variant 4, 1337 amino acids, variant 5, 1310 amino acids, variant 6; 1047 amino acids, variant 7; 1048 amino acids, variant 8; 1340 amino acids and variant 9; 1037 amoni acids. For example, representative embodiments of the invention disposed herein Include: polynudeotides and their encoded peptides themselves encoding about amino acid 1 to about amino acid 10 of the 109P1D4 protein shown in Figure 2 or Figure 3, polynucleotides encoding about amino acid 10 to about amino acid 20 of the 109P1 D4 protein shown in Figure 2 or Figure 3, polynucleotides encoding about amino acid 20 to about amino acid 30 of the 1 09P1 D4 protein shown in Figure 2 or Figure 3, polynucleotides encoding about amino acid 30 to about amino acid 40 of the 109P1 D4 protein shown In Figure 2 or Figure 3, polynucleotides encoding about amino acid 40 to about amino acid 50 of the 109P1 D4 protein shown In Figure 2 or Figure 3, polynucleotides encoding about amino acid 50 to about amino acid 60 of the 1 09P1 D4 protein shown in Figure 2 or Figure 3, polynucleotides encoding about amino acid 60 to about amino acid 70 of the 109P1 D4 protein shown In Figure 2 or Figure 3, polynucleotides encoding about amino acid 70 to about amino acid 80 of the 109P1 D4 protein shown in Figure 2 or Figure 3, polynudeotides encoding about amino acid 80 to about amino acid 90 of the 109P1 D4 protein shown in Figure 2 or Figure 3, polynucleotides encoding about amino acid 90 to about amino acid 100 of the 109P1 D4 protein shown in Figure 2 or Figure 3, in increments of about 10 amino acids, ending at the carboxyl terminal amino acid set forth in Figure 2 or Figure 3. Accordingly, polynucleotides encoding portions of the amino acid sequence (of about 10 amino adds), of amino acids, 100 through the carboxyl terminal amino acid of the 109P1 D4 protein are embodiments of the Invention. Wherein it is understood that each particular amino acid position discloses that position pius or minus five amino acid residues. Polynucleotides encoding relatively long portions of a 109P1 D4 protein are also within the scope of the invention. For example, polynucleotides encoding from about amino acid 1 (or 20 or 30 or 40 etc.) to about amino acid 20, (or 30, or 40 or 50 etc.) of the 109P1D4 protein "or variant" shown in Figure 2 or Figure 3 can be generated by a variety of techniques well known in the art. These polynucleotide fragments can include any portion of the 109P1D4 sequence as shown in Figure 2. Additional illustrative embodiments of the invention disclosed herein include 109P1 D4 polynucleotide fragments encoding one or more of the biological motifs contained within a 109P1 D4 protein "or variant" sequence, including one or more of the motif-bearing subsequences of a 109P1D4 protein "or varianr set forth in Tables VIi-XXI and XXII-XLIX. In another embodiment, typical polynucleotide fragments of the Invention encode one or more of the regions of 109P1D4 protein or variant that exhibit homology to a known molecule. In another embodiment of the invention, typical polynucleotide fragments can encode one or more of the 109P1D4 protein or variant N-glycosylation sites, cAMP and cGMP-dependent protein kinase phosphorylation sites, casein kinase 11 phosphorylation sites or N-myristoylation site and amidation sites. Note that to determine the starting position of any peptide set forth in Tables Vill-XXI and Tables XXII to XLIX (collectively HILA Peptide Tables) respective to its parental protein, e.g., variant 1, variant 2, etc., reference is made to three factors: the particular variant, the length of the peptide in an HLA Peptide Table, and the Search Peptides listed in Table VII. Generally, a unique Search Peptide is used to obtain HLA peptides for a particular variant The position of each Search Peptide relative to Its respective parent molecule Is listed in Table VII. Accordingly, if a Search Peptide begins at position "X", one must add the value "X minus 1" to each position in Tables VlII-XXI and Tables XXII-IL to obtain the actual position of the HILA peptides in their parental molecule. For example If a particular Search Peptide begins at position 150 of Its parental molecule, one must add 150 - 1, i.e., 149 to each HLA peptide amino acid position to calculate the position of that amino acid 25 in the parent molecule. II.A.) Uses of 109P1D4 Polynucleotides ll...) Monitoring of Genetic Abnormalities The polynucleotides of the preceding paragraphs have a number of different specific uses. The human 109P1D4 gene maps to the chromosomal location set forth in the Example entitled "Chromosomal Mapping of 109P1 D4." For example, because the 109P1D4 gene maps to this chromosome, polynucleotides that encode different regions of the 109P1 D4 proteins are used to characterize cytogenetic abnormalities of this chromosomal locale, such as abnormalities that are identified as being associated with various cancers. In certain genes, a variety of chromosomal abnormalities including rearrangements have been identified as frequent cytogenetic abnormalities in a number of different cancers (see e.g. Krajinovic et al., Mutat. Res. 382(3-4): 81-83 (1998); Johansson et al., Blood 86(10): 3905-3914 (1995) and Finger et at., P.NAS. 85(23): 9158-9162 (1988)). Thus, polynudeotides encoding specific regions of the 109P1 D4 proteins provide new tools that can be used to delineate, with greater precision than previously possible, cytogenetic abnormalities In the chromosomal region that encodes 109P1D4 that may contribute to the malignant phenotype. In this context, these polynudeotides satisfy a need in the art for expanding the sensitivity of chromosomal screening In order to identify more subtle and less common chromosomal abnormalities (see e.g. Evans et al., Am. J. Obstet Gynecol 171(4): 1055-1057 (1994)). Furthermore, as 109P1 D4 was shown to be highly expressed in prostate and other cancers, 109P1 D4 polynucleotides are used in methods assessing the status of 109P1D4 gene products in normal versus cancerous tissues. Typically, polynucleotides that encode specific regions of the 109P1D4 proteins are used to assess the presence of perturbations (such as deletions, insertions, point mutations, or alterations resulting in a loss of an antigen etc.) in specific regions of the 109P1D4 gene, such as regions containing one or more motifs. Exemplary assays include both RT-PCR assays as well as single-strand conformation polymorphism (SSCP) analysis (see, e.g., Marrogi et al., J. Cutan. Pathol. 26(8): 369-378 (1999), both of which utilize polynucleotides encoding specific regions of a protein to examine these regions within the protein. IIA.2.) Antisense Embodiments Other specifically contemplated nucleic acid related embodiments of the Invention disclosed herein are genomic DNA, cDNAs, ribozymes, and antisense molecules, as well as nucleic acid molecules based on an alternative backbone; or including alternative bases, whether derived from natural sources or synthesized, and indude molecules capable of inhibiting the RNA or protein expression of 109P1 D4. For example, antisense molecules can be RNAs or other molecules, including peptide nudeic acids (PNAs) or non-nucleic acid molecules such as phosphorothloate derivatives that specifically bind DNA or RNA in a base pair-dependent manner. A skilled artisan can readily obtain these classes of nucleic acid molecules using the 109P1 D4 polynucleotides and polynucleotide sequences disclosed herein. Antisense technology entails the administration of exogenous oligonucleotides that bind to a target polynucleotide located within the cells. The term "antisense' refers to the fact that such oligonudeotides are complementary to their intracellular targets, e.g., 109P1D4. See for example, Jack Cohen, Oligodeoxynucleotides, Antisense Inhibitors of Gene Expression, CRC Press, 1989; and Synthesis 1:1-5 (1988). The 109P1D4 antisense oligonucleotides of the present invention Indude derivatives such as S-oligonucleotides (phosphorothioate derivatives or S-oligos, see, Jack Cohen, supra), which exhibit enhanced cancer cell growth inhibitory action. S-oligos (nudeoside phosphorothloates) are isoelectronic analogs of an oligonucleotide (0-oligo) in which a nonbridging oxygen atom of the phosphate group is replaced by a sulfur atom. The S-oligos of the present invention can be prepared by treatment of the corresponding 0-oligos with 3H-1,2 berizodithiol-3-one-1,1-dioxide, which is a sulfur transfer reagent. See, e.g., lyer, R. P. et at, J. Org. Chem. 55:4693-4698 26 (1990); and lyer, R. P. et al., J. Am. Chem. Soc. 112:1253-1254 (1990). Additional 109P1D4 antisense oligonucleotides of the present invention include morpholino antisense oligonucleotides known in the art (see, e.g., Partridge et aL., 1996, Antisense & Nucleic Acid Drug Development 6:169-175). The 109P1D4 antisense oligonucleotides of the present invention typically can be RNA or DNA that is complementary to and stably hybridizes with the first 1005' codons or last 100 3' codons of a 109P1 D4 genomic sequence or the corresponding mRNA. Absolute complementarity is not required, although high degrees of complementarity are preferred. Use of an olgonucleotide complementary to this region allows for the selective hybridization to 109P1 D4 mRNA and not to mRNA specifying other regulatory subunits of protein kinase. In one embodiment, 109P1D4 antisense oligonucleotides of the present invention are 15 to 30-mer fragments of the antisense DNA molecule that have a sequence that hybridizes to 109P1 D4 mRNA. Optionally, 109P1 D4 antisense oligonucleotide Is a 30-mer oligonucteotide that is complementary to a region in the first 10 5' codons or last 103' codons of 109P1D4. Alternatively, the antisense molecules are modified to employ ribozymes In the inhibition of 109P1 D4 expression, see, e.g., L A. Couture & D. T. Stinchcomb; Trends Genet 12: 510-515 (1996). I1.A.3.) PrImers and Primer Pairs Further specific embodiments of these nucleotides of the invention include primers and primer pairs, which allow the specific amplification of polynudeotides of the invention or of any specific parts thereof, and probes that selectively or specifically hybridize to nucleic acid molecules of the invention or to any part thereof. Probes can be labeled with a detectable marker, such as, for example, a radioisotope, fluorescent compound, biolumInescent compound, a chemiluminescent compound, metal chelator or enzyme. Such probes and primers are used to detect the presence of a 109P1D4 polynudeotide In a sample and as a means for detecting a cell expressing a 109P1D4 protein. Examples of such probes include polypeptides comprising all or part of the human 109P1 D4 cDNA sequence shown in Figure 2. Examples of primer pairs capable of specifically amplifying 109P1 D4 mRNAs are also described in the Examples. As wiU be understood by the skilled artisan, a great many different primers and probes can be prepared based on the sequences provided herein and used effectively to amplify and/or detect a 109P1D4 mRNA. The I 09P1 D4 polynucleotides of the invention are useful for a variety of purposes, induding but not limited to their use as probes and primers for the amplification and/or detection of the 109P1D4 gene(s), mRNA(s), or fragments thereof; as reagents for the diagnosis and/or prognosis of prostate cancer and other cancers; as coding sequences capable of directing the expression of 109P1 D4 polypeptides; as tools for modulating or Inhibiting the expression of the 109P1 D4 gene(s) and/or translation of the 109P1 D4 transcript(s); and as therapeutic agents. The present invention includes the use of any probe as desaibed herein to identify and isolate a 109P1D4 or 109P1D4 related nucleic acid sequence from a naturally occurring source, such as humans or other mammals, as well as the isolated nucleic add sequence per se, which would comprise all or most of the sequences found In the probe used. II.A.4.) Isolation of 109P1D4-Encoding Nucleic Add Molecules The 109P1 D4 cDNA sequences described herein enable the isolation of other polynucleotides encoding 109PI D4 gene productss, as well as the isolation of polynudeotides encoding 109P1 D4 gene product homologs, altematively spliced isoforms, allelic variants, and mutant forms of a 109P1D4 gene product as well as polynucleotides that encode analogs of 109P1D4-related proteins. Various molecular cloning methods that can be employed to isolate ful length cDNAs encoding a 109P1 D4 gene are we known (see, for example, Sambrook, J. et al, Molecular Cloning: A Laboratory Manual, 2d edition, Cold Spring Harbor Press, New York, 1989; Current Protocols in Molecular Biology. Ausubel et at., Eds., Wiley and Sons, 1995). For example, lambda phage cloning methodologies can be conveniently employed, using commercially available cloning systems (e.g., Lambda ZAP Express, Stratagene). Phage clones containing 109P1D4 gene cDNAs can be identified by probing with a labeled 109P1D4 27 cDNA or a fragment thereof. For example, in one embodiment, a 109P1 D4 cDNA (e.g., Figure 2) or a portion thereof can be synthesized and used as a probe to retrieve ovedapping and fuill-length cDNAs corresponding to a 109P1D4 gene. A 109P1D4 gene itself can be isolated by screening genomic DNA libraries, bacterial artificial chromosome libraries (BACs), yeast artificial chromosome libraries (YACs), and the like, with 109P1 D4 DNA probes or primers. II.A.5.) Recombinant Nucleic Acid Molecules and Host-Vector Systems The invention also provides recombinant DNA or RNA molecules containing a 109P1 D4 polynucleotide, a fragment, analog or homologue thereof, including but not limited to phages, plasmids, phagemids, cosmids, YACs, BACs, as well as various viral and non-viral vectors well known In the art, and cells transformed or transfected with such recombinant DNA or RNA molecules. Methods for generating such molecules are well known (see, for example, Sambrook et aL., 1989, supra). The Invention further provides a host-vector system comprising a recombinant DNA molecule containing a 109P1 D4 polynucleotide, fragment, analog or homologue thereof within a suitable prokaryotic or eukaryotic host cell. Examples of suitable eukaryotic host cells include a yeast cell, a plant cell, or an animal cell, such as a mammalian cell or an Insect cell (e.g., a baculovirus-infectible cell such as an Sf9 or HighFive cell). Examples of suitable mammalian cells Include various prostate cancer cell lines such as DU145 and TsuPri, other transfectable or transducible prostate cancer cell lines, primary cells (PrEC), as well as a number of mammalian cells routinely used for the expression of recombinant proteins (e.g., COS, CHO, 293, 293T cells). More paricularly, a polynudeotide comprising the coding sequence of 109P1D4 or a fragment, analog or homolog thereof can be used to generate 109P1 D4 proteins or fragments thereof using any number of host-vector systems routinely used and widely known in the art A wide range of host-vector systems suitable for the expression of 109PI D4 proteins or fragments thereof are available, see for example, Sambrook et al., 1989, supra; Current Protocols in Molecular Biology, 1995, supra). Preferred vectors for mammalian expression include but are not limited to pcDNA 3.1 myc-His-tag (Invitrogen) and the retroviral vector pSRtkneo (Muller et al., 1991, MCB 11:1785). Using these expression vectors, 109P1 D4 can be expressed in several prostate cancer and non-prostate cell lines, including for example 293, 293T, rat-1, NIH 3T3 and TsuPr1. The host-vector systems of the invention are useful for the production of a 109P1 D4 protein or fragment thereof. Such host-vector systems can be employed to study the functional properties of 109P1D4 and 109P1D4 mutations or analogs. . Recombinant human 109P1 D4 protein or an analog or homolog or fragment thereof can be produced by mammalian cells transfected with a construct encoding a 109P1 D4-related nucleotide. For example, 293T cells can be transfected with an expression plasmid encoding 109P1D4 or fragment, analog or homolog thereof, a 109P1 D4-related protein is expressed in the 293T cells, and the recombinant 109P1 D4 protein Is Isolated using standard purification methods (e.g., affinity purification using anti-109P1D4 antibodies). In another embodiment, a 109P1D4 coding sequence Is subcloned into the retroviral vector pSRczMSVtkneo and used to infect various mammalian cell lines, such as NIH 3T3, TsuPrl, 293 and rat-1 in order to establish 109P1 D4 expressing cell lines. Various other expression systems well known in the art can also be employed. Expression constructs encoding a leader peptide joined in frame to a 109P1D4 coding sequence can be used for the generation of a secreted form of recombinant 109P1D4 protein. As discussed herein, redundancy In the genetic code permits variation In 109P1 D4 gene sequences. In particular, it Is known in the art that specific host species often have specific codon preferences, and thus one can adapt the disclosed sequence as preferred for a desired host For example, preferred analog codon sequences typically have rare codons (i.e., codons having a usage frequency of less than about 20% in known sequences of the desired host) replaced with higher frequency codons. Codon preferences for a specific species are calculated, for example, by utilizing codon usage tables available on the INTERNET such as at URL dnaaffrc.go.jp/-nakamura/codon.html. Additional sequence modifications are known to enhance protein expression In a cellular host. These Include 28 elimination of sequences encoding spurious polyadenylation signals, exon/intron splice site signals, transposon-like repeats, and/or other such well-characterized sequences that are deleterious to gene expression. The GC content of the sequence is adjusted to levels average for a given cellular host, as calculated by reference to known genes expressed in the host cell. Where possible, the sequence is modified to avoid predicted hairpin secondary mRNA structures. Other useful modifications include the addition of a translational initiation consensus sequence at the start of the open reading frame, as described In Kozak, Mol. Cell Blol., 9:5073-5080 (1989). Skilled artisans understand that the general rule that eukaryotic ribosomes initiate translation exclusively at the 5' proximal AUG codon Is abrogated only under rare conditions (see, e.g., Kozak PNAS 92(7): 2662-2666, (1995) and Kozak NAR 15(20): 8125-8148 (1987)). il.) 109P1D4-elated Proteins Another aspect of the present invention provides 109P1D4-related proteins. Specific embodiments of 109P1D4 proteins comprise a polypeptide having all or part of the amino acid sequence of human 109P1 D4 as shown in Figure 2 or Figure 3. Alternatively, embodiments of 1 09P1 D4 proteins comprise variant, homolog or analog polypeptides that have alterations in the amino acid sequence of 109P1 D4 shown in Figure 2 or Figure 3. Embodiments of a 109P1D4 polypeptide include: a 109P1D4 polypeptide having a sequence shown in Figure 2, a peptide sequence of a 109P1 D4 as shown in Figure 2 wherein T is U; at least 10 contiguous nucleotides of a polypeptide having the sequence as shown in Figure 2; or, at least 10 contiguous peptides of a polypeptide having the sequence as shown in Figure 2 where T is U. For example, embodiments of 109P1D4 peptides comprise, without limitation: (1) a protein comprising, consisting essentially of, or consisting of an amino acid sequence as shown in Figure 2A-i or Figure 3A-1; (II) a 109P1 D4-related protein that is at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99 or 100% homologous to an entire amino acid sequence shown in Figure 2A-l or 3A-l; (ll) a 109P1D4-related protein that is at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99 or 100% identical to an entire amino acid sequence shown in Figure 2A-I or 3A-1; (IV) a protein that comprises at least one peptide set forth In Tables Vill to XLIX, optionally with a proviso that it is not an entire protein of Figure 2; (V) a protein that comprises at least one peptide set forth in Tables Vll-XX(, collectively, which peptide is also set forth in Tables XXII to XLIX, collectively, optionally with a proviso that it is not an entire protein of Figure Z (VI) a protein that comprises at least two peptides selected from the peptides set forth in Tables VIII-XLIX, optionally with a proviso that it Is not an entire protein of Figure 2; (Vil) a protein that comprises at least two peptides selected from the peptides set forth in Tables VIII to XLIX collectively, with a proviso that the protein is not a contiguous sequence from an amino acid sequence of Figure 2; (ViII) a protein that comprises at least one peptide selected from the peptides set forth in Tables VIII-XX; and at least one peptide selected from the peptides set forth in Tables XXII to XLIX, with a proviso that the protein is not a contiguous sequence from an amino acid sequence of Figure 2; (IX) a polypeptide comprising at least 5, 6, 7, 8, 9, 10,11, 12,13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30,31, 32, 33, 34, 35 amino acids of a protein of Figure 3A, 3B, 3C, 3D and/or 3E in any whole number increment up to 1021, 1054, 1347, 1337, and/or 1310 respectively that includes at least 1, 2, 3, 4, 5, 29 6, 7, 8, 9,10,11, 12,13,14, 15,16,17,18,19, 20, 21, 22, 23, 24,25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Hydrophilicity profile of Figure 5; (X) a polypeptide comprising at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a protein of Figure 3A, 3B, 3C, 3D, and/or 3E, In any whole number increment up to 1021, 1054, 1347, 1337, and/or 1310 respectively respectively that includes at least at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value less than 0.5 in the Hydropathicity profile of Figure 6; (XI) a polypeptide comprising at least 5, 6, 7, 8, 9,10,11, 12,13,14,15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28,29, 30, 31, 32, 33, 34, 35 amino acids of a protein of Figure 3A, 3B, 3C, 3D, and/or 3E, in any whole number increment up to 1021, 1054, 1347, 1337, and/or 1310 respectively respectively that includes at least at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13,14, 15,16,17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Percent Accessible Residues profile of Figure 7; (XII) a polypeptide comprising at least 5, 6, 7, 8, 9,10,11, 12,13,14,15,16,17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a protein of Figure 3A, 3B, 3C, 3D, and/or 3E, in any whole number increment up to 1021, 1054, 1347, 1337, and/or 1310 respectively respectively that includes at least at least 1, 2, 3,4, 5, 6, 7, 8, 9, 10,11, 12,13, 14, 15, 16, 17,18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Average Flexibility profile of Figure 8; (XII) a polypeptide comprising at least 5, 6, 7, 8, 9,10, 11, 12,13, 14,15,16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, amino acids of a protein of Figure 3A, 3B, 3C, 3D, and 3E in any whole number increment up to 1021, 1054, 1347, 1337, and/or 1310 respectively respectively that indudes at least at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Beta-tum profile of Figure 9; (XIV) a polypeptide comprising at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino adds of a protein of Figure 3F, 3G, 3H, and/or 31, in any whole number increment up to 1037, 1048, 1340, and/or 1037 respectively that includes at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12,13,14, 15,16,17,18,19,20,21, 22, 23, 24, 25,26,27,28,29,30,31, 32,33,34,35 amino acid positions) having a value greater than 0.5 in the Hydrophilicty profile of Figure 5; (XV) a polypeptide comprising at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino adds of a protein of Figure 3F, 3G, 3H, and/or 31 In any whole number Increment up to 1037, 1048, 1340, and/or 1037 respectively that includes at least at least 1, Z 3, 4, 5, 6,7, 8,9, 10,11, 12,13,14,15,16,17,18,19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino add position(s) having a value less than 0.5 In the Hydropathicty profile of Figure 6; (XVI) a polypeptide comprising at least 5, 6, 7, 8, 9, 10, 11, 12,13, 14,15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a protein of Figure 3F, 3G, 3H, and/or 31 In any whole number Increment up to 1037, 1048, 1340, and/or 1037 respectively that includes at least at least 1, 2, 3, 4, 5, 6,7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amIno acid positions) having a value greater than 0.5 In the Percent Accessible Residues profile of Figure 7; (XVII) a polypeptide comprising at least 5, 6, 7, 8, 9, 10, 11, 12,13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 30 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a protein of Figure 3F, 3G, 3H, and/or 31 in any whole number increment up to 1037, 1048, 1340, and/or 1037 respectively that includes at least at least 1, 2, 3, 4, 6, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Average Flexibility profile of Figure 8; (XVIII) a polypeptide comprising at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, amino acids of a protein of Figure 3F, 3G, 3H, and/or 31 In any whole number increment up to 1037, 1048, 1340, and/or 1037 respectively that includes at least at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 ,11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Beta-turn profile of Figure 9; (XIX) a peptide that occurs at least twice in Tables VIIl-XXI and XXI to XLIX, collectively; (XX) a peptide that occurs at least three times In Tables VIll-XXI and XXII to XLIX, collectively; (XXI) a peptide that occurs at least four times In Tables Vill-XXI and XXI to XLIX, collectively; (XXII) a peptide that occurs at least five times in Tables Vill-XXI and XXII to XLIX, collectively; (XXill) a peptide that occurs at least once In Tables Vill-XXI, and at least once in tables XXII to XUX; (XXIV) a peptide that occurs at least once in Tables VIII-XXJ, and at least twice In tables XXI to XUX; (XXV) a peptide that occurs at least twice In Tables Vill-XXI, and at least once in tables XXII to XLUX (XXVI) a peptide that occurs at least twice In Tables VIII-XXI, and at least twice in tables XXII to XIX; (XXVII) a peptide which comprises one two, three, four, or five of the following characteristics, or an oligonucleotide encoding such peptide: I) a region of at least 5 amino acids of a particular peptide of Figure 3, In any whole number Increment up to the full length of that protein in Figure 3, that Includes an amino acid position flaving a value equal to or greater than 0.5, 0.6, 0.7, 0.8, 0.9, or having a value equal to 1.0, in the Hydrophiricity profile of Figure 5; ii) a region of at least 5 amino acids of a particular peptide of Figure 3, in any whole number increment up to the full length of that protein in Figure 3, that includes an amino acid position having a value equal to or less than 0.5, 0.4, 0.3, 0.2, 0.1, or having a vaue equal to 0.0, in the Hydropathicity profile of Figure 6; Iii) a region of at least 5 amino acids of a particular peptide of Figure 3, in any whole number increment up to the full length of that protein in Figure 3, that Includes an amino acid position having a value equal to or greater than 0.5, 0.6, 0.7, 0.8, 0.9, or having a value equal to 1.0, In the Percent Accessible Residues profile of Figure 7; iv) a region of at least 5 amino acids of a particular peptide of Figure 3, in any whole number increment up to the full length of that protein In Figure 3, that includes an amino acid position having a value equal to or greater than 0.5, 0.6, 0.7, 0.8, 0.9, or having a value equal to 1.0, in the Average Flexibility profile of Figure 8; or, v) a region of at least 5 amino acids of a particular peptide of Figure 3, In any whole number increment up to the full length of that protein In Figure 3, that Includes an amino acid position having a value equal to or greater than 0.5, 0.6, 0.7, 0.8, 0.9, or having a value equal to 1.0, In the Beta-tum profile of Figure 9;; (XXVillI) a composition comprising a peptide of (INXXVII) or an antibody or binding region thereof together with a pharmaceutical exciplent and/or in a human unit dose form.

31 (XXIX) a method of using a peptide of (IHXXVII), or an antibody or binding region thereof or a composition of (XXVIII) in a method to modulate a cell expressing 109P1D4,; (XXX) a method of using a peptide of (IHXXViI) or an antibody or binding region thereof or a composition of (XXViii) in a method to diagnose, pophylax, prognose, or treat an individual who bears a cell expressing 109P1D4; (XXXI) a method of using a peptide of (I)-(XXVII) or an antibody or binding region thereof or a composition (XXVIII) in a method to diagnose, prophylax, prognose, or treat an individual who bears a cell expressing 109P1D4, said cell from a cancer of a tissue listed in Table I; (XXXI) a method of using a peptide of (I)-(XVl) or an antibody or binding region thereof or a composition of (XXViii) in a method to diagnose, prophylax, prognose, or treat a a cancer; (XX(ilI) a method of using a peptide of (I)-(XXVIl) or an antibody or binding region thereof or a composition of (XXVIII) in a method to diagnose, prophylax, prognose, or treat a a cancer of a tissue listed in Table I; and; (XXXIV) a method of using a a peptide of (l)-(XXVI) or an antibody or binding region thereof or a composition (XXVIII) in a method to Identify or characterize a modulator of a cell expressing 109P1 D4 As used herein, a range is understood to specifically disclose all whole unit positions thereof. Typical embodiments of the Invention disposed herein Include 109P1 D4 polynucleotides that encode specific portions of 109P1 D4 mRNA sequences (and those which are complementary to such sequences) such as those that encode the proteins and/or fragments thereof, for example: (a) 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80,85, 90, 95,100, 105,110,115,120,125,130,135,140,145,150, 155, 160,165, 170, 175, 180,185,190, 195, 200, 225, 250, 275, 300, 325, 350, 375, 400, 425, 450, 475, 500, 525, 550, 575, 600, 625, 650, 675, 700, 725, 750, 775, 800, 825, 850, 875, 900, 925, 950, 975, 1000, 1010, 1020, and 1021 or more contiguous amino acids of 109P1D4 variant 1; the maximal lengths relevant for other variants are: variant 2, 1054 amino acids; variant 3, 1347 amino acids, variant 4, 1337 amino acids, variant 5, 1310 amino acids, variant 6; 1037 amino acids, variant 7; 1048 amino acids, variant 8; 1340 amino acids, and variant 9; 1037 amino acids. . .In general, naturally occurring allelic variants of human 109P1 D4 share a high degree of structural identity and homology (e.g., 90% or more homology). Typically, alleuc variants of a 109P1 D4 protein contain conservative amino acid substitutions within the 109P1D4 sequences described herein or contain a substution of an amino acid from a corresponding position in a homologue of 109P1D4. One cass of109P1D4 allelic variants are proteins that share a high degre of homology with atleast a small region of a particular 109P1D4 amino acid sequence, but further contain a radical departure from the sequence, such as a non-conservative substitution, truncation, insertion or frame shift. In comparisons of protein sequences, the terms, similarity, identity, and homology each have a distinct meaning as appreciated In the field of genetics. Moreover, orthology and paralogy can be important concepts describing the relationship of members of a given protein family in one organism to the members of the same family In other organisms. Amino acid abbreviations are provided in Table II. Conservative amino acid substitutions can frequently be made in a protein without altering either the conformation or the function of the protein. Proteins of the Invention can comprise 1, 2, 3,4, 5, 6, 7, 8, 9,10,11,12,13,14,15 conservative substitutions. Such changes include substituting any of isoleucine (1), valine (V), and leucine (L) for any other of these hydrophobic amino acids; aspartic acid (D) for glutamic acid (E) and vice versa; glutamine (0) for asparagine (N) and vice versa; and serine (S) for threonine (T) and vice versa. Other substitutions 32 can also be considered conservative, depending on the environment of the particular amino acid and its role in the three dimensional structure of the protein. For example, glycine (G) and alanine (A) can frequently be Interchangeable, as can alanine (A) and valine (V). Methionine (M), which Is relatively hydrophobic, can frequently be interchanged with leucine and isoleucine, and sometimes with valine. Lysine (K) and arginine (R) are frequently interchangeable In locations in which the significant feature of the amino acid residue is its charge and the differing pK's of these two amino acid residues are not significant Still other changes can be considered 'conservative' in particular environments (see, e.g. Table III herein; pages 13-15 "Biochemistry" 2nd ED. Lubert Stryer ed (Stanford University); Henikoff et at., PNAS 1992 Vol 89 10915-10919; Lei et at., J Biol Chem 1995 May 19; 270(20):11882-6). Embodiments of the Invention disclosed herein include a wide variety of art-accepted variants or analogs of 109P1D4 proteins such as polypeptides having amino acid insertions, deletions and substitutions. 109P104 variants can be made using methods known In the art such as site-directed mutagenesis, alanine scanning, and PCR mutagenesis. Site directed mutagenesis (Carter et al., Nucl. Acids Res., 13:4331 (1986); Zoller et at., Nuct. Acids Res., 10.6487 (1987)), cassette mutagenesis (Wells et al., Gene, 34:315 (1985)), restriction selection mutagenesis (Wels et al., Phi/s. Trans. R. Soc. London SerA, 317:415 (1986)) or other known techniques can be performed on the cloned DNA to produce the 109P1D4 variant DNA. Scanning amino acid analysis can also be employed to identify one or more amino acids along a contiguous sequence that is involved in a specific biological activity such as a protein-protein Interaction. Among the preferred scanning amino acids are relatively small, neutral amino acids. Such amino acids include alanine, glycine, seine, and cysteine. Alanine is typically a preferred scanning amino acid among this group because it eliminates the side-chain beyond the beta carbon and is less likely to alter the main-chain conformation of the variant Alanine is also typically preferred because it Is the most common amino acid. Further, it is frequently found in both buried and exposed positions (Creighton, The Proteins, (W.H. Freeman & Co., N.Y.); Chothia, J. Mol. Biol., 150:1 (1976)). If alanine substitution does not yield adequate amounts of variant an isosteric amino acid can be used. As defined herein, 109P1D4 variants, analogs or homologs, have the distinguishing attribute of having at least one epitope that is "cross reactive" with a 109P1D4 protein having an amino acid sequence of Figure 3. As used in this sentence, 'cross reactive' means that an antibody or T cell that specifically binds to a 109P1D4 variant also specifically binds to a 109P1 D4 protein having an amino acid sequence set forth in Figure 3. A polypeptide ceases to be a variant of a protein shown in Figure 3, when It no longer contains any epitope capable of being recognized by an antibody or T cell that specifically binds to the starting 109P1D4 protein. Those skilled in the art understand that antibodies that recognize proteins bind to epltopes of varying size, and a grouping of the order of about four or five amino adds, contiguous or not is regarded as a typical number of amino acids in a minimal epitope. See, e.g., Nair et al., J. Immunol 2000 165(12): 6949-6955; Hebbes et at., Mol Immunol (1989) 26(9):865-73; Schwartz et al, J Immunol (1985) 135(4):2598-608. Other classes of 109PID4-related protein variants share 70%, 75%, 80%, 85% or 90% or more similarity with an amino acid sequence of Figure 3, or a fragment thereof. Another specific class of 109P1 D4 protein variants or analogs comprises one or more of the 109P1D4 biological motifs described herein or presently known in the art Thus, encompassed by the present Invention are analogs of 109P1D4 fragments (nucleic or amino add) that have altered functional (e.g. Immunogenic) properties relative to the starting fragment It Is to be appreciated that motifs now or which become part of the art are to be applied to the nudelc or amino acid sequences of Figure 2 or Figure 3. As discussed herein, embodiments of the claimed invention include polypeptides containing less than the full amino acid sequence of a I 09P1 D4 protein shown in Figure 2 or Figure 3. For example, representative embodiments of the invention comprise peptides/proteins having any 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15 or more contiguous amino acids of a .33 109P1 D4 protein shown in Figure 2 or Figure 3. Moreover, representative embodiments of the invention disclosed herein include polypeptides consisting of about amino acid I to about amino acid 10 of a 109P1 D4 protein shown In Figure 2 or Figure 3, polypeptides consisting of about amino acid 10 to about amino add 20 of a 109P1D4 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 20 to about amino acid 30 of a 109P1D4 protein shown In Figure 2 or Figure 3, polypeptides consisting of about amino acid 30 to about amino add 40 of a 109P1 D4 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 40 to about amino acid 50 of a 109P1 D4 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 50 to about amino add 60 of a 109P1D4 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 60 to about amino acid 70 of a 109P104 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 70 to about amino acid 80 of a 109P1 D4 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 80 to about amino acid 90 of a 109P1 D4 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 90 to about amino acid 100 of a 109P1 D4 protein shown in Figure 2 or Figure 3, etc. throughout the entirety of a 109P1D4 amino add sequence. Moreover, polypeptides consisting of about amino add I (or 20 or 30 or 40 etc.) to about amino acid 20, (or 130, or 140 or 150 etc.) of a 109P1D4 protein shown in Figure 2 or Figure 3 are embodiments of the invention. Iis to be appreciated that the starting and stopping positions in this paragraph refer to the specified position as well as that position plus or minus 5 residues. 109P1D4-related proteins are generated using standard peptide synthesis technology or using chemical cleavage methods well known in the art. Alernatively, recombinant methods can be used to generate nucleic acid molecules that encode a 109P1D4-related protein. In one embodiment, nucleic acid molecules provide a means to generate defined fragments of a 109P1 D4 protein (or variants, homologs or analogs thereof). i1.A.) Motif-bearing Protein Embodiments Additional illustrative embodiments of the invention disclosed herein include 109P1D4 polypeptides comprising the amino acid residues of one or more of the biological motifs contained within a 109P104 polypeptide sequence set forth in Figure 2 or Figure 3. Various motifs are known in the art, and a protein can be evaluated for the presence of such motifs by a number of publicly available Internet sites (see, e.g., URL addresses: pfam.wusti.edul; searchlauncher.bcm.tmc.edulseq search/struo-predict.html; psortlms.u-tokyo.ac.jp/; cbs.dtu.dk, ebil.ac.uk/interpro/scan.html; expasy.chltools/scnpstl.html; Epimatixm and Epimer", Brown University, brown.edulReseardh/B-HlVablepimtrWepimatrix.htl; and BIMAS, bimas.dcrtnih.gov/.). Motif bearing subsequences of all 109P1D4 variant proteins are set forth and identified in Tables VlII-XXI and XXIl XLIX. Table V sets forth several frequently occurring motifs based on pfam searches (see URL address pfam.wusti.edu). The columns of Table V list (1) motif name abbreviation, (2) percent identity found amongst the different member of the motif family, (3) motif name or description and (4) most common function; location information is included if the motif is relevant for location. Polypeptides comprising one or more of the 109P1D4 motifs discussed above are useful In elucidating the specific characteristics of a malignant phenotype in view of the observation that the 109P1D4 motifs discussed above are associated with growth dysregulation and because 109P1D4 Is overexpressed in certain cancers (See, e.g., Table 1). Casein kinase 11, cAMP and camp-dependent protein kinase, and Protein Kinase C, for example, are enzymes known to be associated with the development of the malignant phenotype (see e.g. Chen et al., Lab Invest., 78(2): 165-174 (1998); Galddon et al., Endocrinology 136(10): 4331-4338 (1995); Hall et al., Nucleic Acids Research 24(6): 1119-1126 (1996); Peterziel et aL., Oncogene 18(46): 6322-6329 (1999) and O'Brian, Onol. Rep. 5(2): 305-309 (1998)). Moreover, both glycosyiation and 34 myristoylation are protein modifications also associated with cancer and cancer progression (see e.g. Dennis et al., Biochem. Biophys. Acta 1473(1):21-34 (1999); Raju et al., Exp. Cell Res. 235(1): 145-154 (1997)). Amidation is another protein modification also associated with cancer and cancer progression (see e.g. Treston et a., J. Nail. Cancer Inst. Monogr. (13): 169-175 (1992)). In another embodiment, proteins of the invention comprise one or more of the immunoreactive epitopes identified in accordance with art-accepted methods, such as the peptides set forth in Tables Vill-XXI and XIl-XLIX CTL epitopes can be determined using specific algorithms to identify peptides within a 109P1 D4 protein that are capable of optimally binding to specified HLA alleles (e.g., Table IV Eplmatrixr and Epimer T M , Brown University, URL brown.edu/ResearchfTB HVLab/epimatrix/epimabixhift and BIMAS, URL bimas.dcrtnih.gov/.) Moreover, processes for Identifying peptides that have sufficient binding affinity for HLA molecules and which are correlated with being Immunogenic epitopes, are well known In the art, and are carried out without undue experimentation. In addition, processes for Identifying peptides that are immunogenic epitopes, are well known in the art and are carried out without undue experimentation either In vitm or in vivo. Also known in the art are principles for creating analogs of such epitopes in order to modulate immunogenicity. For example, one begins with an epitope that bears a CTL or HTL motif (see, e.g., the HLA Class I and HLA Class I motifs/supermotifs of Table IV). The epitope is analoged by substituting out an amino acid at one of the specified positions, and replacing it with another amino acid specified for that position. For example, on the basis of residues defined In Table IV, one can substitute out a deleterious residue in favor of any other residue, such as a preferred residue; substitute a less preferred residue with a preferred residue; or substitute an originally-occurring preferred residue with another preferred residue. Substitutions can occur at primary anchor positions or at other positions in a peptide; see,.e.g., Table IV. A variety of references reflect the art regarding the identification and generation of epitopes in a protein of interest as well as analogs thereof. See, for example, WO 97/33602 to Chesnut et al.; Sette, Immunogenetics 1999 50(3-4): 201 212; Sette et al., J. Immunol. 2001 166(2): 1389-1397; Sidney et al., Hum. Immunol. 1997 58(1): 12-20; Kondo et al., Immunogenetics 1997 45(4): 249-258; Sidney et a., J. Immunol. 1996 157(8): 3480-90; and Falk et al., Nature 351: 290-6 (1991); Hunt et a., Science 255:1261-3 (1992); Parker et al., J. Immunol. 149:3580-7 (1992); Parker et a, J. Immunol. 152:163-75 (1994)); Kast et al., 1994 152(8): 3904-12; Borras-Cuesta et a!., Hum. Immunol. 2000 61(3): 266-278; Alexander et al., J. Immunol. 2000 164(3); 164(3): 1625-1633: Alexander et al., PMID: 7895164, UI: 95202582; O'Sullivan et al., J. Immunol. 1991147(8): 2663-2669; Alexander et al., Immunity 1994 1(9): 751-761 and Alexander et al., Immunol. Res. 1998 18(2):79-92. Related embodiments of the invention Include polypeptides comprising combinations of the different motifs set forth in Table VI, and/or, one or more of the predicted CTL epitopes of Tables ViI-XXI and XXIl-XLIX, and/or, one or more of the predicted HTL epitopes of Tables XLVI-XLIX, and/or, one or more of the T cell binding motifs known In the art Preferred embodiments contain no Insertions, deletions or substitutions either within the motifs or within the intervening sequences of the polypeptides. In addition, embodiments which include a number of either N-terminal and/or C-terminal amino acid residues on either side of these motifs may be desirable (to, for example, include a greater portion of the polypeptide architecture in which the motif is located). Typically, the number of N-terminal and/or C-terminal amino acid residues on either side of a motif Is between about 1 to about 100 amino acid residues, preferably 5 to about 50 amino acid residues. 109P1 D4-related proteins are embodied In many forms, preferably in isolated form. A purified I 09P1 D4 protein molecule will be substantially free of other proteins or molecules that Impair the binding of 1 09P1 D4 to antibody, T cell or other figand. The nature and degree of isolation and purification will depend on the intended use. Embodiments of a 109P1D4 related proteins include purified 109P1D4-related proteins and functional, soluble 109P1D4-related proteins. In one embodiment, a functional, soluble 109P1 D4 protein or fragment thereof retains the ability to be bound by antibody, T cell or 35 other ligand. The invention also provides 109P1D4 proteins comprising biologically active fragments of a 109P1D4 amino acid sequence shown in Figure 2 or Figure 3. Such proteins exhibit properties of the starting 109P1 D4 protein, such as the ability to elicit the generation of antibodies that specifically bind an epitope associated with the starting 109P1D4 protein; to be bound by such antibodies; to elicit the activation of HTL or CTL; and/or, to be recognized by HTL or CTL that also specifically bind to the starting protein. 109P1 D4-related polypeptides that contain particularly interesting structures can be predicted and/or identified using various analyical techniques well known in the art, including, for example, the methods of Chou-Fasman, Gamier-Robson, Kyte Doolitle, Eisenberg, Karplus-Schultz or Jameson-Wolf analysis, or based on Immunogenicity. Fragments that contain such structures are particularly useful in generating subunit-specific anti-1 09P1 D4 antibodies or T cells or in identifying cellular factors that bind to 109P1D4. For example, hydrophilicity profiles can be generated, and Immunogenic peptide fragments identified, using the method of Hopp, T.P. and Woods, KR., 1981, Proc. Natl. Acad. Sci. U.S.A. 78:3824-3828. Hydropathicity profiles can be generated, and immunogenic peptide fragments identified, using the method of Kyte, J. and Doolittle, R.F., 1982, J. Mol. Biol. 157:105-132. Percent (%) Accessible Residues profiles can be generated, and immunogenic peptide fragments Identified, using the method of Janin J., 1979, Nature 277:491-492. Average Flexibility profiles can be generated, and immunogenic peptide fragments Identified, using the method of Bhaskaran R., Ponnuswamy P.K, 1988, Int. J. Pept. Protein Res. 32:242-255. Beta-turn profiles can be generated, and Immunogenic peptide fragments identified, using the method of Deleage, G., Roux B., 1987, Protein Engineering 1:289-294. CTL epitopes can be determined using specific algorithms to identify peptides within a 109P1D4 protein that are capable of optimally binding to specified HLA alleles (e.g., by using the SYFPEITHI site at World Wide Web URL syfpeithi.bmi heidelberg.con; the listings in Table IV(AHE); Epimatre and Epimer

T

M, Brown University, URL (brown.edu/Research/TB HIVLab/eplmatdepImatrix.htmi); and BIMAS, URL bilmas.dcrtnih.gov/. Illustrating this, peptide epitopes from 109P1D4 that are presented in the context of human MHC Class I molecules, e.g., HLA-A1, A2, A3, All, A24, B7 and B35 were predicted (see, e.g., Tables Vill-XXI, XXII-XLIX). Specifically, the complete amino acid sequence of the 109P1D4 protein and relevant portions of other variants, i.e., for HLA Class I predictions 9 flanking residues on either side of a point mutation or exon juction, and for HLA Class Il predictions 14 flanking residues on either side of a point mutation or exon junction corresponding to that variant, were entered into the HILA Peptide Motif Search algorithm found in the Bioinformatics and Molecular Analysis Section (BIMAS) web site listed above; in addition to the site SYFPEITHI, at URL syfpeithi.bmi heldelberg.com/. The HLA peplide motif search algorithm was developed by Dr. Ken Parker based on binding of specific peptide sequences In the groove of HLA Class I molecules, in particular HLA-A2 (see, e.g., Falk et al., Nature 351: 290-6 (1991); Hunt et al., Science 255:1261-3 (1992); Parker et a., J. Immunol. 149:3580-7 (1992); Parker et a., J. Immunol. 152:163-75 (1994)). This algorithm allows location and ranking of 8-mer, 9-mer, and 10-mer peptides from a complete protein sequence for predicted binding to HLA-A2 as well as numerous other HLA Class I molecules. Many HLA class I binding peptides are 8-, 9-, 10 or 1 1-mers. For example, for Class I HLA-A2, the epitopes preferably contain a leucine (L) or methlonine (M) at position 2 and a valine (V) or leucine (L) at the C-terminus (see, e.g., Parker et a., J. Immunol. 149:3580-7 (1992)). Selected results of 109P1D4 predicted binding peptides are shown In Tables VIII-XXI and XXII-XUX herein. In Tables Vill XXI and XXI-XLVIl, selected candidates, 9-mers and 10-mers, for each family member are shown along with their location, the amino acid sequence of each specific peptide, and an estimated binding score. In Tables XLVI-XLIX, selected candidates, 15-mers, for each family member are shown along with their location, the amino acid sequence of each specific peptide, and an estimated binding score. The binding score corresponds to the estimated half time of dissociation of 36 complexes containing the peptide at 370C at pH 6.5. Peptides with the highest binding score are predicted to be the most tightly bound to HILA Class I on the cell surface for the greatest period of time and thus represent the best immunogenic targets for T-cell recognition. Actual binding of peptides to an HILA allele can be evaluated by stabilization of HLA expression on the antigen processing defective cell line T2 (see, e.g., Xue at a/., Prostate 30:73-8 (1997) and Peshwa et al., Prostate 36:129-38 (1998)). Immunogenicity of specific peptides can be evaluated in vitro by stimulation of CD8+ cytotoxic T lymphocytes (CTL) in the presence of antigen presenting cells such as dendritic cells. It Is to be appreciated that every epitope predicted by the BIMAS site, EpimerTm and EpimatrixTM sites, or specified by the HLA dass I or dass I motifs available in the art or which become part of the art such as set forth In Table IV (or determined using World Wide Web site URL syfpeithi.bmi-heldelberg.coml, or BIMAS, bimas.dcrtnih.gov) are to be "applied" to a 109P1D4 protein in accordance with the invention. As used in this context "applied" means that a 109P1D4 protein is evaluated, e.g., visually or by computer-based patterns finding methods, as appreciated by those of skill in the relevant art. Every subsequence of a 109P1D4 protein of 8, 9, 10, or 11 amino acid residues that bears an HLA Class I motif, or a subsequence of 9 or more amino acid residues that bear an HILA Class i motif are within the scope of the Invention. IlI.B.) Expression of 109P1D4.related Proteins In an embodiment described in the examples that follow, 109P1D4 can be conveniently expressed in cells (such as 293T cells) transfected with a commercially available expression vector such as a CMV-driven expression vector encoding 109P1 D4 with a C-terminal 6XHis and MYC tag (pcDNA3.1/mycHIS, Invitrogen or Tag5, GenHunter Corporation, Nashville TN). The Tag5 vector provides an IgGK secretion signal that can be used to facilitate the production of a secreted 109P1D4 protein in traisfected cells. The secreted HIS-tagged 109P1D4 in the culture media can be purified, e.g., using a nickel column using standard techniques. lIl.C.) Modifications of 1 09P1D4-related Proteins Modifications of 109P1D4-related proteins such as covalent modifications are included within the scope of this invention. One type of covalent modification includes reacting targeted amino acid residues of a 109P1D4 polypeptide with an organic derivatizing agent that is capable of reacting with selected side chains or the N- or C- terminal residues of a 109P1D4 protein. Another type of covalent modification of a 109P1D4 polypeptide included within the scope of this Invention comprises altering the native glycosylation pattern of a protein of the invention. Another type of covalent modification of 109P1D4 comprises Unking a 109P1D4 polypeptide to one of a variety of nonproteinaceous polymers, e.g., polyethylene glycol (PEG), polypropylene glycol, or polyoxyalkylenes, in the manner set forth in U.S. Patent Nos. 4,640,835; 4,496,689; 4,301,144; 4,670,417; 4,791,192 or 4,179,337. The 109P1 D4-related proteins of the present Invention can also be modified to form a chimeric molecule comprising 109P1D4 fused to another, heterologous polypeptide or amino acid sequence. Such a chimeric molecule can be synthesized chemically or recombinantly. A chimeric molecule can have a protein of the invention fused to another tumor associated antigen or fragment thereof. Alternatively, a protein In accordance with the Invention can comprise a fusion of fragments of a 109P1D4 sequence (amino or nucleic acid) such that a molecule Is created that is not, through its length, directly homologous to the amino or nucleIc acid sequences shown In Figure 2 or Figure 3. Such a chimeric molecule can comprise multiples of the same subsequence of 109P1D4. Achimeric molecule can comprise a fusion of a 109P1D4-related protein with a polyhistidine epitope tag, which provides an epitope to which immobilized nickel can selectively bind, with cytokines or with growth factors. The epitope tag is generally placed at the amino- or carboxyl- terminus of a 109P1D4 protein. In an alternative embodiment, the chimeric molecule can comprise a fusion of a 109P1 D4-related protein with an immunoglobulin or a particular region of an immunoglobulin. For a bivalent form of the chimeric molecule (also referred to as an "immunoadhesin"), such a fusion could be to the Fc region of an IgG molecule. The Ig fusions preferably include the substitution of a soluble (transmembrane domain deleted or inactivated) form of a 109P1 D4 polypeptide in place of at least one variable region within an Ig molecule. In a preferred embodiment, the immunoglobulin fusion includes the hinge, CH2 and CH3, or the hinge, CHI, CH2 and CH3 regions of an IgGI molecule. For the production of immunoglobulin fusions see, e.g., U.S. Patent No. 5,428,130 Issued June 27, 1995. 111.0.) Uses of 109P1 04-related Proteins The proteins of the invention have a number of different specific uses. As 109P1D4 is highly expressed in prostate and other cancers, 109P1 D4-related proteins are used in methods that assess the status of 109P1D4 gene products in normal versus cancerous tissues, thereby elucidating the malignant phenotype. Typically, polypeptides from specific regions of a 109P 1D4 protein are used to assess the presence of perturbations (such as deletions, insertions, point mutations etc.) in those regions (such as regions containing one or more motifs). Exemplary assays utilize antibodies or T cells targeting 109P1 D4-related proteins comprising the amino acid residues of one or more of the biological motifs contained within a 109P1D4 polypeptide sequence in order to evaluate the characteristics of this region in normal versus cancerous tissues or to elicit an immune response to the epitope. Alternatively, 109P1D4-related proteins that contain the amino acid residues of one or more of the biological motifs in a 109P1 D4 protein are used to screen for factors that interact with that region of 109P1 D4. 109P1D4 protein fragments/subsequences are particularly useful In generating and charactedizing domain-specific antibodies (e.g., antibodies recognizing an extracellular or intracellular epitope of a 109P1D4 protein), for identifying agents or cellular factors that bind to 109P1D4 or a particular structural domain thereof, and in various therapeutic and diagnostic contexts, including but not limited to diagnostic assays, cancer vaccines and methods of preparing such vaccines. Proteins encoded by the 109P1 D4 genes, or by analogs, homologs or fragments thereof, have a variety of uses, including but not limited to generating antibodies and in methods for identifying ligands and other agents and cellular constituents that bind to a 109P1D4 gene product Antibodies raised against a 1 09P1 D4 protein or fragment thereof are useful in diagnostic and prognostic assays, and imaging methodologies in the management of human cancers characterized by expression of 109P1D4 protein, such as those listed in Table I. Such antibodies can be expressed intracellularly and used in methods of treating patients with such cancers. 109P1D4-related nucleic acids or proteins are also used in generating HTL or CTL responses. Various inmunological assays useful for the detection of 109P1D4 proteins are used, Including but not limited to various types of radiotmmunoassays, enzyme-linked immunosorbent assays (EUSA), enzyme-nked Immunofuorescent assays (ELIFA), immunocytochemical methods, and the like. Antibodies can be labeled and used as immunological Imaging reagents capable of detectng 109P1D 4-expressing cells (e.g., in radioscintigraphic imaging methods). 109P1D4 proteins are also particularly useful in generating cancer vaccines, as further described herein. IV.) 109PID4Antibodies Another aspect of the Invention provides antibodies that bind to 109P1D4-related proteins. Preferred antibodies specifically bind to a 109P1D4-related protein and do not bind (or bind weakly) to peptides or proteins that are not 109P1D4 related proteins under physlological conditions. In this context, examples of physiological conditions include: 1) phosphate buffered salne; 2) Tils-buffered saline containing 25mM Tris and 150 mM NaC; or normal saline (0.9% NaC); 4) animal serum such as human serum; or, 5) a combination of any of 1) through 4); these reactions preferably taking place at pH 7.5, alternatively In a range of pH 7.0 to 8.0, or alternatively in a range of pH 6.5 to 8.5; also, these reactions taking place at a temperature between 40C to 370C. For example, antibodies that bind 109P1 D4 can bind 109P1 D4-related proteins such as the homologs or analogs thereof. I 09P1 D4 antibodies of the invention are particularly useful in cancer (see, e.g., Table 1) diagnostic and prognostic assays, and Imaging methodologies. Similarly, such antibodies are useful in the treatment, diagnosis, and/or prognosis of other cancers, to the extent 109P1D4 is also expressed or overexpressed in these other cancers. Moreover, intracellularly expressed antibodies (e.g., single chain antibodies) are therapeutically useful in treating cancers in which the expression of 109P1D4 is involved, such as advanced or metastatic prostate cancers. The invention also provides various immunological assays useful for the detection and quantification of 109P1D4 and mutant 109P1 D4-related proteins. Such assays can comprise one or more 109P1 D4 antibodies capable of recognizing and binding a 109P1 D44elated protein, as appropriate. These assays are performed within various immunological assay formats well known in the art including but not limited to various types of radimmunoassays, enzyme-linked Immunosorbent assays (EUSA), enzyme-linked Immunofluorescent assays (ELIFA), and the like. Immunological non-antibody assays of the invention also comprise T cell Immunogenicity assays (inhibitory or stimulatory) as well as maor histocompatibility complex (MHC) binding assays. In addition, immunological imaging methods capable of detecting prostate cancer and other cancers expressing 109P1D4 are also provided by the invention, induding but not limited to radioscintigraphic imaging methods using labeled 109P1D4 antibodies. Such assays are clinically useful in the detection, monitoring, and prognosis of 109P1D4 expressing cancers such as prostate cancer. 109P1D4 antibodies are also used In methods for purifying a 109P1 D4-related protein and for isolating 109P1D4 homologues and related molecules. For example, a method of purifying a 109P 104-related protein comprises incubating a 109P1D4 antibody, whidi has been coupled to a solid matrix, with a lysate or other solution containing a 109P1D4-related protein under conditions that permit the 109P1 D4 anybody to bind to the 109PI D4-related protein; washing the solid matrix to eliminate impurities; and eluting the 109P1D4-related protein from the coupled antibody. Other uses of 109P1D4 antibodies in accordance with the invention include generating anti-idiotypic antibodies that mimic a 109P1D4 protein. Various methods for the preparation of antibodies are well known In the art For example, antibodies can be prepared by immunizing a suitable mammalian host using a 109P1 4-related protein, peptide, or fragment in isolated or immunoconjugated form (Antibodies: A Laboratory Manual, CSH Press, Eds., Hadow, and Lane (1988); Harlow, Antibodies, Cold Spring Harbor Press, NY (1989)). In addition, fusion proteins of 109P1D4 can also be used, such as a 109P1D4 GST-fusion protein. In a particular embodiment, a GST fusion protein comprising at or most of the amino acid sequence of Figure 2 or Figure 3 is produced, then used as an immunogen to generate appropriate antibodies. In another embodiment, a 109P1D4-related protein Is synthesized and used as an Immunogen. In addition, naked DNA immunization techniques known in the art are used (with or without purified 109P1D04-related protein or 109P 1D4 expressing cells) to generate an Immune response to the encoded immunogen (for review, see Donnelly et at, 1997, Ann. Rev. Immunol. 15: 617-648). The amino acid sequence of a 109P1D4 protein as shown in Figure 2 or Figure 3 can be analyzed to select specific regions of the 109P1D4 protein for generating antibodies. For example, hydrophobicity and hydrophilicity analyses of a 109P1 D4 amino acid sequence are used to identify hydrophic regions in the 109P1D4 structure. Regions of a 109P1D4 protein that show immunogenic structure, as well as other regions and domains, can readily be Identified using various other methods known In the art, such as Chou-Fasman, Gamler-Robson, Kyte-Doolittle, Elsenberg, Karplus-Schultz or Jameson-Wolf analysis. Hydrophilicity 39 profiles can be generated using the method of Hopp, T.P. and Woods, K.R., 1981, Proc. Natl. Acad. Sci. U.S.A. 78:3824 3828. Hydropathicity profiles can be generated using the method of Kyte, J. and Doolittle, R.F., 1982, J. Mol. Biol. 157:105 132. Percent (%) Accessible Residues profiles can be generated using the method of Janin J., 1979, Nature 277:491-492. Average Flexibility profiles can be generated using the method of Bhaskaran R., Ponnuswamy P.K, 1988, Int. J. Pept Protein Res. 32:242-255. Beta-tum profiles can be generated using the method of Deleage, G., Roux B., 1987, Protein Engineering 1:289-294. Thus, each region Identified by any of these programs or methods Is within the scope of the present invention. Methods for the generation of 109P1D4 antibodies are further ilustrated by way of the examples provided herein. Methods for preparing a protein or polypeptide for use as an immunogen are well known in the art. Also well known in the art are methods for preparing immunogenic conjugates of a protein with a carrier, such as BSA, KLH or other carrier protein. In some circumstances, direct conjugation using, for example, carbodiimide reagents are used; in other instances linking reagents such as those supplied by Pierce Chemical Co., Rockford, fL, are effective. Administration of a 109P1 D4 imimunogen is often conducted by injection over a suitable time period and with use of a suitable adjuvant, as is understood In the art During the immunization schedule, fiters of antibodies can be taken to determine adequacy of antibody formation. 109P1D4 monoclonal antibodies can be produced by various means well known In the art For example, immortalized cell lines that secrete a desired monoclonal antibody are prepared using the standard hybridoma technology of Kohler and Milstein or modifications that immortalize antibody-producing B cells, as is generally known. Immortalized cell lines that secrete the desired antibodies are screened by immunoassay In which the antigen is a 109P1D4-4elated protein. When the appropriate immortalized cell culture is Identified, the cells can be expanded and antibodies produced either from in vit cultures or from ascites fluid. The antibodies or fragments of the invention can also be produced, by recombinant means. Regions that bind specifically to the desired regions of a 109P1D4 protein can also be produced in the context of chimeric or complementarity deternining region (CDR) grafted antibodies of multiple species origin. Humanized or human 109P1 D4 antibodies can also be produced, and are preferred for use in therapeutic contexts. Methods for humanizing murine and other non-human antibodies, by substituting one or more of the non-human antibody CDRs for corresponding human antibody sequences, are well known (see for example, Jones et al., 1986, Nature 321: 522-525; Riechmann et al., 1988, Nature 332: 323-327; Vertoeyen et al., 1988, Science 239: 1534-1536). See also, Carter eta., 1993, Proc. Nat. Acad. Sci. USA 89: 4285 and Sims et al., 1993, J. Immunol. 151: 2296. Methods for producing fully human monoclonal antibodies include phage display and transgenic methods (for review, see Vaughan et al., 1998, Nature Biotechnology 16: 535-539). Fully human 109P1 D4 monoclonal antibodies can be generated using cloning technologies employing large human Ig gene combinatorial libraries (i.e., phage display) (Griffiths and Hoogenboom, Building an In ito immune system human antibodies from phage display libraries. In: Protein Engineering of Antibody Molecules for Prophylactic and Therapeutic Apiplications in Man, Clark, M. (Ed.), Nottingham Academic, pp 45-64 (1993); Burton and Barbas, Human Antibodies from combinatorial libraries. Id., pp 65-82). Fully human 109P1D4 monoclonal antibodies can also be produced using transgenic mice engineered to contain human Immunoglobulin gene loci as described in PCT Patent Application W098/24893, Kucherapati and Jakobovits et at., published December 3,1997 (see also, Jakobovits, 1998, Exp. Opin. Invest. Drugs 7(4): 607-614; U.S. patents 6,162963 issued 19 December 2000; 6,150,584 issued 12 November 2000; and, 6,114598 Issued 5 September 2000). This method avoids the in vit manipulation required with phage display technology and eficienly produces high affinity authentic human antibodies. Reactivity of 109P1 D4 antibodies with a 1 09P1 D4-related protein can be established by a number of well known means, including Western blot, immunopreclpitation, ELISA, and FACS analyses using, as appropriate, 109P1 D4-related proteins, 109P1 D4-expressing cells or extracts thereof. A 109P1 D4 antibody or fragment thereof can be labeled with a detectable marker or conjugated to a second molecule. Suitable detectable markers Include, but are not limited to, a 40 radioisotope, a fluorescent compound, a bioluminescent compound, chemiluminescent compound, a metal chelator or an enzyme. Further, bi-specific antibodies specific for two or more 109P1 D4 epitopes are generated using methods generally known In the art Homodimeric antibodies can also be generated by cross-linking techniques known in the art (e.g., Wolff at al., Cancer Res. 53: 2560-2565). V,) 109PID4 Cellular Immune Responses The mechanism by which T cells recognize antigens has been delineated. Efficacious peptide epitope vaccine compositions of the invention Induce a therapeutic or prophylactic immune responses in very broad segments of the world wide population. For an understanding of the value and efficacy of compositions of the Invention that induce cellular immune responses, a brief review of immunology-related technology is provided. A complex of an HLA molecule and a peptidic antigen acts as the ligand recognized by HLA-restricted T cells (Buus, S. et at., Cell 47:1071, 1986; Babbitt, B. P. at at., Nature 317:359,1985; Townsend, A. and Bodmer, H., Annu. Rev. Immunol. 7:601, 1989; Germain, R. N., Annu. Rev. Immunol. 11:403,1993). Through the study of single amino acid substituted antigen analogs and the sequencing of endogenously bound, naturally processed peptides, critical residues that correspond to motifs required for specific binding to HLA antigen molecules have been identified and are set forth in Table IV (see also, e.g., Southwood, et al., J. lmmunol. 160:3363, 1998; Rammensee, et al., Immunogenetics 41:178,1995; Rammensee et a., SYFPEITHI, access via World Wide Web at URL (134.2.96.221/scripts.hlaserver.dlVhome.htm); Sette, A. and Sidney, J. Curr. Opin. Immunol. 10:478,1998; Engelhard, V. H., Cur. Opin. Immunol. 6:13,1994; Sette, A. and Grey, H. M., Curr. Opin. Immunol. 4:79,1992; Sinigaglia, F. and Hammer, J. Curr. Biol. 6:52, 1994; Ruppert et at., Cell 74:929-937, 1993; Kondo et a., J. Immunol. 155:4307-4312,1995; Sidney et a., J. Immunol. 157:3480-3490,1996; Sidney et al, Human Immunol. 45:79-93, 1996; Sette, A. and Sidney, J. Immunogenetics 1999 Nov; 50(3-4):201-12, Review). Furthermore, x-ray crystallographic analyses of HLA-peptide complexes have revealed pockets within the peptide binding cleft/groove of HLA molecules which accommodate, In an allele-specific mode, residues bome by peptide ligands; these residues In turn determine the HLA binding capacity of the peptides in which they are present. (See, e.g., Madden, D.R. Annu. Rev. Immunol. 13:587,1995; Smith, et al., Immunity 4:203, 1996; Fremont et al., Immunity 8:305, 1998; Stem at al., Structure 2-245,1994; Jones, E.Y. Curr. Opin. Immunol. 9:75, 1997; Brown, J. H. et al., Nature 364:33, 1993; Guo, H. C. at al., Proc. Nat. Aced. Sci. USA 90:8053,1993; Guo, H. C. et at., Nature 360:364,1992; Silver, M. L at al., Nature 360:367, 1992; Matsumura, M. et aL., Science 257:927,1992; Madden et al., Cell 70:1035, 1992; Fremont, D. H. et al., Science 257:919, 1992; Saper, M. A. , Bjorkman, P. J. and Wiley, D. C., J. Mol. Biol. 219:277, 1991.) Accordingly, the definition of class I and dass 11 alele-specific HLA binding motifs, or class I or class Il supermotifs allows Identification of regions within a protein that are correlated with binding to particular HLA antigen(s). Thus, by a process of HLA motif identification, candidates for epitope-based vaccines have been identified; such candidates can be further evaluated by HLA-peptide binding assays to determine binding affinity and/or the time period of association of the epitope and its corresponding HLA molecule. Additional confirmatory work can be performed to select, amongst these vaccine candidates, epitopes with preferred characteristics in terms of population coverage, and/or Immunogenicity. Various strategies can be utilized to evaluate cellular Immunogenicity, including: 1) Evaluation of primary T cell cultures from normal individuals (see, e.g., Wentworth, P. A. et al., Mol. Immunol. 32:603, 1995; Cells, E. et at., Poc. Nat. Acad. Sci. USA 91:2105, 1994; Tsai, V. et at., J. Immunol. 158:1796,1997; Kawashima, I. et al., Human Immunol. 59:1, 1998). This procedure involves the stimulation of peripheral blood lymphocytes (PBL) from normal subjects with a test peptide in the presence of antigen presenting cells ln vitro over a period of several 41 weeks. T cells specific for the peptide become activated during this time and are detected using, e.g., a lymphokine- or 51 Cr-release assay involving peptide sensitized target cells. 2) Immunization of HLA transgenic mice (see, e.g., Wentworth, P. A. et al., J. Immunol. 2697, 1996; Wentworth, P. A. et al., Int. Immunol. 8:651, 1996; Alexander, J. et al., J. Immunol. 159:4753, 1997). For example, in such methods peptides In Incomplete Freund's adjuvant are administered subcutaneously to HIA transgenic mice. Several weeks following immunization, splenocytes are removed and cultured in viro in the presence of test peptide for approximately one week. Peptide-specific T cells are detected using, e.g., a 51 Cr-release assay involving peptide sensitized target cells and target cells expressing endogenously generated antigen. 3) Demonstration of recall T cell responses from immune individuals who have been either effectively vaccinated and/or from chronically ill patients (see, e.g., Rehermann, B. et al., J. Exp. Med. 181:1047, 1995; Doolan, D. L. el al, Immunity 7:97, 1997; Bertonl, R. et al., J. C/in. Invest. 100:503, 1997; Threlkeld, S. C. et al., J. Immunol. 159:1648, 1997; Diepolder, H. M. et al., J. Vir). 71:6011, 1997). Accordingly, recall responses are detected by culturing PBL from subjects that have been exposed to the antigen due to disease and thus have generated an immune response "naturally', or from patients who were vaccinated against the antigen. PBL from subjects are cultured in vitro for 1-2 weeks in the presence of test peptide plus antigen presenting cells (APC) to allow activation of "memory" T cells, as compared to "naive' T cells. At the end of the culture period, T cell activity Is detected using assays Including 51 Cr release involving peptide-sensitized targets, T cell proliferation, or lymphokine release. VI.) 109P1D4 Transgenic Animals Nucleic acids that encode a 109P1 D4-related protein can also be used to generate either transgenic animals or 'knock out" animals that, in tum, are useful in the development and screening of therapeutically useful reagents. In accordance with established techniques, cDNA encoding 109P1D4 can be used to clone genomic DNA that encodes 109P1D4. The cloned genomic sequences can then be used to generate transgenic animals containing cells that express DNA that encode 109P1D4. Methods for generating transgenic animals, particularly animals such as mice or rats, have become conventional in the art and are described, for example, in U.S. Patent Nos. 4,736,866 issued 12 April 1988, and 4,870,009 issued 26 September 1989. Typically, particular cells would be targeted for 109P1D4 transgene incorporation with tissue-specific enhancers. Transgenic animals that include a copy of a transgene encoding 109P1 D4 can be used to examine the effect of increased expression of DNA that encodes 109P1D4. Such animals can be used as tester animals for reagents thought to confer protection from, for example, pathological conditions associated with its overexpression. In accordance with this aspect of the Invention, an animal is treated with a reagent and a reduced Incidence of a pathological condition, compared to untreated animals that bear the transgene, would indicate a potential therapeutic Intervention for the pathological condition. Altematively, non-human homologues of 109P1D4 can be used to construct a 109P1D4 "knock out' animal that has a defective or altered gene encoding 109P1 D4 as a result of homologous recombination between the endogenous gene encoding 109P1 D4 and altered genomic DNA encoding 109P1 D4 Introduced into an embryonic cell of the animal. For example, cDNA that encodes 109P1 D4 can be used to clone genomic DNA encoding 109P1 D4 in accordance with established techniques. A portion of the genomic DNA encoding 109P1D4 can be deleted or replaced with another gene, such as a gene encoding a selectable marker that can be used to monitor Integration. Typically, several kilobases of unaltered flanking DNA (both at the 5' and 3' ends) are included In the vector (see, e.g., Thomas and Capecchi, Cell, :503 (1987) for a description of homologous recombination vectors). The vector is introduced into an embryonic stem cell line (e.g., by electroporation) and cells in which the Introduced DNA has homologously recombined with the endogenous DNA 42 are selected (see, e.g., Li et al, Cel 69:915 (1992)). The selected cells are then injected into a blastocyst of an animal (e.g., a mouse or rat) to form aggregation chimeras (see, e.g., Bradley, in Teratocarcinomas and Embiyonic Stem Cells: A Practical Approach, E. J. Robertson, ed. (IRL, Oxford, 1987), pp. 113-152). A chimeric embryo can then be implanted into a suitable pseudopregnant female foster animal, and the embryo brought to term to create a 'knock out" animal. Progeny harboring the homologously recombined DNA in their germ cells can be identified by standard techniques and used to breed animals In which all cells of the animal contain the homologously recombined DNA Knock out animals can be characterized, for example, for their ability to defend against certain pathological conditions or for their development of pathological conditions due to absence of a 109P1 D4 polypeptide. ViL) Methods for the Detection of 109P1D4 Another aspect of the present invention relates to methods for detecting 109P104 polynucleotides and 109P1D4 related proteins, as wel as methods for identifying a cell that expresses 109P1 D4. The expression profile of 109P1 D4 makes it a diagnostic marker for metastasized disease. Accordingly, the status of 109P1 D4 gene products provides information useful for predicting a variety of factors Induding susceptibility to advanced stage disease, rate of progression, and/or tumor aggressiveness. As discussed in detail herein, the status of 109P1D4 gene products in patient samples can be analyzed by a variety protocols that are wel known in the art Including immunohistochemical analysis, the variety of Northem blotting techniques induding in situ hybridization, RT-PCR analysis (for example on laser capture mIcro-dIssected samples), Western blot analysis and tissue array analysis. More particularly, the invention provides assays for the detection of 109P1 D4 polynucleotides in a biological sample, such as serum, bone, prostate, and other tissues, urine, semen, coil preparations, and the like. Detectable 109P1D4 polynudeotides Include, for example, a 109P1 D4 gene or fragment thereof, 109P1 D4 mRNA, alternative splice variant 109P1D4 mRNAs, and recombinant DNA or RNA molecules that contain a 109P1D4 polynudeotide. A number of methods for amplifying and/or detecting the presence of 109P1D4 polynucleotides are well known in the art and can be employed in the practice of this aspect of the invention. In one embodiment, a method for detecting a 109P1D4 mRNA in a biological sample comprises producing cDNA from the sample by reverse transcription using at least one primer; amplifying the cDNA so produced using a 109P1D4 polynucleotides as sense and antisense primers to amplify 109P1 D4 cDNAs therein; and detecting the presence of the amplified 109P1D4 cONA. Optionally, the sequence of the amplified 109P1D4 cDNA can be determined. In another embodiment, a method of detecting a 109P1 D4 gene In a biological sample comprises first isolating genomic DNA from the sample; ampifying the isolated genomic DNA using 109P1D4 polynucleotides as sense and antisense primers; and detecting the presence of the amplified 109P1D4 gene. Any number of appropriate sense and antisense probe combinations can be designed from a 109P1D4 nucleotide sequence (see, e.g., Figure 2) and used for this purpose. The Invention also provides assays for detecting the presence of a 109P1 D4 protein in a tissue or other biological sample such as serum, semen, bone, prostate, urine, cell preparations, and the like. Methods for detecting a 109P1 D4-related protein are also well known and indude, for example, immunoprecipitation, Immunohistochemical analysis, Western blot analysis, molecular binding assays, ELISA, ELIFA and the like. For example, a method of detecting the presence of a 109P1 D4-related protein In a biological sample comprises first contacting the sample with a 109P1D4 antibody, a 109P1 D4-reactive fragment thereof, or a recombinant protein containing an antigen-binding region of a 109P1 D4 antibody; and then detecting the binding of 109P1D4-related protein in the sample. Methods for identifying a cell that expresses 109P1D4 are also within the scope of the invention. In one embodiment, 43 an assay for identifying a cell that expresses a 109P1D4 gene comprises detecting the presence of 109P1D4 mRNA in the cell. Methods for the detection of particular mRNAs in cells are well known and indude, for example, hybridization assays using complementary DNA probes (such as in situ hybridization usIng labeled 109P1D4 nboprobes, Northern blot and related techniques) and various nucleic acid amplification assays (such as RT-PCR using complementary primers specific for 109P1 D4, and other amplification type detection methods, such as, for example, branched DNA, SISBA, TMA and the like). Alternatively, an assay for identifying a cell that expresses a 109P1D4 gene comprises detecting the presence of 109P1D4-related protein in the cell or secreted by the cell. Va-ious methods for the detection of proteins are well known in the art and are employed for the detection of 109P1D4-related proteins and cells that express 109P1 D4-related proteins. 109P1D4 expression analysis Is also useful as a tool for identifying and evaluating agents that modulate 109P1D4 gene expression. For example, 109P1 D4 expression is significantly upregulated in prostate cancer, and is expressed In cancers of the tissues listed in Table I. Identification of a molecule or biological agent that inhibits 109P1D4 expression or over expression in cancer cells is of therapeutic value. For example, such an agent can be identified by using a screen that quantifies 109P1D4 expression by RT-PCR, nuclelc acid hybridization or antibody binding. Vill.) Methods for Monitoring the Status of 109P1D4-related Genes and Their Products Oncogenesis is known to be a multistep process where cellular growth becomes progressively dysregulated and cells progress from a normal physiological state to precancerous and then cancerous states (see, e.g., Alers et al., Lab Invest 77(5): 437-438 (1997) and Isaacs et aL., Cancer Surv. 23: 19-32 (1995)). In this context, examining a biological sample for evidence of dysregulated cell growth (such as aberrant 109P1 D4 expression in cancers) allows for early detection of such aberrant physiology, before a pathologic state such as cancer has progressed to a stage that therapeutic options are more limited and or the prognosis is worse. In such examinations, the status of 109P1 D4 In a biological sample of interest can be compared, for example, to the status of 109P1D4 in a corresponding normal sample (e.g. a sample from that individual or alternatively another Individual that is not affected by a pathology). An alteration In the status of 109P1D4 In the biological sample (as compared to the normal sample) provides evidence of dysregulated cellular growth. In addition to using a biological sample that is not affected by a pathology as a normal sample, one can also use a predetermined normative value such as a predetermined normal level of mRNA expression (see, e.g., Grever et al., J. Comp. Neurol. 1996 Dec 9; 376(2): 306-14 and U.S. Patent No. 5,837,501) to compare 109P1D4 status in a sample. The term "status' in this context is used according to its art accepted meaning and refers to the condition or state of a gene and its products. Typically, skilled artisans use a number of parameters to evaluate the condition or state of a gene and its products. These indude, but are not limited to the location of expressed gene products (including the location of 109P1 D4 expressing cells) as well as the level, and biological activity of expressed gene products (such as 109P1D4 mRNA, polynucleolides and polypeptides). Typically, an alteration in the status of 109P1D4 comprises a change in the location of 109P1D4 and/or 109P1D4 expressing cells and/or an increase In 109P1D4 mRNA and/or protein expression. 109P1D4 status in a sample can be analyzed by a number of means well known In the art, Induding without limitation, Immunohistodiemical analysis, In situ hybridization, RT-PCR analysis on laser capture micro-dissected samples, Western blot analysis, and tissue array analysis. Typical protocols for evaluating the status of a 109P1 D4 gene and gene products are found, for example In Ausubel et al. eds., 1995, Current Protocols In Molecular Biology, Units 2 (Northem Blotting), 4 (Southern Blotting), 15 (Immunablotting) and 18 (PCR Analysis). Thus, the status of 109P1D4 in a biological sample Is evaluated by various methods utilized by skilled artisans including, but not limited to genomic Southern analysIs (to examine, for example perturbations in a 109P1 D4 gene), Northern analysis and/or PCR analysis of 109P1 D4 mRNA (to examine, for example alterations In the polynudeotide sequences or expression levels of 109P1 D4 mRNAs), and, Western and/or 44 immunohistochemical analysis (to examine, for example alterations in polypeptide sequences, alterations in polypeptide localization within a sample, alterations in expression levels of 109P1D4 proteins and/or associations of 109P1D4 proteins with polypeptide binding partners). Detectable 109P1 D4 polynudeotides indude, for example, a 109P1D4 gene or fragment thereof, 1 09P1 D4 mRNA, alternative splice variants, 109P1 D4 mRNAs, and recombinant DNA or RNA molecules containing a 109P1D4 polynudeolide. The expression profile of 109P1 D4 makes it a diagnostic marker for local and/or metastasized disease, and provides information on the growth or oncogenic potential of a biological sample. In particular, the status of 109P1D4 provides information useful for predicting susceptibility to particular disease stages, progression, and/or tumor aggressiveness. The invention provides methods and assays for determining 109P1D4 status and diagnosing cancers that express 109P1D4, such as cancers of the tissues listed in Table 1. For example, because 109P1D4 mRNA is so highly expressed in prostate and other cancers relative to normal prostate tissue, assays that evaluate the levels of 109P1D4 mRNA trnscripts or proteins in a biological sample can be used to diagnose a disease associated with 109P1D4 dysregulation, and can provide prognostic information useful in defining appropriate therapeutic options. The expression status of 109P1D4 provides Information inducing the presence, stage and location of dysplastic, precancerous and cancerous cells, predicting susceptibility to various stages of disease, and/or for gauging tumor aggressiveness. Moreover, the expression profile makes it useful as an Imaging reagent for metastasized disease. Consequently, an aspect of the invention is directed to the various molecular prognostic and diagnostic methods for examining the status of 109P1 D4 in biological samples such as those from individuals suffering from, or suspected of suffering from a pathology characterized by dysregulated cellular growth, such as cancer. As described above, the status of 109P1D4 in a biological sample can be examined by a number of well-known procedures in the art For example, the status of 109P1D4 in a biological sample taken from a specific location in the body can be examined by evaluating the sample for the presence or absence of 109P1D4 expressing cells (e.g. those that express 109P1D4 mRNAs or proteins). This examination can provide evidence of dysregulated cellular growth, for example, when 109P1D4-expressing cells are found in a biological sample that does not normally contain such cells (such as a lymph node), because such alterations In the status of 109P1D4 in a biological sample are often associated with dysregulated cellular growth. Specifically, one indicator of dysregulated cellular growth is the metastases of cancer cells from an organ of origin (such as the prostate) to a different area of the body (such as a lymph node). In this context, evidence of dysregulated cellular growth is important for example because occult lymph node metastases can be detected in a substantial proportion of patients with prostate cancer, and such metastases are associated with known predictors of disease progression (see, e.g., Murphy et aL, Prostate 42(4): 315-317 (2000);Su et al., Semin. Surg. Oncol. 18(1): 17-28 (2000) and Freeman et al., J Urol 1995 Aug 154(2 Pt 1):474-8). In one aspect, the invention provides methods for monitoring 109P1D4 gene products by determining the status of 109P1D4 gene products expressed by cells from an individual suspected of having a disease associated with dysregulated cell growth (such as hyperplasia or cancer) and then comparing the status so determined to the status of 109P1 D4 gene products In a corresponding normal sample. The presence of aberrant 109P1 D4 gene products in the test sample relative to the normal sample provides an indication of the presence of dysregulated cell growth within the cells of the individual. In another aspect, the invention provides assays useful in determining the presence of cancer in an Individual, comprising detecting a significant Increase In 109P1D4 mRNA or protein expression in a test cell or tissue sample relative to expression levels in the corresponding normal cell or tissue. The presence of 109P1 D4 mRNA can, for example, be evaluated in tissues Including but not limited to those listed In Table 1. The presence of significant 109P1D4 expression in any of these tissues is useful to indicate the emergence, presence and/or severity of a cancer, since the corresponding 45 normal tissues do not express 109P1 D4 mRNA or express it at lower levels. In a related embodiment 109P1 D4 status is determined at the protein level rather than at the nudeic acid level. For example, such a method comprises determining the level of 109P1 D4 protein expressed by cells in a test tissue sample and comparing the level so determined to the level of 109P1D4 expressed in a corresponding normal sample. In one embodiment the presence of 109P1D4 protein is evaluated, for example, using immunohistochemical methods. 109P1D4 antibodies or binding partners capable of detecting 109P1D4 protein expression are used in a variety of assay formats well known in the art for this purpose. In a further embodiment one can evaluate the status of 109P1D4 nucleotide and amino acid sequences in a biological sample in order to identify perturbations In the structure of these molecules. These perturbations can indude insertions, deletions, substitutions and the like. Such evaluations are useful because perturbations in the nucleotide and amino acid sequences are observed in a large number of proteins associated with a growth dysregulated phenotype (see, e.g., Marrogi et al., 1999, J. Cutan. Pathol. 26(8):369-378). For example, a mutation in the sequence of 109P1D4 may be indicative of the presence or promotion of a tumor. Such assays therefore have diagnostic and predicive value where a mutation in 109P1 D4 indicates a potential loss of function or increase In tumor growth. A wide variety of assays for observing petrbatons in nucleotide and amino acid sequences are wel known in the art. For example, the size and structure of nucleic acid or amino acid sequences of 109P1D4 gene products are observed by the Northern, Southern, Western, PCR and DNA sequencing protocols discussed herein. In addition, other methods for observing perturbations in nucleotide and amino acid sequences such as single strand conformation polymorphism analysis are well known in the art (see, e.g., U.S. Patent Nos. 5,382,510 issued 7 September 1999, and 5,952,170 issued 17 January 1995). Additionaly, one can examine the methylation status of a 109P1D4 gene In a biological sample. Aberrant demethylation and/or hypermethylation of CpG islands in gene 5' regulatory regions frequently occurs in immortalized and transformed cells, and can result in altered expression of various genes. For example, promoter hypermethylation of the pi-class glutathione S-transferase (a protein expressed in normal prostate but not expressed in >90% of prostate carcinomas) appears to permanently silence transcription of this gene and is the most frequently detected genomic alteration in prostate carcinomas (De Marzo et al., Am. J. Pathol. 155(6): 1985-1992 (1999)). In addition, this alteration is present in at least 70% of cases of high-grade prostatic intraepithelial neoplasla (PIN) (Brooks et al., Cancer Epidemlol. Biomarkers Prev., 1998, 7:531-536). In another example, expression of the LAGE-l tumor specific gene (which is not expressed in normal prostate but Is expressed in 25-50% of prostate cancers) is Induced by deoxy-azacytidine in lymphoblastoid cells, suggesting that tumoral expression Is due to demethylation (Lethe et al., Int. J. Cancer 76(6): 903-908 (1998)). A variety of assays for examining methylation status of a gene are well known in the art. For example, one can utilize, in Southern hybridization approaches, methylation-sensiive restriction enzymes that cannot cleave sequences that contain methylated CpG sites to assess the methylation status of CpG Islands. In addition, MSP (methylation specific PCR) can rapidly profile the methylation status of all the CpG sites present In a CpG Island of a given gene. This procedure Involves Initial modification of DNA by sodium bisulfite (which will convert all unmelhylated cytosines to uracil) followed by amplification using primers specific for methylated versus unmethylated DNA. Protocols involving methylation interference can also be found for example in Current Protocols In Molecular Biology, Unit 12, Frederick M. Ausubel et al. eds., 1995. Gene amplification is an additional method for assessing the status of 109P1D4. Gene amplification Is measured In a sample directly, for example, by conventional Southern blotting or Northern blotting to quantitate the transcription of mRNA (Thomas, 1980, Proc. Nad. Acad. Sci. USA, 77:5201-5205), dot blotting (DNA analysis), or In situ hybridization, using an appropriately labeled probe, based on the sequences provided herein. Alternatively, antibodies are employed that recognize specific duplexes, including DNA duplexes, RNA duplexes, and DNA-RNA hybrid duplexes or DNA-protein 46 duplexes. The antibodies in turn are labeled and the assay carried out where the duplex is bound to a surface, so that upon the formation of duplex on the surface, the presence of antibody bound to the duplex can be detected. Biopsied tissue or peripheral blood can be conveniently assayed for the presence of cancer cells using for example, Northern, dot blot or RT-PCR analysis to detect 109P1 D4 expression. The presence of RT-PCR amplifiable 109P1D4 mRNA provides an Indication of the presence of cancer. RT-PCR assays are well known in the art RT-PCR detection assays for tumor cells In peripheral blood are currently being evaluated for use in the diagnosis and management of a number of human solid tumors. In the prostate cancer field, these include RT-PCR assays for the detection of cells expressing PSA and PSM (Verkalk et al., 1997, Urol. Res. 25:373-384; Ghossein et al., 1995, J. Clin. Oncol. 13:1195-2000; Heston etal., 1995, Cin. Chem. 41:1687 1688). A further aspect of the invention is an assessment of the susceptibility that an individual has for developing cancer. In one embodiment, a method for predicting susceptibility to cancer comprises detecting 109P1 D4 mRNA or 1091P1D4 protein in a tissue sample, its presence indicating susceptibility to cancer, wherein the degree of 109P1D4 mRNA expression correlates to the degree of susceptibility. In a specific embodiment, the presence of 109P1 D4 In prostate or other tissue is examined, with the presence of 109P1 D4 in the sample providing an indication of prostate cancer susceptibility (or the emergence or existence of a prostate tumor). Similarly, one can evaluate the integrity 109P1D4 nucleotide and amino acid sequences in a biological sample, In order to identify perturbations in the structure of these molecules such as Insertions, deletions, substitutions and the like. The presence of one or more perturbations In 109P1 D4 gene products In the sample Is an indication of cancer susceptibility (or the emergence or existence of a tumor). The invention also comprises methods for gauging tumor aggressiveness. In one embodiment, a method for gauging aggressiveness of a tumor comprises determining the level of 109P1 D4 mRNA or 109P1D4 protein expressed by tumor cells, comparing the level so determined to the level of 109P1D4 mRNA or 109P1D4 protein expressed in a corresponding normal tissue taken from the same individual or a normal tissue reference sample, wherein the degree of 109P1D4 mRNA or 109P1D4 protein expression in the tumor sample relative to the normal sample Indicates the degree of aggressiveness. In a specific embodiment, aggressiveness of a tumor Is evaluated by determining the extent to which 109P1 D4 is expressed in the tumor cells, with higher expression levels indicating more aggressive tumors. Another embodiment Is the evaluation of the integrity of 109P1D4 nucleotide and amino acid sequences In a biological sample, in order to identify perturbations In the structure of these molecules such as insertions, deletions, substitutions and the like. The presence of one or more perturbations indicates more aggressive tumors. Another embodiment of the Invention is directed to methods for observing the progression of a malignancy in an Individual over time. In one embodiment, methods for observing the progression of a malignancy In an Individual over time comprise determining the level of 109P1D4 mRNA or I 09P1D4 protein expressed by cells in a sample of the tumor, comparing the level so determined to the level of 109P1D4 mRNA or 109P1D4 protein expressed in an equivalent tissue sample taken from the same individual at a different time, wherein the degree of 109P1D4 mRNA or 109P1D4 protein expression In the tumor sample over time provides information on the progression of the cancer. In a specific embodiment, the progression of a cancer is evaluated by determining 109P1 D4 expression in the tumor cels over time, where increased expression over lime Indicates a progression of the cancer. Also, one can evaluate the integrity 109P1D4 nucleotide and amino acid sequences in a biological sample in order to identfy perturbations in the structure of these molecules such as insertions, deletions, substitutions and the like, where the presence of one or more perturbations Indicates a progression of the cancer. The above diagnostic approaches can be combined with any one of a wide variety of prognostic and diagnostic protocols known In the art For example, another embodiment of the invention Is directed to methods for observing a coincidence between the expression of 109PI D4 gene and 109P1 D4 gene products (or perturbations In 109P1D4 gene and 109P1 D4 gene 47 products) and a factor that is associated with malignancy, as a means for diagnosing and prognosticating the status of a tissue sample. A wide variety of factors associated with malignancy can be utilized, such as the expression of genes associated with malignancy (e.g. PSA, PSCA and PSM expression for prostate cancer etc.) as well as gross cytological observations (see, e.g., Bocking et at., 1984, Anal. Quant Cytol. 6(2):74-88; Epstein, 1995, Hum. Pathol. 26(2):223-9; Thorson et al., 1998, Mod. Pathol. 11(6):543-51; Balsden etal., 1999, Am. J. Surg. Pathol. 23(8):918-24). Methods for observing a coincidence between the expression of 109P1D4 gene and 109P1D4 gene products (orperturbations in 109P1D4 gene and 109P1D4 gene products) and another factor that is associated with malignancy are useful, for example, because the presence of a set of specific factors that coincide with disease provides information crucial for diagnosing and prognosticating the status of a tissue sample. In one embodiment, methods for observing a coincidence between the expression of 109P1D4 gene and 109P1 D4 gene products (or perturbations in 109P1 D4 gene and 109P1 D4 gene products) and another factor associated with malignancy entails detecting the overexpression of 109P1D4 mRNA or protein in a tissue sample, detecting the overexpression of PSA mRNA or protein In a tissue sample (or PSCA or PSM expression), and observing a coincidence of 109P1D4 mRNA or protein and PSA mRNA or protein overexpression (or PSCA or PSM expression). In a specific embodiment, the expression of 109P1 D4 and PSA mRNA In prostate tissue Is examined, where the coincidence of 109P1D4 and PSA mRNA overexpression in the sample Indicates the existence of prostate cancer, prostate cancer susceptibility or the emergence or status of a prostate tumor. Methods for detecting and quantifying the expression of 109P1D4 mRNA or protein are described herein, and standard nucleic acid and protein detection and quantification technologies are well known in the art Standard methods for the detection and quantification of 109P1D4 mRNA include i situ hybridization using labeled 109P1D4 riboprobes, Northern blot and related techniques using 109P1 D4 potynucleotide probes, RT-PCR analysis using primers specific for 109P1 D4, and other amplification type detection methods, such as, for example, branched DNA, SISBA, TMA and the like. In a specific embodiment, semi quantitative RT-PCR Is used to detect and quantify 109P1 D4 mRNA expression. Any number of primers capable of amplifying 109P1 D4 can be used for this purpose, including but not limited to the various primer sets specifically described herein. In a specific embodiment, polyclonal or monoclonal antibodies specifically reactive with the wil-type 1 09P1 D4 protein can be used in an immunohistochemical assay of blopsied tissue. IX) Identification of Molecules That Interact With 109P1 D4 The 109P1 D4 protein and nucleic add sequences disclosed herein allow a skilled artisan to Identify proteins, small molecules and other agents that interact with 109P1 D4, as well as pathways activated by 109P1 D4 via any one of a variety of art accepted protocols. For example, one can utilize one of the so-called interaction trap systems (also referred to as the "two-hybrid assay). In such systems, molecules interact and reconstitute a transcription factor which directs expression of a reporter gene, whereupon the expression of the reporter gene Is assayed. Other systems Identify protein-protein Interactions in vi through reconstitution of a eukaryotic transcriptional activator, see, e.g., U.S. Patent Nos. 5,955,280 Issued 21 September 1999, 5,925,523 Issued 20 July 1999, 5,846,722 issued 8 December 1998 and 6,004,746 Issued 21 December 1999. Algorithms are also available In the art for genome-based predictions of protein function (see, e.g., Marcotte, et al., Nature 402:4 November 1999,83-86). Alternatively one can screen peptide libraries to identify molecules that Interact with 109P1 D4 protein sequences. In such methods, peptides that bind to 109P1 D4 are Identified by screening libraries that encode a random or controlled collection of amino acids. Peptides encoded by the libraries are expressed as fusion proteins of bacteriophage coat proteins, the bacteriophage particles are then screened against the 109P1 D4 proteIn(s). Accordingly, peptides having a wide variety of uses, such as therapeutic, prognostic or diagnostic reagents, are thus identified without any prior Information on the structure of the expected ligand or receptor molecule. Typical peptide 48 libraries and screening methods that can be used to identify molecules that interact with 109P1D4 protein sequences are disclosed for example in U.S. Patent Nos. 5,723,286 issued 3 March 1998 and 5,733,731 issued 31 March 1998. Alternatively, cell lines that express 109P1 D4 are used to identify protein-protein interactions mediated by 109P1D4. Such Interactions can be examined using immunoprecipitation techniques (see, e.g., Hamilton B.J., et al. Blochem. Biophys. Res. Commun. 1999, 261:646-51). 109P1D4 protein can be Immunoprecipitated from 109P1D4 expressing cell lines using anti-i 09P1 D4 antibodies. Alternatively, antibodies against His-tag can be used in a cell line engineered to express fusions of 109P1 D4 and a His-tag (vectors mentioned above). The immunoprecipitated complex can be examined for protein association by procedures such as Western blotting, 3 5 S-methionine labeling of proteins, protein microsequencing, silver staining and two-dimensional gel electrophoresis. Small molecules and ligands that interact with 109P1 D4 can be identified through related embodiments of such screening assays. For example, small molecules can be identified that interfere with protein function, including molecules that interfere with 109P1D4's ability to mediate phosphorylation and de-phosphorylation, interaction with DNA or RNA molecules as an indication of regulation of cell cycles, second messenger signaling or tumorigenesis. Similarly, small molecules that modulate 109P1 D4-related ion channel, protein pump, or cell communication functions are identified and used to treat patients that have a cancer that expresses 1 09P1 D4 (see, e.g., Hille, B., Ionic Channels of Excitable Membranes 2nd Ed., Sinauer Assoc., Sunderland, MA, 1992). Moreover, ligands that regulate 109P1D4 function can be identified based on their ability to bind 109P1 D4 and activate a reporter construc. Typical methods are discussed for example in U.S. Patent No. 5,928,868 issued 27 July 1999, and include methods for forming hybrid ligands in which at least one ligand is a small molecule. In an illustrative embodiment cells engineered to express a fusion protein of 109P1D4 and a DNA-binding protein are used to co-express a fusion protein of a hybrid ligand/small molecule and a cDNA library transcriptional activator protein. The cells further contain a reporter gene, the expression of which is conditioned on the proximity of the first and second fusion proteins to each other, an event that occurs only if the hybrid ligand binds to target sites on both hybrid proteins. Those cells that express the reporter gene are selected and the unknown small molecule or the unknown ligand is identified. This method provides a means of identifying modulators, which activate or Inhibit 109P1 D4. An embodiment of this invention comprises a method of screening for a molecule that interacts with a 109P1 D4 amino acid sequence shown in Figure 2 or Figure 3, comprising the steps of contacting a population of molecules with a I 09P1 D4 amino acid sequence, allowing the population of molecules and the 109P1 D4 amino acid sequence to interact under conditions that facilitate an interaction, determining the presence of a molecule that interacts with the 109P1D4 amino acid sequence, and then separating molecules that do not Interact with the 109P1D4 amino acid sequence from molecules that do. In a specific embodiment, the method further comprises purifying, characterizing and identifying a molecule that interacts with the 109P1D4 amino acid sequence. The identified molecule can be used to modulate a function performed by 109P1D4. In a preferred embodiment, the 109P1D4 amino acid sequence is contacted with a library of peptides. .) Therapeutic Methods and Compositions The Identification of 109P1 D4 as a protein that is normally expressed In a restricted set of tissues, but which is also expressed In cancers such as those listed in Table I, opens a number of therapeutic approaches to the treatment of such cancers. Of note, targeted antitumor therapies have been useful even when the targeted protein Is expressed on normal tissues, even vital normal organ tissues. A vital organ is one that is necessary to sustain life, such as the heart or colon. A non-vital organ Is one that can be removed whereupon the individual is still able to survive. Examples of non-vital organs are ovary, breast, and prostate.

49 For example, Herceptin@ is an FDA approved pharmaceutical that has as its active ingredient an anybody which is Immunoreactive with the protein variously known as HER2, HER2/neu, and erb-b-2. It is marketed by Genentech and has been a commercially successful antitumor agent. Herceptin sales reached almost $400 million In 2002. Herceptin is a treatment for HER2 positive metastatic breast cancer. However, the expression of HER2 is not limited to such tumors. The same protein is expressed In a number of normal tissues. In particular, it Is known that HER2/neu Is present In normal kidney and heart, thus these tissues are present in all human recipients of Herceptin. The presence of HER2/neu in normal kidney is also confirmed by Latif, Z., et al., B.J.U. International (2002) 89:5-9. As shown In this article (which evaluated whether renal cell carcinoma should be a preferred indication for anti-HER2 antibodies such as Herceptin) both protein and mRNA are produced in benign renal tissues. Notably, HER2/neu protein was strongly overexpressed in benign renal tissue. Despite the fact that HER2/neu is expressed in such vital tissues as heart and kidney, Herceptin Is a very useful, FDA approved, and commercially successful drug. The effect of Herceptin on cardiac tissue, i.e., 'cardiotoxicity," has merely been a side effect to treatment When patients were treated with Herceptin alone, significant cardiotoxicity occurred in a very low percentage of patients. Of particular note, although kidney tissue is indicated to exhibit normal expression, possibly even higher expression than cardiac tissue, kidney has no appreciable Herceptin side effect whatsoever. Moreover, of the diverse array of normal tissues in which HER2 Is expressed, there is very little occurrence of any side effect. Only cardiac tissue has manifested any appreciable side effect at all. A tissue such as kidney, where HER2/neu expression is especially notable, has not been the basis for any side effect Furthermore, favorable therapeutic effects have been found for antitumor therapies that target epidermal growth factor receptor (EGFR). EGFR is also expressed in numerous normal tissues. There have been very limited side effects in normal tissues following use of anti-EGFR therapeutics. Thus, expression of a target protein in normal tissue, even vital normal tissue, does not defeat the utility of a targeting agent for the protein as a therapeutic for certain tumors in which the protein is also overexpressed. Accordingly, therapeutic approaches that inhibit the activity of a 109P1 D4 protein are useful for patients suffering from a cancer that expresses 109P1D4. These therapeutic approaches generally fall into two classes. One ciass comprises various methods for inhibiting the binding or association of a 109P1D4 protein with its binding partner or with other proteins. Another class comprises a variety of methods for inhibiting the transcription of a 109P1D4 gene or translation of 109P1D4 mRNA. X.A.) Anti-Cancer Vaccines The invention provides cancer vaccines comprising a 109P1D4-related protein or 109P1D4-related nucleic acid. In view of the expession of 109P1 D4, cancer vaccines prevent andlor treat 109P1 D4-expressing cancers with minimal or no effects on non-target tissues. The use of a tumor antigen in a vaccine that generates humoral and/or celi-mediated immune responses as anti-cancer therapy is well known in the ait and has been employed in prostate canr using human PSMA and rodent PAP immunogens (Hodge et al., 1995, Int. J. Cancer 63:231-237; Fong et al., 1997, J. Immunol. 159:3113-3117). Such methods can be readily practiced by employing a 109P1D4-related protein, or a 109P1D4-encoding nudelc acid molecule and recombinant vectors capable of expressing and presenting the 109P1 D4 immunogen (which typically comprises a number of antibody or T cell epitopes). Skilled artisans understand that a wide variety of vaccine systems for delivery of immunoreactive epitopes are known in the art (see, e.g., Heryln et al., Ann Med 1999 Feb 31(1):66-78; Maruyarma et al., Cancer Immunol Immunother 2000 Jun 49(3):123-32) Briefly, such methods of generating an Immune response (e.g. humoral and/or cell-mediated) in a mammal, comprise the steps of exposing the mammal's immune system to an 50 immunoreactive epitope (e.g. an epitope present in a 109P1D4 protein shown in Figure 3 or analog or homolog thereof) so that the mammal generates an Immune response that is specific for that epitope (e.g. generates antibodies that specifically recognize that epitope). In a preferred method, a 109P1D4 immunogen contains a biological motif, see e.g., Tables Vill-XXI and XXI-XLIX, or a peptide of a size range from 109P1 D4 Indicated In Figure 5, Figure 6, Figure 7, Figure 8, and Figure 9. The entire 109P1 D4 protein, immunogenic regions or epitopes thereof can be combined and delivered by various means. Such vaccine compositions can include, for example, lipopeptides (e.g.,Vitiello, A. et al., J. Clin. Invest. 95:341, 1995), peptide compositions encapsulated in poly(DL-lactide-co-glycolide) ("PLG") microspheres (see, e.g., Eldridge, et al., Molec. Immunol. 28:287-294,1991: Alonso et al., Vaccine 12:299-306, 1994; Jones et a., Vaccine 13:675-681, 1995), peptide compositions contained in Immune stimulating complexes (ISCOMS) (see, e.g., Takahashi et al., Nature 344:873 875, 1990; Hu et al., Clin Exp Immunol. 113:235-243, 1998), multiple antigen peptide systems (MAPs) (see e.g., Tam, J. P., Proc. Nat. Acad. Sci. U.S.A. 85:5409-5413, 1988; Tam, J.P., J. Immunol. Methods 196:17-32,1996), peptides formulated as multivalent peptides; peptides for use in ballistic delivery systems, typically crystallized peptides, viral delivery vectors (Perkus, M. E. et aL., In: Concepts in vaccine development, Kaufmann, S. H. E., ed., p. 379, 1996; Chakrabarti, S. et al., Nature 320:535, 1986; Hu, S. L et al., Nature 320:537, 1986; Kieny, M.-P. et al., AIDS Blo/Technology 4:790, 1986; Top, F. H. et al., J. Infect. Dis. 124:148, 1971; Chanda, P. K et al., Virology 175:535, 1990), particles of viral or synthetic origin (e.g., Kofler, N. et al., J. Immunol. Methods. 192:25, 1996; Eldridge, J. H. et al., Sem. Hematol. 30:16, 1993; Falo, L. D., Jr. et al., Nature Med. 7:649, 1995), adjuvants (Warren, H. S., Vogel, F. R., and Chedid, L A. Annu. Rev. Immunol. 4:369,1986; Gupta, R. K et al., Vaccine 11:293,1993), liposomes (Reddy, R. et al., J. Immunol. 148:1585, 1992; Rock, K L., Immunol. Today 17:131, 1996), or, naked or particle absorbed cDNA (Ulmer, J. B. et al., Science 259:1745, 1993; Robinson, H. L., Hunt, L A., and Webster, R. G., Vaccine 11:957, 1993; Shiver, J. W. et al., In: Concepts in vaccine development, Kaufmann, S. H. E., ed., p. 423, 1996; Cease, K. B., and Berzofsky, J. A., Annu. Rev. Immunol. 12:923, 1994 and Eldridge, J. H. et al., Sem. Hematol. 30:16, 1993). Toxin-targeted delivery technologies, also known as receptor mediated targeting, such as those of Avant Immunotherapeutics, Inc. (Needham, Massachusetts) may also be used. In patients with 109P1 D4-associated cancer, the vaccine compositions of the Invention can also be used in conjunction with other treatments used for cancer, e.g., surgery, chemotherapy, drug therapies, radiation therapies, etc. including use In combination with immune adjuvants such as IL-2, IL-1 2, GM-CSF, and the like. Cellular Vaccines: CTL epitopes can be determined using specific algoithms to identify peptides within 109P1D4 protein that bind corresponding HLA alleles (see e.g., Table IV; Epimer tm and Epimari"', Brown University (URL brown.edu/Research/TB HIVLableptmatrixleplmatrix.html); and, BIMAS, (URL bimas.dcrtnih.govl; SYFPEITHI at URL syfpeithi.bml-heldelberg.comn). In a preferred embodiment, a 109P1D4 Immunogen contains one or more amino acid sequences identified using techniques well known in the art, such as the sequences shown In Tables VII-XXI and XXII-XLIX or a peptide of 8, 9, 10 or 11 amino acids specified by an HLA Class I motif/supermotif (e.g., Table IV (A), Table IV (D), or Table IV (E)) and/or a peptide of at least 9 amino acids that comprises an HLA Class Il motif/supermotif (e.g., Table IV (B) or Table IV (C)). As is appreciated in the art, the HLA Class I binding groove is essentially closed ended so that peptides of only a particular size range can fit Into the groove and be bound, generally HLA Class I epitopes are 8, 9, 10, or 11 amino acids long. In contrast, the HLA Class 11 binding groove is essentially open endsd; therefore a peptide of about 9 or more amino acids can be bound by an HLA Class I molecule. Due to the binding groove differences between HLA Class I and II, HLA Class I motifs are length specific, i.e., position two of a Class I motif is the second amino acid in an amino to carboxyl direction of the peptide. The amino acid positions in a Class 11 motif are relative only to each other, not the overall peptide, i.e., additional amino acids can be attached to the amino and/or carboxyl termini of a motif-bearing sequence. HLA Class Il epitopes are often 9,10, 11,12,13, 51 14,15, 16, 17, 18, 19, 20, 21, 22, 23, 24, or 25 amino acids long, or longer than 25 amino acids. Antibody-based Vaccines A wide variety of methods for generating an immune response in a mammal are known in the art (for example as the first step in the generation of hybridomas). Methods of generating an immune response In a mammal comprise exposing the mammal's immune system to an immunogenic epitope on a protein (e.g. a 109P1D4 protein) so that an immune response is generated. A typical embodiment consists of a method for generating an immune response to 109P1 D4 in a host, by contacting the host with a sufficient amount of at least one 109P1 D4 B cell or cytotoxic T-cell epitope or analog thereof; and at least one periodic interval thereafter re-contacting the host with the 109P1D4 B cell or cytotoxic T-cell epitope or analog thereof. A specific embodiment consists of a method of generating an immune response against a 109P1D4 related protein or a man-made multiepitopic peptide comprising: administering 1 09P1 D4 Immunogen (e.g. a 109P1 D4 protein or a peptide fragment thereof, a 109P1D4 fusion protein or analog etc.) in a vaccine preparation to a human or another mammal. Typically, such vaccine preparations further contain a suitable adjuvant (see, e.g., U.S. Patent No. 6,146,635) or a universal helper epitope such as a PADRETmpeptide (Epimmune Inc., San Diego, CA; see, e.g., Alexander et a., J. Immunol. 2000 164(3); 164(3): 1625-1633; Alexander et al., Immunity 1994 1(9): 751-761 and Alexander et al., Immunol. Res. 1998 18(2): 79-92). An alternative method comprises generating an Immune response In an individual against a 109P1D4 immunogen by: administering in vivo to muscle or skin of the Individual's body a DNA molecule that comprises a DNA sequence that encodes a 109P1 D4 Immunogen, the DNA sequence operatively linked to regulatory sequences which control the expression of the DNA sequence; wherein the DNA molecule is taken up by cells, the DNA sequence is expressed in the cells and an immune response Is generated against the immunogen (see, e.g., U.S. Patent No. 5,962,428). Optionally a genetic vaccine facilitator such as anionic lipids; saponins; lectins; estrogenic compounds; hydroxylated lower alkyls; dimethyl sulfoxide; and urea is also administered. In addition, an antiidlotypic antibody can be administered that mimics 109P1D4, in order to generate a response to the target antigen. Nucleic Acid Vaccines: Vaccine compositions of the invention include nucleic acid-mediated modalities. DNA or RNA that encode protein(s) of the invention can be administered to a patient. Genetic Immunization methods can be employed to generate prophylactic or therapeutic humoral and cellular Immune responses directed against cancer cells expressing 109P1 D4. Constructs comprising DNA encoding a 109P1 D4-related proteinfimmunogen and appropriate regulatory sequences can be Injected directly into muscle or skin of an individual, such that the cells of the muscle or skin take-up the construct and express the encoded 109P1D4 protein/Immunogen. Alternatively, a vaccine comprises a 109P1D4-related protein. Expression of the 109P1 D4-related protein immunogen results In the generation of prophylactic or therapeutic humoral and cellular immunity against cells that bear a 109P1D4 protein. Various prophylactic and therapeutic genetic immunization techniques known In the art can be used (for review, see information and references published at Intemet address genweb.com). Nucleic acId-based delivery is described, for instance, in Wolff et. al., Science 247:1465 (1990) as well as U.S. Patent Nos. 5,580,859; 5,589,466; 5,804,566; 5,739,118; 5,736,524; 5,679,647; WO 98104720. Examples of DNA based delivery technologies include 'naked DNA', facilitated (bupivicaine, polymers, peptide-mediated) delivery, cationic lipid complexes, and particle-mediated ("gene gun") or pressure-mediated delivery (see, e.g., U.S. Patent No. 5,922,687). For therapeutic or prophylactic Immunization purposes, proteins of the invention can be expressed via viral or bacterial vectors. Various viral gene delivery systems that can be used in the practice of the Invention Include, but are not limited to, vaccinia, fowlpox, canarypox, adenovirus, influenza, poliovirus, adeno-associated virus, lentivirus, and sindbis virus (see, e.g., Restifo, 1996, Curr. Opin. ImmunoL 8:658-663; Tsang et al. J. NaO. Cancer Inst 87:982-990 (1995)). Non-viral delivery systems can also be employed by intoducing naked DNA encoding a 109P1 D4-related protein Into the patient (e.g., intramuscularly or 52 intradermally) to induce an anti-tumor response. Vaccinia virus is used, for example, as a vector to express nucleotide sequences that encode the peptides of the invention. Upon introduction into a host, the recombinant vaccinia virus expresses the protein Immunogenic peptide, and thereby elicits a host immune response. Vacdnia vectors and methods useful in immunization protocols are described in, e.g., U.S. Patent No. 4,722,848. Another vector Is BCG (Bacille Calmette Guerin). BCG vectors are described in Stover et aL., Nature 351:456-460 (1991). A wide variety of other vectors useful for therapeutic administration or immunization of the peptides of the Invention, e.g. adeno and adeno-associated virus vectors, retroviral vectors, Salmonella typhi vectors, detoxified anthrax toxin vectors, and the like, will be apparent to those skilled in the art from the description herein. Thus, gene delivery systems are used to deliver a 109P1D4-related nucleic acid molecule. In one embodiment the full length human 109P1D4 cDNA is employed. In another embodiment, 109P1D4 nucleic acid molecules encoding specific cytotoxic T lymphocyte (CTL) andlor antibody epitopes are employed. Ex Vivo Vaccines Various ex wvo strategies can also be employed to generate an Immune response. One approach involves the use of antigen presenting cells (APCs) such as dendritic cells (DC) to present 109P1D4 antigen to a patient's Immune system. Dendriic cells express MHC class I and I molecules, B7 co-stimulator, and IL-1Z and are thus highly specialized antigen presenting cells. In prostate cancer, autologous dendritic cells pulsed with peptides of the prostate-specific membrane antigen (PSMA) are being used in a Phase I dinical trial to stimulate prostate cancer patients' immune systems (TJoa et al., 1996, Prostate 28:65 69; Murphy et al., 1996, Prostate 29:371-380). Thus, dendritic cells can be used to present 109P1 D4 peptides to T cells in the context of MHC class I or It molecules. In one embodiment autologous dendritic cells are pulsed with 109P1D4 peptides capable of binding to MHC class I and/or dass I molecules. In another embodiment dendritic cells are pulsed with the complete 109P1D4 protein. Yet another embodiment involves engineering the overexpression of a 109P1D4 gene in dendritic cells using various Implementing vectors known in the art, such as adenovirus (Arthur et al., 1997, Cancer Gene Ther. 4:17-25), retrovirus (Henderson et al., 1996, Cancer Res. 56:3763-3770), lentivirus, adeno-associated virus, DNA transfection (Ribas et al., 1997, Cancer Res. 57:2865-2869), or tumor-derived RNA transfection (Ashley et al., 1997, J. Exp. Med. 186:1177-1182). Cells that express 109P1D4 can also be engineered to express immune modulators, such as GM CSF, and used as immunizing agents. X.B.) I 09P1 D4 as a Target for Antibody-based Therapy 109P1 D4 Is an attractive target for antibody-based therapeutic strategies. A number of antibody strategies are known In the art for targeting both extracellular and intracellular molecules (see, e.g., complement and ADCC mediated killing as well as the use of intrabodies). Because 109P1D4 is expressed by cancer cells of various lineages relative to corresponding normal cells, systemic administration of 109P1 04-immunoreactive compositions are prepared that exhibit excellent sensitivity without toxic, non-specific and/or non-target effects caused by binding of the Immunoreactive composition to non-target organs and tissues. Antibodies specifically reactive with domains of 109P1 D4 are useful to treat 109P1D4-expressing cancers systemically, either as conjugates with a toxin or therapeutic agent, or as naked antibodies capable of inhibiting cell proliferation or function. 109P1 D4 antibodies can be introduced into a patient sucl that the antibody binds to 109P1 D4 and modulates a function, such as an Interaction with a binding partner, and consequently mediates destruction of the tumor cells and/or inhibits the growth of the tumor cells. Mechanisms by which such antibodies exert a therapeutic effect can include complement-mediated cytolysis, antibody-dependent cellular cytotoxicity, modulation of the physiological function of 109P1D4, Inhibition of ligand binding or signal transduction pathways, modulation of tumor cell differentiation, alteration of tumor angiogenesis factor profiles, and/or apoptosis. Those skilled in the art understand that antibodies can be used to specifically target and bind immunogenic molecules such as an immunogenic region of a 109P1D4 sequence shown in Figure 2 or Figure 3. In addition, skilled artisans understand that It is routine to conjugate antibodies to cytotoxic agents (see, e.g., Slevers et al. Blood 93:11 3678 3684 (June 1, 1999)). When cytotoxic and/or therapeutic agents are delivered directly to cells, such as by conjugating them to antibodies specific for a molecule expressed by that cell (e.g. 109P1 D4), the cytotoxic agent will exert its known biological effect (i.e. cytotoxicity) on those cells. A wide variety of compositions and methods for using antibody-cytotoxic agent conjugates to kill cells are known in the art. In the context of cancers, typical methods entail administering to an animal having a tumor a biologically effective amount of a conjugate comprising a selected cytotoxic and/or therapeutic agent linked to a targeting agent (e.g. an anti 109P1 D4 antibody) that binds to a marker (e.g. 109P1 D4) expressed, accessible to binding or localized on the cell surfaces. A typical embodiment is a method of delivering a cytotoxic and/or therapeutic agent to a cell expressing 109P1D4, comprising conjugating the cytotoxic agent to an antibody that immunospecifically binds to a 109P1 D4 epitope, and, exposing the cell to the antibody-agent conjugate. Another illustrative embodiment is a method of treating an individual suspected of suffering from metastasized cancer, comprising a step of administering parenterally to said individual a pharmaceutical composition comprising a therapeutically effective amount of an antibody conjugated to a cytotoxic and/or therapeutic agent Cancer immunotherapy using anti-109P1D4 antibodies can be done in accordance with various approaches that have been successfully employed in the treatment of other types of cancer, including but not limited to colon cancer (Arlen et at., 1998, Crit Rev. Immunol. 18:133-138), multiple myeloma (Ozaki et at., 1997, Blood 90:3179-3186, Tsunenari et al, 1997, Blood 90:2437-2444), gastric cancer (Kasprzyk et al., 1992, Cancer Res. 52:2771-2776), B-cell lymphoma (Funakoshi etal., 1996, J. Immunother. Emphasis Tumor Immunol. 19:93-101), leukemia (Zhong et al., 1996, Leuk. Res. 20:581-589), colorectal cancer (Moun et al., 1994, Cancer Res. 54:6160-6166; Velders et al., 1995, Cancer Res. 55:4398-4403), and breast cancer (Shepard of al., 1991, J. Clin. Immunol. 11:117-127). Some therapeutic approaches involve conjugation of naked antibody to a toxin or radioisotope, such as the conjugation of Y91 or 1131 to anti-CD20 antibodies (e.g., Zevalinm, IDEC Pharmaceuticals Corp. or Bexxarm, Coulter Pharmaceuticals), while others involve co-administration of antibodies and other therapeutic agents, such as Herceptina" (trastuzumab) with paclitaxel (Genentech, Inc.). The antibodies can be conjugated to a therapeutic agent To treat prostate cancer, for example, 109P1D4 antibodies can be administered in conjunction with radiation, chemotherapy or hormone ablation. Also, antibodies can be conjugated to a toxin such as calicheamicin (e.g., Mylotarga', Wyeth-Ayerst, Madison, NJ, a recombinant humanized lgG4 kappa antibody conjugated to antitumor antibiotic calicheamicin) or a maytansinold (e.g., taxane-based Tumor-Activated Prodrug, TAP, platform, ImmunoGen, Cambridge, MA, also see e.g., US Patent 5,416,064). Although 109P1 D4 antibody therapy Is useful for all stages of cancer, antibody therapy can be particularly appropriate in advanced or metastatic cancers. Treatment with the antibody therapy of the Invention Is Indicated for patients who have received one or more rounds of chemotherapy. Alternatively, antibody therapy of the invention is combined with a chemotherapeutic or radiation regimen for patients who have not received chemotherapeutic treatment. Additionally, antibody therapy can enable the use of reduced dosages of concomitant chemotherapy, particularly for patients who do not tolerate the toxicity of the chemotherapeutic agent very well. Fan et al. (Cancer Res. 53:4637-4642, 1993), Prewett et al. (Intemational J. of Onco. 9:217-224, 1996), and Hancock at al. (Cancer Res. 51:4575-4580,1991) describe the use of various antibodies together with chemotherapeutic agents. Although 109P1 D4 antibody therapy is useful for all stages of cancer, antibody therapy can be particularly appropriate in advanced or metastatic cancers. Treatment with the antibody therapy of the invention is indicated for patients who have received one or more rounds of chemotherapy. Alternatively, antibody therapy of the invention is combined with a chemotherapeutic or radiation regimen for patients who have not received chemotherapeutic treatment Additionally, antibody therapy can enable the use of reduced dosages of concomitant chemotherapy, particularly for patients who do not tolerate the toxicity of the chemotherapeutic agent very well. Cancer patients can be evaluated for the presence and level of 109P1D4 expression, preferably using immunohistochemical assessments of tumor tissue, quantitative 109P1 D4 imaging, or other techniques that reliably indicate the presence and degree of 109P1D4 expression. Immunohistochemical analysis of tumor biopsies or surgical specimens is preferred for this purpose. Methods for immunohistochemical analysis of tumor tissues are well known in the art. Ant- 09P1 D4 monoclonal antibodies that treat prostate and other cancers include those that Initiate a potent immune response against the tumor or those that are directly cytotoxic. In this regard, anti-109P1D4 monoclonal antibodies (mAbs) can elicit tumor cell lysis by either complement-mediated or antibody-dependent ceO cytotoxicity (ADCC) mechanisms, both of which require an intact Fc portion of the immunoglobufln molecule for interaction with effector cell Fc receptor sites on complement proteins. In addition, anti-109P1D4 mAbs that exert a direct biological effect on tumor growth are useful to treat cancers that express 109P1 D4. Mechanisms by which directly cytotoxic mAbs act include: inhibition of cell growth, modulation of cellular differentiation, modulation of tumor angiogenesis factor profiles, and the induction of apoptosis. The mechanism(s) by which a particular anti-109P1D4 mAb exerts an anti-tumor effect is evaluated using any number of in vitr assays that evaluate cell death such as ADCC, ADMMC, complement-mediated cell lysis, and so forth, as is generally known in the art In some patients, the use of murine or other non-human monoclonal antibodies, or human/mouse chimeric mAbs can induce moderate to strong Immune responses against the non-human antibody. This can result In clearance of the antibody from circulation and reduced efficacy. In the most severe cases, such an immune response can lead to the extensive formation of immune complexes which, potentially, can cause renal failure. Accordingly, preferred monoclonal antibodies used in the therapeutic methods of the invention are those that are either fully human or humanized and that bind specifically to the target 109P1 D4 antigen with high affinity but exhibit low or no antigenicity In the patient Therapeutic methods of the invention contemplate the administration of single anti-I 09P1 D4 mAbs as well as combinations, or cocktails, of different mAbs. Such mAb cocktails can have certain advantages inasmuch as they contain mAbs that target different epitopes, exploit different effector mechanisms or combine directly cytotoxic mAbs with mAbs that rely on immune effector functionality. Such mAbs in combination can exhibit synergistic therapeutic effects. In addition, anti 109P1D4 mAbs can be administered concomitantly with other therapeutic modalities, including but not limited to various chemotherapeutic agents, androgen-blockers, Immune modulators (e.g., IL-2, GM-CSF), surgery or radiation. The anti 109P1D4 mAbs are administered in their *naked'or unconjugated form, or can have a therapeutic agent(s) conjugated to them. Anti- 09P1 D4 antibody formulations are administered via any route capable of delivering the antibodies to a tumor cell. Routes of administration include, but are not limited to, intravenous, intraperitoneal, intramuscular, intratumor, Intradermal, and the like. Treatment generally involves repeated administration of the anti-109P1D4 antibody preparation, via an acceptable route of administration such as intravenous injection (IV), typically at a dose in the range of about 0.1, .2, .3,.4,.5,.6,.7,.8,.9., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, or 25 mg/kg body weight In general, doses in the range of 10-1000 mg mAb per week are effective and well tolerated. Based on clinical experience with the Herceptin"' mAb In the treatment of metastatic breast cancer, an Initial loading dose of approximately 4 mg/kg patient body weight IV, followed by weekly doses of about 2 mg/kg IV of the anti- 109P1 D4 mAb preparation represents an acceptable dosing regimen. Preferably, the initial loading dose is administered as a 90-minute or longer infusion. The periodic maintenance dose is administered as a 30 minute or longer infusion, provided the initial dose was well tolerated. As appreciated by those of skill in the art, various factors can influence the ideal dose regimen in a particular case. Such factors include, for example, the binding affinity and half life of the Ab or mAbs used, (he degree of 109P1D4 expression in the patient, the extent of circulating shed 109P1D4 antigen, the desired steady-state antibody concentration level, frequency of treatment, and the influence of chemotherapeutic or other agents used in combination with the treatment method of the invention, as well as the health status of a particular patient. Optionally, patients should be evaluated for the levels of 109P1D4 in a given sample (e.g. the levels of circulating 109P1D4 antigen and/or 109P1D4 expressing cells) In order to assist In the determination of the most effective dosing regimen, etc. Such evaluations are also used for monitoring purposes throughout therapy, and are useful to gauge therapeutic success In combination with the evaluation of other parameters (for example, urine cytology and/or ImmunoCyt levels in bladder cancer therapy, or by analogy, serum PSA levels in prostate cancer therapy). Anti-Idiotypic anti- 09P1 04 antibodies can also be used in anti-cancer therapy as a vaccine for inducing an immune response to cells expressing a 109P1D4-related protein. In particular, the generation of anti-idiotypic antibodies is well known in the art; this methodology can readily be adapted to generate anti-idiotypic anti-109P1D4 antibodies that mimic an epitope on a 109P1 D4-related protein (see, for example, Wagner et al., 1997, Hybridoma 16: 33-40; Foon et a., 1995, J. Clin. Invest. 96:334-342; Herlyn et al., 1996, Cancer Immunol. Immunother. 43:65-76). Such an anti-Idiotypic antibody can be used in cancer vaccine strategies. X.C.) 109P1D4 as a Target for Cellular Immune Responses Vaccines and methods of preparing vaccines that contain an immunogenically effective amount of one or more HLA-binding peptides as described herein are further embodiments of the invention. Furthermore, vaccines in accordance with the invention encompass compositions of one or more of the claimed peptides. A peptide can be present In a vaccine individually. Alternatively, the peptide can exist as a homopolymer comprising multiple copies of the same peptide, or as a heteropolymer of various peptides. Polymers have the advantage of increased Immunological reaction and, where different peptide epitopes are used to make up the polymer, the additional ability to Induce antibodies and/or CTLs that react with different antigenic determinants of the pathogenic organism or tumor-related peptide targeted for an immune response. The composition can be a naturally occurring region of an antigen or can be prepared, e.g., recombinantly or by chemical synthesis. Carriers that can be used with vaccines of the invention are well known In the art, and include, e.g., thyroglobulin, albumins such as human serum albumin, tetanus toxoid, polyamino acids such as poly L4yslne, poly .- glutamic acid, influenza, hepatitis B virus core protein, and the like. The vaccines can contain a physiologically tolerable (i.e., acceptable) diluent such as water, or saline, preferably phosphate buffered saline. The vaccines also typically include an adjuvant Adjuvants such as incomplete Freund's adjuvant, aluminum phosphate, aluminum hydroxide, or alum are examples of materials well known in the art. Additionally, as disclosed herein, CTL responses can be primed by conjugating peptides of the invention to lipids, such as tripalmitoyl-S-glycerylcysteinlyseryl- seine (P3CSS). Moreover, an adjuvant such as a synthetic cytosine-phosphorothiolated-guaninecontaining (CpG) oligonucleotides has been found to increase CTL responses 10- to 100-fold. (see, e.g. Davila and Cells, J. Immunol. 165:539-547 (2000)) Upon immunization with a peptide composition In accordance with the Invention, via Injection, aerosol, oral, transdermal, transmucosal, intrapleural, Intrathecal, or other suitable routes, the immune system of the host responds to the vaccine by producing large amounts of CTLs and/or HTLs specific for the desired antigen. Consequently, the host becomes 576 at least partially immune to later development of cells that express or overexpress 109P1D4 antigen, or derives at least some therapeutic benefit when the antigen was tumor-associated. In some embodiments, it may be desirable to combine the class I peptide components with components that Induce or facilitate neutralizing antibody and or helper T cell responses directed to the target antigen. A preferred embodiment of such a composition comprises class I and class I epitopes in accordance with the invention. An alternative embodiment of such a composition comprises a class I and/or class Il epitope in accordance with the invention, along with a cross reactive HTL epitope such as PADRET (Epimmune, San Diego, CA) molecule (described e.g., in U.S. Patent Number 5,736,142). A vaccine of the Invention can also include antigen-presenting cells (APC), such as dendritic cells (DC), as a vehicle to present peptides of the Invention. Vaccine compositions can be created in vitro, following dendritic cell mobilization and harvesting, whereby loading of dendritic cells occurs in vitro. For example, dendritic cells are transfected, e.g., with a minigene in accordance with the invention, or are pulsed with peptides. The dendritic cell can then be administered to a patient to elicit immune responses in vivo. Vaccine compositions, either DNA- or peptide-based, can also be administered in vivo in combination with dendritic cell mobilization whereby loading of dendritic cells occurs in vivo. Preferably, the following principles are utilized when selecting an array of epitopes for inclusion in a polyepitopic composition for use In a vaccine, or for selecting discrete epitopes to be included in a vaccine and/or to be encoded by nucleic acids such as a minigene. It is preferred that each of the following principles be balanced In order to make the selection. The multiple epitopes to be incorporated In a given vaccine composition may be, but need not be, contiguous In sequence in the native antigen from which the epitopes are derived. 1.) Epitopes are selected which, upon administration, mimic Immune responses that have been observed to be correlated with tumor dearance. For HLA Class I this includes 3-4 epitopes that come from at least one tumor associated antigen (TM). For HLA Class 11 a similar rationale is employed; again 3-4 epitopes are selected from at least one TAA (see, e.g., Rosenberg et al., Science 278:1447-1450). Epitopes from one TAA may be used in combination with epitopes from one or more additional TAAs to produce a vaccine that targets tumors with varying expression patterns of frequently-expressed TAAs. 2.) Epitopes are selected that have the requisite binding affinity established to be correlated with immunogenicity: for HLA Class I an ICso of 500 nM or less, often 200 nM or less; and for Class II an ICso of 1000 nM or less. 3.) Sufficient supermotif bearing-peptides, or a sufficient array of allele-specific motif-bearing peptides, are selected to give broad population coverage. For example, it is preferable to have at least 80% population coverage. A Monte Carlo analysis, a statistical evaluation known in the art, can be employed to assess the breadth, or redundancy of, population coverage. 4.) When selecting epitopes from cancer-related antigens it is often useful to select analogs because the patient may have developed tolerance to the native epitope. 5.) Of particular relevance are epitopes referred to as 'nested epitopes." Nested epitopes occur where at least two epitopes overlap In a given peptide sequence. A nested peptide sequence can comprise B cell, HLA class I and/or HLA class I epitopes. When providing nested epitopes, a general objective is to provide the greatest number of epitopes per sequence. Thus, an aspect Is to avoid providing a peptide that is any longer than the amino terminus of the amino terminal epitope and the carboxyl terminus of the carboxyl terminal epitope in the peptide. When providing a multi-epitopic sequence, such as a sequence comprising nested epitopes, it is generally important to screen the sequence In order to Insure that It does not have pathological or other deleterious biological properties. 6.) If a polyepitopic protein is created, or when creating a minigene, an objective Is to generate the smallest peptide that encompasses the epitopes of interest. This principle is similar, if not the same as that employed when selecting a peptide comprising nested epitopes. However, with an artificial polyepitopic peptide, the size minimization objective is balanced against the need to integrate any spacer sequences between epitopes in the polyepitopic protein. Spacer amino acid residues can, for example, be introduced to avoid junctional epitopes (an epitope recognized by the immune system, not present in the target antigen, and only created by the man-made juxtaposition of epitopes), or to facilitate cleavage between epitopes and thereby enhance epitope presentation. Junctional epitopes are generally to be avoided because the recipient may generate an Immune response to that non-native epitope. Of particular concern is a junctional epitope that is a "dominant epitope." A dominant epitope may lead to such a zealous response that immune responses to other epitopes are diminished or suppressed. 7.) Where the sequences of multiple variants of the same target protein are present, potential peptide epitopes can also be selected on the basis of their conservancy. For example, a criterion for conservancy may define that the entire sequence of an HLA dass I binding peptide or the entire 9-mer core of a class I binding peptide be conserved in a designated percentage of the sequences evaluated for a specific protein antigen. XC.1. Minigene Vaccines A number of different appraches are available which allow simultaneous delivery of multiple epitopes. Nucleic acids encoding the peptides of the invention are a particularly useful embodiment of the Invention. Epitopes for inclusion in a minigene are preferably selected according to the guidelines set forth In the previous section. A preferred means of administering nucleic acids encoding the peptides of the invention uses minigene constructs encoding a peptide comprising one or multiple epitopes of the invention. The use of multi-epitope minigenes is described below and in, Ishioka et a., J. Immunol. 162:3915-3925, 1999; An, 'L. and Whitton, J. L., J. Vim/. 71:2292,1997; Thomson, S. A. et al., J. Immunol. 157:822, 1996; Whitton, J. L et a., J. Virol. 67:348, 1993; Hanke, R. et al., Vaccine 16:426, 1998. For example, a multi-epitope DNA plasmid encoding supermotif and/or motif-bearing epitopes derived 109P1D4, the PADRE® universal helper T cell epitope or multiple HTL epitopes from 109P1 D4 (see e.g., Tables VIII-XXI and XXI to XLIX), and an endoplasmic reticulum-translocating signal sequence can be engineered. A vaccine may also comprise epitopes that are derived from other TAAs. The immunogenicity of a multi-epitopic minigene can be confirmed In transgenic mice to evaluate the magnitude of CTL induction responses against the epitopes tested. Further, the immunogenicity of DNA-encoded epitopes In vivo can be correlated with the in vitro responses of specific CTL lines against target cells transfected with the DNA plasmid. Thus, these experiments can show that the minigene serves to both: 1.) generate a CTL response and 2.) that the induced CTLs recognized cells expressing the encoded epitopes. For example, to create a DNA sequence encoding the selected epitopes (minigene) for expression In human cells, the amino acid sequences of the epitopes may be reverse translated. A human codon usage table can be used to guide the codon choice for each amino acid. These epitope-encoding DNA sequences may be directly adjoined, so that when translated, a continuous polypeptide sequence is created. To optimize expression and/or Immunogenicity, additional elements can be incorporated into the minigene design. Examples of amino acid sequences that can be reverse translated and Included in the minigene sequence include: HLA class I epitopes, HLA class II epitopes, antibody epitopes, a ubiquitination signal sequence, and/or an endoplasmic reticulum targeting signal. In addition, HLA presentation of CTL and HTL epitopes may be Improved by including synthetic (e.g. poly-alanine) or naturally-occurring flanking sequences adjacent to the CTL or HTL epitopes; these larger peptides comprising the epitope(s) are within the scope of the invention. The minigene sequence may be converted to DNA by assembling oligonucleotides that encode the plus and minus strands of the minigene. Overlapping oligonucleotides (30-100 bases long) may be synthesized, phosphorylated, purified and annealed under appropriate conditions using well known techniques. The ends of the oligonucleotides can be joined, for example, using T4 DNA ligase. This synthetic minigene, encoding the epitope polypeptide, can then be cloned into a desired expression vector. Standard regulatory sequences well known to those of skill in the art are preferably Included in the vector to ensure expression in the target cells. Several vector elements are desirable: a promoter with a down-stream cloning site for minigene insertion; a polyadenylation signal for efficient transcription termination; an E. coliorigin of replication; and an E. coli selectable marker (e.g. ampicillin or kanamycin resistance). Numerous promoters can be used for this purpose, e.g., the human cytomegalovirus (hCMV) promoter. See, e.g., U.S. Patent Nos. 5,580,859 and 5,589,466 for other suitable promoter sequences. Additional vector modifications may be desired to optimize minigene expression and immunogenicity. In some cases, Introns are required for efficient gene expression, and one or more synthetic or naturally-occurring introns could be incorporated into the transcribed region of the minigene. The inclusion of mRNA stabilization sequences and sequences for replication in mammalian cells may also be considered for Increasing minigene expression. Once an expression vector is selected, the minigene is cloned into the polylinker region downstream of the promoter. This plasmid Is transformed into an appropriate E. coil strain, and DNA Is prepared using standard techniques. The orientation and DNA sequence of the minigene, as well as all other elements included in the vector, are confirmed using restriction mapping and DNA sequence analysis. Bacterial cells harboring the correct plasmid can be stored as a master cell bank and a working cell bank. In addition, immunostimulatory sequences (ISSs or CpGs) appear to play a role in the immunogenicity of DNA vaccines. These sequences may be included in the vector, outside the minigene coding sequence, if desired to enhance immunogenicity. In some embodiments, a bi-cistronic expression vector which allows production of both the minigene-encoded epitopes and a second protein (included to enhance or decrease immunogenicity) can be used. Examples of proteins or polypeptides that could beneficially enhance the immune response if co-expressed Include cytokines (e.g., IL-2, IL-1 2, GM CSF), cytokine-inducing molecules (e.g., LeIF), costimulatory molecules, or for HTL responses, pan-DR binding proteins (PADRE"m, Epimmune, San Diego, CA). Helper (HTL) epitopes can be joined to intracellular targeting signals and expressed separately from expressed CTL epitopes; this allows direction of the HTL epitopes to a cell compartment different than that of the CTL epitopes. If required, this could facilitate more efficient entry of HTL epitopes into the HLA class I pathway, thereby improving HTL induction. In contrast to HTL or CTL induction, specifically decreasing the immune response by co-expression of immunosuppressive molecules (e.g. TGF-P) may be beneficial In certain diseases. Therapeutic quantities of plasmid DNA can be produced for example, by fermentation In E coi, followed by purification. Aliquots from the working cell bank are used to inoculate growth medium, and grown to saturation in shaker flasks or a bloreactor according to well-known techniques. Plasmid DNA can be purified using standard bloseparation technologies such as solid phase anion-exchange resins supplied by QIAGEN, Inc. (Valencia, California). If required, supercoiled DNA can be isolated from the open circular and linear forms using gel electrophoresis or other methods. Purified plasmid DNA can be prepared for injection using a variety of formulations. The simplest of these Is reconstitution of lyophilized DNA In sterile phosphate-buffer saline (PBS). This approach, known as "naked DNA," is currently being used for intramuscular (IM) administration in clinical trials. To maximize the Immunotherapeutic effects of minigene DNA vaccines, an alternative method for formulating purified plasmid DNA may be desirable. A variety of methods have been described, and new techniques may become available. Cationic fipids, glycolipids, and fusogenic liposomes can also be used In the formulation (see, e.g., as described by WO 93/24640; Mannino & Gould-Fogerite, BloTechniques 6(7): 682 (1988); U.S. Pat No. 5,279,833; WO 91/06309; and Felgner, et a., Proc. Nat'l Acad. Sci. USA 84:7413 (1987). In addition, peptides and compounds referred to collectively as protective, interactive, non-condensing compounds (PINC) could also be complexed to purified plasmid DNA to Influence variables such as stability, intramuscular dispersion, or trafficking to specific organs or cell types. Target cell sensitization can be used as a functional assay for expression and HLA class I presentation of mlnigene-encoded CTL epitopes. For example, the plasmid DNA is introduced into a mammalian cell line that Is suitable as a target for standard CTL chromium release assays. The transfection method used will be dependent on the final formulation. Electroporation can be used for "naked" DNA, whereas cationic lipids allow direct in vitro transfection. A plasmid expressing green fluorescent protein (GFP) can be co-transfected to allow enrichment of transfected cells using fluorescence activated cell sorting (FACS). These cells are then chromium-51 (51Cr) labeled and used as target cells for epitope-specific CTL fines; cytolysis, detected by 6 1 Cr release, indicates both production of, and HLA presentation of, minigene-encoded CTL epitopes. Expression of HTL epitopes may be evaluated In an analogous manner using assays to assess HTL activity. In vivo immunogenicity Is a second approach for functional testing of minigene DNA formulations. Transgenic mice expressing appropriate human HLA proteins are immunized with the DNA product The dose and route of administration are formulation dependent (e.g., IM for DNA in PBS, intraperitoneal (i.p.) for lipid-complexed DNA). Twenty-one days after immunization, splenocytes are harvested and restimulated for one week in the presence of peptides encoding each epitope being tested. Thereafter, for CTL effector cells, assays are conducted for cytolysis of peptide-loaded, 5 1Cr-labeled target cells using standard techniques. Lysis of target cells that were sensitized by HLA loaded with peptide epitopes, corresponding to minigene-encoded epitopes, demonstrates DNA vaccine function for in vivo induction of CTLs. Immunogenicity of HTL epitopes is confirmed in transgenic mice in an analogous manner. Alternatively, the nuceic acids can be administered using ballistic delivery as described, for instance, in U.S. Patent No. 5,204,253. Using this technique, particles comprised solely of DNA are administered. In a further alternative embodiment, DNA can be adhered to particles, such as gold particles. Minigenes can also be delivered using other bacteria] or viral delivery systems well known In the art, e.g., an expression construct encoding epitopes of the invention can be incorporated into a viral vector such as vaccinia. X.C.2. CombInations of CTL Peptides with Helper Peptides Vaccine compositions comprising CTL peptides of the invention can be modified, e.g., analoged, to provide desired attributes, such as improved serum half life, broadened population coverage or enhanced immunogenicity. For instance, the ability of a peptide to induce CTL activity can be enhanced by linking the peptide to a sequence which contains at least one epitope that is capable of inducing a T helper cell response. Although a CTL peptide can be directly linked to a T helper peptide, often CTL epitopelHTL epitope conjugates are linked by a spacer molecule. The spacer is typically comprised of relatively small, neutral molecules, such as amino acids or amino acid mimetics, which are substantially uncharged under physiological conditions. The spacers are typically selected from, e.g., Ala, Gly, or other neutral spacers of nonpolar amino acids or neutral polar amino acids. It will be understood that the optionally present spacer need not be comprised of the same residues and thus may be a hetero- or homo-oligomer. When present, the spacer will usually be at least one or two residues, more usually three to six residues and sometimes 10 or more residues. The CTL peptide epitope can be linked to the T helper peptide epitope either directly or via a spacer either at the amino or carboxy terminus of the CTL peptide. The amino terminus of either the immunogenic peptide or the T helper peptide may be acylated. In certain embodiments, the T helper peptide is one that is recognized by T helper cells present In a majority of a 60 genetically diverse population. This can be accomplished by selecting peptides that bind to many, most, or all of the HLA class Il molecules. Examples of such amino acid bind many HLA Class I molecules include sequences from antigens such as tetanus toxoid at positions 830-843 QYIKANSKFIGITE; (SEQ ID NO: 40), Plasmodium falc/patum circumsporozoite (CS) protein at positions 378-398 DIEKKIAKMEKASSVFNWNS; (SEQ ID NO- 41), and Streptococcus 18kD protein at positions 116-131 GAVDSILGGVATYGAA; (SEQ ID NO: 42). Other examples include peptides bearing a DR 1-4-7 supermotif, or either of the DR3 motifs. Alternatively, it Is possible to prepare synthetic peptides capable of stimulating T helper lymphocytes, in a loosely HLA-restricted fashion, using amino acid sequences not found in nature (see, eg., PCT publication WO 95107707). These synthetic compounds called Pan-DR-binding epitopes (e.g., PADRETm, Epimmune, Inc., San Diego, CA) are designed, most preferably, to bind most HLA-DR (human HLA class 1l) molecules. For instance, a pan-DR-binding epitope peptide having the formula: xKXVAAWTLKAAx (SEQ ID NO: 43), where "X is either cyciohexytalanine, phenylalanine, or tyrosine, and a is either D-alanine or L-alanine, has been found to bind to most HLA-DR alleles, and to stimulate the response of T helper lymphocytes from most Individuals, regardless of their HLA type. An alternative of a pan-DR binding epitope comprises all L natural amino acids and can be provided in the form of nucleic acids that encode the epitope. HTL peptide epitopes can also be modified to alter their biological properties. For example, they can be modiled to Include D-amino acids to increase their resistance to proteases and thus extend their serum half life, or they can be conjugated to other molecules such as lipids, proteins, carbohydrates, and the like to increase their biological activity. For example, a T helper peptide can be conjugated to one or more palmitic acid chains at either the amino or carboxyl termini. XC.3. Combinations of CTL Peptides with T Cell Priming Agents In some embodiments it may be desirable to include in the pharmaceutical compositions of the invention at least one component which primes B lymphocytes or T lymphocytes. Lipids have been identified as agents capable of priming CTL in vivo. For example, palmitic acid residues can be attached to the e-and a- amino groups of a lysine residue and then linked, e.g., via one or more linking residues such as Gly, Gly-Gly-, Ser, Ser-Ser, or the like, to an immunogenic peptide. The lipidated peptide can then be administered either directly In a micelle or particle, Incorporated Into a liposome, or emulsified in an adjuvant, e.g., Incomplete Freund's adjuvant In a preferred embodiment, a particularly effective immunogenic composition comprises palmitic add attached to e- and a- amino groups of Lys, which is attached via linkage, e.g., Ser-Ser, to the amino terminus of the Immunogenic peptide. As another example of lipid priming of CTL responses, E coli lipoproteins, such as tripalmiltoyl-S glycerylcysteinlyseryl- series (PaCSS) can be used to prime virus specific CTL when covalently attached to an appropriate peptide (see, e.g., Deres, et al., Nature 342561, 1989). Peptides of the invention can be coupled to P3CSS, for example, and the lipopeptide administered to an individual to prime specifically an immune response to the target antigen. Moreover, because the Induction of neutralizing antibodies can also be primed with P3CSS-conjugated epitopes, two such compositions can be combined to more effectively elicit both humoral and cell-mediated responses. XC.4. Vaccine Compositions Comprising DC Pulsed with CTL and/or HTL Peptides An embodiment of a vaccine composItion in accordance with the invention comprises ex vivo administration of a cocktail of epitope-bearing peptides to PBMC, or Isolated DC therefrom, from the patient's blood. A pharmaceutical to facilitate harvesting of DC can be used, such as Progenlpoietin- (Pharmacia-Monsanto, St Louis, MO) or GM-CSFIIL-4. After pulsing the DC with peptides and pdor to reinfuslon Into patients, the DC are washed to remove unbound peptides. In this embodiment, a vaccine comprises peptide-pulsed DCs which present the pulsed peptide epitopes complexed with HLA molecules on their surfaces. The DC can be pulsed ex vivo with a cocktail of peptides, some of which stimulate CTL responses to 109P1 D4.

61 Optionally, a helper T cell (HTL) peptide, such as a natural or artificial loosely restricted HLA Class Il peptide, can be included to facilitate the CTL response. Thus, a vaccine in accordance with the invention is used to treat a cancer which expresses or overexpresses 109P1D4. X.D. Adoptive Immunotherapy Antigenic 109P1 D4-related peptides are used to elicit a CTL and/or HTL response ex vivo, as well. The resulting CTL or HTL cells, can be used to treat tumors in patients that do not respond to other conventional forms of therapy, or will not respond to a therapeutic vaccine peptide or nucleic acid In accordance with the invention. Ex vivo CTL or HTL responses to a particular antigen are Induced by incubating in tissue culture the patients, or genetically compatible, CTL or HTL precursor cells together with a source of antigen-presenting cells (APC), such as dendritic cells, and the appropriate immunogenic peptide. After an appropriate incubation time (typically about 7-28 days), in which the precursor cells are activated and expanded into effector cells, the cells are infused back into the patient where they will destroy (CTL) or facilitate destruction (HTL) of their specific target cell (e.g., a tumor cell). Transfected dendritic cells may also be used as antigen presenting cells. X.E. Administration of Vaccines for Therapeutic or Prophylactic Purposes Pharmaceutical and vaccine compositions of the invention are typically used to treat and/or prevent a cancer that expresses or overexpresses 109P1D4. In therapeutic applications, peptide and/or nucleic acid compositions are administered to a patient in an amount sufficient to elicit an effective B cell, CTL and/or HTL response to the antigen and to cure or at least partially arrest or slow symptoms and/or complications. An amount adequate to accomplish this is defined as "therapeutically effective dose.' Amounts effective for this use will depend on, e.g., the particular composition administered, the manner of administration, the stage and severity of the disease being treated, the weight and general state of health of the patient and the judgment of the prescribing physician. For pharmaceutical compositions, the Immunogenic peptides of the invention, or DNA encoding them, are generally administered to an Individual already bearing a tumor that expresses 109P1 D4. The peptides or DNA encoding them can be administered Individually or as fusions of one or more peptide sequences. Patients can be treated with the Immunogenic peptides separately or in conjunction with other treatments, such as surgery, as appropriate. For therapeutic use, administration should generally begin at the first diagnosis of 109P1 D4-associated cancer. This is followed by boosting doses until at least symptoms are substantially abated and for a period thereafter. The embodiment of the vaccine composition (i.e., including, but not limited to embodiments such as peptide cocktails, polyepitopic polypeptides, minigenes, or TAA-specific CTLs or pulsed dendritic cells) delivered to the patient may vary according to the stage of the disease or the patient's health status. For example, In a patient with a tumor that expresses 109P1 D4, a vaccine comprising 109P1 D4-specific CTL may be more efficacious In killing tumor cells in patient with advanced disease than alternative embodiments. It Is generally important to provide an amount of the peptide epitope delivered by a mode of administration sufficient to stimulate effectively a cytotoxic T cell response; compositions which stimulate helper T cell responses can also be given in accordance with this embodiment of the invention. The dosage for an initial therapeutic Immunization generally occurs in a unit dosage range where the lower value Is about 1, 5, 50, 500, or 1,000 pg and the higher value is about 10,000; 20,000; 30,000; or 50,000 pg. Dosage values for a human typically range from about 500 pg to about 50,000 pg per 70 kilogram patient Boosting dosages of between about 1.0 pg to about 50,000 pg of peptide pursuant to a boosting regimen over weeks to months may be administered depending 62 upon the patient's response and condition as determined by measuring the specific activity of CTL and HTL obtained from the patient's blood. Administration should continue until at least clinical symptoms or laboratory tests indicate that the neoplasia, has been eliminated or reduced and for a period thereafter. The dosages, routes of administration, and dose schedules are adjusted In accordance with methodologies known in the art In certain embodiments, the peptides and compositions of the present invention are employed in serious disease states, that is, life-threatening or potentially life threatening situations. In such cases, as a result of the minimal amounts of extraneous substances and the relative nontoxic nature of the peptides in preferred compositions of the invention, it is possible and may be felt desirable by the treating physician to administer substantial excesses of these peptide compositions relative to these stated dosage amounts. The vaccine compositions of the invention can also be used purely as prophylactic agents. Generally the dosage for an initial prophylactic immunization generally occurs in a unit dosage range where the lower value Is about 1, 5, 50, 500, or 1000 pg and the higher value Is about 10,000; 20,000; 30,000; or 50,000 pg. Dosage values for a human typically range from about 500 pg to about 50,000 pg per 70 kilogram patient This is followed by boosting dosages of between about 1.0 pg to about 50,000 sg of peptide administered at defined intervals from about four weeks to six months after the initial administration of vaccine. The immunogenicity of the vaccine can be assessed by measuring the specific activity of CTL and HTL obtained from a sample of the patient's blood. The pharmaceutical compositions for therapeutic treatment are intended for parenteral, topical, oral, nasal, intrathecal, or local (e.g. as a cream or topical ointment) administration. Preferably, the pharmaceutical compositions are administered parentally, e.g., intravenously, subcutaneously, intradermally, or intramuscularly. Thus, the invention provides compositions for parenteral administration which comprise a solution of the immunogenic peptides dissolved or suspended in an acceptable carrier, preferably an aqueous carter. A variety of aqueous carriers may be used, e.g., water, buffered water, 0.8% saline, 0.3% glycine, hyaluronic acid and the like. These compositions may be sterilized by conventional, well-known sterilization techniques, or may be sterile filtered. The resulting aqueous solutions may be packaged for use as is, or lyophilized, the tyophilized preparation being combined with a sterile solution prior to administration. The compositions may contain pharmaceutically acceptable auxiliary substances as required to approximate physiological conditions, such as pH-adjusting and buffering agents, tonicity adjusting agents, wetting agents, preservatives, and the like, for example, sodium acetate, sodium lactate, sodium chloride, potassium chloride, calcium chloride, sorbitan monolaurate, trethanolamine oleate, etc. The concentration of peptides of the invention In the pharmaceutical formulations can vary widely, i.e., from less than about 0.1%, usually at or at least about 2% to as much as 20% to 50% or more by weight, and will be selected primarily by fluid volumes, viscosities, etc., in accordance with the particular mode of administration selected. A human unit dose form of a composition is typically included in a pharmaceutical composition that comprises a human unit dose of an acceptable carrier, in one embodiment an aqueous carrier, and is administered in a volume/quantity that is known by those of skill In the art to be used for administration of such compositions to humans (see, e.g., Remington's Pharmaceutical Sciences, 17th Edition, A. Gennaro, Editor, Mack Publishing Co., Easton, Pennsylvania, 1985). For example a peptide dose for initial immunization can be from about 1 to about 50,000 pg, generally 100-5,000 pg, for a 70 kg patient For example, for nucleic acids an initial Immunization may be performed using an expression vector in the form of naked nucleic acid administered IM (or SC or ID) In the amounts of 0.5-5 mg at multiple sites. The nuceic acid (0.1 to 1000 pg) can also be administered using a gene gun. Following an incubation period of 3-4 weeks, a booster dose is then administered. The booster can be recombinant fowlpox virus administered at a dose of 5-107 to 5x10 9 pfu.

63 For antibodies, a treatment generally involves repeated administration of the anti-109P1D4 antibody preparation, via an acceptable route of administration such as intravenous injection (IV), typically at a dose in the range of about 0.1 to about 10 mg/kg body weight In general, doses in the range of 10-500 mg mAb per week are effective and well tolerated. Moreover, an initial loading dose of approximately 4 mg/kg patient body weight IV, followed by weekly doses of about 2 mg/kg IV of the ant- 109P1D4 mAb preparation represents an acceptable dosing regimen. As appreciated by those of skill In the art, various factors can Influence the ideal dose in a particular case. Such factors include, for example, half life of a composition, the binding affinity of an Ab, the immunogenicity of a substance, the degree of 109P1 04 expression in the patient, the extent of circulating shed 109P1 D4 antigen, the desired steady-state concentration level, frequency of treatment, and the influence of chemotherapeutic or other agents used In combination with the treatment method of the invention, as well as the health status of a particular patient Non-limiting preferred human unit doses are, for example, 50pg - 1mg, 1mg - 50mg, 50mg - 100mg, 100mg - 200mg, 200mg - 300mg, 400mg - 500mg, 500mg - 600mg, 600mg - 700mg, 700mg 800mg, 800mg -900mg, 900mg - 1g, or 1mg - 700mg. In certain embodiments, the dose Is in a range of 2-5 mg/kg body weight, e.g., with folow on weekly doses of 1-3 mg/kg; 0.5mg, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10mg/kg body weight followed, e.g., In two, three or four weeks by weekly doses; 0.5 - 10mg/kg body weight, e.g., folowed in two, three or four weeks by weekly doses; 225, 250, 275, 300, 325, 350, 375, 400mg m 2 of body area weekly; 1-600mg m 2 of body area weekly; 225-400mg m 2 of body area weekly; these does can be followed by weekly doses for 2, 3, 4, 5, 6, 7, 8, 9, 19, 11, 12 or more weeks. In one embodiment, human unit dose forms of polynucleotides comprise a suitable dosage range or effective amount that provides any therapeutic effect As appreciated by one of ordinary skill in the art a therapeutic effect depends on a number of factors, induding the sequence of the polynudeotide, molecular weight of the polynucleotide and route of administration. Dosages are generally selected by the physician or other health care professional In accordance with a variety of parameters known In the art, such as severity of symptoms, history of the patient and the like. Generally, for a polynudeotide of about 20 bases, a dosage range may be selected from, for example, an Independently selected lower limit such as about 0.1, 0.25, 0.5, 1, 2, 5, 10, 20, 30, 40, 50, 60, 70, 80, 90, 100, 200, 300, 400 or 500 mg/kg up to an independently selected upper limit, greater than the lower limit, of about 60, 80, 100, 200, 300, 400, 500, 750, 1000, 1500, 2000, 3000, 4000, 5000, 6000, 7000, 8000, 9000 or 10,000 mg/kg. For example, a dose may be about any of the following: 0.1 to 100 mg/kg, 0.1 to 50 mg/kg, 0.1 to 25 mg/kg, 0.1 to 10 mg/kg, I to 500 mg/kg, 100 to 400 mg/kg, 200 to 300 mg/kg, 1 to 100 mg/kg, 100 to 200 mg/kg, 300 to 400 mg/kg, 400 to 500 mg/kg, 500 to 1000 mg/kg, 500 to 5000 mg/kg, or 500 to 10,000 mg/kg. Generally, parenteral routes of administration may require higher doses of polynudeotide compared to more direct application to the nuceotide to diseased Ussue, as do polynudeotides of increasing length. In one embodiment, human unit dose forms of T-cells comprise a suitable dosage range or effective amount that provides any therapeutic effect. As appreciated by one of ordinary skill In the art, a therapeutic effect depends on a number of factors. Dosages are generally selected by the physician or other health care professional In accordance with a variety of parameters known in the art, such as severity of symptoms, history of the patient and the like. A dose may be about 104 cells to about 106 cells, about 106 cells to about 108 cells, about 108 to about 1Ol cells, or about 108 to about 5 x 1010 cells. A dose may also about 106 cells/m 2 to about 1010 ces/m 2 , or about 106 cells/m 2 to about 108 cells/m 2 . Proteins(s) of the Invention, and/or nucleic acids encoding the protein(s), can also be administered via Uposomes, which may also serve to: 1) target the proteins(s) to a particular tissue, such as lymphoid tissue; 2) to target selectively to diseases cells; or, 3) to increase the half-life of the peptide composition. IUposomes include emulsions, foams, micelles, Insoluble monolayers, liquid crystals, phospholipid dispersions, lamellar layers and the like. In these preparations, the peptide to be delivered is Incorporated as part of a lposome, alone or in conjunction with a molecule which binds to a receptor prevalent among lymphoid cells, such as monoclonal antibodies which bind to the CD45 antigen, or with other 64 therapeutic or immunogenic compositions. Thus, liposomes either filled or decorated with a desired peptide of the invention can be directed to the site of lymphoid cells, where the liposomes then deliver the peptide compositions. Uposomes for use in accordance with the invention are formed from standard vesicle-forming lipids, which generally include neutral and negatively charged phospholipids and a sterol, such as cholesterol. The selection of lipids Is generally guided by consideration of, e.g., liposome size, acid lability and stability of the liposomes in the blood stream. A variety of methods are available for preparing liposomes, as described in, e.g., Szoka, et a1., Ann. Rev. Biophys. Bioeng. 9:467 (1980), and U.S. Patent Nos. 4,235,871, 4,501,728, 4,837,028, and 5,019,369. For targeting cells of the immune system, a ligand to be incorporated into the Uposome can include, e.g., antibodies or fragments thereof specific for cell surface determinants of the desired immune system cells. A liposome suspension containing a peptide may be administered intravenously, locally, topically, etc. in a dose which varies according to, Inter alia, the manner of administration, the peptide being delivered, and the stage of the disease being treated. For solid compositions, conventional nontoxic solid carriers may be used which include, for example, pharmaceutical grades of mannitol, lactose, starch, magnesium stearate, sodium saccharin, talcum, cellulose, glucose, sucrose, magnesium carbonate, and the like. For oral administration, a pharmaceutically acceptable nontoxic composition is formed by incorporating any of the normally employed exciplents, such as those carriers previously listed, and generally 10 95% of active Ingredient, that is, one or more peptides of the invention, and more preferably at a concentration of 25%-75%. For aerosol administration, immunogenic peptides are preferably supplied in finely divided form along with a surfactant and propellant. Typical percentages of peptides are about 0.01 %-20% by weight, preferably about 1 %-10%. The surfactant must, of course, be nontoxic, and preferably soluble In the propellant Representative of such agents are the esters or partial esters of fatty acids containing from about 6 to 22 carbon atoms, such as caproic, octanoic, lauric, palmitic, stearic, linoleic, linolenic, olesteric and oleic acids with an aliphatic polyhydric alcohol or its cyclic anhydride. Mixed esters, such as mixed or natural glycerides may be employed. The surfactant may constitute about 0.1/-20% by weight of the composition, preferably about 0.25-5%. The balance of the composition is ordinary propellant A carrier can also be included, as desired, as with, e.g., lecithin for intranasal delivery. X.) Diagnostic and Proanostic Embodiments of 109PiD4. As disclosed herein, 109P1D4 polynucleotides, polypeptides, reactive cytotoxic T cells (CTL), reactive helper T cells (HiL) and anti-polypeptide antibodies are used in well known diagnostic, prognostic and therapeutic assays that examine conditions associated with dysregulated cel growth such as cancer, in particular the cancers listed In Table I (see, e.g., both its specific patten of tissue expression as well as its overexpression in certain cancers as described for example In the Example entitled 'Expression analysis of 109P1D4 In normal tissues, and patient specimens". 109P1D4 can be analogized to a prostate associated antigen PSA, the archetypal marker that has been used by medical practitioners for years to identify and monitor the presence of prostate cancer (see, e.g., Merrill et al., J. Urol. 163(2): 503-5120 (2000); Polascik et al., J. Urol. Aug; 162(2):293-306 (1999) and Fortier et al., J. Nat. Cancer Inst 91(19): 1635 1640(1999)). A variety of other diagnostic markers are also used In similar contexts Including p53 and K-ras (see, e.g., Tulchinsky et al., Int J Mol Med 1999 Jul 4(1):99-102 and Minimoto et al., Cancer Detect Prev 2000;24(1):1-12). Therefore, this disclosure of 109P1D4 polynucleotides and polypeptides (as well as 109P1D4 polynucleotide probes and anti-109P1D4 antibodies used to Identify the presence of these molecules) and their properties allows skilled artisans to utilize these molecules in methods that are analogous to those used, for example, In a variety of diagnostic assays directed to examining conditions associated with cancer. Typical embodiments of diagnostic methods which utilize the 109P1 D4 polynucleotides, polypeptides, reactive T 65 cells and antibodies are analogous to those methods from well-established diagnostic assays, which employ, e.g., PSA polynudeotides, polypeptides, reactive T cells and antibodies. For example, just as PSA polynucleotides are used as probes (for example in Northern analysis, see, e.g., Sharief et al., Biochem. Mol. Biol. Int. 33(3):567-74(1994)) and primers (for example In PCR analysis, see, e.g., Okegawa et al., J. Urol. 163(4): 1189-1190 (2000)) to observe the presence and/or the level of PSA mRNAs In methods of monitoring PSA overexpression or the metastasis of prostate cancers, the 109P1 D4 polynucleotides described herein can be utilized In the same way to detect 109P1D4 overexpression or the metastasis of prostate and other cancers expressing this gene. Alternatively, just as PSA polypeptides are used to generate antibodies specific for PSA which can then be used to observe the presence and/or the level of PSA proteins in methods to monitor PSA protein overexpression (see, e.g., Stephan et al., Urology 55(4):560-3 (2000)) or the metastasis of prostate cells (see, e.g., Alanen et al., Pathol. Res. Pract. 192(3):233-7 (1996)), the 109P1D4 polypeptides described herein can be utilized to generate antibodies for use in detecting 109P1D4 overexpression or the metastasis of prostate cells and cells of other cancers expressing this gene. Specifically, because metastases involves the movement of cancer cells from an organ of origin (such as the lung or prostate gland etc.) to a different area of the body (such as a lymph node), assays which examine a biological sample for the presence of cells expressing 109P1 D4 polynucleotides and/or polypeptides can be used to provide evidence of metastasis. For example, when a biological sample from tissue that does not normally contain 109P1 D4-expressing cells (lymph node) is found to contain 109P1D4-expressing cells such as the 109P1D4 expression seen in LAPC4 and LAPC9, xenografts isolated from lymph node and bone metastasis, respectively, this finding is indicative of metastasis. Alternatively 109P1 D4 polynucleotides and/or polypeptides can be used to provide evidence of cancer, for example, when cells in a biological sample that do not normally express 109P1 D4 or express 109P1 D4 at a different level are found to express 109P1D4 or have an increased expression of 109P1D4 (see, e.g., the 109P1D4 expression in the cancers listed in Table I and In patient samples etc. shown in the accompanying Figures). In such assays, artisans may further wish to generate supplementary evidence of metastasis by testing the biological sample for the presence of a second tissue restricted marker (in addition to 109P1 D4) such as PSA, PSCA etc. (see, e.g., Alanen et al., Pathol. Res. Pract 192(3): 233 237 (1996)). The use of Immunohislochemistry to identify the presence of a 109P1D4 polypeptide within a tissue section can indicate an altered state of certain cells within that tissue. It Is well understood in the art that the ability of an antibody to localize to a polypeptide that Is expressed In cancer cells Is a way of diagnosing presence of disease, disease stage, progression and/or tumor aggressiveness. Such an antibody can also detect an altered distribution of the polypeptide within the cancer cells, as compared to corresponding non-malignant tissue. The 109P1 D4 polypeptide and Immunogenic compositions are also useful In view of the phenomena of altered subcellular protein localization in disease states. Alteration of cells from normal to diseased state causes changes in cellular morphology and Is often associated with changes In subcellular protein localization/distribution. For example, cell membrane proteins that are expressed in a polarized manner In normal cells can be altered in disease, resulting In distribution of the protein In a non-polar manner over the whole cell surface. The phenomenon of altered subcellular protein localization in a disease state has been demonstrated with MUCI and Her2 protein expression by use of immunohistochemical means. Normal epithellal cells have a typical apical distribution of MUCI, in addition to some supranuclear locadzation of the glycoprotein, whereas malignant lesions often demonstrate an apolar staining pattern (Diaz et al, The Breast Journal, 7; 40-45 (2001); Zhang et al, Clinical Cancer Research, 4; 2669-2676 (1998): Cao, et al, The Journal of Histochemistry and Cytochemistry, 45:1547-1557 (1997)). In addition, normal breast epithelium is either negative for Her2 protein or exhibits only a basolateral distribution whereas malignant cells can express 66 the protein over the whole cell surface (De Potter, et al, International Journal of Cancer, 44; 969-974 (1989): McCormick, et al, 117; 935-943 (2002)). Alternatively, distribution of the protein may be altered from a surface only localization to include diffuse cytoplasmic expression In the diseased state. Such an example can be seen with MUCI (Diaz, et al, The Breast Journal, 7: 40-45 (2001)). Alteration In the localization/distribution of a protein in the cell, as detected by Immunohistochemical methods, can also provide valuable information concerning the favorability of certain treatment modalities. This last point is illustrated by a situation where a protein may be intracellular in normal tissue, but cell surface In malignant cells; the cell surface location makes the cells favorably amenable to antibody-based diagnostic and treatment regimens. When such an alteration of protein localization occurs for 109P1 D4, the 109P1D4 protein and immune responses related thereto are very useful. Accordingly, the ability to determine whether alteration of subcellular protein localization occurred for 24P4C12 make the 109P1D4 protein and immune responses related thereto very useful. Use of the 109P1D4 compositions allows those skilled in the art to make important diagnostic and therapeutic decisions. Immunohistochemical reagents specific to 109P1D4 are also useful to detect metastases of tumors expressing 109P1 D4 when the polypeptide appears In tissues where 109P1 D4 is not normally produced. Thus, 109P1 D4 polypeptides and antibodies resulting from immune responses thereto are useful in a variety of Important contexts such as diagnostic, prognostic, preventative and/or therapeutic purposes known to those skilled in the art Just as PSA polynucleotide fragments and polynudeotide variants are employed by skilled artisans for use In methods of monitoring PSA, 109P1 D4 polynucleotide fragments and polynudeotide variants are used In an analogous manner. In particular, typical PSA polynucleotides used in methods of monitoring PSA are probes or primers which consist of fragments of the PSA cDNA sequence. Illustrating this, primers used to PCR amplify a PSA polynucleotide must indude less than the whole PSA sequence to function in the polymerase chain reaction. In the context of such PCR reactions, skilled artisans generally create a variety of different polynucleotide fragments that can be used as primers in order to amplify different portions of a polynucleotide of interest or to optimize amplification reactions (see, e.g., Caetano-Anolles, G. Biotechniques 25(3): 472-476,478-480 (1998); Robertson etal., Methods Mol. Biot. 98:121-154(1998)). An additional illustration of the use of such fragments is provided In the Example entitled 'Expresslon analysis of 109P1D4 In normal tissues, and patient specimens," where a 109P1D4 polynudeotide fragment is used as a probe to show the expression of 109P1D4 RNAs in cancer cells. In addition, variant polynucleotide sequences are typically used as primers and probes for the corresponding mRNAs In PCR and Northem analyses (see, e.g., Sawai et al., Fetal Diagn. Ther. 1996 Nov-Dec 11(6):407-13 and Current Protocols In Molecular Biology, Volume 2, Unit 2, Frederick M. Ausubel eta. ads., 1995)). Polynudeotide fragments and variants are useful in this context where they are capable of binding to a target polynucleotide sequence (e.g., a 109P1D4 polynudeotide shown in Figure 2 or variant thereo) under conditions of high stringency. Furthermore, PSA polypeptides which contain an epitope that can be recognized by an antibody or T cell that specifically binds to that epitope are used in methods of monitoring PSA. 109P104 polypeptide fragments and polypeptide analogs or variants can also be used in an analogous manner. This practice of using polypeptide fragments or polypeptide variants to generate antibodies (such as anti-PSA antibodies or T cells) is typical in the art with a wide variety of systems such as fusion proteins being used by practitioners (see, e.g., Current Protocols In Molecular Biology, Volume Z Unit 16, Frederick M. Ausubel et al. eds., 1995). In this context, each epitope(s) functions to provide the architecture with which an antibody or T cell is reactive. Typically, skilled artisans create a variety of different polypeptide fragments that can be used in order to generate Immune responses specific for different portions of a polypeptide of interest (see, e.g., U.S. Patent No. 5,840,501 and U.S. Patent No. 5,939,533). For example it may be preferable to utilize a polypeptide comprising one of the 109P1D4 biological motifs discussed herein or a motif-bearing subsequence which is readily Identified by one of skill In the 67 art based on motifs available in the art. Polypeptide fragments, variants or analogs are typically useful in this context as long as they comprise an epitope capable of generating an antibody or T cell specific for a target polypeptide sequence (e.g. a 109P1D4 polypeptide shown In Figure 3). As shown herein, the 109P1 D4 polynudeotides and polypeptides (as well as the 109P1 D4 polynudeotide probes and anti-09P1 D4 antibodies or T cells used to Identify the presence of these molecules) exhibit specific properties that make them useful in diagnosing cancers such as those listed in Table I. Diagnostic assays that measure the presence of 1 09P1D4 gene products, In order to evaluate the presence or onset of a disease condition described herein, such as prostate cancer, are used to identify patients for preventive measures or further monitoring, as has been done so successful with PSA. Moreover, these materials satisfy a need In the art for molecules having similar or complementary characteristics to PSA In situations where, for example, a definite diagnosis of metastasis of prostatic origin cannot be made on the basis of a test for PSA alone (see, e.g., Alanen et al., Pathol. Res. Pract. 192(3): 233-237 (1996)), and consequently, materials such as 109P1D4 polynudeotides and polypeptides (as well as the 109P1D4 polynucleotide probes and anti 109P1D4 antibodies used to Identify the presence of these molecules) need to be employed to confirm a metastases of prostatic origin. Finally, in addition to their use in diagnostic assays, the 109P1D4 polynucleotides disclosed herein have a number of other utilities such as their use in the Identification of oncogenetic associated chromosomal abnormalities in the chromosomal region to which the 109P1D4 gene maps (see the Example entitled "Chromosomal Mapping of 109P1D4" below). Moreover, in addition to their use in diagnostic assays, the 109P1D4-related proteins and polynudeotides disposed herein have other utilities such as their use in the forensic analysis of tissues of unknown origin (see, e.g., Takahama K Forensic Sci nt 1996 Jun 28;80(1-2): 63-9). Additionally, 109P1 D4-related proteins or polynudeotides of the Invention can be used to treat a pathologic condition characterized by the over-expression of 109P1 D4. For example, the amino acid or nucleic acid sequence of Figure 2 or Figure 3, or fragments of either, can be used to generate an immune response to a 109P1 D4 antigen. Antibodies or other molecules that react with 109P1 D4 can be used to modulate the function of this molecule, and thereby provide a therapeutic benefit Xl.) Inhibition of 109P1 D4 Protein Function The invention Includes various methods and compositions for inhibiting the binding of 109P1 D4 to its binding partner or its association with other protein(s) as well as methods for inhibiting 109P1 D4 function. X11A. Inhibition of 109P1D4 With Intracellular Antibodies In one approach, a recombinant vector that encodes single chain antibodies that specifically bind to 109P1D4 are Introduced Into 1 09P1 D4 expressing cells via gene transfer technologies. Accordingly, the encoded single chain anti 109P1D4 antibody is expressed intracellularly, binds to 109P1D4 protein, and thereby inhibits its function. Methods for engineering such intracellular single chain antibodies are well known. Such intracellular antibodies, also known as Intrabodies", are specifically targeted to a particular compartment within the cell, providing control over where the inhibitory activity of the treatment is focused. This technology has been successfully applied In the art (for review, see Richardson and Marasco, 1995, TIBTECH vol. 13). Intrabodies have been shown to virtually eliminate the expression of otherwise abundant cell surface receptors (see, e.g., Richardson et aL., 1995, Proc. Nat. Acad. Sci. USA 92- 3137-3141; Beerii et al., 1994, J. Biol. Chem. 289: 23931-23936; Deshane et al., 1994, Gene Ther. 1: 332-337). Single chain antibodies comprise the variable domains of the heavy and light chain joined by a flexible linker 68 polypeptide, and are expressed as a single polypeptide. Optionally, single chain antibodies are expressed as a single chain variable region fragment joined to the light chain constant region. Welknown intracellular trafficking signals are engineered into recombinant polynudeotide vectors encoding such single chain antibodies in order to target precisely the intrabody to the desired intracellular compartment For example, intrabodies targeted to the endoplasmic reticulum (ER) are engineered to incorporate a leader peptide and, optionally, a C-terminal ER retention signal, such as the KDEL amino acid motif. Intrabodies intended to exert activity In the nucleus are engineered to Indude a nuclear localization signal. Lpid moieties are joined to intrabodies In order to tether the intrabody to the cytosolic side of the plasma membrane. Intrabodles can also be targeted to exert function In the cytosol. For example, cytosolic intrabodies are used to sequester factors within the cytosol, thereby preventing them from being transported to their natural cellular destination. In one embodiment, intrabodies are used to capture 109PiD4 in the nucleus, thereby preventing its activity within the nucleus. Nuclear targeting signals are engineered into such 109P1D4 intrabodles in order to achieve the desired targeting. Such 109P1D4 intrabodies are designed to bind specifically to a particular 109P1D4 domain. In another embodiment, cytosolic intrabodies that specifically bind to a 1 09P1 D4 protein are used to prevent 109P1 D4 from gaining access to the nucleus, thereby preventing it from exerting any biological activity within the nucleus (e.g., preventing 109PID4 from forming transcription complexes with other factors). In order to specifically direct the expression of such intrabodies to particular cells, the transcription of the intrabody is placed under the regulatory control of an appropriate tumor-specific promoter and/or enhancer. In order to target intrabody expression specifically to prostate, for example, the PSA promoter and/or promoter/enhancer can be utilized (See, for example, U.S. Patent No. 5,919,652 Issued 6 July 1999). XII.B.) Inhibition of 109P1D4 with Recombinant Proteins In another approach, recombinant molecules bind to 109P1D4 and thereby Inhibit 109P1D4 function. For example, these recombinant molecules prevent or inhibit 109P1 D4 from accessing/binding to its binding partner(s) or associating with other protein(s). Such recombinant molecules can, for example, contain the reactive parts) of a 109P1 D4 specific antibody molecule. In a particular embodiment the 109P1D4 binding domain of a 109P1D4 binding partner Is engineered into a dimeric fusion protein, whereby the fusion protein comprises two 109P1 D4 ligand binding domains linked to the Fc portion of a human IgG, such as human IgGI. Such IgG portion can contain, for example, the CH2 and CH 3 domains and the hinge region, but not the CHI domain. Such dimeric fusion proteins are administered in soluble form to patients suffering from a cancer associated with the expression of 109P1D4, whereby the dimeric fusion protein specifically binds to 109P1D4 and blocks 109P1D4 interaction with a binding partner. Such dimeric fusion proteins are further combined into multimeric proteins using known antibody linking technologies. XII.C.) InhIbition of 109P1 D4 Transcription or Translation The present Invention also comprises various methods and compositions for inhibiting the transcription of the 109P1D4 gene. Similarly, the invention also provides methods and compositions for inhibiting the translation of 109P1D4 mRNA into protein. In one approach, a method of inhibiting the transcription of the 109P1D4 gene comprises contacting the 109P1D4 gene with a 109P1D4 antisense polynuclotide. In another approach, a method of inhibiting 109P1 D4 mRNA translation comprises contacting a 109P1 D4 mRNA with an antisense polynucleotide. In another approach, a 109P1 D4 specific ribozyme Is used to cleave a 109P1 D4 message, thereby Inhibiting translation. Such antisense and ribozyme based methods can also be directed to the regulatory regions of the 109PI D4 gene, such as 109P1 D4 promoter and/or enhancer 69 elements. Similarly, proteins capable of inhibiting a 109P1D4 gene transcription factor are used to inhibit 109P1D4 mRNA transcription. The various polynucleotides and compositions useful in the aforementioned methods have been described above. The use of antisense and ribozyme molecules to inhibit transcription and translation Is well known in the art Other factors that inhibit the transcription of 109P1D4 by interfering with 109P1D4 transcriptional activation are also useful to treat cancers expressing 109P1 D4. Similarly, factors that interfere with 109P1 D4 processing are useful to treat cancers that express 109P1 D4. Cancer treatment methods utilizing such factors are also within the scope of the invention. XII.D.) General Considerations for Therapeutic Strategles Gene transfer and gene therapy technologies can be used to deliver therapeutic polynucleotide molecules to tumor cells synthesizing 109P1D4 (i.e., antisense, ribozyme, polynucleoUdes encoding intrabodies and other 109P1D4 inhibitory molecules). A number of gene therapy approaches are known in the art Recombinant vectors encoding 109P1D4 anisense polyniudeotides, nbozymes, factors capable of interfering with 109P1 D4 transcription, and so forth, can be delivered to target tumor cells using such gene therapy approaches. The above therapeutic approaches can be combined with any one of a wide variety of surgical, chemotherapy or radiation therapy regimens. The therapeutic approaches of the invention can enable the use of reduced dosages of chemotherapy (or other therapies) and/or less frequent administration, an advantage for all patients and particularly for those that do not tolerate the toxicity of the chemotherapeutic agent welt. The anti-tumor activity of a particular composition (e.g., antisense, ribozyme, intrabody), or a combination of such compositions, can be evaluated using various in vitro and in vM assay systems. In vtro assays that evaluate therapeutic activity indude cel growth assays, soft agar assays and other assays indicative of tumor promoting activity, binding assays capable of determining the extent to which a therapeutic composition will inhibit the binding of 109P1 D4 to a binding partner, etc. In vo, the effect of a 109P1D4 therapeutic composition can be evaluated in a suitable animal model. For example, xenogenic prostate cancer models can be used, wherein human prostate cancer explants or passaged xenograft tissues are introduced into immune compromised animals, such as nude or SCID mice (Klein et a/., 1997, Nature Medicine 3: 402-408). For example, PCT Patent Application W098/16628 and U.S. Patent 6,107,540 describe various xenograft models of human prostate cancer capable of recapitulating the development of primary tumors, micrometastasis, and the formation of osteoblastic metastases characteristic of late stage disease. Efficacy can be predicted using assays that measure Inhibition of tumor formation, tumor regression or metastasis, and the like. In vivo assays that evaluate the promotion of apoptosis are useful in evaluating therapeutic compositions. In one embodiment xenografts from tumor bearing mice treated with the therapeutic composition can be examined for the presence of apoptotic foci and compared to untreated control xenograft-bearing mice. The extent to which apoptotic foci are found In the tumors of the treated mice provides an Indication of the therapeutic efficacy of the composition. The therapeutic compositions used in the practice of the foregoing methods can be formulated into pharmaceutical compositions comprising a carrier suitable for the desired delivery method. Suitable carriers include any material that when combined with the therapeutic composition retains the anti-tumor function of the therapeutic composition and Is generally non-reactive with the patients immune system. Examples include, but are not limited to, any of a number of standard pharmaceutical carriers such as sterile phosphate buffered saline solutions, bacteriostatic water, and the like (see, generally, Remington's Pharmaceutical Sciences 16e Edition, A. Osal., Ed., 1980). Therapeutic formulations can be solubilized and administered via any route capable of delivering the therapeutic composition to the tumor site. Potentially effective routes of administration Include, but are not limited to, intravenous, parenteral, intraperitoneal, Intramuscular, intratumor, intradermal, intraorgan, orthotopic, and the like. A preferred 70 formulation for intravenous injection comprises the therapeutic composition in a solution of preserved bacteriostatic water, sterile unpreserved water, and/or diluted In polyvinylchloride or polyethylene bags containing 0.9% sterile Sodium Chloride for Injection, USP. Therapeutic protein preparations can be lyophilized and stored as sterile powders, preferably under vacuum, and then reconstituted in bacteriostatic water (containing for example, benzyl alcohol preservative) or in sterile water prior to injection. Dosages and administration protocols for the treatment of cancers using the foregoing methods will vary with the method and the target cancer, and will generally depend on a number of other factors appreciated in the art 1.) Identification, Characterization and Use of Modulators of 109P1D4 Methods to Identify and Use Modulators In one embodiment, screening is performed to identify modulators that induce or suppress a particular expression profile, suppress or induce specific pathways, preferably generating the associated phenotype thereby. In another embodiment having identified differentially expressed genes important in a particular state; screens are performed to identify modulators that alter expression of individual genes, either increase or decrease. In another embodiment, screening is performed to identify modulators that alter a biological function of the expression product of a differentially expressed gene. Again, having identified the importance of a gene in a particular state, screens are performed to Identify agents that bind and/or modulate the biological activity of the gene product In addition, screens are done for genes that are induced in response to a candidate agent After identifying a modulator (one that suppresses a cancer expression pattern leading to a normal expression pattern, or a modulator of a cancer gene that leads to expression of the gene as in normal tissue) a screen is performed to Identify genes that are specifically modulated in response to the agent Comparing expression profiles between normal tissue and agent-treated cancer tissue reveals genes that are not expressed in normal tissue or cancer tissue, but are expressed in agent treated tissue, and vice versa. These agent-specific sequences are identified and used by methods described herein for cancer genes or proteins. In paricular these sequences and the proteins they encode are used in marldng or Identifying agent trated cells. In addition, antibodies are raised against the agent-induced proteins and used to target novel therapeutics to the treated cancer tissue sample. Modulator-related Identification and Screening Assays: Gene Expression-related Assays Proteins, nucleic acids, and antibodies of the invention are used In screening assays. The cancer-associated proteins, antibodies, nucleic acids, modified proteins and cells containing these sequences are used In screening assays, such as evaluating the effect of drug candidates on a "gene expression profile," expression profile of polypeptides or alteration of biological function. In one embodiment, the expression profiles are used, preferably In conjunction with high throughput screening techniques to allow monitoring for expression profile genes after treatment with a candidate agent (e.g., Davis, GF, et al, J Biol Screen 7:69 (2002); Zlokamik, et al., Science 279:84-8 (1998); Held, Genome Res 6:986 94,1996). The cancer proteins, antibodies, nucleic acids, modified proteins and cells containing the native or modified cancer proteins or genes are used in screening assays. That is, the present Invention comprises methods for screening for compositions which modulate the cancer phenotype or a physiological function of a cancer protein of the Invention. This is done on a gene Itself or by evaluating the effect of drug candidates on a "gene expression profile' or biological function. In one embodiment, expression profiles are used, preferably in conjunction with high throughput screening techniques to allow 71 monitoring after treatment with a candidate agent, see Zlokamik, supra. A variety of assays are executed directed to the genes and proteins of the Invention. Assays are run on an individual nucleic acid or protein level. That Is, having identified a particular gene as up regulated in cancer, test compounds are screened for the ability to modulate gene expression or for binding to the cancer protein of the invention. "Modulation' in this context includes an increase or a decrease In gene expression. The preferred amount of modulation will depend on the original change of the gene expression In normal versus tissue undergoing cancer, with changes of at least 10%, preferably 50%, more preferably 100-300%, and in some embodiments 300-1000% or greater. Thus, if a gene exhibits a 4-fold increase in cancer tissue compared to normal tissue, a decrease of about four-fold is often desired; similarly, a 10-fold decrease in cancer tissue compared to normal tissue a target value of a 10-fold increase in expression by the test compound is often desired. Modulators that exacerbate the type of gene expression seen in cancer are also useful, e.g., as an upregulated target In further analyses. The amount of gene expression Is monitored using nucleic acid probes and the quantification of gene expression levels, or, alternatively, a gene product itself is monitored, e.g., through the use of antibodies to the cancer protein and standard immunoassays. Proteomics and separation techniques also allow for quantification of expression. Expression Monitoring to Identify Conmounds that Modify Gene Expression In one embodiment, gene expression monitoring, i.e., an expression profile, is monitored simultaneously for a number of entities. Such profiles will typically involve one or more of the genes of Figure 2. In this embodiment, e.g., cancer nucleic acid probes are attached to blochips to detect and quantify cancer sequences In a particular cell. Alternatively, PCR can be used. Thus, a series, e.g., wells of a microtiter plate, can be used with dispensed primers in desired wells. A PCR reaction can then be performed and analyzed for each well. Expression monitoring Is performed to identify compounds that modify the expression of one or more cancer associated sequences, e.g., a polynucleotide sequence set out in Figure 2. Generally, a test modulator is added to the cells prior to analysis. Moreover, screens are also provided to identify agents that modulate cancer, modulate cancer proteins of the Invention, bind to a cancer protein of the invention, or interfere with the binding of a cancer protein of the invention and an antibody or other binding partner. In one embodiment, high throughput screening methods involve providing a library containing a large number of potential therapeutic compounds (candidate compounds). Such "combinatorial chemical libraries' are then screened in one or more assays to identify those library members (particular chemical species or subclasses) that display a desired characteristic activity. The compounds thus Identified can serve as conventional "lead compounds,' as compounds for screening, or as therapeutics. In certain embodiments, combinatorial libraries of potential modulators are screened for an ability to bind to a cancer polypeptide or to modulate activity. Conventionally, new chemical entities with useful properties are generated by identifying a chemical compound (called a "lead compound') with some desirable property or activity, e.g., inhIbiting activity, creating variants of the lead compound, and evaluating the property and activity of those variant compounds. Often, high throughput screening (HTS) methods are employed for such an analysis. As noted above, gene expression monitoring Is conveniently used to test candidate modulators (e.g., protein, nucleic acid or small molecule). After the candidate agent has been added and the cells allowed to incubate for a period, the sample containing a target sequence to be analyzed is, e.g., added to a biochip. If required, the target sequence is prepared using known techniques. For example, a sample is treated to lyse the cells, using known lysis buffers, electroporation, etc., with purification and/or amplification such as PCR performed as appropriate. For example, an in vitro transcription with labels covalently attached to the nucleotides is performed. Generally, 72 the nucleic acids are labeled with biotin-FITC or PE, or with cy3 or cy5. The target sequence can be labeled with, e.g., a fluorescent, a chemiluminescent, a chemical, or a radioactive signal, to provide a means of detecting the target sequence's specific binding to a probe. The label also can be an enzyme, such as alkaline phosphatase or horseradish peroxidase, which when provided with an appropriate substrate produces a product that is detected. Alternatively, the label Is a labeled compound or small molecule, such as an enzyme Inhibitor, that binds but is not catalyzed or altered by the enzyme. The label also can be a moiety or compound, such as, an epitope tag or biotin which specifically binds to streptavidin. For the example of blotin, the streptavidin is labeled as described above, thereby, providing a detectable signal for the bound target sequence. Unbound labeled streptavidin is typically removed prior to analysis. As will be appreciated by those in the art, these assays can be direct hybridization assays or can comprise "sandwich assays", which include the use of multiple probes, as is generally outlined in U.S. Patent Nos. 5, 681,702; 5,597,909; 5,545,730; 5,594,117; 5,591,584; 5,571,670; 5,580,731; 5,571,670; 5,591,584; 5,624,802; 5,635,352; 5,594,118; 5,359,100; 5,124, 246; and 5,681,697. In this embodiment, in general, the target nucleic acid is prepared as outlined above, and then added to the biochip comprising a plurality of nucleic acid probes, under conditions that allow the formation of a hybridization complex. A variety of hybridization conditions are used in the present invention, including high, moderate and low stringency conditions as outlined above. The assays are generally run under stringency conditions which allow formation of the label probe hybridization complex only in the presence of target. Stringency can be controlled by altering a step parameter that is a thermodynamic variable, including, but not limited to, temperature, formamide concentration, salt concentration, chaotropic salt concentration pH, organic solvent concentration, etc. These parameters may also be used to control non-specific binding, as is generally outlined in U.S. Patent No. 5,681,697. Thus, it can be desirable to perform certain steps at higher stringency conditions to reduce non-specific binding. The reactions outlined herein can be accomplished in a variety of ways. Components of the reaction can be added simultaneously, or sequentially, in different orders, with preferred embodiments outlined below. In addition, the reaction may include a variety of other reagents. These include salts, buffers, neutral proteins, e.g. albumin, detergents, etc. which can be used to facilitate optimal hybridization and detection, and/or reduce nonspecific or background interactions. Reagents that otherwise improve the efficiency of the assay, such as protease Inhibitors, nuclease Inhibitors, anti-microbial agents, etc., may also be used as appropriate, depending on the sample preparation methods and purity of the target. The assay data are analyzed to determine the expression levels of individual genes, and changes in expression levels as between states, forming a gene expression profile. Biological Activity-related Assays The invention provides methods Identify or screen for a compound that modulates the activity of a cancer-related gene or protein of the Invention. The methods comprise adding a test compound, as defined above, to a cell comprising a cancer protein of the invention. The cells contain a recombinant nucleic acid that encodes a cancer protein of the invention. In another embodiment, a library of candidate agents is tested on a plurality of cells. In one aspect, the assays are evaluated in the presence or absence or previous or subsequent exposure of physiological signals, e.g. hormones, antibodies, peptides, antigens, cytokines, growth factors, action potentials, pharmacological agents including chemotherapeutics, radiation, carcinogenics, or other cells (i.e., cell-cell contacts). In another example, the determinations are made at different stages of the cell cycle process. In this way, compounds that modulate genes or proteins of the invention are Identified. Compounds with pharmacological activity are able to enhance or 73 interfere with the activity of the cancer protein of the invention. Once identified, similar structures are evaluated to identify critical structural features of the compound. In one embodiment, a method of modulating ( e.g., inhibiting) cancer cell division is provided; the method comprises administration of a cancer modulator. In another embodiment, a method of modulating ( e.g., inhibiting) cancer is provided; the method comprises administration of a cancer modulator. In a further embodiment, methods of treating cells or individuals with cancer are provided; the method comprises administration of a cancer modulator. In one embodiment, a method for modulating the status of a cell that expresses a gene of the invention Is provided. As used herein status comprises such art-accepted parameters such as growth, proliferation, survival, function, apoptosis, senescence, location, enzymatic activity, signal transduction, etc. of a cell. In one embodiment, a cancer Inhibitor Is an antibody as discussed above. In another embodiment, the cancer inhibitor is an antisense molecule. A variety of cell growth, proliferation, and metastasis assays are known to those of skill in the art, as described herein. High Throughout Screening to Identify Modulators The assays to identify suitable modulators are amenable to high throughput screening. Preferred assays thus detect enhancement or inhibition of cancer gene transcription, Inhibition or enhancement of polypeptide expression, and inhibition or enhancement of polypeptide activity. In one embodiment, modulators evaluated in high throughput screening methods are proteins, often naturally occurring proteins or fragments of naturally occurring proteins. Thus, e.g., cellular extracts containing proteins, or random or directed digests of proteinaceous cellular extracts, are used. In this way, libraries of proteins are made for screening In the methods of the invention. Particularly preferred In this embodiment are libraries of bacterial, fungal, viral, and mammalian proteins, with the latter being preferred, and human proteins being especially preferred. Particularly useful test compound will be directed to the class of proteins to which the target belongs, e.g., substrates for enzymes, or ligands and receptors. Use of Soft Aqar Growth and Colony Formation to Identify and Characterize Modulators Normal cells require a solid substrate to attach and grow. When cells are transformed, they lose this phenotype and grow detached from the substrate. For example, transformed cells can grow in stirred suspension culture or suspended in semi-solid media, such as semi-solid or soft agar. The transformed cells, when transfected with tumor suppressor genes, can regenerate normal phenotype and once again require a solid substrate to attach to and grow. Soft agar growth or colony formation in assays are used to identify modulators of cancer sequences, which when expressed in host cells, inhibit abnormal cellular proliferation and transformation. A modulator reduces or eliminates the host cells' ability to grow suspended In solid or semisolid media, such as agar. Techniques for soft agar growth or colony formation in suspension assays are described in Freshney, Culture of Animal Cells a Manual of Basic Technique (3rd ed., 1994). See also, the methods section of Garkavtsev et al. (1996), supra. Evaluation of Contact Inhibition and Growth Density Limitation to Identify and Characterize Modulators Normal cells typically grow in a flat and organized pattem In cell culture until they touch other cells. When the cells touch one another, they are contact inhibited and stop growing. Transformed cells, however, are not contact Inhibited and continue to grow to high densities in disorganized foci. Thus, transformed cells grow to a higher saturation density than corresponding normal cells. This is detected morphologically by the formation of a disoriented monolayer of cells or cells in foci. Alternatively, labeling index with ( 3 H)-thymidine at saturation density Is used to measure density Ilmitation of growth, similarly an MTT or Alamar blue assay will reveal proliferation capacity of cells and the the ability of modulators to affect same. See Freshney (1994), supra. Transformed cells, when transfected with tumor suppressor genes, can regenerate a normal phenotype and become contact Inhibited and would grow to a lower density.

74 In this assay, labeling index with 3 H)-thymidine at saturation density is a preferred method of measuring density limitation of growth. Transformed host cells are transfected with a cancer-associated sequence and are grown for 24 hours at saturation density in non-limiting medium conditions. The percentage of cells labeling with ( 3 H)-thymidine is determined by incorporated cpm. Contact Independent growth is used to Identify modulators of cancer sequences, which had led to abnormal cellular proliferation and transformation. A modulator reduces or eliminates contact independent growth, and returns the cells to a normal phenotype. Evaluation of Growth Factor or Serum Dependence to Identify and Characterize Modulators Transformed cells have lower serum dependence than their normal counterparts (see, e.g., Temin, J. Nal. Cancer Inst 37:167-175 (1966); Eagle et al., J. Exp. Med 131:836-879 (1970)); Freshney, supra. This Is in part due to release of various growth factors by the transformed cells. The degree of growth factor or serum dependence of transformed host cells can be compared with that of control. For example, growth factor or serum dependence of a cell Is monitored in methods to identify and characterize compounds that modulate cancer-associated sequences of the invention. Use of Tumor-specific Marker Levels to Identify and Characterize Modulators Tumor cells release an increased amount of certain factors (hereinafter 'tumor specific markers') than their normal counterparts. For example, plasminogen activator (PA) is released from human glioma at a higher level than from normal brain cells (see, e.g., Gullino, Angiogenesis, Tumor Vascularization, and Potential Interference with Tumor Growth, in Biological Responses in Cancer, pp. 178-184 (Mihich (ed.) 1985)). Similarly, Tumor Angiogenesis Factor (TAF) is released at a higher level in tumor cells than their normal counterparts. See, e.g., Folkman, Angiogenesis and Cancer, Sem Cancer Biol. (1992)), while bFGF is released from endothelial tumors (Ensoli, B et al). Various techniques which measure the release of these factors are described in Freshney (1994), supra. Also, see, Unkless et al., J. Biol. Chem. 249:4295-4305 (1974); Strickland & Beers, J. Biol. Chem. 251:5694-5702 (1976); Whur et al., Br. J. Cancer 42:305 312 (1980); Gullino, Angiogenesis, Tumor Vascularizalion, and Potential Interference with Tumor Growth, in Biological Responses In Cancer, pp. 178-184 (Mihich (ed.) 1985); Freshney, Anticancer Res. 5:111-130 (1985). For example, tumor specific marker levels are monitored In methods to Identify and characterize compounds that modulate cancer-associated sequences of the invention. Invasiveness into Matrigel to identify and Characterize Modulators The degree of invasiveness into Matrigel or an extracellular matrix constituent can be used as an assay to identify and characterize compounds that modulate cancer associated sequences. Tumor cells exhibit a positive correlation between malignancy and invasiveness of cells into Matrigel or some other extracellular matrix constituent. In this assay, tumorigenic cells are typically used as host cells. Expression of a tumor suppressor gene in these host cells would decrease invasiveness of the host cells. Techniques described in Cancer Res. 1999; 59:6010; Freshney (1994), supra, can be used. Briefly, the level of invasion of host cells is measured by using filters coated with Matrigel or some other extracellular matrix constituent. Penetration Into the gel, or through to the distal side of the filter, is rated as Invasiveness, and rated histologically by number of cells and distance moved, or by prelabeling the cells with M1 and counting the radioactivity on the distal side of the filter or bottom of the dish. See, e.g., Freshney (1984), supra. Evaluation of Tumor Growth In Vwiv to Identify and Characterize Modulators Effects of cancer-associated sequences on cell growth are tested in transgenic or immune-suppressed organisms. Transgenic organisms are prepared in a variety of art-accepted ways. For example, knock-out transgenic organisms, e.g., mammals such as mice, are made, In which a cancer gene Is disrupted or in which a cancer gene is inserted. Knock-out transgenic mice are made by insertion of a marker gene or other heterologous gene Into the endogenous cancer gene site in 75 the mouse genome via homologous recombination. Such mice can also be made by substituting the endogenous cancer gene with a mutated version of the cancer gene, or by mutating the endogenous cancer gene, e.g., by exposure to carcinogens. To prepare transgenic chimeric animals, e.g., mice, a DNA construct is introduced Into the nuclei of embryonic stem cells. Cells containing the newly engineered genetic lesion are injected into a host mouse embryo, which is re implanted into a recipient female. Some of these embryos develop into chimeric mice that possess germ cells some of which are derived from the mutant cell line. Therefore, by breeding the chimeric mice it is possible to obtain a new line of mice containing the introduced genetic lesion (see, e.g., Capecchi at al., Science 244:1288 (1989)). Chimeric mice can be derived according to US Patent 6,365,797, issued 2 April 2002; US Patent 6,107,540 issued 22 August 2000; Hogan at al., Manipulating the Mouse Embryo: A laboratory Manual, Cold Spring Harbor Laboratory (1988) and Teratocarcinomas and Embryonic Stem Cells: A Practical Approach, Robertson, ed., IRL Press, Washington, D.C., (1987). Alternatively, various immune-suppressed or Immune-deficient host animals can be used. For example, a genetically athymic "nude" mouse (see, e.g., Glovanella at al., J. Nati. Cancer Inst 52:921 (1974)), a SCID mouse, a thymectomized mouse, or an irradiated mouse (see, e.g., Bradley at al., Br. J. Cancer 38:263 (1978); Selby et al., Br. J. Cancer 41:52 (1980)) can be used as a host Transplantable tumor cells (typically about 106 cells) Injected into isogenic hosts produce Invasive tumors in a high proportion of cases, while normal cells of similar origin will not In hosts which developed invasive tumors, cells expressing cancer-associated sequences are injected subcutaneously or orthotopically. Mice are then separated into groups, including control groups and treated experimental groups) e.g. treated with a modulator). After a suitable length of time, preferably 4-8 weeks, tumor growth is measured (e.g., by volume or by Its two largest dimensions, or weight) and compared to the control. Tumors that have statistically significant reduction (using, e.g., Student's T test) are said to have Inhibited growth. In Vitro Assays to Identify and Characterize Modulators Assays to identify compounds with modulating activity can be performed in vitro. For example, a cancer polypeptide is first contacted with a potential modulator and incubated for a suitable amount of time, e.g., from 0.5 to 48 hours. In one embodiment, the cancer polypeptide levels are determined in vitro by measuring the level of protein or mRNA. The level of protein is measured using Immunoassays such as Westem blotting, ELISA and the like with an antibody that selectively bInds to the cancer polypeptide or a fragment thereof. For measurement of mRNA, amplification, e.g., using PCR, LCR, or hybridization assays, e. g., Northem hybridization, RNAse protection, dot blotting, are preferred. The level of protein or mRNA is detected using directly or indirectly labeled detection agents, e.g., fluorescently or radioactively labeled nucleic acids, radioactively or enzymatically labeled antibodies, and the like, as described herein. Alternatively, a reporter gene system can be devised using a cancer protein promoter operably linked to a reporter gene such as luciferase, green fluorescent protein, CAT, or P-gal. The reporter construct is typically transfected Into a cell. After treatment with a potential modulator, the amount of reporter gene transcription, translation, or activity is measured according to standard techniques known to those of skill in the art (Davis GF, supra; Gonzalez, J. & Negulescu, P. Curr. Opin. Biotechnol. 1998: 9:624). As outlined above, In vitro screens are done on individual genes and gene products. That Is, having Identified a particular differentially expressed gene as Important in a particular state, screening of modulators of the expression of the gene or the gene product itself is performed. In one embodiment, screening for modulators of expression of specific gene(s) Is performed. Typically, the expression of only one or a few genes Is evaluated. In another embodiment, screens are designed to first find compounds 76 that bind to differentially expressed proteins. These compounds are then evaluated for the ability to modulate differentially expressed activity. Moreover, once initial candidate compounds are identified, variants can be further screened to better evaluate structure activity relationships. Binding Assays to Identify and Characterize Modulators In binding assays in accordance with the Invention, a purified or isolated gene product of the invention is generally used. For example, antibodies are generated to a protein of the invention, and immunoassays are run to determine the amount and/or location of protein. Alternatively, cells comprising the cancer proteins are used in the assays. Thus, the methods comprise combining a cancer protein of the Invention and a candidate compound such as a ligand, and determining the binding of the compound to the cancer protein of the invention. Preferred embodiments utilize the human cancer protein; animal models of human disease of can also be developed and used. Also, other analogous mammalian proteins also can be used as appreciated by those of skill In the art. Moreover, in some embodiments variant or derivative cancer proteins are used. Generally, the cancer protein of the invention, or the figand, is non-diffusibly bound to an Insoluble support. The support can, e.g., be one having isolated sample receiving areas (a microtiter plate, an array, etc.). The insoluble supports can be made of any composition to which the compositions can be bound, is readily separated from soluble material, and is otherwise compatible with the overall method of screening. The surface of such supports can be solid or porous and of any convenient shape. Examples of suitable insoluble supports Include microtiter plates, arrays, membranes and beads. These are typically made of glass, plastic (e.g., polystyrene), polysaccharide, nylon, nitrocelulose, or Teflonm, etc. Microtiter plates and arrays are especially convenient because a large number of assays can be carried out simultaneously, using small amounts of reagents and samples. The particular manner of binding of the composition to the support is not crucial so long as it is compatible with the reagents and overall methods of the invention, maintains the activity of the composition and is nondiffusable. Preferred methods of binding Include the use of antibodies which do not sterically block either the ligand binding site or activation sequence when attaching the protein to the support, direct binding to "sticky" or Ionic supports, chemical crosslinking, the synthesis of the protein or agent on the surface, etc. Following binding of the protein or ligand/binding agent to the support, excess unbound material is removed by washing. The sample receiving areas may then be blocked through incubation with bovine serum albumin (BSA), casein or other innocuous protein or other moiety. Once a cancer protein of the invention is bound to the support, and a test compound is added to the assay. Alternatively, the candidate binding agent Is bound to the support and the cancer protein of the invention is then added. Binding agents Include specific antibodies, non-natural binding agents identified In screens of chemical libraries, peptide analogs, etc. Of particular interest are assays to identify agents that have a low toxicity for human cells. A wide variety of assays can be used for this purpose, including proliferation assays, cAMP assays, labeled in itro protein-protein binding assays, electrophoretic mobility shift assays, immunoassays for protein binding, functional assays (phosphorylation assays, etc.) and the like. A determination of binding of the test compound (ligand, binding agent, modulator, etc.) to a cancer protein of the invention can be done in a number of ways. The test compound can be labeled, and binding determined directly, e.g., by attaching all or a portion of the cancer protein of the invention to a solid support, adding a labeled candidate compound (e.g., a fluorescent label), washing off excess reagent, and determining whether the label Is present on the solid support. Various blocking and washing steps can be utilized as appropriate.

77 In certain embodiments, only one of the components is labeled, e.g., a protein of the invention or ligands labeled. Alternatively, more than one component Is labeled with different labels, e.g., V25, for the proteins and a fluorophor for the compound. Proximity reagents, e.g., quenching or energy transfer reagents are also useful. Competitive Binding to Identify and Characterize Modulators In one embodiment, the binding of the "test compound' is determined by competitive binding assay with a "competitor." The competitor is a binding moiety that binds to the target molecule (e.g., a cancer protein of the invention). Competitors include compounds such as antibodies, peptides, binding partners, ligands, etc. Under certain circumstances, the competitive binding between the test compound and the competitor displaces the test compound. In one embodiment, the test compound is labeled. Either the test compound, the competitor, or both, is added to the protein for a time sufficient to allow binding. Incubations are performed at a temperature that facilitates optimal activity, typically between four and 40*C. Incubation periods are typically optimized, e.g., to facilitate rapid high throughput screening; typical between zero and one hour will be sufficient. Excess reagent Is generally removed or washed away. The second component is then added, and the presence or absence of the labeled component Is followed, to indicate binding. In one embodiment, the competitor is added first, followed by the test compound. Displacement of the competitor is an Indication that the test compound Is binding to the cancer protein and thus is capable of binding to, and potentially modulating, the activity of the cancer protein. In this embodiment, either component can be labeled. Thus, e.g., if the competitor is labeled, the presence of label In the post-test compound wash solution indicates displacement by the test compound. Alternatively, if the test compound is labeled, the presence of the label on the support indicates displacement In an alternative embodiment, the test compound is added first, with incubation and washing, followed by the competitor. The absence of binding by the competitor Indicates that the test compound binds to the cancer protein with higher affinity than the competitor. Thus, if the test compound Is labeled, the presence of the label on the support, coupled with a lack of competitor binding, Indicates that the test compound binds to and thus potentially modulates the cancer protein of the invention. Accordingly, the competitive binding methods comprise differential screening to Identity agents that are capable of modulating the activity of the cancer proteins of the invention. In this embodiment, the methods comprise combining a cancer protein and a competitor in a first sample. A second sample comprises a test compound, the cancer protein, and a competitor. The binding of the competitor is determined for both samples, and a change, or difference in binding between the two samples Indicates the presence of an agent capable of binding to the cancer protein and potentially modulating its activity. That is, if the binding of the competitor is different in the second sample relative to the first sample, the agent is capable of binding to the cancer protein. Alternatively, differential screening is used to identify drug candidates that bind to the native cancer protein, but cannot bind to modified cancer proteins. For example the structure of the cancer protein is modeled and used in rational drug design to synthesize agents that Interact with that site, agents which generally do not bind to site-modified proteins. Moreover, such drug candidates that affect the activity of a native cancer protein are also Identified by screening drugs for the ability to either enhance or reduce the activity of such proteins. Positive controls and negative controls can be used in the assays. Preferably control and test samples are performed in at least triplicate to obtain statistically significant results. Incubation of all samples occurs for a time sufficient to allow for the binding of the agent to the protein. Following Incubation, samples are washed free of non-specifically bound material and the amount of bound, generally labeled agent determined. For example, where a radiolabel Is employed, the samples can be counted in a scintillation counter to determine the amount of bound compound.

78 A variety of other reagents can be included in the screening assays. These include reagents like salts, neutral proteins, e.g. albumin, detergents, etc. which are used to facilitate optimal protein-protein binding and/or reduce non-specific or background interactions. Also reagents that otherwise Improve the efficiency of the assay, such as protease Inhibitors, nudease Inhibitors, anti-microbial agents, etc., can be used. The mixture of components is added In an order that provides for the requisite binding. Use of Polynucleotides to Down-regulate or Inhibit a Protein of the Invention. Polynucleotide modulators of cancer can be introduced into a cell containing the target nucleotide sequence by formation of a conjugate with a igand-binding molecule, as described in WO 91/04753. Suitable figand-binding molecules include, but are not limited to, cell surface receptors, growth factors, other cytokines, or other ligands that bind to cell surface receptors. Preferably, conjugation of the ligand binding molecule does not substantially interfere with the ability of the ligand binding molecule to bind to its corresponding molecule or receptor, or block entry of the sense or antisense oligonucleotide or its conjugated version into the cell. Alternatively, a polynucleotide modulator of cancer can be introduced Into a cell containing the target nucleic acid sequence, e.g., by formation of a polynucleotide-lipid complex, as described in WO 90110448. It is understood that the use of antisense molecules or knock out and knock in models may also be used in screening assays as discussed above, in addition to methods of treatment Inhibitory and Antisense Nucleotides In certain embodiments, the activity of a cancer-assodated protein is down-regulated, or entirely inhibited, by the use of antisense polynucleotide or inhibitory small nuclear RNA (snRNA), i.e., a nucleic acid complementary to, and which can preferably hybridize specifically to, a coding mRNA nucleic acid sequence, e.g., a cancer protein of the invention, mRNA, or a subsequence thereof. Binding of the antisense polynudeotide to the mRNA reduces the translation and/or stability of the mRNA. In the context of this invention, antisense polynucleotides can comprise naturally occurring nucleotides, or synthetic species formed from naturally occurring subunits or their close homologs. Antisense polynucleotides may also have altered sugar moieties or inter-sugar linkages. Exemplary among these are the phosphorothioate and other sulfur containing species which are known for use In the art Analogs are comprised by this invention so long as they function effectively to hybridize with nucleotides of the invention. See, e.g., Isis Pharmaceuticals, Carlsbad, CA; Sequitor, Inc., Natick, MA. Such antisense polynucleotides can readily be synthesized using recombinant means, or can be synthesized In vitro. Equipment for such synthesis Is sold by several vendors, Including Applied Blosystems. The preparation of other oligonucleotides such as phosphorothioates and alkylated derivatives is also well known to those of skill in the art Antisense molecules as used herein include antisense or sense oligonucleotides. Sense oligonucleotides can, e.g., be employed to block transcription by binding to the anti-sense strand. The antisense and sense oligonucleotide comprise a single stranded nucleic acid sequence (either RNA or DNA) capable of binding to target mRNA (sense) or DNA (antisense) sequences for cancer molecules. Antisense or sense oligonucleotides, according to the present invention, comprise a fragment generally at least about 12 nucleotides, preferably from about 12 to 30 nucleotides. The ability to derive an antisense or a sense oligonucleotide, based upon a cDNA sequence encoding a given protein is described in, e.g., Stein &Cohen (Cancer Res. 48:2659 (1988 and van der Krol et al. (BloTechniques 6:958 (1988)). Ribzmes In addition to antisense polynudeotides, ribozymes can be used to target and inhibit transcription of cancer associated nucleotide sequences. A ribozyme Is an RNA molecule that catalytically cleaves other RNA molecules. Different 79 kinds of ribozymes have been described, including group I ribozymes, hammerhead ribozymes, hairpin ribozymes, RNase P, and axhead nbozymes (see, e.g., Castanotto et al., Adv. in Pharmacology 25: 289-317 (1994) for a general review of the properties of different ribozymes). The general features of hairpin ribozymes are described, e.g., in Hampel et al., Nucl. Adds Res. 18:299-304 (1990); European Patent Publication No. 0360257; U.S. Patent No. 5,254,678. Methods of preparing are well known to those of skill in the art (see, e.g., WO 94/26877; Ojwang et al., Proc. Nati. Acad. Sci. USA 90:6340-6344 (1993); Yamada et al., Human Gene Therapy 1:39-45 (1994); Leavitt et al., Proc. Nati. Acad Sci. USA 92:699- 703 (1995); Leavitt et al., Human Gene Therapy 5:1151-120 (1994); and Yamada et al., Virology 205: 121-126 (1994)). Use of Modulators In Phenotypic Screeninq In one embodiment, a test compound is administered to a population of cancer cells, which have an associated cancer expression profile. By 'administration" or 'contacting" herein Is meant that the modulator is added to the cells in such a manner as to allow the modulator to act upon the cell, whether by uptake and intracellular action, or by action at the cell surface. In some embodiments, a nucleic acid encoding a proteinaceous agent (i.e., a peptide) is put Into a viral construct such as an adenoviral or retroviral construct, and added to the cell, such that expression of the peptide agent Is accomplished, e.g., PCT US97/01019. Regulatabie gene therapy systems can also be used. Once the modulator has been administered to the cells, the cells are washed if desired and are allowed to incubate under preferably physiological conditions for some period. The cells are then harvested and a new gene expression profile Is generated. Thus, e.g., cancer tissue is screened for agents that modulate, e.g., induce or suppress, the cancer phenotype. A change in at least one gene, preferably many, of the expression profile indicates that the agent has an effect on cancer activity. Similarly, altering a biological function or a signaling pathway Is indicative of modulator activity. By defining such a signature for the cancer phenotype, screens for new drugs that alter the phenotype are devised. With this approach, the drug target need not be known and need not be represented In the original gene/protein expression screening platform, nor does the level of transcript for the target protein need to change. The modulator inhibiting function will serve as a surrogate marker As outlined above, screens are done to assess genes or gene products. That is, having identified a particular differentially expressed gene as important in a particular state, screening of modulators of either the expression of the gene or the gene product itself is performed. Use of Modulators to Affect Peptides of the Invention Measurements of cancer polypeptide activity, or of the cancer phenotype are performed using a variety of assays. For example, the effects of modulators upon the function of a cancer polypeptide(s) are measured by examining parameters described above. A physiological change that affects activity is used to assess the influence of a test compound on the polypeptides of this invention. When the functional outcomes are determined using intact cells or animals, a variety of effects can be assesses such as, In the case of a cancer associated with solid tumors, tumor growth, tumor metastasis, neovascularization, hormone release, transcriptional changes to both known and uncharacterized genetic markers (e.g., by Northern blots), changes in cell metabolism such as cell growth or pH changes, and changes in Intracellular second messengers such as cGNIP. Methods of Identifying Characterizing Cancer-associated Sequences Expression of various gene sequences Is correlated with cancer. Accordingly, disorders based on mutant or variant cancer genes are determined. In one embodiment, the invention provides methods for identifying cells containing 80 variant cancer genes, e.g., determining the presence of, all or part, the sequence of at least one endogenous cancer gene in a cell. This is accomplished using any number of sequencing techniques. The invention comprises methods of Identifying the cancer genotype of an individual, e.g., determining all or part of the sequence of at least one gene of the invention in the individual. This is generally done in at least one tissue of the individual, e.g., a tissue set forth in Table 1, and may include the evaluation of a number of tissues or different samples of the same tissue. The method may Include comparing the sequence of the sequenced gene to a known cancer gene, i.e., a wild-type gene to determine the presence of family members, homologies, mutations or variants. The sequence of all or part of the gene can then be compared to the sequence of a known cancer gene to determine if any differences exist This is done using any number of known homology programs, such as BLAST, Bestflit, etc. The presence of a difference in the sequence between the cancer gene of the patient and the known cancer gene correlates with a disease state or a propensity for a disease state, as outined herein. In a preferred embodiment, the cancer genes are used as probes to determine the number of copies of the cancer gene In the genome. The cancer genes are used as probes to determine the chromosomal localization of the cancer genes. Information such as chromosomal localization finds use in providing a diagnosis or prognosis In particular when chromosomal abnormalities such as translocations, and the like are Identified In the cancer gene locus. XIV.) KitslAicles of Manufacture For use in the laboratory, prognostic, prophylactic, diagnostic and therapeutic applications described herein, kits are within the scope of the invention. Such kits can comprise a carrier, package, or container that is compartmentalized to receive one or more containers such as vials, tubes, and the like, each of the container(s) comprising one of the separate elements to be used In the method, along with a label or insert comprising Instructions for use, such as a use described herein. For example, the container(s) can comprise a probe that is or can be detectably labeled. Such probe can be an antibody or polynucleotide specific for a protein or a gene or message of the invention, respectively. Where the method utilizes nucleic acid hybridization to detect the target nudeic acid, the kit can also have containers containing nudeotide(s) for amplification of the target nucleic acid sequence. Kits can comprise a container comprising a reporter, such as a biotin binding protein, such as avidin or streptavidin, bound to a reporter molecule, such as an enzymatic, fluorescent, or radioisotope label; such a reporter can be used with, e.g., a nucleic acid or antibody. The kit can include all or part of the amino acid sequences In Figure 2 or Figure 3 or analogs thereof, or a nucleic acid molecule that encodes such amino acid sequences. The kit of the invention will typically comprise the container described above and one or more other containers associated therewith that comprise materials desirable from a commercial and user standpoint, including buffers, diluents, filters, needles, syringes; carrier, package, container, vial and/or tube labels listing contents and/or instrucdons for use, and package Inserts with Instructions for use. A label can be present on or with the container to Indicate that the composition is used for a specific therapy or non therapeuic application, such as a prognostic, prophylactic, diagnostic or laboratory application, and can also indicate directions for either in vivo or in vm use, such as those described herein. Directions and or other information can also be induded on an insert(s) or label(s) which is Included with or on the kit. The label can be on or associated with the container. A label a can be on a container when letters, numbers or other characters forming the label are molded or etched into the container itself; a label can be associated with a container when it is present within a receptacle or carrier that also holds the container, e.g., as a package Insert. The label can Indicate that the composition is used for diagnosing, treating, prophylaxing or prognosing a condition, such as a neoplasia of a tissue set forth in Table I. The terms "kIt" and 'article of manufacture' can be used as synonyms.

81 In another embodiment of the invention, an article(s) of manufacture containing compositions, such as amino acid sequence(s), small molecule(s), nucleic acid sequence(s), and/or antibody(s), e.g., materials useful for the diagnosis, prognosis, prophylaxis and/or treatment of neoplasias of tissues such as those set forth in Table I is provided. The artide of manufacture typically comprises at least one container and at least one label. Suitable containers include, for example, bottles, vials, syringes, and test tubes. The containers can be formed from a variety of materials such as glass, metal or plastic. The container can hold amino acid sequence(s), small molecule(s), nucleic acid sequence(s), cell population(s) and/or antibody(s). In one embodiment the container holds a polynudeotide for use in examining the mRNA expression profile of a cell, together with reagents used for this purpose. In another embodiment a container comprises an antibody, binding fragment thereof or specific binding protein for use in evaluating protein expression of109PiD4 in cells and tissues, or for relevant laboratory, prognostic, diagnostic, prophylactic and therapeutic purposes; indications and/or directions for such uses can be included on or with such container, as can reagents and other compositions or tools used for these purposes. In another embodiment a container comprises materials for eliciting a cellular or humoral immune response, together with associated Indications and/or directions. In another embodiment, a container comprises materials for adoptive Immunotherapy, such as cytotoxic T cells (CTL) or helper T cells (HTL), together with associated indications and/or directions; reagents and other compositions or tools used for such purpose can also be Included. The container can alternatively hold a composition that is effective for treating, diagnosis, prognosing or prophylaxing a condition and can have a sterile access port (for example the container can be an Intravenous solution bag or a vial having a stopper pierceable by a hypodermic injection needle). The active agents In the composition can be an antibody capable of specifically binding 109P1D4 and modulating the function of 109P1D4. The artide of manufacture can further comprise a second container comprising a pharmaceutically-acceptable buffer, such as phosphate-buffered saline, Ringer's solution and/or dextrose solution. It can further include other materials desirable from a commercial and user standpoint, including other buffers, diluents, filters, stirrers, needles, syringes, and/or package inserts with Indications and/or instructions for use. EXAMPLES: Various aspects of the invention are further described and illustrated by way of the several examples that follow, none of which is Intended to limit the scope of the invention. Example 1: SSH-Generated Isolation of cDNA Fragment of the 109P1D4 Gene To Isolate genes that are over-expressed in prostate cancer we used the Suppression Subtractive Hybridization (SSH) procedure using cDNA derived from prostate cancer tissues. The 109P1 D4 SSH cDNA sequence was from an experiment where cDNA derived from LNCaP cells that was androgen-deprived (by growing in the presence of charcoal-stripped serum) was subtracted from cDNA derived from LNCaP cells that were stimulated with mibolerone for 9 hours. Materials and Methods Human Tissues: The patient cancer and normal tissues were purchased from different sources such as the NDRI (Philadelphia, PA). mRNA for some normal tissues were purchased from different companies such as Clontech, Palo Alto, CA. RNA Isolation: Tissues were homogenized in Trizol reagent (Ufe Technologies, Gibco BRL) using 10 ml/ g tissue to Isolate total RNA. Poly A RNA was purified from total RNA using Qiagen's Oligotex mRNA Mini and Midi kits. Total and mRNA were quantified by spectrophotometric analysis (O.D. 260/280 nm) and analyzed by gel electrophoresis.

82 Oligonucleotides: The following HPLC purified oligonucleotides were used. DPNCDN (cDNA synthesis primer): 5'TTTTGATCAAGCTao3' (SEQ ID NO: 44) Adaptor 1: 5'CTAATACGACTCACTATAGGGCTCGAGCGGCCGCCCGGGCAG3' (SEQ ID NO: 45) 3'GGCCCGTCCTAG5' (SEQ ID NO: 46) Adaptor 2: 5'GTAATACGACTCACTATAGGGCAGCGTGGTCGCGGCCGAG3' (SEQ ID NO: 47) 3'CGGCTCCTAG5' (SEQ ID NO: 48) PCR primer 1: 5'CTAATACGACTCACTATAGGGC3' (SEQ ID NO: 49) Nested primer (NPi: 5'TCGAGCGGCCGCCCGGGCAGGA3' (SEQ ID NO: 50) Nested former (NP)2: 5'AGCGTGGTCGCGGCCGAGGA3' (SEQ ID NO: 51) Supression Subtractive Hybridization: Suppression Subtractive Hybridization (SSH) was used to identify cDNAs corresponding to genes that may be differentially expressed in prostate cancer. The SSH reaction utilized cDNA from LNCaP prostate cancer cells. The 109P1 D4 SSH sequence was derived from cDNA subtraction of LNCaP stimulated with mibolerone minus LNCaP in the absence of androgen. The SSH DNA sequence (Figure 1) was Identified. The cDNA derived from androgen-deprived LNCaP cells was used as the source of the "driver" cDNA, while the cDNA from androgen-stimulated LNCaP cells was used as the source of the tester" cDNA. Double stranded cDNAs corresponding to tester and driver cDNAs were synthesized from 2 pg of poly(A)+ RNA Isolated from the relevant xenograft tissue, as described above, using CLONTECH's PCR-Select cDNA Subtraction Kit and I pg of oligonucleotide DPNCDN as primer. First- and second strand synthesis were carried out as described In the Kit's user manual protocol (CLONTECH Protocol No. PT1 117-1, Catalog No. K1804-1). The resulting cDNA was digested with Dpn 11 for 3 hrs at 370C. Digested cDNA was extracted with phenol/chloroform (1:1) and ethanol precipitated. Tester cDNA was generated by diluting I p of Dpn 11 digested cDNA from the relevant tissue source (see above) (400 ng) in 5 pd of water. The diluted cDNA (2 pI, 160 ng) was then ligated to 2 pl of Adaptor 1 and Adaptor 2 (10 pM), in separate lIgation reactions, in a total volume of 10 pd at 16C ovemight using 400 pl of T4 DNA ligase (CLONTECH). Ugation was terminated with 1 pd of 0.2 M EDTA and heating at 720C for 5 min. The first hybridization was performed by adding 1.5 p (600 ng) of driver cDNA to each of two tubes containing 1.5 p (20 ng) Adaptor 1- and Adaptor 2-ligated tester cDNA. In a final volume of 4 pi, the samples were overlaid with mineral oil, denatured In an MJ Research thermal cycler at 98KC for 1.5 minutes, and then were allowed to hybridize for 8 hrs at 68oC. The two hybridizations were then mixed together with an additional 1 pd of fresh denatured driver cDNA and were allowed to hybridize overnight at 680C. The second hybridization was then diluted in 200 pd of 20 mM Hepes, pH 8.3, 50 mM NaCl, 0.2 mM EDTA, heated at 7000 for 7 min. and stored at -200C. PCR Amplification. Cloning and Seauencing of Gene Fraaments Generated from SSH: 83 To amplify gene fragments resulting from SSH reactions, two PCR amplifications were performed. In the primary PCR reaction 1 pl of the diluted final hybridization mix was added to 1 p1 of PCR primer 1 (10 pM), 0.5 pl dNTP mix (10 pM), 2.5 p 10 x reaction buffer (CLONTECH) and 0.5 p 50 x Advantage cDNA polymerase Mix (CLONTECH) in a final volume of 25 d. PCR 1 was conducted using the following conditions: 75oC for 5 min., 940C for 25 sec., then 27 cycles of 940C for 10 sec, 6600 for 30 sec, 720C for 1.5 min. Five separate primary PCR reactions were performed for each experiment The products were pooled and diluted 1:10 with water. For the secondary PCR reaction, 1 p1 from the pooled and diluted primary PCR reaction was added to the same reaction mix as used for PCR 1, except that primers NP1 and NP2 (10 pM) were used instead of PCR primer 1. PCR 2 was performed using 10-12 cycles of 940C for 10 sec, 680C for 30 sec, and 720C for 1.5 minutes. The PCR products were analyzed using 2% agarose gel electrophoresis. The POR products were inserted Into pCR2.1 using the T/A vector cloning kit (Invitrogen). Transformed E. coli were subjected to blue/white and ampicillin selection. White colonies were picked and arrayed into 96 well plates and were grown in liquid culture overnight To identify inserts, PCR amplification was performed on 1 pl of bacterial culture using the conditions of PCR1 and NP1 and NP2 as primers. PCR products were analyzed using 2% agarose gel electrophoresis. Bacterial does were stored in 20% glycerol in a 96 well format Plasmid DNA was prepared, sequenced, and subjected to nucleic acid homology searches of the GenBank, dBest and NCl-CGAP databases. RT-PCR Expression Analysis: First strand cDNAs can be generated from 1 pg of mRNA with oligo (dT)12-18 priming using the Gibco-BRL Superscript Preamplification system. The manufacturer's protocol was used which included an incubation for 50 min at 420C with reverse transcriptase followed by RNAse H treatment at 37oC for 20 min. After completing the reaction, the volume can be increased to 200 pl with water prior to normalization. First strand cDNAs from 16 different normal human tissues can be obtained from Clontech. Normalization of the first strand cDNAs from multiple tissues was performed by using the primers 5'ATATCGCCGCGCTCGTCGTCGACAA3' (SEQ ID NO: 52) and 5'AGCCACACGCAGCTCATTGTAGAAGG 3' (SEQ ID NO: 53) to amplify P-actin. First strand cDNAs (5 pi) were amplified in a total volume of 50 p1 containing 0.4 pM primers, 0.2 pM each dNTPs, 1X PCR buffer (Clontech, 10 mM Tris-HCL, 1.5 mM MgCl2, 50 mM KCI, pH8.3) and 1X Klentaq DNA polymerase (Clontech). Five p of the PCR reaction can be removed at 18, 20, and 22 cycles and used for agarose gel electrophoresis. PCR was performed using an MJ Research thermal cycler under the following conditions: Initial denaturation can be at 940C for 15 sec, followed by a 18, 20, and 22 cycles of 940C for 15, 650C for 2 min, 720C for 5 sec. A final extension at 720C was carried out for 2 min. After agarose gel electrophoresis, the band Intensities of the 283 base pair P-actin bands from multiple tissues were compared by visual inspection. Dilution factors for the first strand cDNAs were calculated to result in equal P-actin band intensities in all tissues after 22 cycles of PCR. Three rounds of normalization can be required to achieve equal band intensities in all tissues after 22 cycles of PCR. To determine expression levels of the 109P1 D4 gene, 5 pl of normalized first strand cDNA were analyzed by PCR using 26, and 30 cycles of amplification. Semi-quantitative expression analysis can be achieved by comparing the PCR products at cycle numbers that give light band intensities. The primers used for RT-PCR were designed using the 109P1D4 SSH sequence and are listed below: 109P1D4.1 5'- TGGTCTCAGGTAATTGCTGTTG -3' (SEQ ID NO. 54) 109P1D4.2 5'- CTCCATCAATGTTATGTTGCCTGT -3' (SEQ ID NO' 55) 84 A typical RT-PCR expression analysis is shown in Figure 15. Example 2: Isolation of Full Length 109P1 D4 encoding DNA The 109P1 D4 SSH sequence of 192 bp (Figure 1) exhibited homology to protocadherin 11 (PCDH1 1), a cell adhesion molecule related to the calcium dependent cadherins. The human cDNA sequence encodes a 1021 amino acid protein with an N terminal leader sequence and a transmembrane domain. 109P1D4 v.1 of 4603bp was cloned from human prostate cancer xenograft LAPC-9AD cDNA library, revealing an ORF of 1021 amino acids (Figure 2 and Figure 3). Other variants (Transcript and SNP) of 109P1D4 were also identified and these are listed sequentially in Figure 2 and Figure 3. Example 3: Chromosomal Mapping of 109PID4 Chromosomal localization can implicate genes in disease pathogenesis. Several chromosome mapping approaches are available including fluorescent in situ hybridization (FISH), human/hamster radiation hybrid (RH) panels (Walter et al., 1994; Nature Genetics 7:22; Research Genetics, Huntsville Al), human-rodent somatic cell hybrid panels such as is available from the Coriell Institute (Camden, New Jersey), and genomic viewers utilizing BLAST homologies to sequenced and mapped genomic clones (NCBI, Bethesda, Maryland). 109P1D4 maps to chromosome Xq21.3 using 109P1D4 sequence and the NCBI BLAST tool: located on the Wodld Wide Web at (.ncbi.nlm.nih.gov/genome/seq/page.cgi?F=HsBlasthtml&&ORG=Hs). 109P1D4 was also Identified on chromosome Ypl 1.2, a region of 99% identity to Xq21. Example 4: Expression Analysis of 109P1D4 In Normal Tissues and Patient Spdecimens Expression analysis by RT-PCR and Northern analysis demonstrated that normal tissue expression of a gene of Figure 2 is restricted predominantly to the tissues set forth In Table I. Therapeutic applications for a gene of Figure 2 include use as a small molecule therapy and/or a vaccine (T cell or antibody) target Diagnostic applications for a gene of Figure 2 include use as a diagnostic marker for local and/or metastasized disease. The restricted expression of a gene of Figure 2 in normal tissues makes it useful as a tumor target for diagnosis and therapy. Expression analysis of a gene of Figure 2 provides information useful for predicting susceptibility to advanced stage disease, rate of progression, and/or tumor aggressiveness. Expression status of a gene of Figure 2 in patient samples, tissue arrays and/or cell lines may be analyzed by: (i) immunohistochemical analysis; (ii) In situ hybridization; (ii) RT-PCR analysis on laser capture micro-dissected samples; (iv) Western blot analysis; and (v) Northern analysis. RT-PCR analysis and Northern blotting were used to evaluate gene expression In a selection of normal and cancerous urological tissues. The results are summarized In Figures 15-19. Figure 14 shows expression of 109P1D4 in lymphoma cancer patient specimens. RNA was extracted from peripheral blood lymphocytes, cord blood isolated from normal individuals, and from lymphoma patient cancer specimens. Northern blots with I Opg of total RNA were probed with the 109P1 D4 sequence. Size standards in kilobases are on the side. Results show expression of 109P1 D4 in lymphoma patient specimens but not in the normal blood cells tested. Figure 15 shows expression of 109P1 D4 by RT-PCR. First strand cDNA was prepared from vital pool I (liver, lung and kidney), vital pool 2 (pancreas, colon and stomach), prostate cancer pool, bladder cancer pool, kidney cancer pool, colon cancer pool, lung cancer pool, ovary cancer pool, breast cancer pool, cancer metastasis pool, and pancreas cancer pool. Normalization was performed by PCR using primers to actin and GAPDH. Semi-quantitative PCR, using primers to 109P1 D4, was performed at 30 cycles of amplification. Results show strong expression of 109P1 D4 in all cancer pools 85 tested. Very low expression was detected in the vital pools. Figure 16 shows expression of 109P1D4 in normal tissues. Two multiple tissue northern blots (Clontech), both with 2 pg of mRNAlane, were probed with the 109P1 D4 SSH fragment Size standards in kilobases (kb) are indicated on the side. Results show expression of approximately 10 Dkb 109P1 D4 transcript in ovary. Weak expression was also detected In placenta and brain, but not in the other normal tissues tested. Figure 17 shows expression of 109P1 D4 in human cancer cell lines. RNA was extracted from a number of human prostate and bone cancer ceu lines. Northern blots with 10 pg of total RNAlane were probed with the 109P1D4 SSH fragment Size standards in kilobases (kb) are indicated on the side. Results show expression of 109P1D4 in LAPC-9AD, LAPC-9A, LNCaP prostate cancer cell lines, and in the bone cancer cell lines, SK-ES-1 and RD-ES. Extensive expression of 109P1 D4 In normal tissues is shown in Figure 18A. A cDNA dot blot containing 76 different samples from human tissues was analyzed using a 1091P D4 SSH probe. Expression was only detected In multiple areas of the brain, placenta, ovary, and fetal brain, amongst all tissues tested. Figure 18B shows expression of 109P1D4 in patient cancer specimens. Expression of 109P1D4 was assayed in a panel of human cancers (T) and their respective matched normal tissues (N) on RNA dot blots. Upregulated expression of 109P1D4 In tumors compared to normal tissues was observed in uterus, lung and stomach. The expression detected in normal adjacent tissues (isolated from diseased tissues) but not In normal tissues (isolated from healthy donors) may indicate that these tissues are not fully nonnal and that 109P1D4 may be expressed in early stage tumors. Figure 19 shows 109P1D4 expression in lung cancer patient specimens. RNA was extracted from normal lung, prostate cancer xenograft LAPC-9AD, bone cancer cell line RD-ES, and lung cancer patient tumors. Northern blots with 10 pg of total RNA were probed with 109P1D4. Size standards In kilobases are on the side. Results show strong expression of 109P1D4 in lung tumor tissues as well as the RD-ES cell line, but not in normal lung. The restricted expression of 109P1D4 in normal tissues and the expression detected In cancer patient specimens suggest that 109P1 D4 is a potential therapeutic target and a diagnostic marker for human cancers. Example 5: Splice Variants of 1 09P1D4 Transcript variants are variants of mature mRNA from the same gene which arise by alternative transcription or alternative splicing. Alternative transcripts are transcripts from the same gene but start transcription at different points. Splice variants are mRNA variants spliced differently from the same transcript In eukaryotes, when a multi-exon gene is transcribed from genomic DNA, the initial RNA is spliced to produce functional mRNA, which has only exons and is used for translation into an amino acid sequence. Accordingly, a given gene can have zero to many alternative transcripts and each transcript can have zero to many splice variants. Each transcript variant has a unique exon makeup, and can have different coding and/or non-coding (5' or 3' end) portions, from the original transcript Transcript variants can code for similar or different proteins with the same or a similar function or can encode proteins with different functions, and can be expressed in the same tissue at the same time, or In different tissues at the same time, or in the same tissue at different times, or in different tissues at different times. Proteins encoded by transcript variants can have similar or different cellular or extracellular localizations, e.g., secreted versus intracellular. Transcript variants are Identified by a variety of art-accepted methods. For example, alternative transcripts and splice variants are identified by full-length zoning experiment or by use of full-length transcript and EST sequences. First all human ESTs were grouped into clusters which show direct or Indirect identity with each other. Second, ESTs in the same duster were further grouped Into sub-clusters and assembled into a consensus sequence. The original gene sequence Is compared to the consensus sequence(s) or other full-length sequences. Each consensus sequence is a potential splice 86 variant for that gene. Even when a variant is identified that is not a full-length clone, that portion of the variant is very useful for antigen generation and for further zoning of the full-length splice variant, using techniques known In the art. Moreover, computer programs are available in the art that identify transcript variants based on genomic sequences. Genomic-based transcript variant identification programs include FgenesH (A. Salamov and V. Solovyev, 'Ab initio gene finding in Drosophila genomic DNA," Genome Research. 2000 April;10(4):516-22); Grail (URL compblo.om.gov/Grail-bin/EmptyGralForm) and GenScan (URL genes.mitedu/GENSCAN.html). For a general discussion of splice variant identification protocols see., e.g., Southan, C., A genomic perspective on human proteases, FEBS Lett. 2001 Jun 8; 498(2-3):214-8; de Souza, S.J., et aL, Identification of human chromosome 22 transcribed sequences with ORF expressed sequence tags, Proc. Nati Acad Sci U S A 2000 Nov 7; 97(23):12690-3. To further confirm the parameters of a transcript variant, a variety of techniques are available in the art, such as full-length cloning, proteomic validation, PCR-based validation, and 5' RACE validation, etc. (see e.g., Proteomic Validation: Brennan, S.O., et al., Albumin banks peninsula: a new termination variant characterized by electrospray mass spectrometry, Blochem Biophys Acta. 1999 Aug 17;1433(1-2):321-6; Ferranti P, et a., Differential splicing of pre-messenger RNA produces multiple forms of mature caprine alpha(sl)-casein, Eur J Biochem. 1997 Oct 1;249(1):1-7. For PCR-based Validation: Wellmann S, of aL, Specific reverse transcription-PCR quantification of vascular endothelial growth factor (VEGF) splice variants by UghtCycler technology, Clin Chem. 2001 Apr;47(4):654-60; Jia, H.P., et aL., Discovery of new human beta defensins using a genomics-based approach, Gene. 2001 Jan 24; 263(1-2):211-8. For PCR-based and 5' RACE Validation: Brigle, KE., et al., Organization of the murine reduced folate carrier gene and identification of variant splice forms, Biochem Biophys Acta. 1997 Aug 7; 1353(2): 191-8). It is known In the art that genonic regions are modulated In cancers. When the genomic region to which a gene maps is modulated in a particular cancer, the alternative transcripts or splice variants of the gene are modulated as well. Disclosed herein is that 109P1 D4 has a particular expression profile related to cancer. Alternative transcripts and splice variants of 109P1D4 may also be involved in cancers in the same or different tissues, thus serving as tumor-associated markerslantigens. Using the full-length gene and EST sequences, 8 transcript variants were Identified, designated as 109P1 D4 v.2, v.3, v.4, v.5, v.6, v.7, v.8 and v.9. The boundaries of the exon In the original transcript, 109P1D4 v.1, were shown in Table LI. Compared with 109P1D4 v.1, transcript variant 109P1D4 v.3 has spliced out 2069-2395 from variant 109P1D4 v.1, as shown in Figure 12. Variant 109P1D4 v.4 spliced out 1162-2096 of variant 109P1D4 v.1. Variant 109P1D4 v.5 added one exon to the 5' and extended 2 bp to the 5' end and 288 bp to the 3' end of variant 109P1D4 v.1. Theoretically, each different combination of exons in spatial order, e.g. exon 1 of v.5 and exons I and 2 of v.3 or v.4, is a potential splice variant Tables LII through LV are set forth on a variant-by-variant basis. Tables Lll(a-(h) show nucleotide sequence of the transcript variants. Tables LIlI(a)h) show the alignment of the transcript variants with nuclelc acid sequence of 109P1D4 v.1. Tables LIV(a)-(h) lay out amino acld translation of the transcript variants for the Identified reading frame orientation. Tables LV(a4h) displays alignments of the amino acid sequence encoded by the splice variants with that of 109P1D4 v.1. Example 6: Single Nucleotide Polymorphisms of 109PiD4 A Single Nucleotide Polymorphism (SNP) is a single base pair variation in a nucleotide sequence at a specific location. At any given point of the genome, there are four possible nucleotide base pairs: A/T, C/G, GJC and T/A. Genotype refers to the specific base pair sequence of one or more locations in the genome of an Individual. Haplotype refers to the base pair sequence of more than one location on the same DNA molecule (or the same chromosome in higher organisms), 87 often in the context of one gene or in the context of several tightly linked genes. SNP that occurs on a cDNA is called cSNP. This cSNP may change amino acids of the protein encoded by the gene and thus change the functions of the protein. Some SNP cause inherited diseases; others contribute to quantitative variations in phenotype and reactions to environmental factors including diet and drugs among individuals. Therefore, SNP and/or combinations of alleles (called haplotypes) have many applications, including diagnosis of inherited diseases, determination of drug reactions and dosage, identification of genes responsible for diseases, and analysis of the genetic relationship between individuals (P. Nowotny, J. M. Kwon and A. M. Goate, " SNP analysis to dissect human traits," Curr. Opin. Neurobiol. 2001 Oct 11(5):637-641; M. Pirmohamed and B. K. Park, "Genetic susceptibility to adverse drug reactions,' Trends Pharmacol. Sci. 2001 Jun; 22(6):298-305; J. H. Riley, C. J. Allan, E. Lai and A. Roses, "The use of single nucleotide polymorphisms in the isolation of common disease genes,* Pharmacogenomics. 2000 Feb; 1(1):39-47; R. Judson, J. C. Stephens and A. Windemuth, "The predictive power of haplotypes In clinical response," Pharmacogenomics. 2000 Feb; 1(1):15-26). SNP are Identified by a variety of art-accepted methods (P. Bean, 'The promising voyage of SNP target discovery," Am. Clin. Lab. 2001 Oct-Nov; 20(9):18-20; K M. Weiss, "In search of human variation,' Genome Res. 1998 Jul; 8(7):691 697; M. M. She, "Enabling large-scale pharmacogenetic studies by high-throughput mutation detection and genotyping technologies,' Clin. Chem. 2001 Feb; 47(2):164-172). For example, SNP can be Identified by sequencing DNA fragments that show polymorphism by gel-based methods such as restriction fragment length polymorphism (RFLP) and denaturing gradient gel electrophoresis (DGGE). They can also be discovered by direct sequencing of DNA samples pooled from different individuals or by comparing sequences from different DNA samples. With the rapid accumulation of sequence date in public and private databases, one can discover SNP by comparing sequences using computer programs (Z. Gu, L. Hillier and P. Y. Kwok, 'Single nucleotide polymorphism hunting in cyberspace,' Hum. Mutat. 1998; 12(4):221-225). SNP can be verified and genotype or haplotype of an individual can be determined by a variety of methods Including direct sequencing and high throughput microarrays (P. Y. Kwok, "Methods for genotyping single nucleotide polymorphisms," Annu. Rev. Genomics Hum. Genet. 2001; 2:235-258; M. Kokoris, K. Dix, K. Moynihan, J. Mathis, B. Erwin, P. Grass, B. Hines and A. Duesterhoeft, 'High-throughput SNP genotyping with the Masscode system," Mol. Diagn. 2000 Dec; 5(4):329-340). Using the methods described above, SNP were identified in the original transcript 109P4D4 v.1, and its variants (see Figure 2J and Figure 2K). These alleles of the SNP, though shown separately here, can occur in different combinations (haplotypes) and in any one of the transcript variants (such as 109P4D4 v.4 or v.5) that contains the site of the SNP. Transcript variants v.4 and v.5 contained those SNP in the exons shared with variant v.3, and transcript variant v.9 contained all the SNP occurred in variant v.6 (see Figure 10). Example 7: Production of Recombinant 109P1D4 in Prokaryotic Systems To express recombinant 109P1D4 and 109P1D4 variants in prokaryotic cells, the ful) or partial length 109P1D4. and 109P1 D4 variant cDNA sequences are cloned into any one of a variety of expression vectors known In the art. One or more of the following regions of 109P1 D4 variants are expressed: the full length sequence presented In Figures 2 and 3, or any 8, 9, 10, 11, 12, 13, 14, 15, 16, 17,18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more contiguous amino acids from 109P1 D4, variants, or analogs thereof. A. In vitro transcription and translation constructs: pCRil: To generate 109P1D4 sense and anti-sense RNA probes for RNA in situ investigations, pCRlI constructs (Invitrogen, Carlsbad CA) are generated encoding either all or fragments of the 109P1 D4 cDNA. The pCRlI vector has Sp6 and T7 promoters flanking the Insert to drive the transcription of 109P1D4 RNA for use as probes in RNA in situ hybridization experiments. These probes are used to analyze the cell and tissue expression of 109P1 D4 at the RNA level. Transcribed 88 109P1D4 RNA representing the cDNA amino acid coding region of the 109P1 D4 gene is used in in vitro translation systems such as the TnTm Coupled Reticulolysate System (Promega, Corp., Madison, WI) to synthesize 109P104 protein. B. Bacterial Constructs: pGEX Constructs: To generate recombinant 109P1D4 proteins in bacteria that are fused to the Glutathione S transferase (GST) protein, all or parts of the 109P1D4 cDNA protein coding sequence are cloned into the pGEX family of GST-fusion vectors (Amersham Pharmacia Biotech, Piscataway, NJ). These constructs allow controlled expression of recombinant 109P1 D4 protein sequences with GST fused at the amino-terminus and a six histidine epitope (6X His) at the carboxyl-terminus. The GST and 6X His tags permit purification of the recombinant fusion protein from induced bacteria with the appropriate affinity matrix and allow recognition of the fusion protein with anti-GST and anti-His antibodies. The 6X His tag is generated by adding 6 histidine codons to the cloning primer at the 3' end, e.g., of the open reading frame (ORF). A proteolytic cleavage site, such as the PreScisslonm recognition site in pGEX-6P-1, may be employed such that it permits cleavage of the GST tag from 109P1D4-related protein. The ampicillin resistance gene and pBR322 origin permits selection and maintenance of the pGEX plasmids In E. coli. pMAL Constructs: To generate, in bacteria, recombinant 109P1D4 proteins that are fused to maltose-binding protein (MBP), all or parts of the 109P1D4 cDNA protein coding sequence are fused to the MBP gene by doning into the pMAL-c2X and pMAL-p2X vectors (New England Biolabs, Beverly, MA). These constructs allow controlled expression of recombinant 109P1D4 protein sequences with MBP fused at the amino-terminus and a 6X His epitope tag at the carboxyl terminus. The MBP and 6X His tags permit purification of the recombinant protein from Induced bacteria with the appropriate affinity matrix and allow recognition of the fusion protein with anti-MBP and anti-His antibodies. The 6X His epitope tag is generated by adding 6 histidine codons to the 3' cloning primer. A Factor Xa recognition site permits cleavage of the pMAL tag from 109P1D4. The pMAL-c2X and pMAL-p2X vectors are optimized to express the recombinant protein in the cytoplasm or periplasm respectively. Periplasm expression enhances folding of proteins with disulfide bonds. In one embodiment, amino acids 24-419 of 109P1D4 variant I was cloned into the pMAL-c2X vector and was used to express the fusion protein. pET Constructs: To express 109P1D4 in bacterial cells, all or parts of the 109P1D4 cONA protein coding sequence are cloned into the pET family of vectors (Novagen, Madison, WI). These vectors allow tightly controlled expression of recombinant 109P1 D4 protein in bacteria with and without fusion to proteins that enhance solubility, such as NusA and thioredoxin (Trx), and epitope tags, such as 6X His and S-Tag "m that aid purification and detection of the recombinant protein. For example, constructs are made utilizing pET NusA fusion system 43.1 such that regions of the 109P1D4 protein are expressed as amino-terminal fusions to NusA. In 2 embodiments, amino acids 24-419 and 24-815 were cloned into pET43.1 vector and used to express the fusion protein. C. Yeast Constructs: pESC Constructs: To express 109P1 D4 in the yeast species Saccharomyces cerevislae for generation of recombinant protein and functional studies, all or parts of the 109P1 D4 cDNA protein coding sequence are cloned into the pESC family of vectors each of which contain I of 4 selectable markers, HIS3, TRP1, LEU2, and URA3 (Stratagene, La Jolla, CA). These vectors allow controlled expression from the same plasmid of up to 2 different genes or cloned sequences containing either FlagTU or Myc epitope tags in the same yeast cell. This system is useful to confirm protein-protein Interactions of 109P1 D4. In addition, expression in yeast yields similar post-translational modifications, such as glycosylations and phosphorylations, that are found when expressed in eukaryotic cells. DESP Constructs: To express 109P1 D4 In the yeast species Saccharmnyces pombe, all or parts of the 109P1 D4 cDNA protein coding sequence are cloned into the pESP family of vectors. These vectors allow controlled high level of 89 expression of a 109P1D4 protein sequence that is fused at either the amino terminus or at the carboxyl terminus to GST which aids purification of the recombinant protein. A FlagTmepitope tag allows detection of the recombinant protein with anti FlagTm antibody. Example 8: Production of Recombinant 109PiD4 In Higher Eukaryotic Systems A. Mammalian Constructs: To express recombinant 109P1D4 in eukaryotic cells, the full or partial length 109P1D4 cDNA sequences were cloned into any one of a variety of expression vectors known in the art One or more of the following regions of 109P1D4 were expressed in these constructs, amino acids I to 1021 or any 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more contiguous amino acids from 109P1D4 v.1; amino acids I to 1054, 1 to 1347, I to 1337, 1 to 1310, 1 to 1037, 1 to 1048, 1 to 1340 of v.2, v.3, v.4, v.5, v.6, v.7, and v.8 respectively; or any 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more contiguous amino acids from 109P1D4 variants, or analogs thereof. The constructs can be transfected into any one of a wide variety of mammalian cells such as 293T cells. Transfected 293T cell lysates can be probed with the anti-109P1D4 polyclonal serum, described herein. pcDNA4/HisMax Constructs: To express 109P1D4 in mammalian cells, a 109P1D4 ORF, or portions thereof, of 109P1D4 are cloned into pcDNA4/HisMax Version A (Invitrogen, Carlsbad, CA). Protein expression is driven from the cytomegalovirus (CMV) promoter and the SP16 translational enhancer. The recombinant protein has XpressUI and six histidine (6X His) epitopes fused to the amino-terminus. The pcDNA4/HisMax vector also contains the bovine growth hormone (BGH) polyadenylation signal and transcription termination sequence to enhance mRNA stability along with the SV40 origin for episomal replication and simple vector rescue in cell lines expressing the large T antigen. The Zeocin resistance gene allows for selection of mammalian cells expressing the protein and the ampicillin resistance gene and ColE 1 origin permits selection and maintenance of the plasmid in E coli. pcDNA3,lMycHis Constructs: To express 109P1 D4 in mammalian cels, a 109P1 D4 ORF, or portions thereof, of 109P1D4 with a consensus Kozak translation initiation site was doned into pcDNA3.1/Mycl-is Version A (Invitrogen, Carlsbad, CA). Protein expression is driven from the cytomegalovirus (CMV) promoter. The recombinant proteins have the myc epitope and 6X His epitope fused to the carboxyl-terminus. The pcDNA3.lMycHls vector also contains the bovine growth hormone (BGH) polyadenylation signal and transcription termination sequence to enhance mRNA stability, along with the SV40 origin for episomal replication and simple vector rescue in cell lines expressing the large T antigen. The Neomycin resistance gene can be used, as It allows for selection of mammalian cells expressing the protein and the ampicillin resistance gene and CoIl origin permits selection and maintenance of the plasmid in E. col. The complete ORF of 109P1 D4 v.1 was cloned into the pcDNA3.1/MycHls construct to generate 109P1D4.pcDNA3.1/MycHis. pcDNA3,I/CT-GFP-TOPO Construct: To express 109P1D4 in mammalian cells and to allow detection of the recombinant proteins using fluorescence, a 109P1 04 ORF, or portions thereof, with a consensus Kozak translation Initiation site are cloned into pcDNA3.1/CT-GFP-TOPO (Invitrogen, CA). Protein expression is driven from the cytomegalovirus (CMV) promoter. The recombinant proteins have the Green Fluorescent Protein (GFP) fused to the carboxyl-terminus facilitating non-Invasive, In vo detection and cell biology studies. The pcDNA3.1CT-GFP-TOPO vector also contains the bovine growth hormone (BGH) polyadenylation signal and transcription termination sequence to enhance mRNA stability along with the SV40 origin for episomal replication and simple vector rescue in cell lines expressing the large T antigen. The 90 Neomycin resistance gene allows for selection of mammalian cells that express the protein, and the ampicillin resistance gene and ColE1 origin permits selection and maintenance of the plasmid in E. coli. Additional constructs with an amino terminal GFP fusion are made In pcDNA3.1/NT-GFP-TOPO spanning the entire length of a 109P1D4 protein. PAPtag: A 109P1D4 ORF, or portions thereof, is cloned Into pAPtag-5 (GenHunter Corp. Nashville, TN). This construct generates an alkaline phosphatase fusion at the carboxyl-terminus of a 109P1D4 protein while fusing the igGK signal sequence to the amino-terminus. Constructs are also generated in which alkaline phosphatase with an amino terminal IgGK signal sequence Is fused to the amino-terminus of a 109P1D4 protein. The resulting recombinant 109P1D4 proteins are optimized for secretion into the media of transfected mammalian cells and can be used to identify proteins such as ligands or receptors that Interact with 109P1 D4 proteins. Protein expression is driven from the CMV promoter and the recombinant proteins also contain myc and 6X His epitopes fused at the carboxyl-terminus that facilitates detection and purification. The Zeocin resistance gene present in the vector allows for selection of mammalian cells expressing the recombinant protein and the ampicillin resistance gene permits selection of the plasmid in E coli. DTaa5: A 109P1D4 ORF, or portions thereof, were cloned into pTag-5. This vector is similar to pAPtag but without the alkaline phosphatase fusion. This construct generated 109P1D4 protein with an amino-terminal igGK signal sequence and myc and 6X His epitope tags at the carboxyl-terminus that facilitate detection and affinity purification. The resulting recombinant 109P1D4 protein was optimized for secretion Into the media of transfected mammalian cells, and was used as immunogen or ligand to identify proteins such as ligands or receptors that interact with the 109P1 D4 proteins. Protein expression is driven from the CMV promoter. The Zeocin resistance gene present in the vector allows for selection of mammalian cells expressing the protein, and the ampicillin resistance gene permits selection of the plasmid in E. coli. PsecFc: A 109P1 D4 ORF, or portions thereof, Is also cloned into psecFc. The psecFc vector was assembled by cloning the human immunoglobulin Gi (IgG) Fc (hinge, CH2, CH3 regions) into pSecTag2 (Invitrogen, California). This construct generates an IgG1 Fc fusion at the carboxyl-terminus of the 109P1 D4 proteins, while fusing the IgGK signal sequence to N-terminus. 109P1D4 fusions utilizing the murine IgG1 Fc region are also used. The resulting recombinant 109P1D4 proteins are optimized for secretion into the media of transfected mammalian cells, and can be used as immunogens or to identify proteins such as ligands or receptors that interact with 109P1 D4 protein. Protein expression is driven from the CMV promoter. The hygromycin resistance gene present in the vector allows for selection of mammalian cells that express the recombinant protein, and the ampicillin resistance gene permits selection of the plasmid in E. co. pSRx Constructs: To generate mammalian cell lines that express 109P1 D4 constitutively, 109P1 D4 ORF, or portions thereof, were cloned into pSRa constructs. Amphotropic and ecotropic retroviruses were generated by transfection of pSRa constructs into the 293T-10A1 packaging line or co-transfection of pSRa and a helper plasmid (containing deleted packaging sequences) into the 293 cells, respectively. The retrovirus is used to infect a variety of mammalian celi Ones, resulting in the Integration of the cloned gene, 109P1D4, into the host cell-lines. Protein expression Is driven from a long terminal repeat (LTR). The Neomycin resistance gene present In the vector allows for selection of mammalian cells that express the protein, and the ampicillin resistance gene and ColEl origin permit selection and maintenance of the plasmid In E coil. The retroviral vectors can thereafter be used for infection and generation of various cell lines using, for example, PC3, NIH 3T3, TsuPri, 293 or rat-1 cells. Additional pSRct constructs are made that fuse an epitope tag such as the FLAGTm tag to the carboxyl-terminus of 109P1D4 sequences to allow detection using anti-Flag antibodies. For example, the FLAGM sequence 5' GAT TAC AAG GAT GAC GAC GAT AAG 3' (SEQ ID NO: 56) is added to cloning primer at the 3' end of the ORF. Additional pSRcL constructs are made to produce both amino-terminal and carboxyl-terminal GFP and myc/6X His fusion proteins of the full length 109P1D4 proteins.

91 Additional Viral Vectors: Additional constructs are made for viral-mediated delivery and expression of 109P1 D4. High virus titer leading to high level expression of 109P1D4 is achieved In viral delivery systems such as adenoviral vectors and herpes amplicon vectors. A 109P1D4 coding sequence or fragments thereof are amplified by PCR and subcloned Into the AdEasy shuttle vector (Stratagene). Recombination and virus packaging are performed according to the manufacturers instructions to generate adenoviral vectors. Alternatively, 109P1 D4 coding sequences or fragments thereof are cloned into the HSV-1 vector (lmgenex) to generate herpes viral vectors. The viral vectors are thereafter used for infection of various cell lines such as PC3, NIH 3T3, 293 or rat-1 cells. Regulated Expression Systems: To control expression of 109P1 D4 In mammalian cells, coding sequences of 109P1 D4, or portions thereof, are cloned into regulated mammalian expression systems such as the T-Rex System (Invitrogen), the GeneSwitch System (Invitrogen) and the tightly-regulated Ecdysone System (Stratagene). These systems allow the study of the temporal and concentration dependent effects of recombinant 109P1 D4. These vectors are thereafter used to control expression of 109P1D4 in various cell lines such as PC3, NIH 3T3, 293 or rat-1 cells. B. Baculovirus Expression Systems To generate recombinant 109P1D4 proteins in a baculovirus expression system, 109P1D4 ORF, or portions thereof, are cloned into the baculovirus transfer vector pBlueBac 4.5 (Invitrogen), which provides a His-tag at the N-terminus. Specifically, pBlueBac-109P1D4 is co-transfected with helper plasmid pBac-N-Blue (Invitrogen) into SF9 (Spodoptera frugiperda) insect cells to generate recombinant baculovirus (see Invilrogen Instruction manual for details). Baculovirus is then collected from cell supernatant and purified by plaque assay. Recombinant 1 09P1 D4 protein is then generated by infection of HighFive insect cells (Invitrogen) with purified baculovirus. Recombinant 109P1D4 protein can be detected using anti-109P1D4 or anti-His-tag antibody. 109P1D4 protein can be purified and used in various cell-based assays or as immunogen to generate polyclonal and monoclonal antibodies specific for 109P1D4. Example 9: Antigenicity Profiles and Secondary Structure Figure(s) 5A-l, Figure 6A-l, Figure 7A-1, Figure 8A-l, and Figure 9A-l depict graphically five amino acid profiles of 109P1 D4 variants 1 through 9, each assessment available by accessing the ProtScale website located on the World Wide Web at (.expasy.ch/cgi-bn/protscae.p) on the ExPasy molecular biology server. These profiles: Figure 5, Hydrophiuicity, (Hopp T.P., Woods K.R., 1981. Proc. Nai. Acad. Sci. U.S.A. 78:3824 3828); Figure 6, Hydropathicity, (Kyle J., Doolittle R.F., 1982. J. Mol. Biol. 157:105-132); Figure 7, Percentage Accessible Residues (Janin J., 1979 Nature 277.491-492); Figure 8, Average Flexibility, (Bhaskaran R., and Ponnuswamy P.K., 1988. Int J. Pept Protein Res. 32:242-255); Figure 9, Beta-tum (Deleage, G., Roux B. 1987 Protein Engineering 1:289-294); and optionally others available In the art, such as on the ProtScale website, were used to identify antigenic regions of each of the 109P1 D4 variant proteins. Each of the above amino acid profiles of 109P1 D4 variants were generated using the following ProtScale parameters for analysis: 1) A window sIze of 9; 2) 100% weight of the window edges compared to the window center; and, 3) amino acid profile values normalized to lie between 0 and 1. Hydrophilicity (Figure 5), Hydropathicity (Figure 6) and Percentage Accessible Residues (Figure 7) profiles were used to determine stretches of hydrophilic amino acids (i.e., values greater than 0.5 on the Hydrophilicity and Percentage Accessible Residues profile, and values less than 0.5 on the Hydropathicity profile . Such regions are likely to be exposed to the aqueous environment, be present on the surface of the protein, and thus available for immune recognition, such as by antibodies. Average Flexibility (Figure 8) and Beta-tum (Figure 9) profiles determine stretches of amino acids (i.e., values 92 greater than 0.5 on the Beta-tum profile and the Average Flexibility profile) that are not constrained in secondary structures such as beta sheets and alpha helices. Such regions are also more likely to be exposed on the protein and thus accessible to Immune recognition, such as by antibodies. Antigenic sequences of the 109P1D4 variant proteins indicated, e.g., by the profiles set forth in Figure 5, Figure 6, Figure 7, Figure 8, and/or Figure 9 are used to prepare immunogens, either peptides or nuceic acids that encode them, to generate therapeutic and diagnostic anti-109P1D4 antibodies. The Immunogen can be any 5, 6, 7, 8, 9, 10,11,12,13,14, 15, 16,17, 18, 19, 20, 21, 22, 23, 24, 25, 30, 35,40,45, 50 or more than 50-contiguous amino acids, or the corresponding nudeic adds that encode them, from the 109P1D4 protein variants listed in Figures 2 and 3. In particular, peptide immunogens of the Invention can comprise, a peptide region of at least 5 amino acids of Figures 2 and 3 in any whole number Increment that Includes an amino acid position having a value greater than 0.5 in the Hydrophilicity profiles of Figure 5; a peptide region of at least 5 amino acids of Figures 2 and 3 in any whole number increment that includes an amino acid position having a value less than 0.5 in the Hydropathicity profile of Figure 6 ; a peptide region of at least 5 amino adds of Figures 2 and 3 in any whole number increment that includes an amino acid position having a value greater than 0.5 in the Percent Accessible Residues profiles of Figure 7; a peptide region of at least 5 amino acids of Figures 2 and 3 in any whole number increment that includes an amino add position having a value greater than 0.5 in the Average Flexibility profiles on Figure 8; and, a peptide region of at least 5 amino acids of Figures 2 and 3 in any whole number increment that includes an amino acid position having a value greater than 0.5 in the Beta-turn profile of Figures 9. Peptide immunogens of the Invention can also comprise nucleic acids that encode any of the forgoing. All immunogens of the invention, peptide or nucleic acid, can be embodied in human unit dose form, or comprised by a composition that includes a pharmaceutical excipient compatible with human physiology. The secondary structure of 109P1 D4 protein variants, namely the predicted presence and location of alpha helices, extended strands, and random coils, are predicted from the primary amino acid sequence using the HNN -Hierarchical Neural Network method (NPS@: Network Protein Sequence Analysis TIBS 2000 March Vol. 25, No 3 [2911:147-150 Combet C., Blanchet C., Geouijon C. and Delbage G., http'J/pbil.ibcp.fr/cgi-binpsa.automat.pl?page=npsa-nn.htm), accessed from the ExPasy molecular biology server located on the World Wide Web at (www.expasy.chltools). This analysis for protein variants I through 9 are shown in Figure 13A through 131 respectively. The percent of structure for each variant comprised of alpha helix, extended strand, and random coil is also Indicated. Analysis for the potential presence of Iransmembrane domains in 109P1 D4 variant proteins was carried out using a variety of transmembrane prediction algorithms accessed from the ExPasy molecular biology server located on the Wold Wide Web at (www.expasy.ch/tools/. Shown graphically in figures 13J-R are the results of analyses using the TMpred program (top panels) and the TMHMM program (bottom panels) of 109P1 D4 protein variants I through 9 respectively. Analyses of the variants using other structural prediction programs are summarized in Table VI and Table L Example 10: Generation of 109P1D4 Polyclonal Antibodies Polyclonal antibodies can be raised in a mammal, for example, by one or more Injections of an immunizing agent and, if desired, an adjuvant Typically, the Immunizing agent and/or adjuvant will be injected in the mammal by multiple subcutaneous or Intraperitoneal injections. In addition to immunizing with a full length 109P1D4 protein vacant, computer algorithms are employed In design of Immunogens that based on amino acid sequence analysis contain characteristics of being antigenic and available for recognition by the Immune system of the immunized host (see the Example entitled "Antigenicity Profiles and Secondary Structure"). Such regions would be predicted to be hydrophilic, flexible, in beta-tum conformations, and be exposed on the surface of the protein (see, e.g., Figure 5, Figure 6, Figure 7, Figure 8, or Figure 9 for 93 amino acid profiles that indicate such regions of 109P1D4 protein variant 1). For example, recombinant bacterial fusion proteins or peptides containing hydrophilic, flexible, beta-tum regions of 109P1D4 protein variants are used as antigens to generate polyclonal antibodies in New Zealand White rabbits or monoclonal antibodies as described In the example entided Generation of 109P1D4 Monoclonal Antibodies (mAbs)'. For example, in 109P1D4 variant 1, such regions include, but are not limited to, amino acids 22-39, amino acids 67-108, amino acids 200-232, amino acids 454-499, amino acids 525-537, amino acids 640-660, amino acids 834-880, and amino acids 929-942. it is useful to conjugate the immunizing agent to a protein known to be immunogenic in the mammal being immunized. Examples of such immunogenic proteins include, but are not limited to, keyhole limpet hemocyanin (KLH), serum albumin, bovine thyroglobulin, and soybean trypsin inhibitor. In 2 embodiments, peptides encoding amino acids 77-90 and amino acids 929-942 of 109P1D4 variant 1 were synthesized, conjugated to KLH, and used to Immunize separate rabbits. Alternatively the immunizing agent may Include all or portions of the 109P1D4 variant proteins, analogs or fusion proteins thereof. For example, the 109P1 D4 variant 1 amino acid sequence can be fused using recombinant DNA techniques to any one of a variety of fusion protein partners that are well known in the art, such as glutathione-S-transferase (GST) and HIS tagged fusion proteins. In 1 embodiment, amino acids 24-419 of 109P1D4 variant 1 was fused to NUSa using recombinant techniques and the pET43.1 expression vector, expressed, purified and used to immunize a rabbit Such fusion proteins are purified from induced bacteria using the appropriate affinity matrix. Other recombinant bacterial fusion proteins that may be employed Include maltose binding protein, LacZ, thioredoxin, NusA, or an immunoglobulin constant region (see the section entitled "Production of 109P1D4 in Prokaryotic Systems" and Current Protocols In Molecular Biology, Volume 2, Unit 16, Frederick M. Ausubul et al. eds., 1995; Linsley, P.S., Brady, W., Umes, M., Grosmaire, L, Damle, N., and Ledbetter, J.(1991) J.Exp. Med. 174, 561-566). In addition to bacterial derived fusion proteins, mammalian expressed protein antigens are also used. These antigens are expressed from mammalian expression vectors such as the Tag5 and Fc-fusion vectors (see the section entitled "Production of Recombinant 109P1D4 in Eukaryotic Systems"), and retain post-translational modifications such as glycosylations found In native protein. In one embodiment, amino acids 24-812 of 109P1D4 variant 1 was cloned Into the Tag5 mammalian secretion vector, and expressed in 293T cells (See Figure 20). The recombinant protein is purified by metal chelate chromatography from Ussue culture supematants of 293T cells stably expressing the recombinant vector. The purified Tag5 109P1D4 protein is then used as immunogen. During the immunization protocol, it Is useful to mix or emulsify the antigen in adjuvants that enhance the immune response of the host animal. Examples of adjuvants include, but are not limited to, complete Freund's adjuvant (CFA) and MPL-TDM adjuvant (monophosphoryl Lipid A, synthetic trehalose dicorynomycolate). In a typical protocol, rabbits are initially immunized subcutaneously with up to 200 jpg, typically 100-200 pg, of fusion protein or peptide conjugated to KLH mixed in complete Freund's adjuvant (CFA). Rabbits are then injected subcutaneously every two weeks with up to 200 pg, typically 100-200 pg, of the immunogen in incomplete Freund's adjuvant (IFA). Test bleeds are taken approximately 7-10 days following each immunization and used to monitor the titer of the antiserum by ELISA. To test reactivity and specificity of immune serum, such as the rabbit serum derived from immunization with the NUSa-fusion of 109P1D4 variant I protein, the ful-length 109P1 D4 variant I cDNA is cloned into pCDNA 3.1 myo-his expression vector (Invitrogen, see the Example entitled 'Production of Recombinant 109P1D4 in Eukaryotic Systems"). After transfection of the constructs into 293T cells, cell lysates are probed with the anti-109P1D4 serum to determine specific reactivity to denatured 109P1D4 protein using the Western blot technique. Probing with anti-His antibody serves as a positive control for expression of 109P1D4 in the transfected cells (See Figure 21). In addition, the immune serum is tested 94 by fluorescence microscopy, flow cytometry and immunoprecipitation against 293T and other recombinant 109P1D4 expressing cells to determine specific recognition of native protein. Western blot, immunoprecipitation, fluorescent microscopy, and flow cytometric techniques using cells that endogenously express 109P1 D4 are also carried out to test reactivity and specificity. Anti-serum from rabbits immunized with 109P1D4 variant fusion proteins, such as GST and MBP fusion proteins, are purified by depletion of antibodies reactive to the fusion partner sequence by passage over an affinity column containing the fusion partner either alone or in the context of an irrelevant fusion protein. For example, antserum derived from a NUSa 109P1D4 variant 1 fusion protein is first purified by passage over a column of MBP protein covalently coupled to AffiGel matrix (BioRad, Hercules, Calif.). The antiserum is then affinity purified by passage over a column composed of a NUSa 109P1D4 fusion protein covalently coupled to Affigel matrix. The serum is then further purified by protein G affinity chromatography to isolate the IgG fraction. Sera from other His-tagged antigens and peptide immunized rabbits as well as fusion partner depleted sera are affinity purified by passage over a column matrix composed of the original protein Immunogen or free peptide. Example 11: Generation of 109PiD4 Monoclonal Antibodies (mAbs) In one embodiment, therapeutic mAbs to 109P1 D4 variants comprise those that react with epitopes specific for each variant protein or specific to sequences in common between the variants that would disrupt or modulate the biological function of the 109P1D4 variants, for example those that would disrupt the interaction with ligands and binding partners. Immunogens for generation of such mAbs indude those designed to encode or contain the entire 109P1D4 protein variant sequence, regions predicted to contain functional motifs, and regions of the 109P1D4 protein variants predicted to be antigenic from computer analysis of the amino acid sequence (see, e.g., Figure 5, Figure 6, Figure 7, Figure 8, or Figure 9, and the Example entitled 'Antigenicity Profiles and Secondary Structure"). Immunogens include peptides, recombinant bacterial proteins, and mammalian expressed Tag 5 proteins and human and murine IgG FC fusion proteins. In addition, cells engineered to express high levels of a respective 109P1D4 variant, such as 293T-109P1D4 variant 1 or 300.19 109P1D4 variant 1murine Pre-B cells, are used to immunize mice. To generate mAbs to a 109P1D4 variant, mice are first immunized intraperitoneally (IP) with, typically, 10-50 pg of protein immunogen or 107 109P1D4-expressing cells mixed In complete Freund's adjuvant Mice are then subsequently immunized IP every 2-4 weeks with, typically, 10-50 pg of protein immunogen or 107 cells mixed in incomplete Freund's adjuvant Alternatively, MPL-TDM adjuvant Is used In immunizations. In addition to the above protein and cell-based Immunization strategies, a DNA-based Immunization protocol is employed in which a mammalian expression vector encoding a 109P1 D4 variant sequence Is used to Immunize mice by direct injection of the plasmid DNA. For example, amino acids 24-812 of 109P1D4 of variant I Is cloned Into the Tag5 mammalian secretion vector and the recombinant vector will then be used as immunogen. In another example the same amino acids are cloned into an Fc-fusion secretion vector in which the 109P1 D4 variant I sequence is fused at the amino-terminus to an IgK leader sequence and at the carboxyl terminus to the coding sequence of the human or murine IgG Fc region. This recombinant vector Is then used as Immunogen. The plasmid Immunization protocols are used In combination with purified proteins expressed from the same vector and with cells expressing the respective 109P1D4 variant Alternatively, mice may be immunized directly into their foolpads. In this case, 10-50 pg of protein immunogen or 107 254P1D6B-expressing cells are injected sub-cutaneously into the footpad of each hind leg. The first Immunization is given with Titermax (SigmaTI) as an adjuvant and subsequent injections are given with Alum-gel In conjunction with CpG oigonucleotide sequences with the exception of the final injection which is given with PBS. Injections are given twice weekly 95 (every three to four days) for a period of 4 weeks and mice are sacrificed 3-4 days after the final injection, at which point lymph nodes immediately draining from the footpad are harvested and the B-cells are collected for use as antibody producing fusion partners. During the immunization protocol, test bleeds are taken 7-10 days following an injection to monitor titer and specificity of the immune response. Once appropriate reactivity and specificity is obtained as determined by ELISA, Western blotting, immunoprecipitation, fluorescence microscopy, and flow cytometidc analyses, fusion and hybidoma generation is then carried out with established procedures well known in the art (see, e.g., Hartow and Lane, 1988). In one embodiment for generating 109P1 D4 monoclonal antibodies, a Tag5 antigen of variant I encoding amino acids 14-812 is expressed in 293T cells and purified from conditioned media. Balb C mice are initially immunized intraperitoneally with 25 pg of the Tag5 109P1 D4 variant I protein mixed In complete Freund's adjuvant. Mice are subsequently immunized every two weeks with 25 pg of the antigen mixed In incomplete Freund's adjuvant for a total of three immunizations. ELISA using the Tag5 antigen determines the titer of serum from immunized mice. Reactivity and specificity of serum to full length 109P1 D4 variant I protein Is monitored by Western blotting, immunoprecipitation and flow cytometry using 293T cells transfected with an expression vector encoding the 109P1D4 vacant 1 cDNA (see e.g., the Example entitled 'Production of Recombinant 109P1D4 in Higher Eukaryotic Systems" and Figure 21). Other recombinant 109P1D4 variant 1-expressing cells or cells endogenously expressing 109P1D4 variant 1 are also used. Mice showing the strongest reactivity are rested and given a final Injection of antigen In PBS and then sacrificed four days later. The spleens of the sacrificed mice are harvested and fused to SPO/2 myeloma cells using standard procedures (Haulow and Lane, 1988). Supematants from HAT selected growth wells are screened by ELISA, Western blot, Immunoprecipitation, fluorescent microscopy, and Row cytometry to identify 109P1D4 specific antibody-producing clones. To generate monoclonal antibodies that are specific for a 109P1D4 variant protein, immunogens are designed to encode sequences unique for each variant In one embodiment, an antgenic peptide composed of amino acids 1-29 of 109P1D4 variant 2 Is coupled to KLH to derive monoclonal antibodies specific to 109P1D4 variant 2. In another embodiment, an antigenic peptide comprised of amino acids 1-23 of 109P1 D4 variant 6 is coupled to KLH and used as immunogen to derive varalant 6 specific MAbs. In another example, a GST-fusion protein encoding amino acids 1001-1347 of variant 3 Is used as immunogen to generate antibodies that would recognize variants 3, 4, 5, and 8, and distinguish them from variants 1, Z 6, 7and 9. Hybridoma supematants are then screened on the respective antigen and then further screened on cells expressing the specific variant and cross-screened on cells expressing the other variants to derive variant specific monoclonal antibodies. The binding affinity of 109P1D4 variant specific monoclonal antibodies are determIned using standard technologies. Affinity measurements quantify the strength of antibody to epitope binding and are used to help define which 109P1D4 variant monoclonal antibodies preferred for diagnostic or therapeutic use, as appreciated by one of skill in the art. The BlAcore system (Uppsala, Sweden) is a preferred method for determining binding affinity. The BlAcore system uses surface plasmon resonance (SPR, Welford K 1991, Opt Quant Elect 23:1; Morton and Myszka, 1998, Methods in Enzymology 295: 268) to monitor blomolecular Interactions in real time. BlAcore analysis conveniently generates association rate constants, dissociation rate constants, equilibrium dissociation constants, and affinity constants. Alternatively, equilibrium binding analysis of MAbs on 109P1D4-expressing cells can be used to determine affinity. Example 12: HLA Class I and Class i Binding Assays HLA class I and class I binding assays using purified HLA molecules are performed in accordance with disposed protocols (e.g., PCT publications WO 94/20127 and WO 94/03205; Sidney et al., Current Protocols In Immunology 18.3.1 96 (1998); Sidney, et aL, J. Immuno. 154:247 (1995); Sette, et at., Mol. Immunol. 31:813 (1994)). Briefly, purified MHC molecules (5 to 500 nM) are incubated with various unlabeled peptide inhibitors and 1-10 nM Wadiolabeled probe peptides as described. Following incubation, MHC-peptide complexes are separated from free peptide by gel filtration and the fraction of peptide bound is determined. Typically, in preliminary experiments, each MHC preparation Is titered In the presence of fixed amounts of radiolabeled peptides to determine the concentration of HLA molecules necessary to bind 10 20% of the total radioactivity. Al subsequent inhibition and direct binding assays are performed using these HLA concentrations. Since under these conditions Yabe]<[HLA] and lCse[HLA], the measured ICso values are reasonable approximations of the true Ko values. Peptide Inhibitors are typically tested at concentrations ranging from 120 pg/mI to 1.2 nglml, and are tested In two to four completely Independent experiments. To allow comparison of the data obtained in different experiments, a relative binding figure is calculated for each peptide by dividing the lC9o of a positive control for Inhibition by the lCso for each tested peptide (typically unlabeled versions of the radiolabeled probe peptide). For database purposes, and inter-experiment comparisons, relative binding values are compiled. These values can subsequently be converted back Into ICso nM values by dividing the lCso nM of the positive controls for Inhibition by the relative binding of the peptide of Interest This method of data compilation Is accurate and consistent for comparing peptides that have been tested on different days, or with different lots of purified MHC. Binding assays as outlined above may be used to analyze HLA supermotif and/or HLA motif-bearing peptides (see Table IV). Example 13: Identification of HLA Supermotif- and Motif-BearIng CTL Candidate Epitopes HLA vaccine compositions of the invention can Include multiple epitopes. The multiple epitopes can comprise multiple HLA supermotifs or motifs to achieve broad population coverage. This example illustrates the identification and confirmation of supermotif- and motif-bearing epitopes for the inclusion in such a vaccine composition. Calculation of population coverage is performed using the strategy described below. Computer searches and algorithms for identification of supermotif and/or moluf-bearing epitopes The searches performed to identify the motif-bearing peptide sequences in the Example entitled "Antgenicity Profiles" and Tables Vill-XXI and XXJI-XLIX employ the protein sequence data from the gene product of 109P1D4 set forth in Figures 2 and 3, the specific search peptides used to generate the tables are listed in Table Vl. Computer searches for epitopes bearing HLA Class I or Class If supermotifs or motifs are performed as follows. All translated 109P1D4 protein sequences are analyzed using a text string search software program to identify potential peptide sequences containing appropriate HLA binding motifs; such programs are readily produced in accordance with information in the art in view of known motif/supermotif disclosures. Furthermore, such calculations can be made mentally. Identified A2-, A3-, and DR-supermotif sequences are scored using polyroial algorithms to predict their capacity to bind to specific HLA-Class I or Class Il molecules. These polynomial algorithms account for the Impact of different amino acids at different positions, and are essentially based on the premise that the overall affinity (or AG) of peptide-HLA molecule interactions can be approximated as a linear polynomial funclon of the type: "G'= ai x a2 x av...... x as where aV is a coefficient which represents the effect of the presence of a given amino acid (j) at a given position (I) along the sequence of a peptide of n amino acids. The crucial assumption of this method is that the effects at each position are essentially Independent of each other (I.e., Independent binding of Individual side-chains). When residue j occurs at position I in the pepide, it is assumed to contribute a constant amount Jf to the free energy of binding of the peptide 97 irrespective of the sequence of the rest of the peptide. The method of derivation of specific algorithm coefficients has been described in Gulukota et aL., J. MoL Biol. 267:1258-126,1997; (see also Sidney et a., Human Immunol. 45:79-93,1996; and Southwood et a., J. ImmunoL 160:3363 3373, 1998). Briefly, for all I positions, anchor and non-anchor alike, the geometric mean of the average relative binding (ARB) of all peptides carrying jis calculated relative to the remainder of the group, and used as the estimate of j. For Class I peptides, if multiple alignments are possible, only the highest scoring alignment Is utilized, following an iterative procedure. To calculate an algorithm score of a given peptide in a test set the ARB values corresponding to the sequence of the peptide are multiplied. If this product exceeds a chosen threshold, the peptide is predicted to bind. Appropriate thresholds are chosen as a function of the degree of stringency of prediction desired. Selection of HLA-A2 supertype cross-reactive peptides Protein sequences from 109P1D4 are scanned utilizing motif Identification software, to Identify 8-, 9- 10- and 11 mer sequences containing the HLA-A2-supermotif main anchor specificity. Typically, these sequences are then scored using the protocol described above and the peptides corresponding to the positive-scoring sequences are synthesized and tested for their capacity to bind purified HLA-A'0201 molecules in vfto (HLA-A*0201 is considered a prototype A2 supertype molecule). These peptides are then tested for the capacity to bind to additional A2-supertype molecules (A*0202, A*0203, A*0206, and A*6802). Peptides that bind to at least three of the five A2-supertype alleles tested are typically deemed A2 supertype cross-reactive binders. Preferred peptides bind at an affinity equal to or less than 500 nM to three or more HLA A2 supertype molecules. Selection of HLA-A3 suermotif-bearina epitopes The 109P1 D4 protein sequence(s) scanned above is also examined for the presence of peptides with the HLA-A3 supermotif primary anchors. Peptides corresponding to the HLA A3 supermotif-bearing sequences are then synthesized and tested for binding to HLA-A*0301 and HLA-A*1101 molecules, the molecules encoded by the two most prevalent A3 supertype alleles. The peptides that bind at least one of the two alleles with binding affinities of 500 nM, often s 200 nM, are then tested for binding cross-reactivity to the other common A3-supertype alleles (e.g., A*3101, A*3301, and A*6801) to identify those that can bind at least three of the five HLA-A3-supertype molecules tested. Selection of HLA-87 supermotif bearing epitopes The 109P1 D4 protein(s) scanned above Is also analyzed for the presence of 8-, 9- 10-, or I 1-mer peptides with the HLA-87-supermotif. Corresponding peptides are synthesized and tested for binding to HLA-B*0702, the molecule encoded by the most common B7-supertype allele (i.e., the prototype B7 supertype allele). Peptides binding B'0702 with ICso of s500 nM are Identified using standard methods. These peptides are then tested for binding to other common B7-supertype molecules (e.g., B*3501, B*5101, B*5301, and B*5401). Peptides capable of binding to three or more of the five B7 supertype alleles tested are thereby Identified. Selection of Al and A24 motif-bearing eltooes To further Increase population coverage, HLA-A1 and -A24 epitopes can also be incorporated Into vaccine compositions. An analysis of the 109P1D4 protein can also be performed to Identify HLA-A1- and A24-motif-containing sequences.

98 High affinity and/or cross-reactive binding epitopes that bear other motif and/or supermotifs are identified using analogous methodology. Example 14: Confirmation of Immunogenicity Cross-eactive candidate CTL A2-supermotif-bearing peptides that are identified as described herein are selected to confirm In vit lmmunogenicity. Confirmation is performed using the following methodology Target Cell Lines for Cellular Screening: The .221A2.1 cell line, produced by transferring the HLA-A2.1 gene into the HLA-A, -B, -C null mutant human B lymphoblastoid cell line 721.221, is used as the peptide-loaded target to measure activity of HLA-A2.1-restricted CTL This cell line is grown in RPMI-1640 medium supplemented with antibiotics, sodium pyruvate, nonessential amino acids and 10% (v/v) heat inactivated FCS. Cells that express an antigen of interest, or transfectants comprising the gene encoding the antigen of Interest, can be used as target cells to confirm the ability of peptide-specific CTLs to recognize endogenous antigen. Primary CTL Induction Cultures: Generation of Dendritic Cells (DC): PBMCs are thawed in RPMI with 30 pg/mI DNAse, washed twice and resuspended in complete medium (RPMI-1640 plus 5% AB human serum, non-essential amino acids, sodium pyruvate, L glutamine and penicillin/streptomycin). The monocytes are purified by plating 10 x 106 PBMC/wel In a 6-well plate. After 2 hours at 37'C, the non-adherent cells are removed by gently shaking the plates and aspirating the supematants. The wells are washed a total of three times with 3 ml RPMI to remove most of the non-adherent and loosely adherent cells. Three ml of complete medium containing 50 nglmI of GM-CSF and 1,000 Ulml of IL-4 are then added to each well. TNFo: is added to the DCs on day 6 at 75 ng/ml and the cells are used for CTL induction cultures on day 7. Induction of CTL with DC and Peptide: CD8+ T-cells are Isolated by positive selection with Dynal immunomagnefic beads (Dynabeads@ M-450) and the detacha-bead@ reagent Typically about 200-250x106 PBMC are processed to obtain 24x106 CD8 T-cels (enough for a 48-well plate culture). Briefly, the PBMCs are thawed in RPMI with 30pg/ml DNAse, washed once with PBS containing 1% human AB serum and resuspended In PBS11% AB serum at a concentration of 20x1Ocells/mi. The magnetic beads are washed 3 times with PBS/AB serum, added to the cells (1 40 pl beads/20x106 cells) and incubated for 1 hour at 4*C with continuous mixing. The beads and cells are washed 4x with PBSIAB serum to remove the nonadherent cells and resuspended at 100x10 6 cells/mI (based on the original cell number) in PBSIAB serum containing 100pl/mI detacha-beadO reagent and 30 pg/ml DNAse. The mixture is incubated for 1 hour at room temperature with continuous mixing. The beads are washed again with PBSIAB/DNAse to collect the CD8+ T-cells. The DC are collected and centrifuged at 1300 rpm for 5-7 minutes, washed once with PBS with 1% BSA, counted and pulsed with 40pg/ml of peptide at a cell concentration of 1-2x106/ml in the presence of 3pg/ml 12- microglobulln for 4 hours at 200C. The DC are then irradiated (4,200 rads), washed I time with medium and counted again. Setting up Induction cultures: 0.25 ml cytokine-generated DC (at 1x105 cells/mI) are co-cultured with 0.25ml of CD8+ T-cells (at 2x106 cell/mi) In each well of a 48-well plate in the presence of 10 ng/mI of IL-7. Recombinant human IL-10 Is added the next day at a final concentration of 10 ng/mI and rhuman IL-2 Is added 48 hours later at 10 IU/mI. Restimulation of the induction cultures with peptide-pulsed adherent cells: Seven and fourteen days after the primary Induction, the cells are restimulated with peptide-pulsed adherent cells. The PBMCs are thawed and washed twice with RPMI and DNAse. The cells are resuspended at 5x1 06 cells/mI and irradiated at -4200 rads. The PBMCs are plated at 2x106 In 0.5 ml complete medium per well and Incubated for 2 hours at 370C. The plates are washed twice with RPMI by tapping the plate gently to remove the nonadherent cells and the adherent cells pulsed with 10pgml of peptide in the 99 presence of 3 pg/ml 82 microglobulin in 0.25ml RPMI/5%AB per well for 2 hours at 37*C. Peptide solution from each well is aspirated and the wells are washed once with RPMI. Most of the media is aspirated from the induction cultures (CD8+ cells) and brought to 0.5 ml with fresh media. The cells are then transferred to the wells containing the peptide-pulsed adherent cells. Twenty four hours later recombinant human IL-10 is added at a final concentration of 10 ng/ml and recombinant human 112 is added the next day and again 2-3 days later at 50lU/ml (Tsai et al., Critical Reviews in Immunology 18(1-2):65-75, 1998). Seven days later, the cultures are assayed for CTL activity in a 5 1 Cr release assay. In some experiments the cultures are assayed for peptide-specfic recognition In the in situ IFNy ELISA at the time of the second restimulation followed by assay of endogenous recognition 7 days later. After expansion, activity is measured In both assays for a side-by-side comparison. Measurement of CTL lytic activity by 51Cr release. Seven days after the second restimulation, cytotoxicity is determined In a standard (5 hr) 5t Cr release assay by assaying individual wells at a single E:T. Peptide-pulsed targets are prepared by Incubating the cells with 1Opg/ml peptide overnight at 37*C. Adherent target cells are removed from culture flasks with trypsIn-EDTA. Target cells are labeled with 200pCi of 51 Cr sodium chromate (Dupont, Wilmington, DE) for 1 hour at 37*C. Labeled target cells are resuspended at 106 per ml and diluted 1:10 with K562 cells at a concentration of 3.3x10 6 /mi (an NK-sensitive erythroblastoma cell Une used to reduce non specific lysis). Target cells (100 pl) and effectors (100pl) are plated in 96 well round-bottom plates and incubated for 5 hours at 370C. At that time, 100 pl of supernatant are collected from each well and percent lysis Is determined according to the formula: [(cpm of the test sample- cpm of the spontaneous 5 1 Cr release sample)/(cpm of the maximal 51 Cr release sample cpm of the spontaneous 5'Cr release sample)] x 100. Maximum and spontaneous release are determined by incubating the labeled targets with 1% Triton X-100 and media alone, respectively. A positive culture is defined as one in which the specific lysis (sample- background) is 10% or higher In the case of individual wells and is 15% or more at the two highest E:T ratios when expanded cultures are assayed. In situ Measurement of Human IFNy Production as an Indicator of Peptide-speclfic and Endogenous Recognition Immulon 2 plates are coated with mouse anti-human IFNy monoclonal antibody (4 pg/mI 0.1M NaHCO3, pH8.2) overnight at 40C. The plates are washed with Ca 2 +, Mg 2 -free PBS/0.05% Tween 20 and blocked with PBS/10% FCS for two hours, after which the CTLs (100 p1/well) and targets (100 p1/weI) are added to each well, leaving empty wells for the standards and blanks (which received media only). The target cells, either peptide-pulsed or endogenous targets, are used at a concentration of xI106 cells/ml. The plates are incubated for 48 hours at 370C with 5% C02. Recombinant human IFN-gamma Is added to the standard wells starting at 400 pg or 1200pg/100 microliter/well and the plate incubated for two hours at 37*C. The plates are washed and 100 p1 of blotinylated mouse anti-human IFN gamma monoclonal antibody (2 microgram/mI In PBS/3%FCS/0.05% Tween 20) are added and incubated for 2 hours at room temperature. After washing again, 100 microliter HRP-streptavidin (1:4000) are added and the plates incubated for one hour at room temperature. The plates are then washed 6x with wash buffer, 100 microliter/well developing solution (TMB 1:1) are added, and the plates allowed to develop for 5-15 minutes. The reaction Is stopped with 50 microliter/well IM H3PO4 and read at OD450. A culture Is considered positive If It measured at least 50 pg of IFN-gamma/well above background and is twice the background level of expression. CTL Expansion. Those cultures that demonstrate specific lytic activity against peptide-pulsed targets and/or tumor targets are expanded over a two week period with anti-CD3. Briefly, 5x104 CD8+ cells are added to a T25 flask containing the following: 100 1x106 Irradiated (4,200 rad) PBMC (autologous or allogeneic) per ml, 2x10 5 irradiated (8,000 rad) EBV- transformed cells per ml, and OKT3 (anti-CD3) at 30ng per mi in RPMI-1640 containing 10% (vlv) human AB serum, non-essential amino acids, sodium pyruvate, 25pM 2-mercaptoethanol, L-glutamine and penicillin/streptomycin. Recombinant human 1L2 is added 24 hours later at a final concentration of 2001U/ml and every three days thereafter with fresh media at 50lUlml. The cells are split if the cell concentration exceeds I x10/mI and the cultures are assayed between days 13 and 15 at E:T ratios of 30, 10, 3 and 1:1 in the s 5 Cr release assay or at 1x106/mI in the in situ IFNy assay using the same targets as before the expansion. Cultures are expanded in the absence of anti-CD3+ as follows. Those cultures that demonstrate specific lytic activity against peptide and endogenous targets are selected and 5x10 4 CD8+ cells are added to a T25 flask containing the following: 1x106 autologous PBMC per ml which have been peptide-pulsed with 10 Ig/mI peptide for two hours at 37'C and irradiated (4,200 rad); 2x105 Irradiated (8,000 rad) EBV-transformed cells per ml RPMI-1640 containing 10%(v/v) human AB serum, non-essential AA, sodium pyruvate, 25mM 2-ME, L-glutamine and gentamicin. lmmunogenicity of A2 supermoif-bearing peplides A2-supermotif cross-reactive binding peptides are tested in the cellular assay for the ability to induce peptide specific CTL in normal individuals. In this analysis, a peptide Is typically considered to be an epitope If it induces peptide specific CTLs In at least Individuals, and preferably, also recognizes the endogenously expressed peptide. Immunogenicity can also be confirmed using PBMCs isolated from patients bearing a tumor that expresses 109P1D4. Briefly, PBMCs are isolated from patients, re-stimulated with peptide-pulsed monocytes and assayed for the ability to recognize peptide-pulsed target cells as well as transfected cells endogenously expressing the antigen. Evaluation of A*03/A1 1 Immunogenicity HLA-A3 supermotif-bearing cross-reactive binding peptides are also evaluated for immunogenicity using methodology analogous for that used to evaluate the Immunogenicity of the HLA-A2 supermotif peptides. Evaluation of B7 immunogenicitv Immunogenicity screening of the B7-supertype cross-reactive binding peptides identified as set forth herein are confirmed in a manner analogous to the confirmation of A2-and A3-supermotif-bearing peptides. Peptides bearing other supermotifs/motifs, e.g., HLA-Al, HLA-A24 etc. are also confirmed using similar methodology Example 15: Implementation of the Extended SupeRmnotif to Improve the Binding Capacity of Native EpItopes by Cratng AnalonS HLA motifs and supermotifs (comprising primary and/or secondary residues) are useful In the identification and preparation of highly cross-reactive native peptides, as demonstrated herein. Moreover, the definition of HLA motifs and supermotifs also allows one to engineer highly cross-reactive epltopes by identifying residues within a native peptide sequence which can be analoged to confer upon the peptide certain characteristics, e.g. greater cross-reactivity within the group of HLA molecules that comprise a supertype, and/or greater binding affinity for some or all of those HLA molecules. Examples of analoging peptides to exhibit modulated binding affinity are set forth in this example. Analoging at Primary Anchor Residues Peptide engineering strategies are Implemented to further increase the cross-reactivity of the epitopes. For example, the main anchors of A2-supermotif-bearing peptides are altered, for example, to Introduce a preferred L, I, V, or M at position 2, and I or V at the C-terminus. To analyze the cross-reactivity of the analog peptides, each engineered analog is initially tested for binding to the prototype A2 supertype allele A'0201, then, if A*0201 binding capacity is maintained, for A2-supertype cross-reactivity.

101 Alternatively, a peptide is confirmed as binding one or all supertype members and then analoged to modulate binding affinity to any one (or more) of the supertype members to add population coverage. The selection of analogs for immunogenicity in a cellular screening analysis is typically further restricted by the capacity of the parent wild type (WT) peptide to bind at least weakly, L.e., bind at an ICso of 5000nM or less, to three of more A2 supertype alleges. The rationale for this requirement is that the WT peptides must be present endogenously in sufficient quantity to be biologically relevant. Analoged peptides have been shown to have increased immunogenicity and cross reactivity by T cells specific for the parent epitope (see, e.g., Parkhurst at al., J. Immunol. 157:2539, 1996; and Pogue et al., Proc. NatL. Acad. Sci. USA 92:8166,1995). In the cellular screening of these peptide analogs, it is important to confirm that analog-specific CTLs are also able to recognize the wild-type peptide and, when possible, target cells that endogenously express the epitope. Analoging of HLA-A3 and B7-supermotif-bearing Deptides Analogs of HLA-A3 supermof-bearing epitopes are generated using strategies similar to those employed in analoging HLA-A2 supermotif-bearing peptides. For example, peptides binding to 3/5 of the A3-supertype molecules are engineered at primary anchor residues to possess a preferred residue (V, S, M, or A) at position 2. The analog peptides are then tested for the ability to bind A'03 and A*11 (prototype A3 supertype alleles). Those peptides that demonstrate s 500 nM binding capacity are then confirmed as having A3-supertype cross-reactivity. Similarly to the A2- and A3- motif bearing peptides, peptides binding 3 or more B7-supertype alleles can be improved, where possible, to achieve increased cross-reactive binding or greater binding affinity or binding half life. B7 supermotif-bearing peptides are, for example, engineered to possess a preferred residue (V, I, L, or F) at the C-terminal primary anchor position, as demonstrated by Sidney et al. (J. Immunol. 157:3480-3490, 1996). Analoging at primary anchor residues of other motif and/or supermotif-bearing epitopes is performed in a like manner. The analog peptides are then be confirmed for Immunogenicity, typically in a cellular screening assay. Again, it Is generally important to demonstrate that analog-specfic CTLs are also able to recognize the wild-type peptide and, when possible, targets that endogenously express the epitope. Analoging at Secondary Anchor Residues Moreover, HLA supermotifs are of value in engineering highly cross-reactive peptides and/or peptides that bind HLA molecules with increased affinity by Identifying particular residues at secondary anchor positions that are associated with such properties. For example, the binding capacity of a B7 supermotif-bearing peptide with an F residue at position I is analyzed. The peptde is then analoged to, for example, substitute L for F at position 1. The analoged peptide is evaluated for increased binding affinity, binding half life and/or increased cross-reactivity. Such a procedure identifies analoged peptides with enhanced properties. Engineered analogs with sufficiently improved binding capacity or cross-reactivity can also be tested for Immunogenicity in HLA-B7-transgenlc mice, following for example, IFA immunization or lipopeptide immunization. Analoged peptides are additionally tested for the ability to stimulate a recall response using PBMC from patients with 109P1 D4 expressing tumors. Other analoging strategies Another form of peptide analoging, unrelated to anchor positions, involves the substitution of a cysteine with .

amino butyric acid. Due to its chemical nature, cysteine has the propensity to form disufide bridges and sufficiently alter the 102 peptide structurally so as to reduce binding capacity. Substitution of a-amino butyric acid for cysteine not only alleviates this problem, but has been shown to improve binding and crossbinding capabilities in some Instances (see, e.g., the review by Sette et al., In: Persistent Viral Infections, Eds. R Ahmed and I. Chen, John Wiley & Sons, England, 1999). Thus, by the use of single amino acid substitutions, the binding properties and/or cross-reactivity of peptide igands for HLA supertype molecules can be modulated. Example 16: Identification and confirmation of 109P1D4-derived sequences with HLA-DR binding motifs Pepfide epitopes bearing an HLA class I supermotif or motif are Identified and confirmed as outlined below using methodology similar to that described for HLA Class I peptides. Selection of HLA-DR-supermotif-bearing epitopes. To identify 109P1D4-derived, HLA class 1i HTL epitopes, a iO9P1 D4 antigen is analyzed for the presence of sequences bearing an HLA-DR-motif or supermotif. Specifically, 15-mer sequences are selected comprising a DR supermotif, comprising a 9-mer core, and three-residue N- and C-terminal flanking regions (15 amino acids total). Protocols for predicting peptide binding to DR molecules have been developed (Southwood et al., J. Immunol. 160:3363-3373, 1998). These protocols, specific for individual DR molecules, aflow the scoring, and ranking, of 9-mer core regions. Each protocol not only scores peptide sequences for the presence of DR-supermotif primary anchors (i.e., at position 1 and position 6) within a 9-mer core, but additionally evaluates sequences for the presence of secondary anchors. Using allele-specific selection tables (see, e.g., Southwood et al., Ibid.), it has been found that these protocols efficiently select peptide sequences with a high probability of binding a particular DR molecule. Additionally, it has been found that performing these protocols In tandem, specifically those for DR1, DR4w4, and DR7, can efficiently select DR cross-reactive peptides. The 109P1 D4-derived peptides identified above are tested for their binding capacity for various common HLA-DR molecules. All peptides are initially tested for binding to the DR molecules in the primary panel: DR1, DR4w4, and DR7. Peptides binding at least two of these three DR molecules are then tested for binding to DR2w2 p1, DR2w2 p2, DR6w1 9, and DR9 molecules in secondary assays. Finally, peptides binding at least two of the four secondary panel DR molecules, and thus cumulatively at least four of seven different DR molecules, are screened for binding to DR4w15, DR5w11, and DR8w2 molecules in tertiary assays. Peptides binding at least seven of the ten DR molecules comprising the primary, secondaryand tertiary screening assays are considered cross-reactive DR binders. 109P1D4-derived peptides found to bind common HLA-DR alleles are of particular interest Selection of DR3 motif Deptides Because HLA-DR3 is an allele that Is prevalent In Caucasian, Black, and Hispanic populations, DR3 binding capacity is a relevant criterion in the selection of HTL epitopes. Thus, peptides shown to be candidates may also be assayed for their DR3 binding capacity. However, in view of the binding specificity of the DR3 motif, peptides binding only to DR3 can also be considered as candidates for infusion in a vaccine formulation. To efficiently identify peptides that bind DR3, target 109P1 D4 antigens are analyzed for sequences carrying one of the two DR3-specific binding motifs reported by Geluk et aL (J. Immuno. 152:5742-5748, 1994). The corresponding peptides are then synthesized and confirmed as having the ability to bind DR3 with an affinity of 1pM or better, i.e., less than 1 pM. Peptides are found that meet this binding criterion and qualify as HLA class Il high affinity binders. DR3 binding epitopes Identified in this manner are included in vaccine compositions with DR supermotif-bearing peptide epitopes. Similarly to the case of HLA class I motif-bearing peptides, the class Il motif-bearing peptides are analoged to 103 improve affinity or cross-reactivity. For example, aspartic acid at position 4 of the 9-mer core sequence is an optimal residue for DR3 binding, and substitution for that residue often improves DR 3 binding. Example 17: Immunogenicity of 109P1D4-derived HTL epitopes This example determines immunogenic DR supermotif- and DR3 motif-bearing epitopes among those identified using the methodology set forth herein. Immunogenicity of HTh epitopes are confirmed In a manner analogous to the determination of immunogenicity of CTL epitopes, by assessing the ability to stimulate HTL responses and/or by using appropriate transgenic mouse models. Immunogenicity is determined by screening for 1.) in vitro primary induction using normal PBMC or 2.) recall responses from patients who have 109P1D4-expressing tumors. Example 18: Calculation of phenotilc frequencles of HLA-supertypes In various ethnic backgrounds to determine breadth of population coverage This example illustrates the assessment of the breadth of population coverage of a vaccine composition comprised of multiple epitopes comprising multiple supermotifs and/or motifs. In order to analyze population coverage, gene frequencies of HLA alleles are determined. Gene frequencies for each HLA allele are calculated from antigen or allele frequencies utlizing the binomial distribution formulae gf-l(SQRT(1 af)) (see, e.g., Sidney et al., Human Immunol. 45:79-93, 1996). To obtain overall phenotypic frequencies, cumulative gene frequencies are calculated, and the cumulative antigen frequencies derived by the use of the inverse formula [af=-(1-Cgf)J. Where frequency data is not available at the level of DNA typing, correspondence to the serologically defined antigen frequencies is assumed. To obtain total potential supertype population coverage no linkage disequilibrium is assumed, and only alleles confirmed to belong to each of the supertypes are included (minimal estimates). Estimates of total potential coverage achieved by Inter-loc combinations are made by adding to the A coverage the proportion of the non-A covered population that could be expected to be covered by the B alleles considered (e.g., total=A+B*(1-A)). Confirmed members of the A3-like supertype are A3, Al1, A31, A*3301, and A*6801. Although the A3-like supertype may also include A34, A66, and A*7401, these alleles were not included in overall frequency calculations. Ukewise, confirmed members of the A2-like supertype family are A*0201, A*0202, A*0203, A*0204, A*0205, A*0206, A*0207, A6802, and A*6901. Finally, the 87-like supertype-confirmed alleles are: B7, B*3501-03, B51, B*5301, B*5401, B*5501-2, B*5601, B*6701, and B*7801 (potentially also B'1401, B*3504-06, B*4201, and B*5602). Population coverage achieved by combining the A2-, A3- and B7-supertypes is approximately 86% In five major ethnic groups. Coverage may be extended by induding peptides bearing the Al and A24 motifs. On average, Al is present in 12% and A24 in 29% of the population across five different major ethnic groups (Caucasian, North American Black, Chinese, Japanese, and Hispanic). Together, these alleles are represented with an average frequency of 39% in these same ethnic populations. The total coverage across the major ethnicities when Al and A24 are combined with the coverage of the A2-, A3- and B7-supertype alleles Is >95%, see, e.g., Table IV (G). An analogous approach can be used to estimate population coverage achieved with combinations of class 11 motif-bearing epitopes. Immunogenicity studies in humans (e.g., Bertoni et al., J. Clin. Invest. 100:503,1997; Doolan et al., Immunity 7:97, 1997; and Threlkeld et al., J. Immunol. 159:1648,1997) have shown that highly cross-reactive binding peptides are almost always recognized as epitopes. The use of highly cross-reactive binding peptides is an important selection criterion In identifying candidate epitopes for inclusion in a vaccine that is immunogenic in a diverse population. With a sufficient number of epitopes (as disclosed herein and from the art), an average population coverage is 104 predicted to be greater than 95% in each of five major ethnic populations. The game theory Monte Carlo simulation analysis, which is known in the art (see e.g., Osborne, M.J. and Rubinstein, A. "A course in game theory' MIT Press, 1994), can be used to estimate what percentage of the individuals In a population comprised of the Caucasian, North American Black, Japanese, Chinese, and Hispanic ethnic groups would recognize the vaccine epitopes described herein. A preferred percentage is 90%. A more preferred percentage is 95%. Example 19: CTL Recognition Of Endogenously Processed Antigens After Priming This example confirms that CTL induced by native or analoged peptide epitopes identified and selected as described herein recognize endogenously synthesized, i.e., native antigens. Effector cells isolated from transgenic mice that are immunized with peptide epitopes, for example HLA-A2 supermotif-bearing epitopes, are re-stimulated in vtro using peptide-coated stimulator cells. Six days later, effector cells are assayed for cytotoxicity and the cell lines that contain peptide-specific cytotoxic activity are further re-stimulated. An additional six days later, these cell lines are tested for cytotoxic activity on 5 1 Cr labeled Jurkat-A2.1/Kb target cells in the absence or presence of peptide, and also tested on 5 1 Cr labeled target cells bearing the endogenously synthesized antigen, i.e. cells that are stably transfected with 109P1D4 expression vectors. The results demonstrate that CTL lines obtained from animals primed with peptide epitope recognize endogenously synthesized 109P1 D4 antigen. The choice of transgenic mouse model to be used for such an analysis depends upon the epitope(s) that are being evaluated. In addition to HLA-A*0201/Kb transgenic mice, several other transgenic mouse models including mice with human Al1, which may also be used to evaluate A3 epitopes, and B7 alleles have been characterized and others (e.g., transgenic mice for HLA-A1 and A24) are being developed. HLA-DR1 and HIA DR3 mouse models have also been developed, which may be used to evaluate HTL epitopes. Example 20: Activity Of CTL-HTL Conjugated Eotopes In Transaenic Mice This example Illustrates the induction of CTLs and HTLs in transgenic mice, by use of a 109P1 D4-derived CTL and HTL peptide vaccine compositions. The vaccine composition used herein comprise peptides to be administered to a patient with a 109P1D4-expressing tumor. The peptide composition can comprise multiple CTL and/or HTL epitopes. The epitopes are identified using methodology as described herein. This example also Illustrates that enhanced immunogenicity can be achieved by inclusion of one or more HT epitopes in a CTL vaccine composition; such a peptide composition can comprise an HTL epitope conjugated to a CTL epitope. The CT epitope can be one that binds to multiple HLA family members at an affinity of 500 nM or less, or analogs of that epitope. The peptides may be lipidated, if desired. Immunization procedures: Immunization of transgenic mice is performed as described (Alexander et at., J. Immunol. 159:4753-4761, 1997). For example, A2/K mice, which are transgenic for the human HLA A2.1 allele and are used to confirm the immunogenicity of HLA-A*0201 motif- or HLA-A2 supermotif-bearing epitopes, and are primed subcutaneously (base of the tail) with a 0.1 ml of peptide in Incomplete Freund's Adjuvant, or If the peptide composition is a lpidated CTL/HTL conjugate, in DMSO/saline, or if the peptide composition is a polypeptide, in PBS or Incomplete Freund's Adjuvant Seven days after priming, splenocytes obtained from these animals are restimulated with syngenic irradiated LPS activated lymphoblasts coated with peptide. Cell lines: Target cells for peptide-specific cytotoxicity assays are Jurkat cells transfected with the HLA-A2.1/Kb chimeric gepe (e.g., Vitiello et at., J. Exp. Med. 173:1007,1991) ifnvt CTL activation: One week after priming, spleen cells (30x1 06 cells/flask) are co-cultured at 37'C with syngeneic, irradiated (3000 rads), peptide coated lymphoblasts (10x10 6 cells/flask) In 10 ml of culture medium/T25 flask.

105 After six days, effector cells are harvested and assayed for cytotoxic activity. Assay for cytotoxic activity: Target cells (1.0 to 1.5x10 6 ) are incubated at 37'C in the presence of 200 p of 5 1 Cr. After 60 minutes, cells are washed three times and resuspended In R10 medium. Peptide is added where required at a concentration of 1 pghnl. For the assay, 104 5 1 Cr-labeled target cells are added to different concentrations of effector cells (final volume of 200 pl) In U-bottom 96-wel plates. After a six hour incubation period at 37'C, a 0.1 ml aliquot of supernatant Is removed from each well and radioactivity is determined in a Micromedic automatic gamma counter. The percent specific lysis Is determined by the formula: percent specific release = 100 x (experimental release - spontaneous release)/(maximum release - spontaneous release). To facilitate comparison between separate CTL assays run under the same conditions, % 5 1Cr release data Is expressed as lytic unIts/106 cells. One lytic unit is arbitrarily defined as the number of effector cells required to achieve 30% lysis of 10,000 target cells in a six hour 5 1 Cr release assay. To obtain specific lytic units/1 06, the lytic units/106 obtained in the absence of peptide is subtracted from the lytic units/106 obtained in the presence of peptide. For example, if 30% s 1 Cr release Is obtained at the effector (E): target (T) ratio of 50:1 (i.e., 5x1 05 effector cells for 10,000 targets) in the absence of peptide and 5:1 (i.e., 5x10 4 effector cells for 10,000 targets) In the presence of peptide, the specific lytic units would be: [(1/50,000)-(1/500,000)1 x 106 =18 LU. The results are analyzed to assess the magnitude of the CTL responses of animals injected with the immunogenic CTLJHTL conjugate vaccine preparation and are compared to the magnitude of the CTL response achieved using, for example, CTL epitopes as outlined above In the Example entitled 'Confirmation of Immunogenicity." Analyses similar to this may be performed to confirm the Immunogenicity of peptide conjugates containing multiple CTIL epitopes and/or multiple HTL epitopes. In accordance with these procedures, it is found that a CTL response is induced, and concomitantly that an HTL response is induced upon administration of such compositions. Example 21: Selection of CT, and HTL epitopes for Inclusion In a 109P1D4-specific vaccine. This example illustrates a procedure for selecting peptide epitopes for vaccine compositions of the Invention. The peptides In the composition can be In the form of a nucleic acid sequence, either single or one or more sequences (i.e., minigene) that encodes peptide(s), or can be single and/or polyepitopic peptides. The following principles are utilized when selecting a plurality of epitopes for inclusion In a vaccine composition. Each of the following principles Is balanced in order to make the selection. Epitopes are selected which, upon administration, mimic Immune responses that are correlated with 109P1D4 clearance. The number of epitopes used depends on observations of patients who spontaneously clear 109PID4. For example, If It has been observed that patients who spontaneously dear 109P1D4-expressing cels generate an Immune response to at least three (3) epitopes from 109P1D4 antigen, then at least three epitopes should be included for HLA class I. A similar rationale is used to determine HLA class I epitopes. Epitopes are often selected that have a binding affinity of an ICso of 500 nM or less for an HLA class I molecule, or for class 11, an ICso of 1000 nM or less; or HLA Class I peptides with high binding scores from the BIMAS web site, at URL bimas.dcrtnih.gov/. In order to achieve broad coverage of the vaccine through out a diverse population, sufficient supermotif bearing peptides, or a sufficient array of allele-specific motif bearing peptides, are selected to give broad population coverage. In one embodiment, epitopes are selected to provide dt least 80% population coverage. A Monte Carlo analysis, a statistical evaluation known In the art, can be employed to assess breadth, or redundancy, of population coverage. When creating polyepitopic compositions, or a minigene that encodes same, it Is typically desirable to generate the smallest peptide possible that encompasses the epitopes of Interest The principles employed are similar, if not the same, as 106 those employed when selecting a peptide comprising nested epitopes. For example, a protein sequence for the vaccine composition Is selected because it has maximal number of epitopes contained within the sequence, i.e., it has a high concentration of epitopes. Epitopes may be nested or overlapping (i.e., frame shifted relative to one another). For example, with overlapping epitopes, two 9-mer epitopes and one 10-mer epitope can be present in a 10 amino acid peptide. Each epitope can be exposed and bound by an HLA molecule upon administration of such a peptide. A multi-epitopic, peptide can be generated synthetically, recombinantly, or via cleavage from the native source. Alternatively, an analog can be made of this native sequence, whereby one or more of the epitopes comprise substitutions that alter the cross-reactivity and/or binding affinity properties of the polyepitopic peptide. Such a vaccine composition is administered for therapeutic or prophylactic purposes. This embodiment provides for the possibility that an as yet undiscovered aspect of immune system processing will apply to the native nested sequence and thereby facilitate the production of therapeutic or prophylactic immune response-inducing vaccine compositions. Additionally such an embodiment provides for the possibility of motif bearing epitopes for an HLA makeup that is presently unknown. Furthermore, this embodiment (absent the creating of any analogs) directs the immune response to multiple peptide sequences that are actually present In 109P1D4, thus avoiding the need to evaluate any junctional epitopes. Lastly, the embodiment provides an economy of scale when producing nudeic acid vaccine compositions. Related to this embodiment, computer programs can be derived in accordance with principles in the art, which identify in a target sequence, the greatest number of epitopes per sequence length. A vaccine composition comprised of selected peptides, when administered, is safe, efficacious, and elicits an immune response similar In magnitude to an immune response that controls or clears cells that bear or overexpress 109P1D4. Example 22: Construction of "inigene" Multi-Epitope DNA Plasmids This example discusses the construction of a minigene expression plasmid. Minigene plasmids may, of course, contain various configurations of B cell, CTL and/or HTL epitopes or epitope analogs as described herein. A minigene expression plasmid typically includes multiple CTL and HTL peptide epitopes. In the present example, HLA-A2, -A3, -87 supermotif-bearing peptide epitopes and HLA-A1 and -A24 motif-bearing peptide epitopes are used in conjunction with DR supermotif-bearing epitopes and/or DR3 epitopes. HLA class I supermotif or motif-bearing peptide epitopes derived 109P1D4, are selected such that multiple supermotifs/motifs are represented to ensure broad population coverage. Similarly, HLA class I epitopes are selected from 109P1 D4 to provide broad population coverage, I.e. both HLA DR-1-4-7 supermotif-bearing epitopes and HLA DR-3 motif-bearing epitopes are selected for inclusion in the minigene construct. The selected CTL and HTL epitopes are then incorporated into a minigene for expression in an expression vector. Such a construct may additionally include sequences that direct the HTL epitopes to the endoplasmic reticulum. For example, the Ii protein may be fused to one or more HTL epitopes as described in the art, wherein the CLIP sequence of the 1I protein is removed and replaced with an HLA class 11 epitope sequence so that HLA class 11 epitope Is directed to the endoplasmic reticulum, where the epitope binds to an HLA class Il molecules. This example illustrates the methods to be used for construction of a minigene-bearing expression plasmid. Other expression vectors that may be used for minigene compositions are available and known to those of skill in the art. The minigene DNA plasmid of this example contains a consensus Kozak sequence and a consensus murine kappa Ig-light chain signal sequence followed by CTL and/or HTL epitopes selected in accordance with principles disclosed herein. The sequence encodes an open reading frame fused to the Myc and His antibody epitope tag coded for by the pcDNA 3.1 Myc-HIs vector. Overlapping oligonucleotides that can, for example, average about 70 nucleotides in length with 15 nucleotide 107 overlaps, are synthesized and HPLC-purified. The oligonucleotides encode the selected peptide epitopes as well as appropriate linker nucleotides, Kozak sequence, and signal sequence. The final multiepitope minigene is assembled by extending the ovedapping oligonucleotides in three sets of reactions using PCR. A Perkin/Elmer 9600 PCR machine Is used and a total of 30 cycles are performed using the following conditions: 950C for 15 sec, annealing temperature (5' below the lowest calculated Tm of each primer pair) for 30 sec, and 72*C for 1 min. For example, a minigene is prepared as follows. For a first PCR reaction, 5 pg of each of two oligonudeotides are annealed and extended: In an example using eight oligonucleotides, i.e., four pairs of primers, oligonudeotides 1+2, 3+4, 5+6, and 7+8 are combined in 100 pl reactions containing Pfu polymerase buffer (1x 10 mM KCL, 10 mM (NH4)2SO4, 20 mM Tris-chloride, pH 8.75, 2 mM MgSO4, 0.1% Triton X-100, 100 pghnl BSA), 0.25 mM each dNTP, and 2.5 U of Pfu polymerase. The full-length dimer products are gel-purified, and two reactions containing the product of 1+2 and 3+4, and the product of 5+6 and 7+8 are mixed, annealed, and extended for 10 cycles. Half of the two reactions are then mixed, and 5 cycles of annealing and extension carded out before flanking primers are added to amplify the full length product. The full length product is gel-purified and cloned into pCR-blunt (Invitrogen) and individual clones are screened by sequencing. Example 23: The Plasmid Construct and the Degree to Which It Induces Immunooenicity. The degree to which a plasmid construct, for example a plasmid constructed in accordance with the previous Example, is able to Induce immunogenicity is confirmed in vitro by determining epitope presentation by APC following transduction or transfection of the APC with an epitope-expressing nudeic acid construct Such a study determines 'antigenicity" and allows the use of human APC. The assay determines the ability of the epitope to be presented by the APC in a context that is recognized by a T cell by quantifying the density of epitope-HLA class I complexes on the cell surface. Quantitation can be performed by directly measuring the amount of peptide eluted from the APC (see, e.g., Sijts et el., J. Immunol. 156:683-692, 1996; Demotz et al., Nature 342:682-684, 1989); or the number of peptide-HLA class I complexes can be estimated by measuring the amount of lysis or lymphokine release induced by diseased or transfected target cells, and then determining the concentration of peptide necessary to obtain equivalent levels of lysis or lymphokine release (see, e.g., Kageyama et al., J. Immunol. 154:567-576, 1995). Alternatively, immunogenicity is confirmed through in vivo injections into mice and subsequent in vitro assessment of CTL and HTL activity, which are analyzed using cytotoxicity and proliferation assays, respectively, as detailed e.g., in Alexander et al., ImmunIty 1:751-761, 1994. For example, to confirm the capacity of a DNA minigene construct containing at least one HLA-A2 supermotif peptide to induce CTLs in vivo, HLA-A2.1/1K transgenic mice, for example, are immunized intramuscularly with 100 pg of naked cDNA. As a means of comparing the level of CTLs Induced by cDNA Immunization, a control group of animals is also immunized with an actual peptide composition that comprises multiple epitopes synthesized as a single polypeptide as they would be encoded by the minigene. Splenocytes from immunized animals are stimulated twice with each of the respective compositions (peptide epitopes encoded in the minigene or the polyepitopic peptide), then assayed for peptide-specific cytotoxic activity In a 5 Cr release assay. The results indicate the magnitude of the CTL response directed against the A2-restricted epitope, thus indicating the In vivo immunogenicity of the minigene vaccine and polyepitopic vaccine. It is, therefore, found that the minigene elicits immune responses directed toward the HLA-A2 supermotif peptide epitopes as does the polyepitopic peptide vaccine. A similar analysis is also performed using other HLA-A3 and HLA-B7 transgenic mouse models to assess CTL induction by HLA-A3 and HLA-B7 motif or supermotif epitopes, whereby It is also found that the minigene elicits appropriate immune responses directed toward the provided epitopes.

108 To confirm the capacity of a class Il epitope-encoding minigene to induce HTLs in vivo, DR transgenic mice, or for those epitopes that cross react with the appropriate mouse MHC molecule, I-Ab-restricted mice, for example, are immunized intramuscularly with 100 pg of plasmid DNA. As a means of comparing the level of HTLs Induced by DNA immunization, a group of control animals is also Immunized with an actual peptide composition emulsified in complete Freund's adjuvant. CD4+ T cells, I.e. HTLs, are purified from splenocytes of immunized animals and stimulated with each of the respective compositions (peptides encoded in the minigene). The HTL response is measured using a 3 H-thymidine incorporation proliferation assay, (see, e.g., Alexander et a. Immunity 1:751-761, 1994). The results indicate the magnitude of the HTL response, thus demonstrating the in vivo immunogenicity of the minigene. DNA minigenes, constructed as described in the previous Example, can also be confirmed as a vaccine in combination with a boosting agent using a prime boost protocol. The boosting agent can consist of recombinant protein (e.g., Bamett of al., Aids Res. and Human Retroviruses 14, Supplement 3:S299-S309, 1998) or recombinant vaccinia, for example, expressing a minigene or DNA encoding the complete protein of Interest (see, e.g., Hanke et al, Vaccine 16:439 445, 1998; Sedegah et at., Proc. Nati. Acad. Sc/ USA 95:7648-53, 1998; Hanke and McMichael, Immunol. Letters 66:177 181, 1999; and Robinson et al., Nature Med. 5:526-34, 1999). For example, the efficacy of the DNA minigene used In a prime boost protocol is initially evaluated in transgenic mice. In this example, A2.1/Kb transgenic mice are immunized IM with 100 pg of a DNA minigene encoding the immunogenic peptides including at least one HLA-A2 supermotif-bearing peptide. After an incubation period (ranging from 3 9 weeks), the mice are boosted IP with 107 pfulmouse of a recombinant vaccinia virus expressing the same sequence encoded by the DNA minigene. Control mice are immunized with 100 pg of DNA or recombinant vaccinia without the minigene sequence, or with DNA encoding the minigene, but without the vaccinia boost After an additional Incubation period of two weeks, splenocytes from the mice are Immediately assayed for peptide-specific activity in an ELISPOT assay. Additionally, splenocytes are stimulated In vitro with the A2-restricted peptide epitopes encoded in the minigene and recombinant vaccinia, then assayed for peptide-specific activity in an alpha, beta and/or gamma IFN ELISA. It is found that the minigene utilized In a prime-boost protocol elicits greater Immune responses toward the HLA-A2 supennotif peptides than with DNA alone. Such an analysis can also be performed using HLA-A1 1 or HLA-B7 transgenic mouse models to assess CTL induction by HLA-A3 or HLA-B7 motif or supermotif epitopes. The use of prime boost protocols in humans is described below in the Example entitled "Induction of CTL Responses Using a Prime Boost Protocol." Example 24: Peptide Compositions for Prophylactic Uses Vaccine compositions of the present Invention can be used to prevent 109PID4 expression In persons who are at risk for tumors that bear this antigen. For example, a polyepitopic peptide epitope composition (or a nucleic acid comprising the same) containing multiple CTL and HTL epitopes such as those selected In the above Examples, which are also selected to target greater than 80% of the population, is administered to individuals at risk for a 109P1 D4-associated tumor. For example, a peptide-based composition is provided as a single polypeptide that encompasses multiple epitopes. The vaccine is typically administered in a physiological solution that comprises an adjuvant, such as Incomplete Freunds Adjuvant The dose of peptide for the initial immunization is from about I to about 50,000 pg, generally 100-5,000 pg, for a 70 kg patient The initial administration of vaccine is followed by booster dosages at 4 weeks followed by evaluation of the magnitude of the Immune response In the patient, by techniques that determine the presence of epitope specific CTL populations in a PBMC sample. Additional booster doses are administered as required. The composition Is found to be both safe and efficacious as a prophylaxis against 109P1D4-associated disease. Alternatively, a composition typically comprising transfectIng agents is used for the administration of a nucleic acId- 109 based vaccine in accordance with methodologies known in the art and disclosed herein. Example 25: PolvepitopIc Vaccine Compositions Derived from Native 109P1D4 Sequences A native 109P1 D4 polyprotein sequence is analyzed, preferably using computer algodthms defined for each class I and/or class Il supermoif or motif, to identify "relatively short" regions of the polyprotein that comprise multiple epitopes. The 'relatively short" regions are preferably less in length than an entire native antigen. This relatively short sequence that contains multiple distinct or overlapping, "nested" epitopes can be used to generate a minigene construct The construct is engineered to express the peptide, which corresponds to the native protein sequence. The 'relatively short" peptide is generally less than 250 amino acids in length, often less than 100 amino acids in length, preferably less than 75 amino acids in length, and more preferably less than 50 amino acids in length. The protein sequence of the vaccine composition is selected because it has maximal number of epitopes contained within the sequence, i.e., it has a high concentration of epitopes. As noted herein, epitope motifs may be nested or overlapping (i.e., frame shifted relative to one another). For example, with overlapping epitopes, two 9-mer epitopes and one 1O-mer epitope can be present in a 10 amino acid peptide. Such a vaccine composition Is administered for therapeutic or prophylactic purposes. The vaccine composition will Include, for example, multiple CTL epitopes from 109P1D4 antigen and at least one HTL epitope. This polyepitopic native sequence is administered either as a peptide or as a nucleic acid sequence which encodes the peptide. Alternatively, an analog can be made of this native sequence, whereby one or more of the epitopes comprise substitutions that alter the crossreactivity and/or binding affinity properties of the polyepitopic peptide. The embodiment of this example provides for the possibility that an as yet undiscovered aspect of immune system processing will apply to the native nested sequence and thereby facilitate the production of therapeutic or prophylactic immune responseinducing vaccine compositions. Additionally, such an embodiment provides for the possibility of motif bearing epitopes for an HLA makeup(s) that Is presently unknown. Furthermore, this embodiment (excluding an analoged embodiment) directs the Immune response to multiple peptide sequences that are actually present in native 109P1 D4, thus avoiding the need to evaluate any junctional epitopes. Lastly, the embodiment provides an economy of scale when producing peptide or nucleic acid vaccine compositions. Related to this embodiment, computer programs are available in the art which can be used to identify in a target sequence, the greatest number of epitopes per sequence length. Example 26: Polvepitopic Vaccine Compositions from Multiple Antigens The 109P1 D4 peptide epitopes of the present invention are used in conjunction with epitopes from other target tumor-associated antigens, to create a vaccine composition that is useful for the prevention or treatment of cancer that expresses 109P1 D4 and such other antigens. For example, a vaccine composition can be provided as a single polypeptide that incorporates multiple epitopes from 109P1 D4 as well as tumor-associated antigens that are often expressed with a target cancer associated with 109P1 D4 expression, or can be administered as a composition comprising a cocktail of one or more discrete epiopes. Alternatively, the vaccine can be administered as a minigene construct or as dendritic cells which have been loaded with the peptide epitopes in vitro. Example 27: Use of peptides to evaluate an Immune response Peptides of the invention may be used to analyze an Immune response for the presence of specific antibodies, CTL or HTL directed to 1 09P1 D4. Such an analysis can be performed In a manner described by Ogg et al., Science 279:2103-2106,1998. In this Example, peptides in accordance with the invention are used as a reagent for diagnostic or 110 prognostic purposes, not as an immunogen. In this example highly sensitive human leukocyte antigen tetrameric complexes (tetramers") are used for a cross sectional analysis of, for example, 109P1D4 HLA-A*0201-specific CTL frequencies from HLA A*0201-positive Individuals at different stages of disease or following immunization comprising a 109P1D4 peptide containing an A*0201 motif. Tetrameric complexes are synthesized as described (Musey et at., N. EngL. J. Med. 337:1267, 1997). Briefly, purified HLA heavy chain (A*0201 in this example) and p2-microglobulin are synthesized by means of a prokaryotic expression system. The heavy chain is modified by deletion of the transmembrane-cytosolic tail and COOH-terminal addition of a sequence containing a BirA enzymatic biotinylation site. The heavy chain, P2-microglobulin, and peptide are refolded by dilution. The 45-kD refolded product is isolated by fast protein liquid chromatography and then blotinylated by BirA in the presence of biotin (Sigma, St Louis, Missouri), adenosine 5' triphosphate and magnesium. Streptavidin-phycoerythrin conjugate is added in a 1:4 molar ratio, and the tetrameric product Is concentrated to I mg/ml. The resulting product is referred to as tetramer phycoerythrdn. For the analysis of patient blood samples, approximately one million PBMCs are centrifuged at 300g for 5 minutes and resuspended in 50 pl of cold phosphate-buffered saline. Tri-color analysis Is performed with the tetramer-phycoerythin, along with anti-CD8-Tricolor, and anti-CD38. The PBMCs are incubated with tetramer and antibodies on ice for 30 to 60 min and then washed twice before formaldehyde fixation. Gates are applied to contain >99.98% of control samples. Controls for the tetramers include both A*0201-negative Individuals and A*0201-positive non-diseased donors. The percentage of cells stained with the tetramer is then determined by flow cytometry. The results indicate the number of cells in the PBMC sample that contain epitope-restricted CTLs, thereby readily indicating the extent of immune response to the 109P1 D4 epitope, and thus the status of exposure to 109PI D4, or exposure to a vaccine that elicits a protective or therapeutic response. Example 28: Use of Peptide Epitopes to Evaluate Recall Responses The peptide epitopes of the invention are used as reagents to evaluate T cell responses, such as acute or recall responses, In patients. Such an analysis may be performed on patients who have recovered from 109P1D4-associated disease or who have been vaccinated with a 109P1 D4 vaccine. For example, the class I restricted CTL response of persons who have been vaccinated may be analyzed. The vaccine may be any 109P1 D4 vaccine. PBMC are collected from vaccinated individuals and HLA typed. Appropriate peptide epitopes of the invention that optimally, bear supermotifs to provide cross-reactivty with multiple HLA supertype family members, are then used for analysis of samples derived from Individuals who bear that HLA type. PBMC from vaccinated Individuals are separated on Ficoll-Histopaque density gradients (Sigma Chemical Co., St Louis, MO), washed three times in HBSS (GIBCO Laboratories), resuspended in RPMI-1640 (GIBCO Laboratories) supplemented with L-glutamine (2mM), penicillin (50U/ml), streptomycin (50 pg/ml), and Hepes (10mM) containing 10% heat-inactivated human AB serum (complete RPMI) and plated using microculture formats. A synthetic peptide comprising an epitope of the invention Is added at 10 pg/mi to each well and HBV core 128-140 epitope is added at I pg/ml to each well as a source of T cell help during the first week of stimulation. In the microculture format, 4 x 105 PBMC are stimulated with peptide in 8 replicate cultures in 96-well round bottom plate in 100 p/well of complete RPMI. On days 3 and 10, 100 pl of complete RPMI and 20 U/mI final concentration of rlL-2 are added to each well. On day 7 the cultures are transferred into a 96-well flat-bottom plate and restimulated with peptide, rlL-2 and 105 Irradiated (3,000 rad) autologous feeder cells. The cultures are tested for cytotoxic activity on day 14. A positive CTL response requires two or more of the eight replicate cultures to display greater than 10% specific 5 1 Cr release, based on comparison with non-diseased control subjects as previously described (Rehermann, et at., Nature Med.

111 2:1104,1108, 1996; Rehermann et al., J. Clin. Invest. 97:1655-1665, 1996; and Rehermann et al. J. Clin. Invest. 98:1432 1440, 1996). Target cell lines are autologous and allogenelc EBV-transformed B-LCL that are either purchased from the American Society for Histocompatiblity and Immunogenetics (ASH I, Boston, MA) or established from the pool of patients as described (Guilhot, et al. J. Virol. 66:2670-2678, 1992). Cytotoxicity assays are performed in the following manner. Target cells consist of either allogeneic HLA-matched or autologous EBV-transformed B lymphoblastoid cell line that are incubated ovemight with the synthetic peptide epitope of the Invention at 10 pM, and labeled with 100 pLCi of 5 1 Cr (Amnersham Corp., Arlington Heights, IL) for 1 hour after which they are washed four times with HBSS. Cytolytic activity is determined in a standard 4-h, split wel 5 iCr release assay using U-bottomed 96 well plates containing 3,000 targets/well. Stimulated PBMC are tested at effectoritarget (E/T) ratios of 20-501 on day 14. Percent cytotoxicity is determined from the formula: 100 x [(experimental release-spontaneous release)/maximum release spontaneous release)j. Maximum release is determined by lysis of targets by detergent (2% Triton X-100; Sigma Chemical Co., St Louis, MO). Spontaneous release is <25% of maximum release for aU experiments. The results of such an analysis Indicate the extent to which HLA-restricted CTL populations have been stimulated by previous exposure to 109P1D4 or a 109P1D4 vaccine. Similarly, Class I restricted HTL responses may also be analyzed. Purified PBMC are cultured in a 96-well flat bottom plate at a density of 1.5x10 5 cells/well and are stimulated with 10 pg/ml synthetic peptide of the invention, whole 109P1D4 antigen, or PHA. Cells are routinely plated in replicates of 4-6 wells for each condition. After seven days of culture, the medium is removed and replaced with fresh medium containing IOU/mi IL-2. Two days later, I pCi 3H-thymidine is added to each well and incubation is continued for an additional 18 hours. Cellular DNA is tien harvested on glass fiber mats and analyzed for 3 H-thymidine incorporation. Antigen-specific T cell proliferation is calculated as the ratio of 3H thymidine incorporation In the presence of antigen divided by the 3 H-thymidine incorporation In the absence of antigen. Example 29: Induction Of Specific CTL Response In Humans A human clinical trial for an immunogenic composition comprising CTL and HTL epitopes of the Invention is set up as an IND Phase 1, dose escalation study and carried out as a randomized, double-blind, placebo-controlled trial. Such a trial is designed, for example, as follows: A total of about 27 individuals are enrolled and divided Into 3 groups: Group 1: 3 subjects are injected with placebo and 6 subjects are Injected with 5 pg of peptide composition; Group il: 3 subjects are injected with placebo and 6 subjects are Injected with 50 pg peptide composition; Group Ill: 3 subjects are injected with placebo and 6 subjects are injected with 500 pg of peptide composition. After 4 weeks following the first injection, all subjects receive a booster inoculation at the same dosage. The endpoints measured In this study relate to the safety and tolerability of the peptide composition as well as Its Immunogenlcity. Cellular immune responses to the peptide composition are an index of the intrinsic activity of this the peptide composition, and can therefore be viewed as a measure of biological efficacy. The following summarize the clinical and laboratory data that relate to safety and efficacy endpoints. Safety: The incidence of adverse events Is monitored In the placebo and drug treatment group and assessed in terms of degree and reversibility. Evaluation of Vaccine Efficacy: For evaluation of vaccine efficacy, subjects are bled before and after Injection. Peripheral blood mononuclear cells are isolated from fresh heparinized blood by Ficoll-Hypaque density gradient 112 centrifugation, aliquoted in freezing media and stored frozen. Samples are assayed for CTL and HTL activity. The vaccine is found to be both safe and efficacious. Example 30: Phase If Trials In Patients Expressina 109PD4 Phase I trials are performed to study the effect of administering the CTL-HTL peptide compositions to patients having cancer that expresses 109P1 D4. The main objectives of the trial are to determine an effective dose and regimen for inducing CTLs in cancer patients that express 109P1D4, to establish the safety of inducing a CTL and HTL response in these patients, and to see o what extent activation of CTLs improves the clinical picture of these patients, as manifested, e.g., by the reduction and/or shrinking of lesions. Such a study is designed, for example, as follows: The studies are performed In multiple centers. The trial design is an open-label, uncontrolled, dose escalation protocol wherein the peptide composition is administered as a single dose followed six weeks later by a single booster shot of the same dose. The dosages are 50, 500 and 5,000 micrograms per Injection. Drug-associated adverse effects (severity and reversibility) are recorded. There are three patient groupings. The first group is injected with 50 micrograms of the peptide composition and the second and third groups with 500 and 5,000 micrograms of peptide composition, respectively. The patients within each group range in age from 21-65 and represent diverse ethnic backgrounds. All of them have a tumor that expresses 109P1D4. Clinical manifestations or antigen-specific T-cell responses are monitored to assess the effects of administering the peptide compositions. The vaccine composition is found to be both safe and efficacious in the treatment of 109P1D4 associated disease. Example 31: Induction of CTL Resonses Using a Prime Boost Protocol A prime boost protocol similar in its underlying principle to that used to confirm the efficacy of a DNA vaccine In transgenic mice, such as described above in the Example entitled "The Plasmid Construct and the Degree to Which It Induces lmmunogenicity,' can also be used for the administration of the vaccine to humans. Such a vaccine regimen can include an initial administration of, for example, naked DNA followed by a boost using recombinant virus encoding the vaccine, or recombinant protein/polypeptide or a peptide mixture administered in an adjuvant. For example, the initial immunization may be performed using an expression vector, such as that constructed in the Example entitled 'Construction of "Minigene" Multi-Epitope DNA Plasmids" in the form of naked nucleic acid administered IM (or SC or ID) in the amounts of 0.5-5 mg at multiple sites. The nucleic acid (0.1 to 1000 pg) can also be administered using a gene gun. Following an incubation period of 3-4 weeks, a booster dose Is then administered. The booster can be recombinant fowlpox virus administered at a dose of 5-107 to 5x109 pfu. An alternative recombinant virus, such as an MVA, canarypox, adenovirus, or adeno-associated virus, can also be used for the booster, or the polyepitopic protein or a mixture of the peptides can be administered. For evaluation of vaccine efficacy, patient blood samples are obtained before immunization as well as at Intervals following administration of the Initial vaccine and booster doses of the vaccine. Peripheral blood mononuclear cells are isolated from fresh heparinized blood by Ficoll-Hypaque density gradient centrifugation, allquoted in freezing media and stored frozen. Samples are assayed for CTL and HTL activity. Analysis of the results indicates that a magnitude of response sufficient to achieve a therapeutic or protective immunity against 109P1 D4 is generated. Example 32: AdmInistration of Vaccine Compositlons Using Dendritic Cells (DC) 113 Vaccines comprising peptide epitopes of the invention can be administered using APCs, or "professional" APCs such as DC. In this example, peptide-pulsed DC are administered to a patient to stimulate a CTL response in vivo. In this method, dendritic cells are isolated, expanded, and pulsed with a vaccine comprising peptide CTL and HTL epitopes of the invention. The dendritic cels are infused back into the patient to elicit CTL and HTL responses in vivo. The induced CTL and HTL then destroy or facilitate destruction, respectively, of the target cells that bear the 109P1D4 protein from which the epitopes In the vaccine are derived. For example, a cocktail of epitope-comprising peptides is administered ex vivo to PBMC, or isolated DC therefrom. A pharmaceutical to facilitate harvesting of DC can be used, such as Progenlpoletinm (Monsanto, St. Louis, MO) or GM CSF/L-4. After pulsing the DC with peptides, and prior to reinfusion into patients, the DC are washed to remove unbound peptides. As appreciated clinically, and readily determined by one of skill based on clinical outcomes, the number of DC reinfused Into the patient can vary (see, e.g., Nature Med. 4:328, 1998; Nature Med. 2:52, 1996 and Prostate 32:272, 1997). Although 2-50 x 106 DC per patient are typical administered, larger number of DC, such as 107 or 108 can also be provided. Such cell populations typically contain between 50-90% DC. In some embodiments, peptide-loaded PBMC are injected into patients without purification of the DC. For example, PBMC generated after treatment with an agent such as Progenipoletin'" are Injected into patients without purification of the DC. The total number of PBMC that are administered often ranges from 108 to 101. Generally, the cell doses Injected into patients is based on the percentage of DC in the blood of each patient, as determined, for example, by immunofluorescence analysis with specific anti-DC antibodies. Thus, for example, If ProgenlpoietinTm mobilizes 2% DC In the peripheral blood of a given patient, and that patient Is to receive 5 x 106 DC, then the patient will be Injected with a total of 2.5 x 108 peptide-loaded PBMC. The percent DC mobilized by an agent such as Progenlpoletin T m is typically estimated to be between 2-10%, but can vary as appreciated by one of skill In the art. Ex vivo activation of CTUHTL responses Alternatively, ex vivo CTL or HTL responses to 109P1D4 antigens can be induced by incubating, in tissue culture, the patients, or genetically compatible, CTL or HTL precursor cells together with a source of APC, such as DC, and immunogenic peptides. After an appropriate Incubation time (typically about 7-28 days), In which the precursor cells are activated and expanded Into effector cells, the cells are Infused into the patient, where they will destroy (CTL) or facilitate destruction (HTL) of their specific target cels, l.e., tumor cells. Example 33: An Alternative Method of Identifying and Confirming Motif-Bearing Peptides Another method of Identifying and confirming motif-bearing peptides Is to elute them from cells bearing defined MHC molecules. For example, EBV transformed B cel lines used for tissue typing have been extensively characterized to determine which HLA molecules they express. In certain cases these cells express only a single type of HLA molecule. These cells can be transfected with nucleic acids that express the antigen of interest, e.g. 109P1 D4. Peptides produced by endogenous antigen processing of peptides produced as a result of transfection will then bind to HLA molecules within the cell and be transported and displayed on the cell's surface. Peptides are then eluted from the HLA molecules by exposure to mild acid conditions and their amino acid sequence determined, e.g., by mass spectral analysis (e.g., Kubo et al., J. Immunol. 152:3913, 1994). Because the majority of peptides that bind a particular HLA molecule are motif-bearing, this is an alternative modality for obtaining the motif-bearing peptides correlated with the particular HLA molecule expressed on the cell. Alternatively, cell lines that do not express endogenous HLA molecules can be transfected with an expression 114 construct encoding a single HLA allele. These cells can then be used as described, i.e., they can then be transfected with nucleic acids that encode 109P1D4 to isolate peptides corresponding to 109P1D4 that have been presented on the cell surface. Peptides obtained from such an analysis will bear motif(s) that correspond to binding to the single HLA allele that is expressed in the cell. As appreciated by one in the art, one can perform a similar analysis on a cell bearing more than one HLA allele and subsequently determine peptides specific for each HLA allele expressed. Moreover, one of sill would also recognize that means other than transfection, such as loading with a protein antigen, can be used to provide a source of antigen to the cell. Example 34: Complementary Polynucleotides Sequences complementary to the 109P1D4-encoding sequences, or any parts thereof, are used to detect, decrease, or Inhibit expression of naturally occurring 109P1D4. Although use of oligonudeotides comprising from about 15 to 30 base pairs Is described, essentially the same procedure is used with smaller or with larger sequence fragments. Appropriate oligonucleotides are designed using, e.g., OLIGO 4.06 software (National Biosciences) and the coding sequence of 109P1D4. To inhibit transcription, a complementary oligonucleotide is designed from the most unique 5' sequence and used to prevent promoter binding to the coding sequence. To inhibit translation, a complementary oligonucleotide Is designed to prevent ribosomal binding to a 109P1D4-encoding transcript. Example 35: Purification of Naturally-occurrin or Recombinant 109P1D4 Using I09P1D4-Specific Antibodies Naturally occurring or recombinant 109P1 D4 is substantially purified by Immunoaffinity chromatography using antibodies specific for 109P1D4. An Immunoaffinity column is constructed by covalently coupling anti-109PiD4 antibody to an activated chromatographic resin, such as CNBr-activated SEPHAROSE (Amersham Pharmacia Biotech). After the coupling, the resin is blocked and washed according to the manufacturer's instructions. Media containing 109P1 D4 are passed over the immunoaffinity column, and the column is washed under conditions that allow the preferential absorbance of I 09P1 D4 (e.g., high ionic strength buffers in the presence of detergent). The column is eluted under conditions that disrupt antibody/1 09P1 D4 binding (e.g., a buffer of pH 2 to pH 3, or a high concentration of a chaotrope, such as urea or thiocyanate Ion), and GCR.P Is collected. Example 36; identIfication of Molecules Which Interact with 109PiD4 109P1D4, or biologically active fragments thereof, are labeled with 121 1 Bolton-Hunter reagent (See, e.g., Bolton at aL. (1973) Biochem. J. 133:529.) Candidate molecules previously arrayed in the wells of a multi-we plate are Incubated with the labeled 109P1D4, washed, and any wells with labeled 109P1D4 complex are assayed. Data obtained using different concentrations of 109P1D4 are used to calculate values for the number, affinity, and association of 109P1D4 with the candidate molecules. Example 37: In Vivo Assay for 109PiD4 Tumor Growth Promotion The effect of a 109P1D4 protein on tumor cell growth is evaluated in vivo by gene overexpresson in tumor-bearing mice. For example, SCID mice are injected subcutaneously on each flank with I x 106 of either PC3, DU145 or 3T3 cells containing tkNeo empty vector or a nucleic acid sequence of the invention. At least two strategies can be used: (1) Constitutive expression under regulation of a promoter such as a constitutive promoter obtained from the genomes of viruses such as polyoma virus, fowIpox virus (UK 2,211,504 published 5 July 1989), adenovirus (such as Adenovirus 2), bovine 115 papilloma virus, avian sarcoma virus, cytomegalovirus, a retrovirus, hepatitis-B virus and Simian Virus 40 (SV40), or from heterologous mammalian promoters, e.g., the actin promoter or an immunoglobulin promoter, provided such promoters are compatible with the host cell systems, and (2) Regulated expression under control of an Inducible vector system, such as ecdysone, tet etc., provided such promoters are compatible with the host cell systems. Tumor volume Is then monitored at the appearance of palpable tumors and followed over time to determine if the cells expressing a gene of the invention grow at a faster rate and whether tumors of a 109P1 D4 protein-expressing cells demonstrate characteristics of altered aggressiveness (e.g. enhanced metastasis, vascularization, reduced responsiveness to chemotherapeutic drugs). Additionally, mice can be Implanted with 1 x 105 of the same cells orthotopically to determine if a protein of the invention has an effect on local growth in the prostate or on the ability of the cells to metastasize, specifically to lungs, lymph nodes, and bone marrow. The assay is also useful to determine the inhibitory effect of candidate therapeutic compositions, such as for example, 109P1D4 protein-related intrabodies, 109P1D4 gene-related antisense molecules and ribozymes. Example 38: 109Pi D4 Monocional Antibody-mediated Inhibition of Tumors In Vvo The significant expression of 109P1 D4 proteins In the cancer tissues of Table I and its restrictive expression in normal tissues, together with its expected cell surface expression, makes 1 09P1 D4 proteins excellent targets for antibody therapy. Similarly, 109PID4 proteins are a target for T cell-based Immunotherapy. Thus, for 109P1D4 genes expressed, e.g., in prostate cancer, the therapeutic efficacy of anti-109P1 D4 protein mAbs in human prostate cancer xenograft mouse models is evaluated by using androgen-independent LAPC-4 and LAPC-9 xenografts (Craft, N., et aL.,. Cancer Res, 1999. 59(19): p. 5030-6) and the androgen Independent recombinant cell line PC3-of 109P1D4 (see, e.g., Kalghn, M.E., et al., Invest Urol, 1979. 17(1): p. 16-23); analogous models are used for other cancers. Antibody efficacy on tumor growth and metastasis formation Is studied, e.g., in a mouse orthotopic prostate cancer xenograft models and mouse kidney xenograft models. The antibodies can be unconjugated, as discussed in this Example, or can be conjugated to a therapeutic modality, as appreciated in the art Anti-I 09P1 D4 protein mAbs inhibit formation of both the androgen-dependent LAPC-9 and androgen-independent PC3-109P1D4 protein tumor xenografts. And-109P1D4 protein mAbs also retard the growth of established orthotopic tumors and prolonged survival of tumor-bearing mice. These results Indicate the utility of anti-109P 1D4 protein mAbs in the treatment of local and advanced stages of prostate cancer. (See, e.g., (Saffran, D., et al., PNAS 10:1073-1078 or World Wide Web URL ww.pnas.orglcgVdol0.1073/pnas.051624698). Administration of the anti-109P1D4 protein mAbs lead to retardation of established orthotopic tumor growth and inhibItion of metastasis to distant sites, resulting In a significant prolongation In the survival of tumor-bearing mice. These studies indicate that proteins of the invention are attractive targets for immunotherapy and demonstrate the therapeutic potential of anti-109P1D4 protein mAbs for the treatment of local and metastatic cancer. This example demonstrates that unconjugated 109P1D4 protein-related monoclonal antibodies are effective to Inhibit the growth of human prostate tumor xenografts and human kidney xenografls grown in SCID mice; accordingly a combination of such efficacious monoclonal antibodies Is also effective. Tumor Inhibition using multiple unconjugated mAbs Materials and Methods 109P1D4 Protein-related Monoclonal Antibodies: Monoclonal antibodies are raised against proteins of the invention as described In the Example entitled "Generation of 109P1 D4 Monoclonal Antibodies". The antibodies are characterized by ELISA, Western blot, FACS, and 116 immunoprecipitation for their capacity to bind to the respective protein of the invention. Epitope mapping data for, e.g., the anti-109P1D4 protein mAbs, as determined by ELISA and Western analysis, indicate that the antibodies recognize epitopes on the respective 109P1 D4 protein. Immunohistochemical analysis of prostate cancer tissues and cells with these antibodies is performed. The monoclonal antibodies are purified from ascites or hybridoma tissue culture supematants by Protein-G Sepharose chromatography, dialyzed against PBS, filter sterilized, and stored at -20*C. Protein determinations are performed by a Bradford assay (Bio-Rad, Hercules, CA). A therapeutic monoclonal antibody or a cocktail comprising a mixture of Individual monoclonal antibodies is prepared and used for the treatment of mice receiving subcutaneous or orthotopic Injections of LAPC-9 prostate tumor xenografts. Cancer Xenografts and Cell Lines The LAPC-9 xenograft, which expresses a wild-type androgen receptor and produces prostate-specific antigen (PSA), is passaged in 6- to 8-week-old male ICR-severe combined immunodeficient (SCID) mice (Taconic Farms) by s.c. trocar implant (Craft, N., et at., supra). The prostate carcinoma cell line PC3 (American Type Culture Collection) is maintained in RPMI supplemented with L-glutamine and 10% FBS. Recombinant PC3 and 3T3- cell populations expressing a protein of the invention are generated by retroviral gene transfer as described in Hubert R.S., et al., STEAP' a prostate-specific cell-surface antigen highly expressed in human prostate tumors. Proc Nati Acad Sci U S A, 1999. 96(25): p. 14523-8. Anti-protein of the invention staining is detected by using an FITC-conjugated goat anti-mouse antibody (Southem Biotechnology Associates) followed by analysis on a Coulter Epics-XL flow cytometer. Xenograft Mouse Models, Subcutaneous (s.c.) tumors are generated by Injection of I x 10 6 LAPC-9, PC3, recombinant PC3-protein of the invention, 3T3 or recombinant 3T3-protein of the Invention cells mixed at a 1:1 dilution with Matrigel (Collaborative Research) in the right flank of male SCID mice. To test antibody efficacy on tumor formation, i.p. antibody injections are started on the same day as tumor-cell injections. As a control, mice are injected with either purified mouse IgG (ICN) or PBS; or a purified monoclonal antibody that recognizes an irrelevant antigen not expressed in human cells. In preliminary studies, no difference is found between mouse IgG or PBS on tumor growth. Tumor sizes are determined by vernier caliper measurements, and the tumor volume Is calculated as length x width x height. Mice with s.c. tumors greater than 1.5 cm in diameter are sacrificed. PSA levels are determined by using a PSA ELISA kit (Anogen, Mississauga, Ontario). Circulating levels of, e.g., anti-109P1D4 protein mAbs are determined by a capture ELISA kit (Bethyl Laboratories, Montgomery, TX). (See, e.g., Saffran, D., et al., PNAS 10:1073-1078 or www.pnas.org/cgi/ doi10.1073/pnas.051624698) Orthotopic injections are performed under anesthesia by using ketamine/xylazine. For prostate orthotopic studies, an Incision is made through the abdominal muscles to expose the bladder and seminal vesicles, which then are delivered through the Incision to expose the dorsal prostate. LAPC-9 or PC3 cells (5 x 105) mixed with Matigel are injected Into each dorsal lobe In a 10-pl volume. To monitor tumor growth, mice are bled on a weekly basis for determination of PSA levels. The mice are segregated Into groups for the appropriate treatments, with anti-protein of the invention or control mAbs being injected i.p. Anti-109P1D4 Protein mAbs Inhibit Growth of Respective 109P1D4 Protein-Expressinq Xenograft-Cancer Tumors The effect of antl-109P1D4 protein mAbs on tumor formation Is tested by using LAPC-9 and recombinant PC3 protein of the invention orthotopic models. As compared with the s.c. tumor model, the orthotopic model, which requires injection of tumor cells directly in the mouse prostate or kidney, respectively, results In a local tumor growth, development of metastasis In distal sites, deterioration of mouse health, and subsequent death (Saffran, D., et al., PNAS supra; Fu, X, et al., 117 Int J Cancer, 1992. 52(6): p. 987-90; Kubota, T., J Cell Biochem, 1994. 56(1): p. 4-8). The features make the orthotopic model more representative of human disease progression and allowed us to follow the therapeutic effect of mAbs on clinically relevant end points. Accordingly, tumor cells are Injected into the mouse prostate or kidney, and 2 days later, the mice are segregated into two groups and treated with either: a) 200-500pg, of anti-109P1 04 protein Ab, or b) PBS three times per week for two to five weeks. A major advantage of the orthotopic prostate-cancer model is the ability to study the development of metastases. Formation of metastasis in mice bearing established orthotopic tumors is studied by IHC analysis on lung sections using an antibody against a prostate-specific cell-surface protein STEAP expressed at high levels in LAPC-9 xenografts (Hubert, R.S., et at., Proc Nad Acad Sd U S A, 1999. 96(25): p. 14523-8). Mice bearing established orthotopic LAPC-9 or recombinant PC3-109P1D4 protein tumors are administered 10OOpg injections of either anti-109P1D4 protein mAbs or PBS over a 4-week period. Mice in both groups are allowed to establish a high tumor burden (PSA levels greater than 300 ng/ml for IAPC-9), to ensure a high frequency of metastasis formation in mouse lungs. Mice then are killed and their prostate and lungs are analyzed for the presence of tumor cells by IHC analysis. These studies demonstrate a broad anti-tumor efficacy of anti-109P1D4 protein antibodies on initiation and progression of prostate cancer In xenograft mouse models. Anti-1 09P1 D4 protein antibodies inhibit tumor formation of both androgen-dependent and androgen-independent tumors, retard the growth of already established tumors, and prolong the survival of treated mice. Moreover, anti-109P1D4 protein mAbs demonstrate a dramatic Inhibitory effect on the spread of local prostate tumor to distal sites, even in the presence of a large tumor burden. Thus, anti-109P1D4 protein mAbs are efficacious on major clinically relevant end points (tumor growth), prolongation of survival, and health. Example 39: Therapeutic and Diagnostlc use of AntI-109P1D4 Antibodies In Humans. Anti- 09P1 D4 monoclonal antibodies are safely and effectively used for diagnostic, prophylactic, prognostic and/or therapeutic purposes in humans. Western blot and immunohistochemical analysis of cancer tissues and cancer xenografts with anti-109P1D4 mAb show strong extensive staining in carcinoma but significantly lower or undetectable levels in normal tissues. Detection of 109P1 D4 In carcinoma and in metastatic disease demonstrates the usefulness of the mAb as a diagnostic and/or prognostic indicator. Anti-i09P1D4 antibodies are therefore used in diagnostic applications such as immunohistochemistry of kidney biopsy specimens to detect cancer from suspect patients. As determined by flow cytometry, anti-109P1D4 mAb specificaly binds to carcinoma cells. Thus, anti-1 09P1 D4 antibodies are used in diagnostic whole body imaging applications, such as radiolmmunoscintigraphy and radioimmunotherapy, (see, e.g., Potamianos S., et al. Anticancer Res 20(2A):925-948 (2000)) for the detection of localized and metastatic cancers that exhibit expression of 109P1D4. Shedding or release of an extracellular domain of 109P1D4 into the extracellular milieu, such as that seen for alkaline phosphodiesterase B10 (Meerson, N. R., Hepatology 27:563-568 (1998)), allows diagnostic detection of 109P1D4 by anti-109P1D4 antibodies In serum and/or urine samples from suspect patients. Anti-109P1D4 antibodies that specifically bind 109P1D4 are used in therapeutic applications for the treatment of cancers that express 109P1D4. Anti-109P1D4 antibodies are used as an unconjugated modality and as conjugated form In which the antibodies are attached to one of various therapeutic or imaging modalities well known in the art, such as a prodrugs, enzymes or radioisotopes. In preclinical studies, unconjugated and conjugated anti-109P1D4 antibodies are tested for efficacy of tumor prevention and growth Inhibition in the SCID mouse cancer xenograft models, e.g., kidney cancer 118 models AGS-K3 and AGS-K6, (see, e.g., the Example entitled '109P1D4 Monoclonal Antibody-mediated Inhibition of Bladder and Lung Tumors In ivo"). Either conjugated and unconjugated anti-109P1 D4 antibodies are used as a therapeutic modality in human clinical trials either alone or in combination with other treatments as described in following Examples. Example 40: Human Clinical Trials for the Treatment and Diagnosis of Human Carcinomas through use of Human Anti-109PiD4 AntibodIes In vivo Antibodies are used In accordance with the present invention which recognize an epitope on 109P1 D4, and are used in the treatment of certain tumors such as those listed in Table I. Based upon a number of factors, including 109P1D4 expression levels, tumors such as those listed in Table I are presently preferred indications. In connection with each of these Indications, three clinical approaches are successfully pursued. I.) Adjunctive therapy' In adjunctive therapy, patients are treated with anti-109P1D4 antibodies In combination with a chemotherapeutic or antineoplastic agent and/or radiation therapy. Primary cancer targets, such as those listed in Table I, are treated under standard protocols by the addition anti-1l09P1D4 antibodies to standard first and 'second line therapy. Protocol designs address effectiveness as assessed by reduction in tumor mass as well as the ability to reduce usual doses of standard chemotherapy. These dosage reductions allow additional and/or prolonged therapy by redudng dose-related toxicity of the chemotherapeutic agent. Anti-I 09P1 D4 antibodies are utilized in several adjunctive clinical trials in combination with the chemotherapeutic or antineoplastic agents adriamycin (advanced prostrate carcinoma), cisplatin (advanced head and neck and lung carcinomas), taxol (breast cancer), and doxorubicin (preclinical). II.) Monotherapy in connection with the use of the anti-109P1D4 antibodies In monotherapy of tumors, the antibodies are administered to patients without a chemotherapeutic or antineoplastic agent In one embodiment, monotherapy Is conducted clinically in end stage cancer patients with extensive metastatic disease. Patients show some disease stabilization. Trials demonstrate an effect in refractory patients with cancerous tumors. Ill.) Imaging Agent: Through binding a radionuclide (e.g., iodine or yttrium (113, Y9) to anti-109P1D4 antibodies, the radiolabeled antibodies are utilized as a diagnostic and/or imaging agent In such a role, the labeled antibodies localize to both solid tumors, as well as, metastatic lesions of cells expressing 109P1D4. In connection with the use of the anti-109P1D4 antibodies as imaging agents, the antibodies are used as an adjunct to surgical treatment of solid tumors, as both a pre-surgical screen as well as a post-operative follow-up to determine what tumor remains and/or returns. In one embodiment, a (i' In)-109P1D4 antibody is used as an Imaging agent in a Phase I human clInical trial In patients having a carcinoma that expresses 109P1D4 (by analogy see, e.g., Divgi et al. J. Nati. Cancer Inst. 83:97-104 (1991)). Patients are followed with standard anterior and posterior gamma camera. The results indicate that primary lesions and metastatic lesions are Identified. Dose and Route of Administration As appreciated by those of ordinary skill in the art, dosing considerations can be determined through comparison with the analogous products that are in the clinic. Thus, anti-1 09P1 D4 antibodies can be administered with doses in the range of 5 to 400 mg/m 2 , with the lower doses used, e.g., in connection with safety studies. The affinity of anti-109P1D4 antibodies relative to the affinity of a known antibody for its target is one parameter used by those of skill in the art for determining analogous dose regimens. Further, anti-109P1D4 antibodies that are fully human antibodies, as compared to the chimeric antibody, have slower clearance; accordingly, dosing in patients with such fully human anti-109P1D4 antibodies can be lower, perhaps in the range of 50 to 300 mg/m 2 , and still remain efficacious. Dosing in mg/m2, as opposed to the conventional measurement of dose In mg/kg, is a measurement based on surface area and is a convenient dosing measurement that Is designed to include patients of all sizes from infants to adults.

119 Three distinct delivery approaches are useful for delivery of anti-109PID4 antibodies. Conventional intravenous delivery is one standard delivery technique for many tumors. However, in connection with tumors in the peritoneal cavity, such as tumors of the ovaries, biliary duct, other ducts, and the like, Intraperitoneal administration may prove favorable for obtaining high dose of antibody at the tumor and to also minimize antibody clearance. In a similar manner, certain solid tumors possess vasculature that is appropriate for regional perfusion. Regional perfusion allows for a high dose of antibody at the site of a tumor and minimizes short term clearance of the antibody. Clinical Development Plan (CDP) Overview: The CDP follows and develops treatments of anti-1 09P1 D4 antibodies in connection with adjunctive therapy, monotherapy, and as an imaging agent Trials initially demonstrate safety and thereafter confirm efficacy in repeat doses. Trails are open label comparing standard chemotherapy with standard therapy plus anti-1 09P104 antibodies. As will be appreciated, one criteria that can be utilized in connection with enrollment of patients is 109P1D4 expression levels in their tumors as determined by biopsy. As with any protein or antibody Infusion-based therapeutic, safety concerns are related primarily to (i) cytoidne release syndrome, I.e., hypotension, fever, shaking, chils; (ii) the development of an Immunogenic response to the material (i.e., development of human antibodies by the patient to the antibody therapeutic, or HAHA response); and, (iii) toxicity to normal cells that express 109P1D4. Standard tests and follow-up are utilized to monitor each of these safety concerns. Anti-109P1D4 antibodies are found to be safe upon human administration. Example 4: Human Clinical Trial Adiunctive Therapy with Human Anti-109P1D4 Antibody and Chemotherapeutic Agent A phase I human clinical trial is initiated to assess the safety of six intravenous doses of a human anti-1 09P1 D4 antibody in connection with the treatment of a solid tumor, e.g., a cancer of a tissue listed in Table I. In the study, the safety of single doses of antl-109P1 D4 antibodies when utilized as an adjunctive therapy to an antineoplastic or chemotherapeutic agent as defined herein, such as, without limitation: cisplatin, topotecan, doxorubicin, adriamycin, taxol, or the like, is assessed. The trial design Includes delivery of six single doses of an anti-109P1D4 antibody with dosage of antibody escalating from approximately about 25 mg/m 2 to about 275 mg/m 2 over the course of the treatment In accordance with the following schedule: Day 0 Day 7 Day 14 Day 21 Day 28 Day 35 mAb Dose 25 75 125 175 225 275 mg/m 2 mg/m 2 mg/m 2 mg/m 2 mg/m 2 mg/m 2 Chemotherapy + + + + + + (standard dose) Patients are closely followed for one-week following each adminIstration of antibody and chemotherapy. In particular, patients are assessed for the safety concems mentioned above: (1) cytokine release syndrome, i.e., hypotension, fever, shaking, chills; (ii) the development of an immunogenic response to the material (i.e., development of human antibodies by the patient to the human antibody therapeutic, or HAHA response); and, (iii) toxicity to normal cells that express 109P1 D4. Standard tests and follow-up are utilized to monitor each of these safety concerns. Patients are also assessed for clinical outcome, and particularly reduction In tumor mass as evidenced by MRI or other Imaging.

120 The anti-109P1D4 antibodies are demonstrated to be safe and efficacious, Phase i trials confirm the efficacy and refine optimum dosing. ExampIe 42: Human Clinical Trial: Monotherapy with Human Anti-109P1D4 Antibody Anti-109P1D4 antibodies are safe in connection with the above-discussed adjunctive trial, a Phase II human clinical trial confirms the efficacy and optimum dosing for monotherapy. Such trial Is accomplished, and entails the same safety and outcome analyses, to the above-described adjunctive trial with the exception being that patients do not receive chemotherapy concurrently with the receipt of doses of anti-109P1D4 antibodies. Example 43: Human Clinical Trial: Diagnostic Imaging with Anti-109P1D4 Antibody Once again, as the adjunctive therapy discussed above is safe within the safety criteria discussed above, a human clinical trial is conducted concerning the use of anti-109P1D4 antibodies as a diagnostic imaging agent. The protocol is designed in a substantially similar manner to those described In the art, such as In Divgi et al. J. Natg. Cancer Inst. 83:97-104 (1991). The antibodies are found to be both safe and efficacious when used as a diagnostic modality. Example 44: 109PID4 Functional Assays I. Phosphorlation of 109P1D4 on tvrosine residues One hallmark of the cancer cell phenotype Is the active signal transduction of surface bound receptor molecules, such as the EGF receptor, through tyrosine phosphorylation of their cytoplasmic domains and their subsequent interaction with cytosolic signaling molecules. To address the possibility that 109P1D4 is phosphorylated on its cytoplamsic tyrosine residues, 293T ceils were transfected with the 109P1D4 gene In an expression plasmid such that the 109P1D4 gene was fused with a Myc/His tag, and were then stimulated with pervanadate (a 1:1 mixture of NasV4 and H202). After solubilization of the cells In Triton X-100, the 109P1 D4 protein was Immunoprecipitated with anti-His polyclonal antibody (pAb), subjected to SDS-PAGE and Western blotted with anti-phosphotyrosine. Equivalent immunoprecipitates were Westem blotted with anti-His antibody. In Figure 22, 109P1D4 exhibits tyrosine phosphorylation only upon cell treatment with pervanadate and not without treatment. This suggests that pervanadate, which inhibits Intracellular protein tyrosine phosphatases (PTPs), allows the accumulation of phosphotyrosine (tyrosine kinase activity) on 109P1D4. Further, a large amount of the I 09P1D4 protein is sequestered Into the Insoluble fraction upon pervanadate activation, suggesting its association with cytoskeletal components. Similar effects of partial insolubility in Triton X-100 have been observed for cadherins, proteins that are related to protocadherins based on homology of their extracellular domains. Cadherins are known to Interact with cytoskeletal proteins including acin, which are not readily soluble in the detergent conditions used in this study. Together, these data indicate that 109P1D4 is a surface receptor with the capacity to be phosphorylated on tyrosine and to bind to signaling molecules that possess SH2 or PTB binding domains, Including but not limited to, phospholipase-Cyl, Grb2, Shc, Crk, PI-3-kinase p85 subunit, rasGAP, Src-family kinases and abl-family kinases. Such Interactions are important for downstream signaling through 109P1D4, leading to changes In adhesion, proliferation, migration or elaboration of secreted factors. In addition, 109P1D4 protein interacts with cytoskeletal components such as actin that facilitates its cell adhesion functions. These phenotypes are enhanced in 109P1D4 expressing tumor cells and contribute to their increased capacity to metastasize and grow In vivo. Thus, when 109P1D4 plays a role in cell signaling and phosphorylation, it is used as a target for diagnostic, prognostic, preventative and/or therapeutic purposes. Example 45: 109P1D4 RNA Interference (RNAQi 121 RNA interference (RNAi) technology is implemented to a variety of cell assays relevant to oncology. RNA is a post-transcriptional gene silencing mechanism activated by double-stranded RNA (dsRNA). RNAi induces specific mRNA degradation leading to changes in protein expression and subsequently in gene function. In mammalian cells, these dsRNAs called short interfering RNA (siRNA) have the correct composition to activate the RNAI pathway targeting for degradation, specifically some mRNAs. See, Elbashir S.M., ef. at., Duplexes of 21-nucleotide RNAs Mediate RNA interference in Cultured Mammalian Cells, Nature 411(6836):494-8 (2001). Thus, RNAi technology is used successfully in mammalian cells to silence targeted genes. Loss of cell proliferation control Is a hallmark of cancerous cells; thus, assessing the role of 109P1D4 in cell survivallproliferation assays Is relevant. Accordingly, RNAI was used to investigate the function of the 109P1D4 antigen. To generate siRNA for 109P1 D4, algorithms were used that predict oligonucleotides that exhibit the critical molecular parameters (G:C content, melting temperature, etc.) and have the ability to significantly reduce the expression levels of the 109P1D4 protein when introduced into cells. Accordingly, three targeted sequences for the 109P1D4 siRNA are: 5' AAGAGGATACTGGTGAGATCT3'(SEQIDNO: 57)(oligo109P1D4.a),5'AAGAGCAATGGTGCTGGTAAA3'(SEQID NO: 58)(ollgo 109P1D4.c), and 5' AACACCAGAAGGAGACAAGAT 3' (SEQ ID NO: 59)(oligo 109P1D4.d). In accordance with this Example, 109P1D4 siRNA compositions are used that comprise sIRNA (double stranded, short Interfering RNA) that correspond to the nucleic acid ORF sequence of the 109P1 D4 protein or subsequences thereof. Thus, sIRNA subsequences are used in this manner are generally 5, 6, 7, 8, 9, 10, 11, 12,13,14, 15,16,17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30,31, 32, 33, 34, 35 or more than 35 contiguous RNA nucleotides in length. These siRNA sequences are complementary and non-complementary to at least a portion of the mRNA coding sequence. In a preferred embodiment, the subsequences are 19-25 nucleotides in length, most preferably 21-23 nucleotides in length. In preferred embodiments, these siRNA achieve knockdown of 109P1D4 antigen in cells expressing the protein and have functional effects as described below. The selected siRNAs (109P1 D4.a, 109P1D4.c, 109P1D4.d oligos) were tested in LNCaP cells in the 3 H-thymidine incorporation assay (measures cellular proliferation). Moreover, the oligonudeotides achieved knockdown of 109P1D4 antigen in cells expressing the protein and had functional effects as described below using the following protocols. Mammalian sIRNA transfections: The day before siRNA transfection, the different cell lines were plated in media (RPMI 1640 with 10% FBS w/o antibiotics) at 2x10 3 cells/well in 80 p (96 well plate format) for the proliferation assay. In parallel with the 109P1 D4 specific siRNA oligo, the following sequences were Included In every experiment as controls: a) Mock transfected cells with Lipofectamine 2000 (Invitrogen, Carlsbad, CA) and annealing buffer (no siRNA); b) Luclferase-4 specific sIRNA (targeted sequence: 5'-AAGGGACGAAGACGAACACUUCTT-3') (SEQ ID NO: 60); and, c) Eg5 specific siRNA (targeted sequence: 5'-AACTGAAGACCTGAAGACAATAA-3') (SEQ ID NO 61). SiRNAs were used at 10nM and pg/ml Upofectamine 2000 final concentration. The procedure was as follows: The siRNAs were first diluted In OPTIMEM (serum-free transfection media, Invitrogen) at 0.1 pM (10-fold concentrated) and Incubated 5-10 min RT. Upofectamine 2000 was diluted at 10 pg/ml (10 fold concentrated) for the total number transfections and incubated 5-10 minutes at room temperature (RT). Appropriate amounts of diluted 10-fold concentrated Llpofectanine 2000 were mixed 1:1 with diluted 10-fold concentrated siRNA and Incubated at RT for 20-30" (5-fold concentrated transfection solution). 20 pis of the 5-fold concentrated transfection solutions were added to the respective samples and incubated at 370C for 96 hours before analysis. 3H-Thymidine IncoMoration assay The proliferation assay Is a 3H-thymildine Incorporation method for determining the proliferation of viable cells by uptake and incorporation of label into DNA. The procedure was as follows: Cells growing in log phase are trypsinized, washed, counted and plated In 96-well 122 plates at 1000-4000 cells/well in 10% FBS. After 4-8 hrs, the media is replaced. The cells are incubated for 24-72 hrs, pulsed with 3 H-Thy at 1.5 pCi/ml for 14 hrs, harvested onto a filtermat and counted in scintillation cocktail on a Microbeta trilux or other counter. In order to address the function of 109P1 D4 in cells, 109P1 D4 was silenced by transfecting the endogenously expressing 109P1D4 cell line (LNCaP) with the 109P1D4 specific sIRNAs (109P1D4.a, 109P1D4.c, and 109P1D4.d) along with negative siRNA controls (Luc4, targeted sequence not represented in the human genome), a positive siRNA control (targeting Eg5) and no siRNA oligo (LF2K) (Figure 23). The results indicated that when these cells are treated with siRNA specifically targeting the 109P1D4 mRNA, the resulting '109PID4 deficient cells' showed diminished cell proliferation as measured by this assay (e.g., see oligo 109P1 D4.a treated cells). These data indicate that 109P1 D4 plays an important role in the proliferation of cancer cells and that the lack of 109P1D4 dearly decreases the survival potential of these cells. It is to be noted that 109P1D4 is constitutively expressed In many tumor cell lines. 109P1D4 serves a role in malignancy; Its expression is a primary indicator of disease, where such disease is often characterized by high rates of uncontrolled cell proliferation and diminished apoptosis. Correlating cellular phenotype with gene knockdown following RNA treatments is important, and allows one to draw valid conclusions and rule out toxicity or other non-spedfic effects of these reagents. To this end, assays to measure the levels of expression of both protein and mRNA for the target after RNAI treatments are important, including Westem blotting, FACS staining with antibody, Immunoprecipitation, Northern blotting or RT-PCR (Taqman or standard methods). Any phenotypic effect of the siRNAs in these assays should be correlated with the protein and/or mRNA knockdown levels in the same cell lines. 109P1D4 protein is reduced after treatment with siRNA oligos described above (e.g., 109P1D4.a, etc.) A method to analyze 109P1 D4 related cell proliferation Is the measurement of DNA synthesis as a marker for proliferation. Labeled DNA precursors (i.e. 3 H-Thymidine) are used and their incorporation to DNA is quantified. Incorporation of the labeled precursor into DNA is directly proportional to the amount of cell division occurring in the culture. Another method used to measure cell proliferation is performing clonogenic assays. In these assays, a defined number of cells are plated onto the appropriate matrix and the number of colonies formed after a period of growth following siRNA treatment is counted. In 109P1D4 cancer target validation, complementing the cell survival/proliferation analysis with apoptosis and cell cycle profiling studies are considered. The biochemical hallmark of the apoptotic process is genomic DNA fragmentation, an Irreversible event that commits the cell to die. A method to observe fragmented DNA in cells is the immunological detection of histone-complexed DNA fragments by an immunoassay (i.e. cell death detection ELISA) which measures the enrichment of histone-complexed DNA fragments (mono- and oligo-nudeosomes) in the cytoplasm of apoptotic cells. This assay does not require pre-tabeling of the cells and can detect DNA degradation in cells that do not proliferate in vitro (i.e. freshly isolated tumor cells). The most Important effector molecules for triggering apoptotic cell death are caspases. Caspases are proteases that when activated cleave numerous substrates at the carboxy-terminal she of an aspartate residue mediating very early stages of apoptosis upon activation. All caspases are synthesized as pro-enzymes and activation involves cleavage at aspartate residues. In particular, caspase 3 seems to play a central role in the initiation of cellular events of apoptosis. Assays for determination of caspase 3 activation detect early events of apoptosis. Following RNAI treatments, Western blot detection of active caspase 3 presence or proteolytic cleavage of products (i.e. PARP) found in apoptotic cells further support an active Induction of apoptosis. Because the cellular mechanisms that result In apoptosis are complex, each has its advantages and limitations. Consideration of other criterialendpoints such as cellular morphology, chromatin condensation, membrane blabbing, apoptotic bodies help to further support cell death as apoptotic. Since not all the gene targets that 123 regulate cell growth are anti-apoptotic, the DNA content of permeabilized cells is measured to obtain the profile of DNA content or cell cycle profile. Nuclei of apoptotic cells contain less DNA due to the leaking out to the cytoplasm (sub-G1 population). In addition, the use of DNA stains (.e., propidium iodide) also differentiate between the different phases of the cell cycle in the cell population due to the presence of different quantities of DNA in GO/G1, S and G2/M. In these studies the subpopulations can be quantified. For the 109P1 D4 gene, RNAi studies facilitate the understanding of the contribution of the gene product in cancer pathways. Such active RNAi molecules have use in identifying assays to screen for mAbs that are active anti-tumor therapeutics. Further, siRNA are administered as therapeutics to cancer patients for reducing the malignant growth of several cancer types, Including those listed in Table 1. When 109P1D4 plays a role in cell survival, cell proliferation, tumorigenesis, or apoptosis, it is used as a target for diagnostic, prognostic, preventative and/or therapeutic purposes. Throughout this application, various website data content, publications, patent applications and patents are referenced. (Websites are referenced by their Uniform Resource Locator, or URL, addresses on the World Wide Web.) The present invention is not to be limited in scope by the embodiments disclosed herein, which are intended as single illustrations of individual aspects of the Invention, and any that are functionally equivalent are within the scope of the invention. Various modifications to the models and methods of the invention, in addition to those described herein, will become apparent to those skilled In the art from the foregoing description and teachings, and are similarly intended to fall within the scope of the Invention. Such modifications or other embodiments can be practiced without departing from the true scope and spirit of the invention.

124 TABLES: TABLE 1: Tissues that Express 109PiD4when malignant: Prostate Bladder ldney Colon Lymphoma Lung Pancreas Ovary Breast Uterus Stomach Rectum Cervix Lymph Node Bone TABLE i: Amino Acid Abbreviations SINGLE LETTER THREE LETTER FULL NAME F Phe phenylalanine L Leu leucine S Ser serine Y Tyr tyrosine C Cys cysteine W Trp tryptophan P Pro proline H His hisfidine Q Gin glutamine R Arg arginine I_ lie isoleucine M Met methionine T Thr threonine N Asn asparagine K Lys lysine V Val valine A Ala alanine D Asp aspartic acid E Gu glutamic acid G Gly glycine 125 TABLE III: Amino Acid Substitution Matrix Adapted from the GCG Software 9.0 BLOSUM62 amino acid substitution matrix (block substitution matrix). The higher the value, the more likely a substitution Is found in related, natural proteins. (See world wide web URL ikp.unibe.ch/manual/blosum62.html) A C D E F G H I K L M N P Q R S T V W Y. 4 0 -2 -1-2 0 -2 -1-1-1-1-2 -1 -1-1 1 0 0 -3 -2 A 9 -3 -4 -2 -3 -3 -1 -3 -1 -1 -3 -3 -3 -3 -1 -1 -1 -2 -2 C 6 2 -3 -1 -1 -3 -1 -4 -3 1 -1 0 -2 0 -1 -3 -4 -3 D 5 -3 -2 0 -3 1-3 -2 0 -1 2 0 0 -1-2 -3 -2 E 6 -3 -1 0 -3 0 0 -3 -4 -3 -3 -2 -2 -1 1 3 F 6 -2 -4 -2 -4 -3 0 -2 -2 -2 0 -2 -3 -2 -3 G 8 -3 -1 -3 -2 1 -2 0 0 -1 -2 -3 -2 2 H 4 -3 2 1 -3 -3 -3 -3 -2 -1 3 -3 -1 I 5 -2 -1 0 -1 1 2 0 -1 -2 -3 -2 K 4 2 -3 -3 -2 -2 -2 -1 1 -2 -1 L 5 -2 -2 0 -1 -1 -1 1 -1 -1 M 6 -2 0 0 1 0 -3 -4 -2 N 7 -1 -2 -1 -1 -2 -4 -3 P 5 1 0 -1 -2 -2 -1 Q 5 -1 -1 -3 -3 -2 R 4 1 -2 -3 -2 S 5 0 -2 -2 T 4 -3 -1 V 11 2 W 7 Y 126 TABLE IV: HLA Class MIli Motifs/Supermotifs TABLE IV (A): HLA Class I SupermotifslMotifs SUPERMOTIF POSITION POSITION POSITION 2 (Primary Anchor) 3 (Primary Anchor) C Terminus (Primary Anchor) Al TIL VMS FWY A2 LIVMATQ IVMATL A3 VSMATU RK A24 YFWIVLMT FlYWLM B7 P VILFMWYA 827 RHK FYLWMIVA B44 ED FWYUMVA B58 ATS FWYUVMA B62 QLIVMP FWYMIVLA MOTIFS Al TSM Y Al DEAS Y A2.1 LMVQIAT VIMAT A3 LMVISATFCGD KYRHFA All VTMLISAGNCDF KRYH A24 YFWM FLIW A*3101 MVTAUS RK A*3301 MVALFIST RK A*6801 AVTMSL1 RK B*0702 P LMFWYAIV B*3501 P LMFWYVA B51 P LIVFWYAM B*5301 P IMFWYALV B*5401 P ATIVLMFWY Bolded residues are prefermd, Italicized residues are less preferred: A peptide is considered motif-bearing if it has primary anchors at each primary anchor position for a motif or supermotif as specified In the above table. TABLE IV (B): HLA Class Il Supermotif 1 6 9 W, F, Y, V, .I, L A, V, 1, L, P, C, S, T A, V, 1, L, C, S, T, M, Y 127 TABLE IV (C): HLA Class I Motifs MOTIFS 1* anchor 1 2 3 4 5 1* anchor 6 7 8 9 DR4 preferred FMIYUVW M T I VSTCPALJM MH MH deleterious W R WDE DRI preferred MFLJVWY PAMQ VMATSPLIC M AVM deleterious C CH FD CWD GDE D DR7 preferred MFUVWY M W A IVMSACTPL M IV deleterious C G GRD N G DB3 MOTIFS 1* anchor 1 2 3 1* anchor 4 5 1* anchor 6 Motif a preferred UVMFY D Motif b preferred LIVMFAY DNQEST KRH DR Supermotif MFUVWY VMSTACPU Italicized residues Indicate less preferred or "tolerated" residues TABLE IV (D): HLA Class I Supermotfs POSITION: 1 2 3 4 5 6 7 8 C-terminus

SUPER

MOTIFS Al 1' Anchor * Anch TILVMS FWY A2 1* Anchor 1* Anchor LVMATQ UVMAT , A3 Preferred 1* Anghor YFW YFW YFW P 1* Anchor VSMATLI (4/5) (3/5) (4/5) (4/5) RK deleterious DE (3/5); DE P (5/5) (4/5) A24 1* Anchor 1* Anchor YFWIVLMT FIYWLM B7 Preferred FWY (5/5) 1* chor FWY FWY 1*Anchor UVM (3/5) P (4/5) (3/5) VILFMWYA deleterious DE (3/5); DE G QN DE P(5/5); (3/5) (4/5) (4/5) (4/5) G(4/5); A(3/5); QN(3/5) B27 1* An 1*An RHK FYLWMIVA 844 1 A l' Aco ED FWYUMVA 858 1* An0 ' PAnchor ATS FWYLIVMA 862 1* r 1* Anchor QUVMP FWYMIVLA Italicized residues indicate less preferred or "tolerated" residues 128 TABLE IV (E): HLA Class I Motifs POSITION1 2 3 4 5 6 7 8 9 C terminus or C-terminus Al preferred GFYW 1*Anchor DEA YFW P DEON YFW I*Anc 9-mer STM Y deleterious DE RHKUVMP A G A Al preferred GRHK ASTCUVM 1*Anchor GSTC ASTC UVM DE 1*Anchor 9-mer DEAS Y deleterious A RHKDEPYFW DE PQN RHK PG GP Al preferred YFW I Anchor DEAQN A YFWQN PASTC GDE P 1 Anchor 10- STM Y mer deletedous GP RHKGUVM DE RHK QNA RHKYFW RHK A Al preferred YFW STCUVM 1*Anc A YFW PG G YFW 1*Anchor 10- DEAS Y mer deleterious RHK RHKDEPYFW P G PRHK QN A2.1 preferred YFW 1*Anchor YFW STC YFW A P I1Anchr 9-mer LMIVQAT VUMAT deleterious DEP DERKH RKH DERKH POSITION:1 2 3 4 5 6 7 8 9 C Terminus A21 preferred AYFW I*Anchor LVIM G G FYWL 1*Anchor 10- LMIVQ4T ViM VUMAT mer deleterious DEP DE RKHA P RKH DERKHRKH A3 preferred RHK I*Anchor YFW PRHKYF A YFW P I*Anchor LMVISATFCGD W KYRHFA deleterious DEP DE All preferred A l'Ancho YFW YFW A YFW YFW P 1*Anchor VTLMISAGNCD KRYH F deleterious DEP A G A24 preferred YFWRHK 1*Anchor STC YFW YFW I*Ancho 9-mer YFWM FUW deleterious DEG DE G QNP DERHKG AQN A24 Preferred ch P YFWP P 1* 10- YFWM FLW mer Deleterious GDE QN RHK DE A QN DEA A3101 PReferred RHK 1*Anch YFW P YFW YFW AP I*Anchor MVTAUS RK Deleterious DEP DE ADE DE DE DE A3301 Preferred 1*Anghor YFW AYFW 1*Ancho MVALFIST RK Deleterious GP DE A6801Preferred YFWSTC lAnchor YFWUV YFW P lAnchor AVTMSUI M RK deleterious GP DEG RHK A B0702Preferred RHKFWY l*Anchor RHK RHK RHK RHK PA 1*Anchor P LMFWYA V deleterious DEQNP DEP DE DE GDE QN DE 129 POSITIONi 2 3 4 5 6 7 8 9 C terminus or C-terminus Al preferred GFYW l'Anh DEA YFW P DEQN YFW iAnchor 9-mer STM y deleterious DE RHIKVMP A G A Al preferred GRHK ASTCUVM I Anchor GSTC ASTC LIVM DE I*Anchor 9-mer DEAS y deleterious A RHKDEPYFW DE PQN RHK PG GP B35O1Prefered FWYLIVM I*Anchor FWY FWY 1*Anchor P LMFWYIV A deleterious AGP G G 651 Prefeed LVMIFWY Anch FWY STC FWY G FWY 1*Anchor P UVFWYA M deleterious AGPDER DE G DEQN GDE HKSTC B5301 preferred UVMFWY 1 *Anchor FWY STC FWY LVMFWYFWY 1*Anchor P IMFWYAL deleterious AGPQN G RHKQN DE B5401 preferred FWY 1*Anco FWYLIVM LVM ALIVM FWYA 1*Anchor P P ATVLMF deleterious GPQNDE GDESTC RHKDE DE QNDGE DE 130 TABLE IV (F): Summary of HLA-supertypes ral phenotypic frequencies of HLA-supertypes In different ethnic populations Specificity Phenotypic freque ncy pertypeosition 2 inaucasia n .A Black< apanesehhines anic Average 7 3.2 5.1 7.1 3.0 9.3 9.5 A3 ALMVST 7.5 2.1 5.8 . 93.1 .2 A2___ALUM __ ALMV_ 5.8 3.0 124__ .59__ 3.0 2.__ 4 P F (V )( M 3.9 .9 .6 00.1 8.3 90.0 B4 (D) FWYMVA 43.0 21.2 42.9 39.1 39.0 37.0 A l(LVMS)_ 47NY 1. 1 - 2.8_ 1.7_ 26.3_ 25.2 B27 RHK FL (WMI1) 28.4 2.1 13.3 13.9 35.3 23.4 2 QL_(IVMP_ Y (MV) 12___36___ 2__1_1__ __6.5 5.4 1.1 8.1 258 AS VY(LIV) 10.0 25.1 1.6 9.0 5.9 10.3 TALE IV (G): Calculated population coverage afforded by different HLA-supertype combinations HLA-supertypes Phenotypic frequency ucasian .A Blacks Japanese hinese fisanic rage 3.0 6.1 37.5 38.4 6.3 6.2 A2, A3 and B7 9.5 a8.1 100.0 9.5 .4 .3 _A, A3, B7, A24, B449.9 _9.6 100.0 99.8 9.9 99.8 nd A1 AA3, B7, A24, 84, A1, B27, B62, d B 58 oifs indicate the residues defining supert9% specficites. The motifs incorporate residues determined on the basis of published data to be recognized by multiple alleges within the supertype. Residues within brackets are additional residues also predicted to be tolerated by multiple alleles within the supertype. Table V: Frequently Occurring Motifs Name av. * description Iotential Function 1ucleic acid-binding protein functions as ranscdption ior, nuclear location zf-C2H2 34% Zinc finger, C2H-2 type probable Cytochrome b(N- membrane bound oxidase, generate cytochrome-bN 38% ermina hb6/petB h superonde otains are one hundred amino acids ong and include a conserved I9 19% Immunoglobulln domain intradomain disuffide bond. tandem repeats of about 40 residues, tach containing a Trp-Asp motif. Function in signal transduction and WD40 18% WD domain, G-beta repeal protein interaction may function in targeting signaling DDZ 23% PDZ domain molecules to sub-membranous sites JRR 28% teucine Rich Repeat short sequence motifs Involved In protein-protein interactions unserved catalytic core common to Ith serine/threonine and tyrosine protein kinases containing an ATP Pknase 23% Protein Inase domain inding site and a catalytic site 131 pIeckstin homology involved in ntracellular signaling or as constituents PH 16% PH domain of the cytoskeleton 30-40 amino-acid long found in the extracellular domain of membrane EGF 34% EGF-like domain bound proteins or in secreted proteins Reverse transcriptase (RNA-dependent DNA Rvt 49% polymerase) Cytoplasmic protein, associates integral Ank 25% Ank repeat membrane proteins to the cytoskeleton NADH- membrane associated. Involved in Ubiquinone/plastoquinone oton translocation across the Oxidoredql 32% (complex I), various chains membrane calcium-binding domain, consists of a12 -esidue loop flanked on both sides by a Ethand 24% EF hand 12 residue alpha-helical domain Retroviral aspartyl Aspartyl or acid proteases, centered on Rvp 79% protease a catalytic aspartyl residue extracellular structural proteins involved n formation of connective tissue. The Collagen triple helix repeat sequence consists of the G-X-Y and the Collagen 42% 20 copies) polypeptide chains forms a triple helix. Located in the extracellular ligand onding region of receptors and is about 200 amino acid residues long with two )airs of cysteines involved in disulfide rn3 20% Fibronectin type Il domain 3onds ven hydrophobic transmembrane ions, with the N-terminus located transmembrane receptor axtracellularly while the C-terminus is /tm.1 19% [rhodopsin family) asmic. Signal through G proteins Table VI: Post-translational modifications of 109P1D4 0-lycoation sites 231 S 238 S 240 T 266 T 346 T 467 T 551 T 552 S 555 T 595 T 652 S 654 S 660 T 790 T 795 T 798 T 804 S 808 S 923 T 927 T 954 T 979 S 982 S 983 S 132 985 S 986 S 990 S 999 T 1000 T 1006 S 1017 S 1020 T Serine phosphorvlation sites 50 DLNLSLIPN (SEQ ID NO: 62) 147 VINISIPEN (SEQ ID NO: 63) 152 IPENSAINS (SEQ ID NO: 64) 238 ILQVSVTDT (SEQ ID NO: 65) 257 EIEVSIPEN (SEQ ID NO: 66) 428 LDYESTKEY (SEQ ID NO: 67) 480 PENNSPGIQ (SEQ ID NO: 68) 489 LTKVSAMDA (SEQ ID NO: 69) 495 MDADSGPNA (SEQ ID NO: 70) 559 TVFVSIIDQ (SEQ ID NO: 71) 567 QNDNSPVFT (SEQ ID NO: 72) 608 AVTLSILDE (SEQ ID NO: 73) 630 RPNISFDRE (SEQ ID NO- 74) 638 EKQESYTFY (SEQ ID NO: 75) 652 GGRVSRSSS (SEQ ID NO: 76) 654 RVSRSSSAK (SEQ ID NO: 77) 655 VSRSSSAKV (SEQ ID NO: 78) 656 SRSSSAKVT (SEQ ID NO: 79) 714 EVRYSIVGG (SEQ ID NO: 80) 789 LVRKSTEAP (SEQ ID NO: 81) 805 ADVSSPTSD (SEQ ID NO: 82) 808 SSPTSDYVK (SEQ ID NO: 83) 852 NKQNSEWAT (SEQ ID NO: 84) 877 KKKHSPKNL (SEQ ID NO: 85) 898 DDVDSDGNR (SEQ ID NO: 86) 932 FKPDSPDLA (SEQ ID NO: 87) 941 RHYKSASPQ (SEQ ID NO: 88) 943 YKSASPQPA (SEQ ID NO: 89) 982 ISKCSSSSS (SEQ ID NO: 90) 983 SKCSSSSSD (SEQ ID NO: 91) 984 KCSSSSSDP (SEQ ID NO: 92) 985 CSSSSSDPY (SEQ ID NO: 93) 990 SDPYSVSDC (SEQ ID NO- 94) 1006 EVPVSVHTR (SEQ ID NO: 95) Threonine phosphoryation sites 29 EKNYTIREE (SEQ ID NO: 96) 81 IEEDTGEIF (SEQ ID NO: 97) 192 DVIETPEGD (SEQ ID NO: 98) 252 VFKETEIEV (SEQ ID NO- 99) 310 TGLITIKEP (SEQ ID NO: 100) 320 DREETPNHK (SEQ ID NO: 101) 551 VPPLTSNVT (SEQ ID NO: 102) 790 VRKSTEAPV (SEQ ID NO: 103) 856 SEWATPNPE (SEQ ID NO: 104) 924 NWVTTPTTF (SEQ ID NO: 105) 927 TTPTTFKPD (SEQ ID NO: 106) 999 GYPVTTFEV (SEQ ID NO: 107) 1000YPVTTFEVP (SEQ ID NO: 108) Tyrosine phosphorvlation sites 67 FKLVYKTGD (SEQ ID NO, 109) 133 158 INSKYTLPA (SEQ ID NO: 110) 215 EKDTYVMKV (SEQ ID NO: 111) 359 IDIRYIVNP (SEQ ID NO: 112) 423 ETAAYLDYE (SEQ ID NO: 113) 426 AYLDYESTK (SEQ ID NO: 114) 432 STKEYAIKL (SEQ ID NO: 115) 536 KEDKYLFTI (SEQ ID NO: 116) 599 TDPDYGDNS (SEQ ID NO' 117) 642 SYTFYVKAE (SEQ ID NO: 118) 682 SNCSYELVL (SEQ ID NO: 119) 713 AEVRYSIVG (SEQ ID NO: 120) 810 PTSDYVKIL (SEQ ID NO: 121) 919 TMGKYNWVT (SEQ ID NO: 122) 989 SSDPYSVSD (SEQ ID NO: 123) 996 SDCGYPVTT (SEQ ID NO: 124) Table VII: Search Peotides 109P1D4 v.1 - 9-mers, 10-mers and 15-mers (SEQ ID NO: 125) MDLLSGTYIF AVLLACVVFH SGAQEKNYTI REEMPENVLI GDLLKDLNLS LIPNKSLTTA 60 MQFKLVYKTG DVPLIRIEED TGEIETTGAR IDREKLCAGI PRDEHCFYEV EVAILPDEIF 120 RLVKIRFLIE DINDNAPLFP ATVINISIPE NSAINSKYTL PAAVDPDVGI NGVQNYELIK 180 SQNIFGLDVI ETPEGDKMPQ LIVQKELDRE EKDTYVMKVK VEDGGFPQRS STAILQVSVT 240 DTNDNHPVFK ETEIEVSIPE NAPVGTSVTQ LHATDADIGE NAKIHFSFSN LVSNIARRLF 300 HLNATTGLIT IKEPLDREET PNHKLLVLAS DGGLMPARAM VLVNVTDVND NVPSIDIRYI 360 VNPVNDTVVL SENIPLNTKI ALITVTDKDA DHNGRVTCFT DHEIPFRLRP VFSNQFLLET 420 AAYLDYESTK EYAIKLLAAD AGKPPLNQSA MLFIKVKDEN DNAPVETQSF VTVSIPENNS 480 PGIQLTKVSA MDADSGPNAK INYLLGPDAP PEFSLDCRTG MLTVVKKLDR EKEDKYLETI 540 LAKDNGVPPL TSNVTVFVSI IDQNDNSPVF THNEYNFYVP ENLPRHGTVG LITVTDPDYG 600 DNSAVTLSIL DENDDETIDS QTGVIRPNIS FDREKQESYT FYVKAEDGGR VSRSSSAKVT 660 INVVDVNDNK PVFIVPPSNC SYELVLPSTN PGTVVFQVIA VDNDTGMNAE VRYSIVGGNT 720 RDLFAIDQET GNITLMEKCD VTDLGLHRVL VKANDLGQPD SLFSVVIVNL FVNESVTNAT 780 LINELVRKST EAPVTPNTEI ADVSSPTSDY VKILVAAVAG TITVVVVIFI TAVVRCRQAP 840 HLKAAQKNKQ NSEWATPNPE NRQMIMMKKK KKKKKHSPKN LLLNFVTIEE TKADDVDSDG 900 NRVTLDLPID LEEQTMGKYN WVTTPTTFKP DSPDLARHYK SASPQPAFQI QPETPLNSKH 960 HIIQELPLDN TFVACDSISK CSSSSSDPYS VSDCGYPVTT FEVPVSVHTR PVGIQVSNTT 1020 F 1021 109P1D4 v.2 (both ends diff from v.1) N' terminal 9-mers aa -30 to 8 MRTERQWVLIQIFQVLCGLIQQTVTSVPGMDLLSGTY (SEQ ID NO: 126) 10-mers aa -30 to 9 MRTERQWVLIQIFQVLCGLIQQTVTSVPGMDLLSGTYI (SEQ ID NO: 127) 15-mers aa -30 to 14 MRTERQWVLIQIFQVLCGLIQQTVTSVPGMDLLSGTYIFAVLL (SEQ ID NO: 128) 109P1D4 v.2 C' Terminal 9 mers: aa 1004 to 1025 PVSVHTRPTDSRTSTIEICSEI (SEQ ID NO: 129) 10 mers: aa1003 to 1025 VPVSVHTRPTDSRTSTIEICSEI (SEQ ID NO: 130) 15 mers: aa 997 to 1025 VTTFEVPVSVHTRPTDSRTSTIEICSEI (SEQ ID NO: 131) 109P1D4 v.3 9 mers: aa1004 to 1347 (SEQ ID NO: 132) PVSVHTRPPMKEVVRSCTPMKESTTMEIWIHPQPQRKSEGKVAGKSQRRVTFHLPEGSQESSSDG GLGDHDAGSLTSTSHGLPLGYPQEEYFDRATPSNRTEGDGNSDPESTFI PGLKKAAEITVQPTVE EASDNCTQECLIYGHS DACWMPASLDHSSSSQAQASALCHSPPLSQASTQHHSPRVTQTIALCHS PPVTQTIALCHSPPPIQVSALHHSPPLVQATALH

HSPPSAQASALCYSPPLAQAAAISHSSPLPQ

134 VIALHRSQAQSSVSLQQGWVQGADGLCSVDQGVQGSATSQFYTMSERLHPSDDSIKVI PLTTFTP RQQARPSRGDSPMEEHPL 10 mers: aa1003 to 1347 (SEQ ID NO: 133) VPVSVHTRPPMKEVVRSCTPMKESTTMEIWIHPQPQRKSEGKVAGKSQRRVTFHLPEGSQESSS D GGLGDHDAGSLTSTSHGLPLGYPQEEYFDRATPSNRTEGDGNSDPESTFIPGLKKAAEITVQPTV EEASDNCTQECLIYGHSDACWMPASLDHSSSSQAQASALCHSPPLSQASTQHHSPRVTQTIALCH SPPVTQTIALCHSPPPIQVSALHHSPPLVQATALHHSPPSAQASALCYSPPLAQAAAISHSSPLP QVIALHRSQAQSSVSLQQGWVQGADGLCSVDQGVQGSATSQFYTMSERLHPSDDSIKVIPLTTFT PRQQARPSRGDS PMEEHPL 15 mers: aa 998 to 1347 (SEQ ID NO: 134) VTTFEVPVSV HTRPPMKEVV RSCTPMKEST TMEIWIHPQP QRKSEGKVAG KSQRRVTFHL PEGSQESSSD GGLGDHDAGS LTSTSHGLPL GYPQEEYFDR ATPSNRTEGD GNSDPESTFI PGLKKAAEIT VQPTVEEASD NCTQECLIYG HSDACWMPAS LDHSSSSQAQ ASALCHSPPL SQASTQHHSP RVTQTIALCH SPPVTQTIAL CHSPPPIQVS ALHHSPPLVQ ATALHHSPPS AQASALCYSP PLAQAAAISH SSPLPQVIAL HRSQAQSSVS LQQGWVQGAD GLCSVDQGVQ GSATSQFYTM SERLHPSDDS IKVIPLTTFT PROQARPSRG DSPMEEHPL 109P1D4 v.4 (deleting 10 aa, 1039-1048, from v.1) 9-mers aa 1031-1056 (deleting 10 aa, 1039-1048, from v.1) IWIHPQPQSQRRVTFH (SEQ ID NO: 135) 10-mers aa 1030- 1057 (deleting 10 aa, 1039-1048, from v.1) EIWIHPQPQSQRRVTFHL (SEQ ID NO: 136) 15-mers aa 1025- 1062 (deleting 10 aa, 1039-1048, from v.1) ESTTMEIWIHPQPQSQRRVTFHLPEGSQ (SEQ ID NO: 137) 109P1 D4 v.5 (deleting 37 aa, 1012-1048, from v.1) 9-mers aa 1004-1056 (deleting 37 aa, 1012-1048, from v.1) PVSVHTRPSQRRVTFH (SEQ ID NO: 138) 10-mers aa 1003-1057 (deleting 37 aa, 1012-1048, from v.1) VPVSVHTRPSQRRVTFHL (SEQ ID NO: 139) 15-mers aa 998-1062 (deleting 37 aa, 1012-1048, from v.1) VTTFEVPVSVHTRPSQRRVTFHLPEGSQ (SEQ ID NO: 140) 109P1D4 v.6 (both ends diff from v.1) N' terminal 9-mers: aa -23 to 10 (excluding I and 2) MTVGFNSDISSVVRVNTTNCHKCLLSGTYIF (SEQ ID NO: 141) 10-mers: aa -23 to 11 (excluding I and 2) MTVGFNSDISSVVRVNTTNCHKCLLSGTYIFA (SEQ ID NO: 142) 15-mers: aa -23 to 17 (excluding 1 and 2) MTVGFNSDISSVVRVNTTNCHKCLLSGTYIFAVLLVC (SEQ ID NO: 143) 109P1D4 v.6 C' terminal 9-mers: aa 1004-1016 PVSVHTRPTDSRT (SEQ ID NO: 144) 10-mers: aa 1003-1016 VPVSVHTRPTDSRT (SEQ ID NO: 145) 15-mers: aa 998-1016 VTTFEVPVSVHTRPTDSRT (SEQ ID NO: 146) 109P1 D4 v.7 (N-terminal 21 aa diff from those in v.6) 135 N' terminal 9-mers aa -21 to 10 exudingg 1 and 2) MFRVGFLIISSSSSLSPLLLVSVVRVNTT (SEQ ID NO: 147) 10-mers aa -21 to 11 (excluding 1 and 2) MFRVGFLIISSSSSLSPLLLVSVVRVNTTN (SEQ ID NO: 148) 15-mers aa -21 to 16 (excluding I and 2) MFRVGFLIISSSSSLSPLLLVSVVRVNTTNCHKCL (SEQ ID NO: 149) 109P1D4 v.8 9-mers aa1099-1126 exudingg 1117 and 1118) TFIPGLKKEITVQPTV (SEQ ID NO: 150) 10-mers aa 1098-1127 (excluding 1117 and 1118) STFIPGLKKEITVQPTVE (SEQ ID NO: 151) 15-mers aa 1093-1131 (excluding 1117 and 1118) NSDPESTFIPGLKKEITVQPTVEEASDN (SEQ ID NO: 152) 109P1D4 v.1, v.2 and v.3 SNP variants A15V 9-ners TYIFAVLLVCVVFHSGA (SEQ ID NO: 153) 1(-mers GTYIFAVLLVCVVFHSGAQ (SEQ ID NO: 154) 15-mers MDLLSGTYIFAVLLVCVVFHSGAQEKNYT (SEQ ID NO: 155) 109P1D4 v.1, v.2 and v.3 SNP variants M341 9-mers KNYTIREEIPENVLIGD (SEQ ID NO: 156) 10-mers EKNYTIREEIPENVLIGDL (SEQ ID NO: 157) 15-mers HSGAQEKNYTIREEIPENVLIGDLLKDLN (SEQ ID NO: 158) 109P1D4 v.1, v.2 and v.3 SNP variants M341 and D42N 9-mers KNYTIREEIPENVLIGN (SEQ ID NO: 159) 10-mers EKNYTIREEIPENVLIGNL (SEQ ID NO: 160) 15-mers HSGAQEKNYTIREEIPENVLIGNLLKDLN (SEQ ID NO: 161) 109P1D4 v.1, v.2 and v.3 SNP variants D42N 9-mers MPENVLIGNLLKDLNLS (SEQ ID NO: 162) 10-mers EMPENVLIGNLLKDLNLSL (SEQ ID NO: 163) 15-mers YTIREEMPENVLIGNLLKDLNLSLIPNKS (SEQ ID NO: 164) 109P1D4 v.1, v.2 and v.3 SNP variants D42N and M341 9-mers IPENVLIGNLLKDLNLS (SEQ ID NO: 165) 10-mers EIPENVLIGNLLKDLNLSL (SEQ ID NO: 166) 136 15-mers YTIREEIPENVLIGNLLKDLNLSLIPNKS (SEQ ID NO: 167) 109P1D4 v.1, v.2 and v.3 SNP variants A60T 9-mers IPNKSLTTTMQFKLVYK (SEQ ID NO: 168) 10-mers LIPNKSLTTTMQFKLVYKT (SEQ ID NO: 169) 15-mers DLNLSLIPNKSLTTTMQFKLVYKTGDVPLI (SEQ ID NO: 170) 109P1D4 v.1, v.2 and v.3 SNP variants 1154V 9-mers ISIPENSAVNSKYTLPA (SEQ ID NO: 171) 10-mers NISIPENSAVNSKYTLPAA (SEQ ID NO: 172) 15-mers PATVINISIPENSAVNSKYTLPAAVDPDV (SEQ ID NO: 173) 109P1D4 v.1, v.2 and v.3 SNP variants V2921 9-mers IHFSFSNLISNIARRLF (SEQ ID NO: 174) 10-mers KIHFSFSNLISNIARRLFH (SEQ ID NO: 175) 15-mers IGENAKIHFSFSNLISNIAPRLFHLNATT (SEQ ID NO: 176) 109P1D4 v.1, v.2 and v.3 SNP variants T420N 9-mers FSNQFLLENAAYLDYES (SEQ ID NO: 177) 10-mers VFSNQFLLENAAYLDYEST (SEQ ID NO: 178) 15-mers FRLRPVFSNQFLLENAAYLDYESTKEYAI (SEQ ID NO: 179) 109P1D4 v.1, v.2 and v.3 SNP variants T486M 9-mers NNSPGIQLMKVSAMDAD (SEQ ID NO: 180) 10-mers ENNSPGIQLMKVSAMDADS (SEQ ID NO: 181) 15-mers TVSIPENNSPGIQLMKVSAMDADSGPNAK (SEQ ID NO: 182) 109P1D4 v.1, v.2 and v.3 SNP variants T486M and M491T 9-mers NNSPGIQLMKVSATDAD (SEQ ID NO: 183) 1O-mers ENNSPGIQLMKVSATDADS (SEQ ID NO: 184) 15-mers TVSIPENNSPGIQLMKVSATDADSGPNAK (SEQ ID NO: 185) 109P1D4 v.1, v.2 and v.3 SNP variants T486M and M491T and K500E 15-mers TVSIPENNSPGIQLMKVSATDADSGPNAE (SEQ ID NO: 186) 137 109P1D4 v.1, v.2 and v.3 SNP variants T486M and K500E 15-mers TVSIPENNSPGIQLMKVSAMDADSGPNAE (SEQ ID NO: 187) 109P1D4 v.1, v.2 and v.3 SNP variants M491T 9-mers IQLTKVSATDADSGPNA (SEQ ID NO: 188) 10-mers GIQLTKVSATDADSGPNAK (SEQ ID NO: 189) 15-mers ENNSPGIQLTKVSATDADSGPNAKINYLL (SEQ ID NO: 190) 109P1D4 v.1, v.2 and v.3 SNP variants M491T and T486M 9-mers IQLNKVSATDADSGPNA (SEQ ID NO: 191) 10-mers GIQLNKVSATDADSGPNAK (SEQ ID NO: 192) 15-mers ENNSPGIQLNKVSATDADSGPNAKINYLL (SEQ ID NO: 193) 109P1 D4 v.1, v.2 and v.3 SNP variants M491T and T486M and K500E 10-mers GIQLNKVSATDADSGPNAE (SEQ ID NO: 194) 15-mers ENNSPGIQLNKVSATDADSGPNAEINYLL (SEQ ID NO: 195) 109P1D4 v.1, v.2 and v.3 SNP variants M491T and K500E 15-mers ENNSPGIQLTKVSATDADSGPNAEINYLL (SEQ ID NO: 196) 109P1D4 v.1, v.2 and v.3 SNP variants K500E 9-mers DADSGPNAEINYLLGPD (SEQ ID NO: 197) 10-mers MDADSGPNAEINYLLGPDA (SEQ ID NO: 198) 15-mers TKVSAMDADSGPNAEINYLLGPDAPPEFS (SEQ ID NO: 199) 109P1D4 v.1, v.2 and v.3 SNP variants K500E and M491T 10-mers TDADSGPNAEINYLLGPDA (SEQ ID NO: 200) 15-mers TKVSATDADSGPNAEINYLLGPDAPPEFS (SEQ ID NO: 201) 109P1D4 v.1, v.2 and v.3 SNP variants K500E and M491T and T486M 15-mers MKVSATDADSGPNAEINYLLGPDAPPEFS (SEQ ID NO: 202) 109P1D4 v.1, v.2 and v.3 SNP variants K500E and T486M 15-mers MKVSAMDADSGPNAEINYLLGPDAPPEFS (SEQ ID NO: 203) 109P1D4 v.1, v.2 and v.3 SNP variants 138 C517R 9-mers APPEFSLDRRTGMLTVV (SEQ ID NO: 204) 10-ners DAPPEFSLDRRTGMLTVVK (SEQ ID NO: 205) 15-mrs INYLLGPDAPPEFSLDRRTGMLTVVKKLDRE (SEQ ID NO: 206) 109P1D4 v, v.2 and v.3 SNP variants N576K 9-mers PVFTHNEYKFYVPENLP (SEQ ID NO: 207) 10-mers SPVFTHNEYKFYVPENLPR (SEQ ID NO: 208) 15-mers DQNDNSPVFTHNEYKFYVPENLPRHGTVG (SEQ ID NO: 209) 109P1D4 v.1, v.2 and v.3 SNP variants S678Y 9-mers KPVFIVPPYNCSYELVLPS (SEQ ID NO: 210) 10-mers NKPVFIVPPYNCSYELVLPST (SEQ ID NO: 211) 15-mers VDVNDNKPVFIVPPYNCSYELVLPSTNPG (SEQ ID NO: 212) 109P1D4 v.1, v.2 and v.3 SNP varants S678Y and C680Y 9-mers KPVFIVPPYNYSYELVLPS (SEQ ID NO: 213) 10-mers NKPVFIVPPYNYSYELVLPST (SEQ ID NO: 214) 15-mers VDVNDNKPVFIVPPYNYSYELVLPSTNPG (SEQ ID NO: 215) 109P1D4 v.1, v.2 and v.3 SNP variants C680Y 9-mers VFIVPPSNYSYELVLPS (SEQ ID NO: 216) 10-mers PVFIVPPSNYSYELVLPST (SEQ ID NO: 217) 15-mers VNDNKPVFIVPPSNYSYELVLPSTNPGTV (SEQ ID NO: 218) 109P1D4 v.1, v.2 and v.3 SNP variants C680Y and S678Y 9-mers VFIVPPYNYSYELVLPS (SEQ ID NO: 219) 10-mers PVFIVPPYNYSYELVLPST (SEQ ID NO: 220) 15-mers VNDNKPVFIVPPYNYSYELVLPSTNPGTV (SEQ ID NO: 221) 109P1D4 v.1, v.2 and v.3 SNP variants T7901 9-mers INELVRKSIEAPVTPNT (SEQ ID NO: 222) 10-mers LINELVRKSIEAPVTPNTE (SEQ ID NO: 223) 15-mers VTNATLINELVRKSIEAPVTPNTEIADVS (SEQ ID NO: 224) 139 109P1D4 v.1, v.2 and v.3 SNP variants K846M 9-mers HLKAAQKNMQNSEWATP (SEQ ID NO 225) 10-mers PHLKAAQKNMQNSEWATPN (SEQ ID NO: 226) 15-mers RCRQAPHLKAAQKNMQNSEWATPNPENRQ (SEQ ID NO: 227) 109P1D4 v.1, v.2 and v.3 SNP variants F855V 9-mers SPKNLLLNVVTIEETKA (SEQ ID NO: 228) 10-mers HSPKNLLLNVVTIEETKAD (SEQ ID NO: 229) 15-ners KKKKKHSPKNLLLNVVTIEETKADDVDSD (SEQ ID NO: 230) 109P1D4 v.1, v.2 and v.3 SNP variants S958L 9-mers IQPETPLNLKHHIIQEL (SEQ ID NO: 231) 10-mers QIQPETPLNLKHHIIQELP (SEQ ID NO: 232) 15-mers PQPAFQIQPETPLNLKHHIIQELPLDNTF (SEQ ID NO: 233) 109P1D4 v.1, v.2 and v.3 SNP variants K980N 9-mers FVACDSISNCSSSSSDP (SEQ ID NO: 234) 10-mers TFVACDSISNCSSSSSDPY (SEQ ID NO: 235) 15-mers LPLDNTFVACDSISNCSSSSSDPYSVSDC (SEQ ID NO: 236) 140 Tables Vill -)MX: ~~~~ beII- OPD4v.1 -Al- Tal VI -I9PID4v.l - Al- jTable VII-I 109P1D4v.lI -Al-I 9-es .9-mers J __9-mers Each peptide Is a portion of 1Each peptide Is a portion of iEach peptide is a portion of1 SEQ ID NO: 3; each start SEQ ID NO: 3; each start'j SEQ ID NO: 3; each start position is specified, the position Is specified, the j position is specified, the length of peptide Is 9 amino I length of peptide is 9 amino length of peptide is 9 amino acids, and the end position forl acids, and the end position for' acids, and the end position for each peptide is the start each peptide is the start L each pepide is the start position plus eight _j position plus eight L positionn pus eight. KtI Fu-equece j e ~ Subquence 1s -~ ISubseuence f~~r F91i0jDLEEQT-MGlF 90.000 F5'[1 L1VVKKLDR 1 1.2508 ~95 DVS D GN R V 0O. 500 P J -FTDHEI-PfR~ 4m 25 TOO TG A-RID-R 11125 Po700 I JT@ml 6-566 1 189 1LETPE G DK800 779f [J]UELVR =.250. 3R-1 EDDHNGRVTI .0 [ C9JF TDPDYGDR- - 1250 I2['EDKMPqJ 1.2082j VSTD _.0 2-78 GEAfH 111.250j NPNMI .15 EDGRS 0.500 [27511 D-iG=ENAK][ooo [L48UnSssJ 1.1540] [ppLU .5=00 19211 2.ADSGPNAJ(3 10.000J 59-ffLff!MRPrDY J] 1.ooI ~ j~pq~~[os [ D7O 1. LSENIPLNT Fj-L50J~ ~D37I iLoooj 1725 AIQTN Dn~ STNPGTF :5P]0 l[1 IDSpTS 11.000 705I E II~1L~DIHY CQ9o ___ .j Y.?.P.qCYYi 5.000 [ _LA DA KPN j F 0741![ 1__ATGLIII ] o-31oo [ A6]FVDVG]JS.0 972[fVA\ CDSISK JL.O0j E9[-IiJLCDSI-KCS =0.5001 111 IA~~R~LWi518 LrMTkLoO J L=V!s =.450% FL42]iL DPfft!Y!j5.000 I - 1~APPNI00 f1 i~s 8___Pt N _______________ VGFL _11.45L1 ,[lf ( 5 yq G 1L4.500_ l11EhG~~1Q9 N- [ 25 JPE-NAP J[_.45FL 807[TSYVILV 3.750 .jELDREK[090 BU 4O1HEiPLR f .450j MI A " SGLPI3750 FL-6iI w ivjfjIA-R IJ sKLLAAG 0.40051 F5- AQFYJ .5 0=0 [316j D ETN 090 78-0] LNLR .0 7=38 KDTLL[?.00 I2.JWE NA 0.900 256jlyr NAVJ0.0 [F35 IDI4IV 2.500 [_ SDLR Y 0.5 40KAPQP 0.300 []L~Y~LD!E93L19 [I[]HSA4KY10.5 = 5 NEWTJ0.2700 F[-3] sFwi-8f-soJ Ii ssssDPYI 0.7501 7jLGRVK0.5 [iLEQMK'f2.250] L5]iLA M.Fil9 EDGMNA yJ[.20 [79SEVTPNJ 2250 W (LQESTFYV L6 6=6 [W---F I5 1231 EIVSE ,( 1P 80fF72flI RD;TG NTI F:!1675i] F387IIKD A~ l) 18971DSGRT 1.500 6[-9 TDVPLIRI FqT625- I ! 730DNP-j-S IOIR! Fi .250 [47?911 NSPGIQLTKT 6-2 1550 1 K96 j~DFls~.% P §I591N DN t 92f ~ ISDYDlj F.o 1 -56 R_~~o ! 981 ESCYV~1.501 i845 SSPtSDVIN [0.600I____ rq~ 68L [ l KTDVLI 111250 2f~VDGPRI0 JT67 Table IX- 1O9PID4v.- 04[ I,[ q-LGLiI1.5 l-I-10me_ 2-73] AFA0I9E[ 1.50ILDENDDFT 0.500 157091 E TN YNf Y FT1250 892 DDDI 0.500:1 Each peptide is aportion of I abelX-O D4v.1-.I Table IX- 1O9PID4v.1 SEQ ID NO: 3; each start All-ers jAI-1O-mers pstoisspecfied, the Each peptide is a portion of Each peptide is a portion of lgth of peptide Is 10 ammno SEQ ID NO: 3; each start SEQ ID NO: 3; each start ais, and the end position for position is specified, the position is specified, the each peptide is the start length of peptide is 10 amino, length of peptide is 10 amino - pu PnP!9i ._ acids, and the end position for! acids, and the end position forl PEJi;Nsuqn J[ §coreJ each peptide is the start each peptide Is the start RJ9~ jj FjET-YJ-- - pus nine. position plus nine. (68 L~~jLEPRFSLo bsL-quen-ej~is D IjtosILSbse~cjso 266 ODSGPnAJ(INY I 37.i09j [41E IPPPJM FL' ]F8-L[KE PIDRETJ9.5q 142 , LS~P NT 11700 FlRGITWK =1.0900 FJqLJJK 0.400Ai!iI9A '1951YLD YeSTE lL25ooo EIiAThln! LI9P 0.0 416 JK GRVSRj 8.0. [[ TNWnHPVF .0 703 DPDAR ! 000 101 IAD9L R 1500 E11 A=DHnGRVTC [ ~ 28l VSIPeN APVG 10.300 366 " [VDdYD :l~5g0 5 'I. !!.!!S DR ILP2.99] o fKK l 7 389 TID qTGV1R 10.0o0 [EIEFsIPEAJ 0.0 6E]&ADD GNRI020 FT 7I 1S~SVD 7.00?L4N i].i 21LQ-saMLR-K5LO50] F1~ 2 NVsI2R Fj_.20 8NS fHNEY =.750~ 17 NDgM NAEV 0 .250] 11 J~iP RI~ tFSNLV1iARJ[.7501 701 [K PDLA HJ 0.250-L 15751 VSSF!LSDjYVK[ 000] -{ ]I PDA P ES.I06? i_ ji5.30iQPDSIF§VVI Fl-.251. 445 FI~SCY500FliI20] vPI L . * 3 NAvTSFL..5 561 p FrNTj =.5W0 E331 E@ aPyFTJ[E.625 F _I-L~t.HK J 025 F48-1 NA 1YiV 7so 1E 1438VNDWkPVFI - 06] L Elavl ~ 79 SD:vKILV (I 3750 8 Ig lkE _jL0.500- L [~I F) LE 0 q 92?5j 13081 [ ILDEnDDTj q j?~ LYYpj .0 209 I303EE~ :=kT =0.2251 L472 AVD T GMN1L2500 I~5 ~g 7 L J(- F.500 12411 4-] P-C i[LP :2 -I E5 g?] KRLeEDK [0 ] ElQLIQ~eTP J 000 351 VPENIPRHGT Lf2K I 28 f&D _YML]E .5 0 =1LD PF S ~I 0.500I 1 v I11I[I~vDNPj 500 K92)GI~Vi .50121 K~ILL .2 [(gU NMSPgQLTK =2.500 169FLTAi?!F? =0.5001G~aI 0.22K~!L5i 501[ LGNmIME 2.500 1 *IRLAI [T 7E?~ [75J[ EIPFrLP j .200 [476[ IDTG AV RYJ L2.5OOJ P0 RY ~ JL~ F M3[ LEdYISK 276 ___ -L YYR1L ISC~ .5GdAPEFJ 2.000]sI 020 763 VS D YPVTT [jp([!1~ I .0 ~ LLLPGT =L.~ §7351 FtO E!: LP N TF 7 II 1.35]DO~ .50 _________ I513II~gK~ 1(1.250 1 _ RTbl -19PDv1 ;I'2~~ MD~dGPIA~if~ImEach peptide Is a portion of jIiLvTDTnDNHlPV IL 1.250 I I'~ q------ COO~ i SEQ ID NO, 3; each start F 6.30 NPEhlrQMIMM L[ I.IM I151 0 KC DVtLGLH Fj050 position is specified, the L _ - --length of peptide Is 9 amino ~y~IEL1.12 F \0§0P1 acids, and the end position for ~I29I AA~gPPL~(1.000 R9 PI4~ AD QeTG NI F10 50 eachi peptide is the start ( 964j( DADEPN qlJt00 _.Ls~Aoi 050_ position plus. eight 3627 GLIvTPD 1K0 L72CS Ss S S DYjL ~~ P.ojsLsNence 11 ~reI F3-6 2] ' I F "JL _z~ 51 LG~RVVK I FI-6- J 50 NTIELR050 FLETAAYLJI81989101 142 Table X- 109P1D4v.1- Table X- 1O9P1D4v.1- Table 109 PID4v.1 A0201-9-mers A0201-9-mers A0201-9-mers j Each peptide is a portion of Each peptide is a portion of Each peptide is a portion of SEQ ID NO: 3; each start SEQ ID NO: 3; each start SEQ ID NO: 3; each start position is specified, the position is specified, the position is specified, the length of peptide Is 9 amino length of peptide is 9 amino length of peptide is 9 amino acids, and the end position for acids, and the end position for acids, and the end position for each peptide is the start each peptide is the start each peptide is the start position plus eight. position plus eight. _ I position plus eight_ __ poitio _ L__ _ 2.0 _tol eqiuence Score _S'ieq ec] Scor s. Sequec [cr [6J QPSLFS 385.691 8GLHRVLVKA_1.426 JFVTIEETKAJL _.000 GLP 1NLFVNESVT 11.305 1 LPLDNTFVA 1989 GLMPARAM 1L =.989 25[342MQF 10.931 F T 1.956 GM T Y INPVNDT 1084 iNFLLEAA I .[864 5 VVV 1WF TAV 90.423 274 LMPARAMV - YNVT 1 . _857 280 L VNVTD Z74] __10.754 I F r v 043 1- F . 10 ~75 MPARAMVL _____________247 LGLrnKEPLJ 10.468 VM1.775 820 N 210 QLHATDA 0.433 40M[GPNAKINYLJ 1764 6L IL L 888 IQPETPL 9.963 266 LVLASGGL 1.528 ILDENDFT 599249LTSNVTVF 9.032 VTDGLHRV 1.511 -I T 3- 8 DLplDL 7.652 KNLLLNFVT .49 L598 I |NDVIL48991 :231LQLTKVSAMF 7287 [I361LNQSAMLFIj1.465 E3] NIARRLFHLJL3918 1[i8 RVLVKANDL _6.916 7[ FITA 1. 479ILAKDNGV 35.385 ThNEYNFY VNLFVNESV 1.399 __ ___ _ v 6.317 L08 !yEJ~. F= 0ES VIVNLFVL33.472 V J .[ L FT~~~~~[l VL =4El:Dk SENIL 1.195 4 KLVYKTGDV 31.646 1 81GVPPLTSNV I( [YNFYVPENLI 3 QTMGKYNW[ 29.487 I T DVjI076L NPGTVVFQj j LIQZjVDT TI[63j__s.7 7 RQAP2HL9._ 1.159 753 ILVAAVAGTJL29.137_ 1757 AVAGTITV579N 90-5 LEN TFVyIi 28.90 DL LHRVL 5.16 E2]SLDCRTGM E F RLFHLNATT[27.572_ 30 IVNPVNDTV 5.069 ]54 L 121 |SQNIFGLDVIL 26.797 7 IFITAV 4.242 ]913F ACDSISKC 10J SVSDCGYPKEDKYLFTI 3.789 267 VLASDGGL 1.098 S75 NAPLFPATV 3.671 M ] [ TLMEJKCD 22.7 763 TVVVVIFTF 3.56 370 KEYAIKLLA 1.082 251KF L 19.33. *116 YELIKSQNL 03 JTSFVTVSlL105 r5 61]FTiDSQTV 219 F LI EDINDN 3233 TP64EIAD .04 17 JLTVVVVIFJ 38. 42101 SjP79QLTKy1.044 j 8 55 .. 16.550 rI ETElEVSI 2.911 11 STAILQVSV 0.966 1TFEVS 14.654_ APVFTQSFV 2.497. IliAAVAGI 0.96 T§3LVqVIV 13.997 P FSLDCRTG 2.263 KLLVLASDG 0.965 625 VIPSTNPG T12.668 3- M6 YESTKYA0933 2 NVTDVNDN YV IVL J SVHTPV .913 v 1743 VSSPTSD 2.080 658 GNTRDLFA| 0.908 VVLSENPLIL1. i6 DAlDQET ][ 68 VSNQFLLj088 143 Table X- 1D - 1ableI- 9D4v-A)201 Tae X - 109P D4v.A02 A0201-9-mers 10-mers 10-mers Each peptide is a portion of Each peptide Is a portion of SEQ Each peptide Is a portion of SEQ SEQ ID NO. 3; each start ID NO: 3; each start position Is ID NO: 3; each start position is position is specified, the specified, the length of peptide is specified, the length of peptide is length of peptide is 9 amino 10 amino acids, and the end 10 amino adds, and the end acids, and the end position for position for each peptide Is the position for each peptide Is the each peptide is the start start position plus nine. start position plus nine. -- postinplus eigh. Subsequence S pubse q ne Fo-seguenceJ _Score V~tWCFDePR 314 IPLNTKIAL [ 0 I LEKCDV SLrTGMLT =72981 Table X - 109PID4v.1-A0201- 94j T l 10-mers AI73 L SVTDLT _ 8720 19 GINGvQNYEL .937. Each peptide Is a portion of SEQ IFG9DVIET P ID NO: 3; each start position is 9341[CGYPvTTFEV 22FSFSnLVSNI specified, the length of peptide is P L 10 amino adds, and the end489D TFV =.16[571 position for each peptide is the 902 IlQEIPLDNT 8049 30 KEYAIKLLAA F~osubseqence ELDrEEKDT 7.693 LIKSNIFGL 2 LT M PkAMV Gi96407 [Wi1 GMNAeVRYSI 2lIII VFPDIRYiI sioI I 5LPlFRLV 85LINVRKST L452 VVAGT 2 30 701 LSLFSvViVNL l0 IL DQnDNSPV j =TWQVIA [ LDEnDFTI RVSRsSSAKV 929[ YSVSdCGYPV AlPdEIFRL 14498 [LAADaGKPPL12.068 tI TH e 11.751 [20 KSQNiFGLDV 77J3L PLaTVlNl1 1.953 SKlHFsFSNVj S27PEnN SP8i 1 [NA vRYS1[V (29 AM~vVTV402 _NAPVfTQSFV 842 LdLPIDL 1.869 764f WVViFITAV [9=IVNLfVNESV 1TsENIPL =_186j TTPaVDPDVALITvTDKDA 233 SNIArRLFHL ]FLIEdNDNA 8 KTGDvPL4RI 435 SGPNaKINYL 548 SILDeNDDFT 41.91LLV GGGLVNDNkPVFIV =i.689 27 GLMPaRAMVL FVACdSISKC 272 GGLMpARAMV1.680 752] KILVaAVAGT 30I519GV819 KNLLINFVT1 0LQ LP521 DF 9EQTMg SVSicGYPVT 69 GQPDsLFSW DTDIGLHRV 938 VTeFVPVSV [2][ YlVNpVNDTVJI N23]0 L5-VIARRL 7422 [ VAAVaGTITyj1.642 2 NLPRhGTVGL 65 WfTAW [ LPLnTVAC 9 1.589 l1i.TITVvWIFI 1T T 430IO IVNPvNDTW 4l 42 ( IGiQLVSM [57 (7 T II 1817R7[1 52 VPrPT SPnVGT _7 V .549 52 LLNFvTIEET P4102771 F07 WIDVnDNKPV 104]LVP 1 FLTyipvGNGVJ 1.549 81 NQSAmLFKV 62[ LVLPsTNPGT605_jl DVNDnKPVFI .544 FVNEsAT 1 82 r259 TQLHaTDADI (39P14 L29] CSYEIVLPST 31 FLS V NLFV LM E148[ I!!51EI-KcDVTDL 3|8| 1AMDAdSGPNA 4 f LGQPdSLFSV 734 VTPNIEIADV L85_ 734 N1SpENSJ i435J LVYKtGVPL 636 FQVIaVDNDTF3.476 144 TableXII-1O9PID4v.1- Table Xli - 109P1 D4v.1- Table XlI - (9P1D4v.1 A3-9-mers A3-9-mers A3-9-mers Each peptide is a portion of SEQ Each peptide Is a portion of SEQ Each peptide is a portion of SEQ ID NO: 3; each start position is ID NO- 3; each start position is ID NO: 3; each start position Is specified, the length of peptide is 9 specified, the length of peptide Is 9 specified, the length of peptide is 9 amino acids, and the end position amino acids, and the end position amino acids, and the end position for each peptideIs the start for each peptide is the start i for each peptide Is the start position plus eighposiosition plus eight position plus eight. -Pos Subsequence score Pos [ nSubsequce _Su bPsLSeguence I Score LiK7MP1. _!JLQLqIVQK [00i T T 64m VVVVIFITA - 10.270 KLAA 90.000 2 1AITVTDK jgAR] 234 1RLFHLII.01 =67 LROKLEow. i"LLAK§J LK.! o 96 D=5o KLDREKEDKJL60000J~~-nw 11_lE=SNF 09045 KL~lK 0.270 720 ILTLNELVRK 51.000 __58_[ RLVKIR 10.900 64dL KIRFLIEDI 0.270 2_LjGQNYELIK I [36.000 _701 _SLFSVVN0.900 6800DVTDLGLHR 40 (j | DLEEQTMGK 18.000| 83891j SAMLFIKVK 0.675 [47611 YLFTILAKD ILO.225I 805.LMMKKKKKKj[15.000J L RQMIMMKKK 182 [75641 TLMEKCDVT 0.225 803 JQMIMMKKKK 115.000 L7607 JIG6216081 DLFAIDQET 0.225 781 HL QKNK |10.000 [719_ILATLINELVR 0.600 872 SPDLARHYK0 200I MMKKKKKK I 0.000j |21 j[__QLHATDADI 0_600 F775]LRCRQAPHLK =.200 230 NLVSIARR 19.0006 L j VPPSNCSY_ FTHNEYNFYO2 GMLTVKL 6.075J L49: IPTT VFw .60VK L REK ]0.200 NVVDVNDNK JYisij L95 GlQVSNTTF_ 0.600 AP AQK . 6 LVKFLr]iAI .0500GPRHCF 6849J J LGLHRVLVK DiD7 GUTIKEPL I44_0560 2]I LTVVKKLDR 0 _ 0DCRTGML 41I F A D I K .000 5 _J LTG ARDR 1 0.600 KVKVELnn DGGF .8 L1 ~ iI q L iiLj I I E2L 7F493=- 0=3 .7L~ I1__1 86_J WTTTFK 3.000 [ i TIKr EPLTVFQIA L829 NLLLNFV1L700I L493L NVVFVSil0.540 LFITAC L ILPDEIFRL KIHFSFSNLJ 0.540 E598 KVn PINVVD L563 GVIRPNISF J.700I F QESYTFYVK D.540 1 D VSSPTSDY " 0.1 387 INQSAMLFIK |2.700 709 IVNESVT L0.500 [241I HLNATTGLI 1180 [244 AL[2_.2501 238 _LFHLNAT 0.500 VV3081 LSENIPL 80 767 VIFITAVVR |2.000 19' NSPGIQLTK 0450 575 KQESYTFYV 0.162 [ 590 RVSRSSSAK |[2.0001 753 ILVAAVAGT 050 3 MLFIKVKDE F81 KTGDVPLIR |1 ]80(I 891 QPETPLNSK 050 910 NTFVACDSI Ji50 53 I AILPDEIFR |1.800 762_ ITVVFI 4628_SPGVVF 0.150 _804f MIMMKKXKK |1_.500 531 LVTDPDY 0I400 _273J_ GLMPAM =[1.350 35 PLNQSAMLF =0400 Table XIII - 109P1D4v.1-A3 LII r~y50[ J Fi1 PSDAj0.3 60 L lO-mers .1 L685_3 LHVLVKA 89 PP- Each peptide isa portion of SEQ 68 G K |EPVSVHR 0 360 ID NO: 3; each start position is I141 _IVQKELDR .2_00 SSPTSDYK_ specified, the length of peptide is 291 NVPSIDIRY I[1.200 3 FTDHE!PFR 0 10 amino acids, and the end 27=4-~j~2 f-0_IQSTD.[770 position for each peplide Is the J2 ILMPAAMV 1_.2007 LQVSVTDTI0 start positon plus nine. 458 J1 RTGMLTWK 1.000 SILDENDDF Subsequence lScore 695 DLGQPLF 0.900 3 68 J TKEYAKL 0 3 DLGLhRVLVK 36000 1 VIETPEGDK 110.9001 I 821_j LLLNFVTIE 2319| KIALITVTDK 18.000 _855 TTMGKYNWVT .90 [4__ KLVYKTGDV 0.270 GLJI vTDPYj 145 Table Xill -109P1D4v.1-A3- Table XII- 109P1 D4v.1-A3- Table XIll - 109P1D4v.1-A3 10-mers 10-mers 10-mers Each peptide is a portion of SEQ Each peptide is a portion of SEQ Each peptide Is a portion of SEQ ID NO- 3; each start position is ID NO: 3; each start position is ID NO: 3; each start position is specified, the length of peptide Is specified, the length of peptide is specified, the length of peplide Is 10 amino adds, and the end 10 amino acids, and the end 10 amino adds, and the end position for each peptide is the position for each peptide is the position for each peptide is the start position plusnine. start position plus nine. start position plus nine. [P][ Subsequence Fso] fl Subsequence Su bLsequen]e Scr f 75KQESyTFYVK j I6.-9pJ AILPdEIFRL F0608] [r37 LTCFTdHEIPj0.200j 80QMIMmKKKKKDVIEtPEGDK L430 JIMDdSGPNA 02 Mjk_KKKK VVIlFiTAVR 7758 QA][cPHIAAQK o~ [i[QLIUVqKELDR_ EL J 1522 NLPRhGTVGL 4||_SLD] [CrGMLT .0 [467fl KReKEDKY -2 00) 86UETY3[LNQSaMK 806] MMKKkKKKKK 761 TITvVVI 418 |NNSPgIQLTK 3 RLRPvFSNQF 0) VLSEnPLNT [111] NGVQnYEUK 0.180 LGMNAeVRYS 82RQMImMK 9056 _ELPLdNTFVA10).80 [273 GLMPaRAVL8.100 NIFGIDVIET 450 DIGEnAKHF 461 [ ML'VvKKLDR ] [743 V1SS6SD 456 3071L TVsENiJP0L 180 E7LLE aAYLDY J .000- 7I3j _lLV-VAGTI 4 385 PiLNQsAMLFI [ { LSLFvIVNL 6[550 TGvPLRI oA_ ILRViiRFUE KVEDgGFPQR DgTGVIRq2230 KHFsFSNLV 0180 _A3YLdYEK 3.000] [4Q24[TKvSAMDA . 422 LGQKVSAM .10 44.LLGPdA DFI[3000 [i97 VGlnGVQNYj 0.360 [866lTTFpDSPDLJL0150 1 R T__MTVVK 06 ]939 FvP LLNFvTEET -150 F2LFFFFI 57 [[IPJENsAINSK [ =.30MkKE 0 2.700~ i!3 T~JLN ik m -i IFIIjq-! i0.5 0 564LVIRPnlSFDR_2.700 1 1655jI IVGGnTRDLF L3 I TvTDKDA u 01 I AT~nELVR 50 L MENFVlEEKFDePR 0.35 890 IQPEtPLNSK 5161 REEdTGEIF 230jNLVSnLARRL =760 GTITvVVVIF 5.025 LVYKtGDVPL =5FLLEt 363 YLDYeSTKEY 7.4 LrAMVLV 0 300 764 VVFITAV 0.135 675I ,LMEKcDVTDL] 1.0 767 j[VIFItAVVRC SS LPDEiFRLVK T800NHPVFK 0Table XIV-109P1D4v.1-A1101 3_IP~kdEHCFY_ 50[99 TPVDPD ~ Each peptdeIs a portion of F391 [IPiIEH1FP1 vD99V F0.- SEQ ID NO. 3; each start L E' 22 [ P position is specified, the length 6=9L7Gt!LE .90076] [-JIYYYITA [ 0.270 1 of peptie Is 9 amino adds, and ETG~TLMK TV~vtjh_ end posito for achn F131 FIVPpSNCSY . 03.00 11137 KMPQIIVQKE peptide is the start position plus [8_jLFRVKIF 90 2[ GTwfQVIt eiht. __ j 3 VQKEIDREEK 0.0 25 LLVLaSDGGL i10 27.i Subseq [i AMwVvV 1 82 NLLnFVTiE 22 GVQNYEUK II 1 GINGvQNYEL 1 0.810 F11815 UKSqNIFGL RVSR SSS AK ____o E t LDLEEgjMGK 0.8 [ 0LSENiPLNTK FVACDSISK F [ LIkEPLDR __ 0388 QSAMIFIKVK 0.225 475 KYLFTILAK 3600 FUEdlNDNA _1 0HLNATG 02 [R ] TGMLTWK 1 46 Table XJV-1 09P1 D4v.1 -Al1101- ITable XIV-109P1D04v.1-A1 101- (Table XIV-109P1D04v.1-Al1101 9-mers 9-mners { 9-mers Each peptide is a portion of Each peptide is a portion of Each peptide Is a portion of SEQID NO: 3; each start SEQID NO: 3; each start SEQID NO:3; each start position is specified, the length position Is specified, the length posIion is specified, the length of peptide is 9 amino acids, and of peptide Is 9 amino acids, and of peptide is 9 amino acids, and Ithe end position for each the end position for each the end position for each peptide is the start position plus, peptide is the start position plus peptide Is the start position plus eight. ___ eight. J____eght [Ps1Subsequence(Scr []SubsequenceI crj Ls Subsequencescoj NWJ[~yDVNDNK VV3.K 1 L~iIKKLDREKJ02019 LTGMvLTVVKKJ f~ WiVTPTFK (20003 ~ j]GRPNISF GYP_10] ~VTEVi99 [3fl NQSAMLFK 1800 [~ VIFITAVR .61 2f KDTYVMKVKJ(00] '[ lL PAADAGKJI ]L 21QESYLFYVFYVK :0 843]LVTL iLPD I.~ ~RQMIMMKKK j!80j j NLVSNIARR]12 VV76 IFITAW 0I 0.00 L3 KMPQLIVQK_ 20I []~ SVVHTR[ 0MV020 L/LVNVTDV 4[eJKLDREKEDK 1.200] []RVLVKAND [D01L1LVLASDGGL _ (KTGDVPLIR[ 1.200KKHSPKl I TWVV~Il j244] ATTGLITIK 1.0 ~ ]LGLHiRVVK] VV~](65 FITAV .30 [kL TNELVRK K i~ V i~jNWDV8 IEFRLVKRM J~4 F49] ~LTLEPLDR ]f000] 215 ]DGEAKI[006] []1]LRREKLCAJ 0.24] [7I RCRQAPHLK[ 0.0 764] VVVVIFITA Joo](23GLMPARAMVI002 [ 191 !lNELVRJ[9j DTGMNAEVR][0003 10J ENRQldllMM]002 1362 |AYLDYESTK 704 SWIVNLFV TTFEVPVSV [L1 lMK1KIij 00!42IDADSGPA 0.6 2]TVTDKDADH 1 [ ~YVKEGGRI T.0oVVFQVIAV 0.6 3jSTKEYAIKL ~p~ L~lETPGDK20 GTSVTQLHA [Lo 73(WRCRQAPH 0.2 30j(IALITVTDK 015038i~j KVKVEDGGF 0.6 ~SVHTRPVGI' .2 (824 ILNFVTIEETK RRoiI~ LVlRFU ~ 50YVKILVAAV 0.020 [80]L DVTDLGLHRJL4] 6sLQPSS KKPDSIA I LKQSxYTFYV TableXV109PIDv.1 L5J AJLPDEIFR 22.201L |i GEIFTTGAR Each05] AepiIeris tono E 65]DLEEQTMGKJJ241 L9YG i_TITWW IID NO:3; each start posItion Is 4JJVQED 020V 13 rQVIA______ specified, the length of peptide Is FYV EN PR 020 S~11 VSDCGYPV .00 position for each peptie is the ~l39jSALFIKVKJ(. L8OII NRQMiMKK 0 start posItion plus nine. 7 TfHLKAAQKNK [0200 744] SSPTSDYVK(( 0.4 osi Subsequence Score I82[SPDlARHK 0.0' I.JTGNITLMEK K_0QE4yTFYVK__.600_ 77 MMKKKKKK 0.200 IO7 NSlQT 4__ 4I RT~_TK 30_ LAPH0:KAAQK ] TNDNHPVFK - RQ0.mMKKKKIL1800t [891 IQPETPLNSKj 0.200 J 291 |NVSIDIRY (040719 ATLnELVRK (30_ FTDHEIPFR 0.20 794j |WATPNPENR 0.0]3JKIAUJTVTDK |L1.00_ 147 Fjjrable XV.- IDID4v.1 Table XV - 109131 D4v.1 - Tbe XV - 109P1 D4v.1 1- - lll-l-me-rs 7 All01-O-mers A1l01-Omr Each peptide is a portion of SEQ Each pptide is a portion of SEQ Each peptide is a portion of SEQ ID NO: 3; each start position Is ID NO: 3; eac stat position is 10ONO: 3; each start position Is specified, the length of peptide Is specified, the length of peptide Is specified, the ength of peptide is 10 amino acids, and the end 10 amino acids, and the end 10 amino acids, and the end Position for each peptide is the position for each peptide is the position for each peptide is the 1__.tarpsitionplus nine. s._.tartposition plus nine. start position plus nine. =PsFs--auencel core UP 7oS u.bs-q-niienr' Pos II Subsequence Score Liw1 KVyEDgGFPQR 1L1.26 5 0.8 -57T~fR ~ ~ IzzI [12 I VI~PEGK .90 3 181 NSqglTK lF F7-Q AVNAvNtV 0.020J (669 ETNFREK L.60 I 33LNFVUEETK L 0.080 IVLVNS-0.2 FTl~'iTLcO v! 1~ 0.66 F823- _Z~FRE~LI~ I70]1 VKIAL 0.0201 [16:]L VQKEIDREK Eqj 00_ 11135 1GV107LI 0.615 LRe 0.020 E-j 1fitPNJ J 0.600 J 849 U DQMjJ000j6jppSDj .2 F~~IJLIMM~kK~KKR 0.0 j (0jK Pj [3TF IAPVAHJ.0201 I 611L EK[ 0.400 F2E~EAK 9~6 457 [RTf l TW 0.020 1K01 i =PD6FLYK8=49O LE~PYKRJLI 0.06[0 kDPv~a~ EfL~U n~F([.0 ROE1Ld-vNTNK !LP.P I. -o D7ff\1 -C H2GT YiA: .020 Fffl=5Ll F2.4x, 007 0 11 0: [EiIxc b1 0020 [6~J RYSvGGTK 0.2400j 36j [E-vWIj00 45= [][RPD~pPEFVj] =002 1L5 F DfJ L VKy~ .409 I P L 0 I = ~ 7fQ~sFV' EE18 Kf T 0.200 J 57]CF~EIF IV-.40 [4611l MEKKSItpj 0.160 6-3 E[Do][N v-TpriIFAK oj .0e2s [ l1 I- R0.160] L9: [ZYi1[ vwiFKVi 0.0300 EacpepiMsaoTKoo I j ll~ .6 ~ rFD~j 0.004ps8o ssecfetelnt L842 LY§~dPD 0.1240=0 [F T v\AeY FIV1LQ-.1 (]E D.ght 1 5 4 AIpDEFR f 1201 76sI WffTA J1~ 0.04500G 'kqoPjjSubsequn .018 6= 83 f_ lG 0REK ~I ~ iI?409 T4n GI~ Q Y L 9 0.04 ~ [ 7JV K GO P fL :q.oD J 7=7 ]~gRV rSSSK If0.00 5 9"f PEtkg IFi0 -. l[lFdMJL ll 71__ATNEVR 0.00 E ,M-vGDATPA 10.040: RPFNFf1.00 L F1gRI 080 37] D-E4(L:0 1RVWN1~i40 148 Table XVI-1 091D1A24 - Tale XV1-1 09131D4v.-A4 Table XVI-109P1D4.1-A24 j 9-mers 9-mers I 9-mers IEach peptide Is a portion of Each peptide is a orio= f Each peptide is a porton of position is specified, the length position is specified, the length position is specified, the length of peptide is 9 amino acids, and of peptide Is 9 amino acids, and, of peptIde is 9 amino adds, and the end position for each the end position foreach the end position for each peptide Is the start position plus. peptide is the start pston plus peptide Is the start position plus eight J___ egt- ih Pos E&Ii jsubseuence[ Scorej (I Posj(bequencje e s 6 Sec oreJ 59 FR=LVKIRFj 1400 f 368ffj( AI 5.280iL5892 ;AJ§Y iLZ2 0 I 338 T DH'Fj 2000 371 IALAA00 iIIPFRLRPVF][ 2.400 621 1YLLS IL 10501 -i]E INVNEL[A0 17 I SPKNLLLf L.4001 I[7479 YKIVAf 10.500 28-]LGIDREK-L[ 4.400 1 F 312 ENIPLNTKI J .7 =M51 N EKSQN JJ EPT- [i61LvKRu 4.200 F7 ~J GIWV J 10 509]IVfTHNEYNFf 1000 ~ IDGKPPL[4.0 76[jyVIj[20I 223] EKIHFSFSNLf 9.600 ] 8=3 ED =NRF D=00 [ DlqGQPDSLF =2.000 [~]IGML~wiF880I 9.4 []KSA SPQPAF] 4.0 6[56GNTDF .0 F8-43 PILI 8.650 GNRJ 933] DC GYPVUF2.o Y 8.40 39E .FSHMLJ(±00 I E3 ij8-IIESIL80-j F24711 GLIT1KEP 840] []StNCSYELV I 09-06JDWLEI .0 FW 1 VTTtL 8 .250 [54] LL =iA000 ILg =NDVPSIL±9 F6714 -NFVPENJ 8.250 j [] 656TGL[ .0 12IMDYG L 1 K F1VN 7.00[231 LPRHGTVGL 4.000J 6 IDf MNAEVRY SI L!. U 5-j =DYILTtI 7.20 1-o- [=6 L PPfl L!-qi Iji[AvPNE 11.6501 5j76 IPDEIFRNL 7.200 F44 [12~~~_.60j I~Fl[GVNEUIL150 3564 =LEAY .200 SILEND2] =3.600 Ellj FRAI 1.0 717 [3TINELJ 6.137 EifIELIKSQNIF][.0I___________ 6&7 6.000~ff F65 Table XVII - IO9PID4v.1 FI4 6.00 [K2GI~ ] ~ L ~ A24 - IlO-mers 417 Each peptide is a portion of SEQ F, 81 SPGIQL IL[9..] ID) NO: 3; each start position Is ~31] PLIEKAL 6000 J [ ~_DNNAP.F = .6001 specified, the length of peptide is 30 PNTLI600 2 TNGVF 6010 amIno acids, and the end []'~!!iL8 PGTIAT ]L3 position for each peptide Is the ______ ____________________= M start p~son plus nine. j L92 ~ ~ ~ ~ Pk1 IISAJSKYT F .00(F1 GI 9 k-I IF~osl Subsequence II Score ~I~1~x P~16.0 1 F-KKPLPDE K>LOOO 514I YEgN i 420.000 jO-_, ff :N TPHKLLYL 1 .00 F1I GVRPfNISF 3.000 3IYmL25.0 ____ ~ ~ ~ ~ ~ -QQEP ~ ~ l SIRL .0 i1s N3,jjYEUKSQNI j 240-000 1 LVSIARRTLJ .0 [i NKHS .0 8872 AfQjTL [j~l [515 ~ ~ ~ ~ ~ ~ ~ FNYVEN s.6o j [76 TIVVF .0 [iL x -L 149 Table XVII - 109131 D4v.1- Tble XVII - 109P1 D40.1- Table XVII - 109P1 D4v.1 t2-1-mrs A24 -1 -mes A24 - 1-mersJ Each peptide Is a portion of SEQ Each peptide is a portion of SEQ Each peptide is a portion of SEQ ID NO: 3; each start position Is ID NO: 3; each start position Is ID NOr 3; each start position is specified, the length of peptide is specified, the length of peptide is specified, the length of peptide is 10 amino acids, and the end 10 amino acids, and the end 10 amino acids, and the end position for each peptide Is the ,position for each peptide is the position for each peptide Is the I -startposition plus nine. 11I staqyositon plus nine. jj start position plus nine._._ iI] [ojSubs-equence Ijcrej Pos I Subsequence Score F P05 I Subsequence]E Scre K_-1 rCFYVIL. F24.O~J-60000 [2k1E-~-Lv47511i KYLtILK1 2.3101 r2-3-11 LHuTGJFI20-.000- F1 132 TPE~d vIPQL 6.000 I I] F!fTD~fHEI[ F2.200 F5- 91 _IF R Lv K I FT L[T20.00] R] SIN T DLj F7% F7 EP eN M 1 L. 2.160] [~ ~ ~ IOO RYIE nPVNDT F 76~~L G? NI~ L M VRsI 100 F702] LFSIVNLF L!o.i 701 MI S FSY\WNL I 57 [E]I _ Q~Sl EjJLj00 j~]RPDsQFL L o j 1481 I LAKnGVPPLI [-800 6-30 I NPGTvVFQVI J[-QOIj Ii~IKP LnSMt 12001 F37 ILAaKPLI480 5 Yni 2.000 EM ] EVdLPIDL J[9.600 jf[ =IVTLRVL II-f 4.0 1 3 TCF=TdHEIPF 2.0 J45 Ds TG MLtvVKKL1 9:.240]~ F27IGARIDR6 J 46600 1231 FIj "RF J[ -M7 13811-P 67L~ LFJESTK A KLM9i L~ t!] .4 F85] ~nqf -§ fi1 SYE vPSTN1L9=.000 90MF - P Tjj 4.3201 15561 f11DsQTGVI JET1.800 1749 .. PY!YYJ@LVAyIE 9!.000]- I P-91i GfyvYVIj '1200 605]FpVNn--rKPVF .0 12461 [TGLRtIKEPL] 8.400 j 77:3] QPHi 4.000 j]fA:IkqETGNI lLE .j ______F67q FIfsT -i1L -"--iL~ I D o c RFLeDINDN L-N 1.800 436 GFEkNLLLAOE F8-661ja~qSPDL F4.000E-7 1P14]1 SPSPG I iFi.8oo0 1065~ GFP- rsj TAI T FL1 [1-811i~I9I FYE4@_-9 00 1 73 PYI I_!.650.I I89flN SK Mf~hI 7-.392][7IN QPSJ49p b4ISPsDYYKII [ 1.650 L~JRI~dTEI j.200] G IAf ETE00 Ij-]I [AIUd E I FRLJ F.o 5411[N TSII .0 Table XVI1-I09PI D4v.1 -13 L4~isGPaKI~h1 7.0 1 5ILV-YKtGDVPL]4.0j f2-7i 3LaAML 7.200 ] liISTYVL r400 Each peptide Is a portion of W E G SEQ ID NO: 3; each start 1~]FSDCTGLI7.00 ~ GIrDHC 360 position Is specified, the 6151 FP~CYL 860816]HPnL .0 length of peptide is 9 amino 109 IN~vNYE ~ 89 KNUNFTI 3600acids, and the end position for 5-R9=6-00 [7KNWN~rIeach peptide Is the start 3131 3I-43IL 6.00] EI3.PV 9O] position plus eight. [87]RKSaSPQPAL 6.000 LS [s-ILBqENDDF I~ O FOSu ece[] 171211 VNESvTNATL 6.05 YGIQvSNTTF Fq3.00J ,5IPETN GLI 6-.000o ![562,I TG~r-PNISF II 3.000 'Fq218 f FIREi~8O tGOf 1loIL~~1 6.00 ['1o1_NAPvFTQSF L -288.J EK .g § 6.-ooo [5-1[En -MvKIW 11 2.800 Wl D 1 180.0001Fi §TA71L F n 444 F[LG]d EI. 64i il41.6.IlGPNAXINYL 1180.0001 11751 ILMEKcDTLR6.00 F Iq- E[9lIfW IVS 11 2.520 1 if 260lE77t~l II 80.000] r1- FK- vTi F O i I K2F-LdR~M] 2.500: 932.1 NPMPTWL 000 F23] SNI*R LFHL =~6.000 I 211717 DIGEnAKJHF f24072AVPEI3.0 301 IVNPWDyA .900 I j~GDvPLIRI 1F401 6 If 6PFP1 3[!.000 150 jTable XVIII - 1O9P1D4v.1-B7 jTable XVIII -109PID4v.1-B7 [Tble XVIHI- 109P104v.1-B71 9-mers I] 9-mers j 9-mers Each peptide is a portion of Each peptide Is a portion of Each peptide is a portion of SEQ ID NO: 3; each start SEQ ID NO: 3; each start SEQ ID NO:* 3; each start position is specified, the position is specified, the position is specified, the length of peptide Is 9 amino length of peptide is 9 amino length of peptide Is 9 amino acids, and the end position for acids, and the end position for acids, and the end position for each peptide is the start each peptide is the star each peptide Is the start psition Pus eight _Iposition ls elght j ___ positionjius eight [P-js Subsequence 'J screi jSubseqe-eJ Sor II~ !Jc 19neqiF = 796 ITPNPEN PMJI 2.000 32 ?J LIf.Gyl 4.000 1591YGiAiLFL9 pq 1YGGNTRDL 20=000 8-43 L~y1DL IL [1L!96067J [DqEtTLq ][ 200J ~~RVLVKANDL~~ 2000 I54 I SVLH. 00I EiSLDCRTGML]W ] 12311 VNIA RRL J[2.00O[] PROEHO@FY ~40] 1.000 9§KPPI 4 ffM[ §fl 1001 AL'PDV 4.0 ____ __ [=M rVADGJ2.0J5-15,1 =YF YVENIL [4-.00[=8 FIZNVM'P E_2] SANKTF[1.0J7-17 Lr!TINEL] f 7W UKLY-AV1 =.000] 378[MA.GKPPL [10.8001 110-!Of F9 300 =SVSDCGYPVI[. 166 QRSS§TA I 8.0 771 VGrWJ3OO 745 SPTDYVKI =-O :]U IJLTP~Lp9 5][z j Li~ 341PPLNQSAML F8.000o- 41511 IPENNSPGI 1[ 2.400 I[NLVNW_[I' 186 =T 2PFKF03LOO KIvqTST-\!1[ F- 20=0 E58! F-nNVVDjjf [29 ] VSD IRYIJI00 9-0 6 LIDNTFVA]2.0J 423 1A9LT1S L Ii ff"9[j1TPLNsKHH EII§ WRoP o] 2.000 svv] ]2671F v[S P~ j(~ I616E[SNCSYELJ =8.000 1 296.1 E704NVJ2.0! lJSW N~VI ~[ I FPTLjI6.000 _] qN _ F G[L=MPARAMV [.5i7 449 PFLD .0 [3--0 PVFNQLL2.00] l Ei NV [ fl [F41 TN-SRG IQJ.00 [4 LVM.VAqTll 2.000 (78 PERQI [00 j[~ CRGMTV2.0 Table XIX - 1109131 D4v.1 -137 F7_8 ___10]ijI 200-l-mers 1735 TPNEIAV iF~ 1Each peptide Is a portion of ji-35 j L 7JLLJSNVTELMo SEQ ID NO: 3; each start F8]DNR D D90 51 Alff ]F~!LKO9J position is specified, the D63 fF][HTRPVGIOj=4.000 F94I t--- I-V ength of peptldelIs 10amino 2751 MPARAMVL F84I [JIDE 2. 00 0 acids, and the end position for 4.001 __ ___ ___each peplde Is the start 460GM LTWKKL [4=0 51 SSSK .0000] _ position plus nine. I[23J U~FFSN1L4000i D882 fT§PQP i 10800PVtVTL 200 II420[SPGQLTK~( 4000? 2 43 INTLK120 =fi~, I PNid 24~0.00!~ P]I KIF-EIj .00 [202 0PVIG .0j(~ P~NFL~ ooo IF6-] FPIETMYIL !=4.000 :: 69 PFS W-G J 1 .20 .~I~ 0P~1GIL~ Tble XIX - 10911D4.1-137 Table XX - 19P1D40.- [Table XX-IOPi D4v.1 10l-mers ]B3501-9-mers j [ 3501-9-mars j Each peptide is a portion of Each peptide Is a portion of Each peptide is a portion of1 SEQ ID NO: 3; each start SEQ ID NO: 3; each start SEQ ID NC~. 3; each start position Is specified, the position Is specified, the position is specified, the length of peptide is 10 amino length of peptide is 9 amino length of peptide Is 9 amino acids, and the end position for adds, and the end position for acids, and the end position for I each peptide Is the start I each peptide Is the start each peptide is the start position plus nine. position plus eight Iposition plus ei hL PosISubeqFelc- Se] 1L un .c E[osJ Su bsejue nc e iL&o.i Fp_ -usqec F~wI [5FLRV482000 ESLML DDF D][30.00]o 138 _PUQE 80.000 I R PI F667o] 5 I[ IPDEIF~ 13. 0=ol [ KPPKnQSAML 8092000 F28 DG67JIVDASDGGLM] 3.000 1 16 6]FQsTI 80.000 _ I~ L _Is!L~9h j~~] ST~dYVIL 80000 Ii VPDRYI 1 2.000 111 PNSG ~~. j~ ~ ~ ~ ~~~F39 LPIIEQT I 009]Ii THH RIl E.0JIR?IHS [ 2.00] W imtGy- 240O 7 01NE I800IL2 DSPSY[200 FL1~ LAKnGPPL1200 F8-6 E- t.oJ LJ ±~gi3: F842I E92~IR 11.0 16] VFEE 1 8.000 1356 I FLLTMYqL 2.0=0 1 IFiT!v J 20000 8094 TPTID 8.000 1 K2J VPPt--§SNVTI2.00 Tabl XX __j FT F-8J61VSNIRRLF- 71 5.000 1 356]L=NIY L2. I S37]EM ID PP~i NO: 3; eac6 star -542 STAL 8IL (1 38~ ASPAFI 2.000 3501 eunecre 1z3 [593IR RYi1' JP44.000 =AKI NYPF 2.000 postio LPisGV specified, th Rd8471 qM LPLET4.0J lengt oPPNf 60.000e is ain ,ids7 SaFTNd 40000sto orF 3 OEPGT V [71 PV!YSJ 400 41~ LGPD TAEF I aooO 302 to pu eght 30 000 I[KLJP =VF I P 0 79 200071 D5931 IPLNTKIAL 202] 000' VF .00 [40:]EPR:D=EHCFY _ 51R NYFYj0o 1181YIGVJ 453 FSDCRTGM20.00 4023 [1APVFTQSF [2- 0I7I E0DY 1.0 j4396ffGPAiNYl]IR 60.000j 152 Tle XX- I O9PID4v.1- Table XXI - 10911D4v.1I -] Table XXI - 10911D4v.1 -1 B3501-9-mers 833501-lO-mers JB3501-10-rners Each peptide is a portion of Each peptide Is a portion of Each peptide is a portion of SEQ ID N0. 3; each start SEQ ID NO: 3; each start SEQ ID NO: 3; each start position is specified, the position is specified, the position Is specified, the length of peptide Is 9 amnino length of peptide is 9 amino length of peptide Is 9 amnino acids, and the end position for acids, and the end position adds, and the end position each peptide is the start for each peptide is the start for each peptide Is the start -position plus eight position plus eight ___pos tion plus eight [§~Jsu-bweuenceJ Score SC1 20~o~ ' ~ 4 11 FH3fYY.SYEiI!- 1100!, @179j1 REKEDKY~jJ 1.800 -W r~ 6-11lLKPV iPPN R P I~I!~YDENNAI1.80 7+]I S~y7VKIL r011 [9Io CLIQ\!9V5 =40 5-96F lsA YKl~vj 1.0 F- - 87I[ FvPU tNV~vIr oo ~3j~RyLJ .501 166 10R5TL% 626 [ Tw 0ool .95N I[!±UAA 1500 I 1151 PP6CSEL[ Lq- C [4n 902 [I=SDPYSV =1.500 jLLI 1 [6:64]li3.00 [3I08 WLSENIPLJ =.500 jjjLKnVPl18.00 [Z44] SSPTsDYVKI [3.000 ~~ 1.500] 0 w- 3.000NFET'J~ 391 GIREO .089711 SKHhIIQEL 150 EllJ 18 LKNIG 19 IVSPEAP = .500 F9J NErMM H00 266 [LVLAs=GGLMII] q7 1200 - -I]LYAPLi30 RlPLqD!S 1.200 8171SPKILLNFV M20 391 ][qlldEHqfyjao F6QPDLFSW 1.2001 L_ - - 95!_NSKtLPVF I[Ai NAGLITIJ12J f453 7SDCTG9510 IiApNpNRQMI3 0 ~~I10sI1 DPVIG1R.0J1681QDIFSWI~ =2.400I r b350M- 109Pmers. - DS- AIY1.01IIlTI99 1351I1- 56 NSPVfTHE 226 LVSNI JIO992 Each peptide is a portion of _L68 IAdDG SEQ ID NO: 3; each start ___________________M F637 position is specied, the 79llfAv [CyOiI8 112-011 KSQMFD LDYJ0]01 length of peptide is 9 amnIno IFijLLtKJA -ao 1 VPrEET[ I adand the end position E PTYFV FIVE:SCSY for each peptide is the start LI8:9SY F61311 mition plus eight 2 TLNsKHHI!] 8.000 ~ ] P~pT1j~~ su~squnc 1 Scor} 1547 LSIENDDF 7.5001 L2~sGgT~j~ f-I[K][ STEyAILLj160 384 .0 [~ LIDEETMf1o] GPO46 PEFS 6 945VS VH 2.0070 !LIDPSVDC~j4%OJ ~ JTP~dMPL] 6 000 fJD:iTvM Y =27! 000~ S1 [53'I7 EP0rETN9[0~ GIQDKVsAM -Y].099l 39J RPVFsNQFLL, 0001 [8161 H-SPKILLLNF 15 0001 I FRIRPVFS !IlF [53 RHg1VGLI .24.00 [ ENPS:00:1 .00 _________ 0 I-AI1y7s . 709~ i72l8i KTEaPVPNIK F_ .M GPNARINYLLFII2%00]~ IjjYP FEVP 1.OOOi'F: [3ENdV:rLsj i H4][:N:1:: 9 VPSIdIRYIV I± T~nE 920KC~sSDP 40001 [64141 DIG.0A00] 153 Table XXI - 109PI04v.1 - KTable IX - 109PI D4v. I - Table IX - 109PI D4v.1I ________________JI Al-lO-mers Al-10-mers Each peptide is a portion of Each peptide Is a portion of 1Each peptide is a portion of SEQ ID NO: 3; each start SEQ ID NO: 3; each start SEQ ID NO: 3; each start position Is specified, the Position is specified, the length position is specified, the length length of peptide is 9 amino of peptide Is 10 amino acidsI of peptide Is 10 amino acids, acids, and the end position and the end position for eac and the end position for each for each peptide Is the start peptide is the start position plus peptide is the start position plus! psition plus eight j nine. j__ nine. 'Ii~~iIPY~lnGVQ 2. L0]~ 00] 67jKDeEY1250 F10-1 DH G-I GVQNI I E_ ___lel F J26jPNkLLLAL~DLEqTMGKY 1 =?IVDdTMN_030 F7-1L DV EI r4000 LJJDSGPnAKINY 37.50rr 2.250~ 49,]_TNtFS 12OI31 S~PNK93111 VSDCgYPVT 1Wi-oo [ vtFv 1 aooo -II 125.00 E31 j 1.350 W~1 PPLTsNTW 2.000_ W F 3 3 j FL~SKYJ 213 ATDAdIGENA II-250 (~~~~J~ DPD6DSAV1.00 VTDL L-RL .5 F8] KGWvLIRI .0 []6 KVDgGFPQRJ,71%00jIPEQM MI.25 [~LS~EKQ I~o F.60 -- j F7--81 NP__IMF-2 53769 dIFL 8 KAEDgGRVS J1 8.00 ~ II91IL -T levSIPE L.125I [37:]~ ENP :10 _I 181[ DTNqnHPF - i00 178 N'[..... ASDGgIMPAR ~fhoj378 AAD~gKPiNh'l 0-0 K2[]S sDPY IS F5-0 5 LPDEiFRLVK jf1256] 215g DADIgENAKI] 1.000 JfI1i NPVnDTrVWV- El5OO 1250 [1-6[_LPDiETPG 111.0001 _ Il1 W 5-i50-0 [0LT~dGN F[68Jj1 DLGLhRVLVK =L000 H ~ ~ F i50 WL.CTVI {0o 1458]j RTGMFyISVKK 1h.000 5 F2G7 JDREIL10 ____________R R I_ 11 ATLMnELVR-K _ [l@ 1L9~ 16l L-RIEPE1i~Fj 9.000 1530 [ GLTvTDPDY 1 *l@ I F8-4]lGRtDL120 I95J'17D5001 C DADHnGRVTC 1.0001 [4]I IRDeHqFY jEt200 309 I ~ tlPRL 6250] 3_ i;]=.0 69-2]E KADIGQPDS 1200 DM L :DNVPsIDNRY][850 TILKP MDNAVFi ] _____ 6.5 [8271_ TI~iA ]0.9001 1-6 RIEdTGEIF 11.20 743 VSSPtSDVK- F_6-66-6- [12]Lg 1W] KLRKED~~ =120D7 . KQESyTWK Fi[sA00l 1 EEsPN~~~0 .5073 REK eSYTFY E=1.200j 613 FIVPpSNCSY- 5.00 0J IL4PMV ENEY ]FO7iso Table IX- IO9PID4v.1- STEPVPN ][-] 16~ [T -1 -mrs-'j=401 128881--Vn- vPLuD E[626 L l-lO-mer l IENSAINSK_ P.5[001 [ VNDN~kPVI_1o-.62f Each peptideIs a portion of Fq - _ _ TffKILA 0 NDVFTQ- 09.25 S EQ ID NO: 3; each start I77 SDv position Is specified, the length Fi4181 NNSPgIQlTK 4J- I N721 INDqNaPLPA 9I.6251 of peptide Is 10u amino acids, F146JEL-DReEKDTY - 2-500 -I0~QDsPFh 0625j I and the end position for each ______ PAES peptide is the start position plus I LTIn EVY ]F2.5o J44-6[ qi[AfUS A nine., jqJIDnDFI_!250' ' ~ CKSS [ i Subequnc Sori SLDCrTGTjr2j[1-] lE7811 KCDVtDLGLH IIAp P _________ 2851 VTDWnDNVPS 2.0 I78NATLNLR050 154 Table IX- lO9PlD4v. 1 - Each peptide isa portion of Table VI-109P1D4v.2 Al-10-mers SEQ ID NO: 5; each start N terminal - A1-9-mers Each peptide is a portion o position Is specified, the length Each peptide Is a portion of SEQ ID NO: 3; each start of peptide is9 amino acids, and SEQ ID NO: 5; each start position is specified the length the end position for each position Is specified, the length of peptide is 10 amino acids, peptide is the start position plus of peptide is 9 amino acids, and and the end position for each eight. I the end position for each peptide is the start position plus E[o_4 Subsequence I Scre peptide is the start position plus nine. RTSTIEICS 12eight DIG-5nA lHF PTDSRTSl 1025F6 LCGLIQQTV -10 24 L .IFR L SIECS.l F 0 IQIFQVLCG F0.003 DTyVMKKDHSRTsIl I QWLIF 430AMDdSGPNA T ERQW _KAD00SDGN RPLT S CGLIQQVT 0.003 231GLMPaRAMVL ]W I[]TSTIEICSE R.~LQWVIlQIF 0.2 QIQPeTPLNS L ] [LPSVHTRPT G i z II h iiI VIRPnSFDR_ 0.51 MRT__ _EQ V 0L _IMLTVvKLDRJ[SRTST!IEi IFiTEQVL 00 L TCFTdHEIPF TRP T S =3 TER QWVLQ llDnDNSPTDSRTTIE[ j PG DLLSGT DAPPeLD 0.50IQQTVTSVP 140l QLIVqELDR 0.500 [Table VIl7 -109P1D4v.2- 1 ]DVGInGVQNY N terminal- A1-9mers[ Table ViII - 0P1D4v.3 52 S IO[_V 5p e start Each peptide is a portion of SEQ GTITvVVVIF position Is specified, the length ID NO: 7; each start position is I '121KCSSsSSDPY jj05jof peptide is 9 amino acids, and specified, the length of peptide Is I~] AS~qAFQIJ~ osoothe end position for each 9 amino acids, and the end SA~PFl050peptide is the start position plus position for each peptide is the 60LV eight. start position plus eight. 26 TTGArlDREK Su.0 ~ I 0 ~ bsequen j l]SubseuenceI _Scorej _55LDVSdGNRVTI G] 3 MDLLSGTYJ 125017KSEGKVAG~j| 540001 ]07 AIDQeTGNI I NmRTERW VU A 106 NSDPESTFij| 7.500 132 TPEGQQL]0.4500 TSVPGMDLL 507 TSHGLPLGY 3750 25 KEPIDREETIJO__ 4 IVTSVPGMDL I01545HSDACWMPA| 3.750 71 LANESvTATL 0.4R 0 I SVPGMDLLSJL-sr ] pp STFIPGLKK |2r.i 950jI QAPHIKAAQK 0.500 Qi i 9nCGLIQQds, and speNCTQECLY I| 2.500 ] 19 VjSIPeNAPVG QTVSVGM 55 SAQASAxLj 2.00] 35~I QSA~1~'(lFKVK_ 7 WVUiQFQV 0.050 1I2IWiHPQPQRKj| 2.000 DSPD0ARHYK GhLTT 0t20 DPESTFlPGn 1.12 .6 -) ISIPeNSAIN 0_0I - -) IQlFQVLC TVEElADJ.900_ __SPDLaRHYKS 7* VPGMDLLSG 0.01 1112LAAEITVQPTI| 0.900) 8336 D1 dDG1 R .25 0.00 LIQQTVT S I APS NCTQEC _ S _750 [[VLIQIFQVL_ SSDGGLGDHiI 0.750 TableVi- O9P1D4v.2 I QIFQVLCGL 012 SVDQGVQGS|| [. C' Terminal-A1-9-mers VLCGUQQT H SSSSjl.500 155 Table VIII - 109P1 D4v.3 Table VIII - 109P1D4v.3 Table VI -109P1D4v.3 A1-9-mers L A1-9-mers A1-9-mers Each peptide Is a portion of SEQ Each peptide is a portion of SEQ Each peptide is a portion of SEQ 1) NO: 7; each start position is ID NO: 7; each start position is ID NO: 7; each start position is specified, the length of peptide Is specified, the length of peptide Is specified, the length of peptide Is 9 amino adds, and the end 9 amino acids, and the end 9 amino acids, and the end position for each peptide Is the position for each peptide is the position for each peptide is the Start position plus eight Jtart position plus eight start option plus eight s Subseguencejj Score P I-] Subsequence IL Score Pos [Subseuncej Score 25L TMEIWIHPQ]|_ 0.4501 [i]!LVQATALHH 0.050 SALHHSPPL [ .020 I SVHTRPPMK 0.400 STSHGLPLG 0.050 iA' .CHSPV __0.020 P ESTPL 0.300 14 iLCYSPPLAQ 0.050 S P = .=020_ 1371TQECLIYGH !E.270 1 LCHSPPLSQ 0.050 H_ V LPEGj0.020-1 84L1f L Q F 250 RPP!EVVR 0.050 56) ALHHSPPSjl 0.020 | 20M T 0.225 80 H 0.050 274|SLQQGWVQG 0.020 LPGQES 0.225 S.~HTQHHSPRVi 0.050 192 LCHSPPVTQ 0.020 j 0.225j [i?-L8 pH sP- v RTEGDGNSD 0.225 246 LAAISH I 0.0500 20 LCHSPPPQi 0.020 j F HSLV 0.150 I L162QAQASALCH 0.050 6e6 LGLGDHDAGSj 0.020 HS QAS 0.1_50 P R VQTIALC .20 1 HSPPLVQAT 0.10 PGYPQEEYD o 0.050 I F147DACWMPASLJ[ 0.020] j171J ASTQHHSPR 0.150 2-GAGLCSVDfl 0.050 LHSPPVQT 0.150 7[_SPPQVSA FL 050 1 Table VIl -109P1D4v.4 206HSPPPQVS 0150 LMKEVRSCT 0.045 A1-9-mers [10-iWRSC D O1 Each peptide is a portion of SEQ 11HSPPLSQASf 0.150 j8 1 QEEYFDRATjj0Ecetd 45o F170 - - -PS s 0. 150 D8 [ll -I=AvT 0.045 ID NO: 9; each start position isI 242]1 YSPPLAQAA 0. 150 12 LEASDNT .5 specified, the length of peptide is 9, SQESSSDGG 0.135 1 amino acids, and the end position (V 0.030 for each peptide is the start E11--~fA c 0.125 .. position plus eit 136 CTE=G0125 157 FHSSSSQAQA 0.030 S I67 1 LGDHDAL[ 0.125 255][SSPLPQVIA 0.030 HPQPQSQRR 29 QGSATSQFY 0.125 SSSQAQASA . LHPQPQS10Q 5 SLVIL .25( 12 VSVH=TRPPM] 0.030 L1 IQPQSQR 86 0YPQEEYFDR 0125 304 OF-MSERLHPSD 0.027~ 69 DHDAGSLTS 0.125 3IPThiLTF.0 6 III QPQSQRRVT 0.003 198 VTQTIALCH 0.12 297 ATSQFYTMS 0.025 jSQRVTF 258 LPQVIALHR 0.125 149 CMAD 0.025 12IHPQPQS 0.001 1333 RGDSPMEEH 0125 HTRPPMKEV| 0.025 PQPQSQRRV I 0 jI~ISCTPMKEST IL0.100 J 110L1GNSDPESTFIjl 0.0251_ _________ KVIPLTTFT 0.100 95I ATPSNRTEGI| 0.025 Table IX-109P1D4v.4 73071I RLHPSDDSI 0.100 I CHSPPPQV !. 0.025 A1-10-ers 124 LVQPTVEEA 0.100 J SJTjTMEWIHJL 0.02 Each peptide is a portion of SEQ _________0.__25 ID NO: 9; each start position Is 1 KVAGKSQRR 0.100s CTPMKESTT 0.25 s fi, the length of peptide is 31o PSDDSIKV Ls .075- L F. 10 amino acids, and the end i76 TSTSHGLPL 0.075 TTFTPRQQA 2 I position for each peptide Is the 1I~~ES1TMEIWI 'LT 0.075 1 LsI LLJ o start position plus nine. ]2 ESTTMEM/l_ 0.07 VHPGS 005Pos ISubsuence_| GSATSQFYT 0.075 215 ALHHSPPLV 0.020 3 1WIHPqP QR|[1.000 LSHSSPLPQ 0.075 167[LHSPPLS L0.020 7 QPQSgRVTF j[ 156 Table IX- 109P1 D4v.4 Table XI - 109P D4v.4 Table XIV- 109PID4v.4 Al-10-mers A0201-10-mers A1101-9-mers Each peptide is a portion of SEQ Each peptide is a portion of SEQ Each peptide is a portion of SEQ ID NO: 9; each start position Is ID NO: 9; each start position is ID NO: 9; each start position is sped, the length of peptide i specified, the length of peptide is specified, the length of peptide Is 9 10 amino acids, and the end 10 amino acids, and the end amino acids, and the end position position for each peptide is the position for each peptide Is the for each peptide is the start start position plus nine. start position plus nine. position plus eight. Subsequence Subquence j SubsequenceII|_or 5JLPQPqSQ ~ 0.025 [jJLPQSqRRVTF 00001 HPQPQSQRR| 0.040]j F9 QSQRrVTFHL L J IHPQpQSQRR 10.000 IHPQPQSQRjl 0.004 L 19:][ IHWHpQpQPQSQ F0. 0L PQSQRRVTFj= 0.001 LELWlhPQQS [WiQPqSQ| 0.000| LLJWiHpQPSQ[001 [ Table XII-109P1D4v.4 1 -[EQQSQ[RVTHj0 __6__1 __ __ __ _ KsLooRv1~iovo PQP__sQRRVT I n PQPQSQRRV 0.000 =8 L _PQSrRVTFH[ 00 Each peptIde is a portion of SEQIHPQ 0.000 f ill PG QRRVT IIID NO, 9; each start position is _________ specified, the length of peptide is 9 PQQRV| 000 TabeX-109P1D4v.4 minor acids, and the end position A0201-9-mners - j for each peptide Istar Table XV -19P1D4v.4 Each peptide is a portion of SEQ piuseighi. A0l1-1-mers j ID NO: 9; each start position is L Sub2seuence [I specified, the length of peptide is 9.EcpetdIsaorinf Q amino acids, and the end position I HPQPQSQRR 0.060 ID N. 9; each start position Is for each peptide Is the start 3 IHPQPQSQR _ specified, the length of peptide is f~~ pu egt 10 amino acids, and the end positionplus eg.T _Q RVposition for each peptide is the Ps Subseuence [_WIHPQPQSQ start position plus nine. PQPQSQRRV 0.031 QSQRRVTFH 0.003 L E i -Subsequence lore L 2 L WIHPQPQSQ]_[.009 QPSQRRVT 0.00000 IPPQSQR QSQRRVTFH I IW1HPQPQS 4 IHPQpQSQRR 16 OPQSQRRVT PL004 IL7I L QPiQSQRRV E___ QQSqRRVTF 0.004 L7[ PQSQRRVTF 1L0.000 F L PQSQrRVTFH 0.1 [M] lHPQSR_ JL 00 TableXIl- 109PID4v.4 1 Q91SQRrVTFHL 0.PI FTL WIHPQPQS -fJ0000J A3-10-mers I ILhOPQS o0oool 4 HPQPQSQRR IL0000J Each peptide Is a portion of SEQ HPQPqSQRRV 0.000 ________________ ~~ID NO: 9; each start position is___ _________ -.--. _specified, the length of peptideis [2 IWHpQPQSQ_[.000 Table XI-109P1 D4v.4 10 amino acids, and the end .iiiiPQPQsQRRVT1pt r e A0201 -1 0-mers posi for each peptide Is the Each peptide is a portion of SEQ start position plus nine.-9I ID NO: 9; each start position is =o Subsquen eTalXV 091v. specfied, the length of peptide is [0 WIHqPQSQR i ers 10 amino acids, and the end - Each peptide is a portion of SEQ position for each peptide Is the ... . PQq yRVT .0 ID NO: 9; each start position is _[start position plus nine. 9VTFL .1 specified, the length of peptide is 9 [osd Subsequence 1 || EIWlhPQPQS 0. amino ads, and the end position 9 ___________ ______ for each peptide Is the start 1 QSQrVTFH 4 LIHPQpQSQRR 0041 position plus eight. 3 WIHPgPQSQR 0.009 8_ _ PQSrRVTFH.0. Subsequence0021 E TL2 ELWhPQPQS 0.006 f 5 HPqQR V 1 0.000, PqSQRRVTF P020 I HPQPSQRRV 0.00 1PQPQsQRRVT [ 0.00LQP(QSQ V 15 [-j PQSQrRVTFH 0.002 = 1 lH PQSQ __1 | IWHPQPQS 0.150] 6_PQP)sQRR VT 0.001 4 HQQQR 002 157 Table XVI -109P v r _ TabI 19P A24-9-mers Table XIX -109P1 D4v.4 83501-10-mers Each peptide is a portion of SEQ B37-1 0niers Each peptide is a portion of SEQ ID NO: 9; each start position is Each peptide Is a portion of SEQ ID NO: 9; each start position is specified, the length of peptide Is 9 ID NO: 9; each start position Is specified, the length of peptide Is amino acids, and the end position specified, the length of peptide is 9 amino acids, and the end for each peptide is the start 10 amino adds, and the end position for each peptide Is the position plus _eight. position for each peptide is the start position plus eight Subsequent startposition plus nine. -- 1o Subsequence reI QSQRRVTFH Po s sequence H QgSQRRV 4 [ _. QPQSQRRV 9 .11 i ~ I QSQRrVTFHL Elo [~WlhPQS 010 WIH=PQPQSQ 5 HPQgSQRRVPQ SQRRT L HPQSQR 7i QPQSgRRVTF WIHPPQSQR ________EIWlhPQPQS P~] ' i Q I~rRVTFH Table XVII - 109P1D4v.4 iHPqPQSQR IWIHpQ A24-10-mers P QPQsQRRVT IHPQpQSQRR Each peptide is a portion of SEQ 8 [PQSQrRVTFH If 0.001 ID NO: 9; each start position is , specified, the length of peptide is2 iwH QSQ U01 Table VIII-109P1D4v.5 10 amino acids, and the end [LHPQpQSQRR A1-9-mers position for each peptide is the Each peptide is a portion of SEQ start position plus nine. Table XX 109P1D4v.4 ID NO: 11; each start position is Subs euence _ b3501-9e specified, the length of peptide Is L -- - -- ... 9aminoacids, and the end 9 QSQRrVTFHL 8 400 Each peptide is a portion of SEQ position for each peptide is the QPQSqRRVTF 3.000 ID NO- 9; each start position is start position plus eight. HPQP SQRRVo ads, adte edposto [SLubsequence lScorel LJL!fQ I RRV J specified, the length of peptide is 9 o ,L bsqe Swr = LjE l IWlhPQPQS joi for each peptide is the start SVHTRPSQR ] 0=00 F j-WjH pQPQSQ Lo.0I position plus eight RPSQRRVTF 0.050 6 PQPQsQRRVT 0s _ubsequence S w VSVHTRPSQ 0.030 3 0WIHPqPQSQR . PQSQRRVT 2 5 HTRPSQRRV IHPQpQS H02PQSQRR 0.200 PVSVHTRPS P =Q TH I VIHTRPSQRR 0.601 QSQRRVTFH T0.050 [:7][T RPSQRRVT _]ao0j Table XVll -109P1D4v.4 I PQPQSQRRV 0.020 8KQRRVTFH LB7-9-mers IWIHPQPQS 0.010 Each peptide is a portion of SEQ IHPQ 0.010 Table IX-109PID4v.5 ID NO: 9; each start position isIHQQ R 0.1 1A-O er specified, ie length of peptide Is 9 IHPQPQSQR 0A1-10-mers amino acids, and the end position Each peptide is a portion of SEQ for each peptide is the start Table XXI- I09P1D4v.4 ID NO- 11; each start position is positiongpl .ght- B3501-10-mers _ specified, the length of peptide Is F 1 L - - - - 10 amino acids, and the end _Pos Subseguence Scre Each peptide is a portion of SEQ position for each peptide is the ID NO: 9; each start position is start posItion plus nine. FI .f ±HPQP9SQRR. I specified, the length of pptide Is; ___________________ adds, and the end ________________e Score LPQPQSQRRV 0.020 position for each peptide is the i VSV(RPSQR QSQRRVTF start position plus eight. I SVHT IQ 2 WIHPQPQSQ Po Subsequence 6[ HTRPsQRRV F025 QSRVF -P1qRT 20.00 T F1 IW1IHPQPQS ||0. |0 71 TRPSqRRVTF0[ 3 IHPQPQSQR _|0002 j | QSQ§rVTFHSLP0V03v 158 Table IX-109P1D4v.5 Table XI-109P1D4v.5 Table XV-109P1D4v.5 Al-10-mers A0201-10-mers A1101-10-mers Each peptide Is a portion of SEQ Each peptide is a portion of SEQ Each peptide is a portion of SEQ ID NO' 11; each start position I ID NO:11; each start position is ID NO: 11; each start position is specified, the length of peptide is specified, the length of peptide is specified, the length of peptide is 10 amino acids, and the end 10 amino acids, and the end 10 amino acids, and the end position for each peptide is the position for each peptide is the position for each peptide is the start positionusnne. start position plus nine. stat position plus nine. IPosSub[sequence Scre Subsequence [S Ee [P s -egunce j [ j ...- 8 RPS R.H TRsQRVT 0 SVHTrPSQRR 040 ELILR RVF&_q.0Z 3 FW6 ~TIT95 LfE P:00~o1 2 PVLSVh

T

RPSIL00 TRPSqRRVTF 30 VSVHtRPSQ 10006 8 RPSrRTF0000 ___ ~ ~ ~ ~ ~ ~ 1 I__ -- A______ ~r y .iP~ 9 PSQ(rVTFHL Table XII-109P1D4v.5 TPSRR 115 ~ ~ A3-9-mers ___F~ V~TPQIo-0i 5 VHTRpSQRR E- p e2 0.000 _S~TRS ________ -___ =0_000 Each peptide is aportion of SEQ . _____________.___1 ID NO: 11; each start position is 6 HTRPsQRRVT 0.000 Table X-109P1D4v.5 specified, the length of peptide Is 9 PSQRrVTFHL A0201-9-mers amino acids, and the end position i0.000 Each peptide is a portion of SEQ position plus eight 5 VTRpSQRRV 0.000 ID NO:I11; each start position Is Ps Sb uner specfied, the length of peptide is 9 s T R Subsequence Teore amino acids, and the end position [ LSVHTRPSQR Table XVI-109D4v.5 for each peptide is the start T4 RPSQRRVTF ILO 020 positionplus eight. j -500:6] Each peptide is a portion of SEQ ID Ssu L VHTRPSQRR NO- 11; each start position is ----- 5 HTRPSQ specified, the length of pepfide is 9 SVHTSQ1 ---- amino acids, and the end position for HT5 ffhRPSQR 0.00 each peptide Is the start position plus RPSQRRVTF VSVHTRPSQ eight VSVHTRQ P TRPS i - o Subsequence score I 8 LTRPSQRRVT 7 RPSQRRVTF L I~ ~ ~ 1DO00 v.5SM lIVjL Q RRo - -E 0 0]0 Table XV-1 09PI D4v.5 -6 FL0-V1 IL--.IPVSHTPS .00] I All 01-9-mers-- E1 i 1 1 0.01 !EVHPSQRR Each peptide Is a portion of SEQ P V YSfRPSQ O.M] ID NO'.11; each start position is L 0-010 Table X-109P1D4v.5 specified, the length of peptide is 9 7 SVHTRPSQR A0201-10-mers amino acids, and the end position [ PSQRRV_1HLO.002I for each peptide is the start Each peptideIs a portion of SEQ position VHTRPRR ID NO: 11; each start position Is S ubsequence Score specified, the length of peptide is Table. ]t I-1iI1IID1 1 10 amino acids, and the end SV§l0TrerSQRRs al e P1 position for each peptidelis the VSVO-.RPSQR start position plus nine. - Each peptide is a portion of SEQ @29-1 _jSubsequence 0 RPSQrRFH ID NO: 11; each start position is I pRrVTHL 0.002 specified, the length of peptide is ____________ 10 amino acids, and the end VHTRpSQRRV 1 RrVTFHL position for each peptide is the VH8 006IHTRP1QRRVT 00startposition plus nine. F-771 SVHTrPSQRR - 0.001 Fs I Sbqne ) VPVSvH

T

RS 0.000EVPvHTRPS PSRVTH 0.0 [ VSVHtRPSQR 0LV0-0 pSQRR JLMi L TR~RVF 04 [ 3]PVSVhTRPSQ 00 VTRP SV T S = 1 PVSVMS:Q:] ] F- 7 TR~sQRRVTr 0120 159 Table XVII-109PID4v.5 Table XIX-109P1D4v.5 Each peptide is a portion of SEQ A24-10-mers B7-110-mers ID NO: 11; each start position is Each peptide Is a portion of SEQ Each peptide is a portion of SEQ ID spefied the legth of pep s 9 ID NO: 11; each start position Is NO: 11; each start position Is amino acids, ard the end position specified, the length of peptide is specified, the length of peptide is 10 for each peptide Is the start 10 amino acids, and the end amino adds, and the end position for position for each peptide is the each peptide Is the start position plus ___ _ _S _uenc____e start position plus nine. nine. 0HTPTDSRT Subsequence Pos Sbsequence I SVHTRPTDS [o = PSrRVTF [ 07 TRPqRRVTF 0.003 - VSVHTRPTD 0 L3 VLY SVtRPSQR ----- -- - RPT]. .SVH~rPS R 0 21 TbeX-0P1 D4v.5 VHTRPTDSR1 915_J I[,. -I ___ ___ __ ___ __ VTRSQRV B3501-9-mers

--

pinfI T I Fa peptide sa potion s Table IX-109PID4v.6 specified, the length of peptide is 9 C' terminal-Al-10-mers Table XVIII-109PID4v.5 amino acids, and the end position Each peptide is a portion of SEQ ID L 1B7-9-mers for each peptide Is the start NO: 13; each start position Is Each peptide Is a portion of SEQ position plus eight specified, the length of peptide is 10 ID NO: 11; each start position Is [Pos | Subsequence Score, amino acids, and the end position for specified, the length of peptide is 9 7 RPSQRRVTF each peptide is the start position plus amino acids, and the end position [ H TRRI nine. for each peptide Is the start L HTRPSQRRVPos | SubsequenceI Scorej position plus eight. [ VSVHTRPSQ o[ 4 iSVHTPTDSR 0. 100 Po s ibsqunce! Score 6 RSRRVE.003 VS RTDES_ 0015 = 1 HTRPSQRRV PVSVHTRPS 0.010 VPVSvHTRPT 0.003 7 ~0 RPQRVT 0VHRPQ 0.010 PVShRT 0.000 T L6VHTRPSQR U =.5 ] PSQRRVTFHl0 - L5J VHTRpTDSRT IL._ [IT jLns~~v I fL fl 1 IlfLP . OOII__________ TRPSQRRVT .- 0.015 ... .-..-. Table X-109P1D4v.6 PVSVHTRPS 010 Table XXI-109P1D4v.5 C' terminal-A0201-9-mers VHTRPSQRR B3501-10-mers Each peptide is a portion of SEQ ID =8[- l 0701 l Each peptide is a portion of SEQ ID NO: 13; each start position Is --8_ - H NO: 11; each start position is specified, the length of peptideIs 9 specified, the length of peptide is 10 amino acids, and the end position for Table XIX-109P1D4v.5 amino acids, and the end position for each peptide Is the start position plus B7-10-mers each peptide is the start position plus eight. Each peptide Is a portion of SEQ ID -_nine. Pos Suuence| Score NO: 11; each start position Is =Po S u uen re 0.007 3 specified, the length of peptide is 10 W VPVSVHTRPS 2.000 1 PVSVHTRPT 0.003 amino acids, and the end position for I each peptide is the start position plus PQRrVTFHL ]0.500 5L HTRPTDSRTJ 0.0 nine. RPSQrRVTFH 0.4 2 fl VSVHTRPTD 0.000 Ls JI Subseuence .JIScorel i L H TRPsQ T T.0.300. ~4 VHTRPTDSR I0.000 L e ,jLHTRPsQRRVT 5 ( F7 TRP7qRRVTF q1.500 0.050.____ __________ .7... -. Q6RrVFHL -[ 3 VVRooPSQR 0.50 Table XI-109P1D4v.6 _L__ VPVSvHTRPS Hpj 0Q R 0 termina-A0201-10-mers L7~7. 8 RPSrR7. 4 SVHTrPSQRRF .010j Each peptide Is a portion of SEQ rRR P ID NO: 13; each start position is II IL J[0:7 1 L PVSVh-P [0-0-9. specified, the length of peptide Is L5JI yVHTRpSQRRV 0 .020 __L 10 amino acids, and the end 3] |VSVHtRPSQR 0.010 Table VIII-109P1D4v.6 position for each peptide Is the _ 2 PShTPSQ 8 C' terminal-Al-9-mere start position plus nine.

160 jPos 11 Subsequence Score Table XIV-109PID4v.6 Table XVII-109P1 D4v.6 SVPVSvHTRPT 0.017 C' terminal-A1101-9-mers C' terminal-A24-10-mers 50VHT0pTDSRTEach peptide is a portion of SEQ Each peptide Is a portion of SEQ -- ID NO 13; each start position Is ID NO: 13; each start position is F3 VSVHRPTDS 0.001 specified, the length of peptide is 9 specified, the length of peptide is 4L SVHTrPDS o001 amino acids, and the end position 10 amino acids, and the end ~ for each peptide is the start position for each peptide Is the TL VShTRTDpositionplus eight. start position plus nine.

Pos Subsequence]Subsequence Score Table XII-IO9PID1v.6 I_________ P~uieuclsoe C'terminal-A3-9-mes 1 000 L ? PVSVHTRPT V1[0 Each peptide is a portion of SEQ SVHTrPTDSR ID NO: 13; each start position is Table XV-109P1D4v.6 VTRpTDSRT U .101 specified, the length of peptide is 9 C' terminal-A11-10-mers v RP' I' 0 amino adds, and the end position Each peptide is a portion of SEQ ID for each peptide Is the start NO: 13; each start position is - position plus eight specified, the length of peptide is 10 Table XVIII-109P1D4v.6 Pos S n Score amino acids, and the end position for C' terminal-87-9-mers 5 HTRPTDSRT each peptide is the start position plus Each peptide Is a portion of SEQ I J t I _nine. ID NO: 13; each start position is VHTRPTDSR .006 os Subsequence specified, the length of peptide Is 9 S TRPTDS 0. -0 amino acids, and the end position VSVHTRPTD 0.000 2 P S R T po.l4e00 E for each peptide is the start 1F1 vsvHTRPT FqL 2][ Gst-Lm Pm] O poitonpseight. .1 ~ ~ ~ ~ ~ ~ =o ___[v'1trpsWI p j sequence lScorel rDTable XIII-139P;D4v.6 i Table X-19Dv. [VSV-HTRPTD II92=j i Cte lengt1ofmeps C' terminal249-meDSRT VHTRP TD_.SR Each peptide Is a portion of SEQ 1 N IvVHRTI~o ID NO: 13; each start position Is Table XVI-IO9P1D4v.6 '[ 2 SVTPD iO05 speciie, the length of peptide is IC' termlnal-A24-9-mers I I40[072hS 10 amino acids, and the end Each peptide is a portion of SEQ ~ position for each peptide is the ID NO: 13; each start position Is start position plus nine. specified, the length of peptide is 9, Table XJX-109P1D4v.6 S q S amino acids, and the end position C'terminal-87-10-mers 4 SVHTrPTDSR for each peptide is the start Each peptide is a portion of SEQ ___R 0.600 position plus eight ID NO: 13; each start position is SSVHtRPTDS Subsequence I specified, the length of peptide is 1 IPVS\(hTRPTDIF ! 1 i 10 amino adds, and the end P T 0.00 HRP T .120 position for each peptide is the VPVSvHTRPT SVTRPTDS start position plus nine. j VHTRpTDSRT 01 VSVHTRPTD 0.015_PosJLSubsequence llScore TablePVSV HTRPT 0.01] [ 1 VPVSvHTRPT 2.000 C terminal-A1 01-9-mers j I LVHTRPTDSR iL4 SVHTTsLR 0.075 Each peptide is a portion of SEQ -- --- --.

0 ID NO- 13; each start position is Table XVII-109P1D4v.6 VTp ST 0 specified, the length of peptide Is 9 C' terminalA24-10-mers 2 PVSVhTRPTD 0008 amino acids, and the end position Each peptide is a portion of SEQ for each peptide Is the start ID NO 13; each start position is position plus eight specified, the length of peptide is Table XX-1 09P1 D4v.6 | [Subsequence 10 amino acids, and the end 'termal-B3501-9-mers I 4L7i[ VHTIRPTDSRIf position for each peptide Is the Each peptide is a portion of SEQ start position plus nine. ID NO: 13; each start position is cSVHTRoTDS Su ene specified, the length of peptide is 9 HTRPTDSRT 0.001] aino ads, and the end position .0J000 for.eaV T peptide Is the start ii~~~~ I_ _. =L poiinpuIih 161 [ODS] Subsequene I ] Table VIII-109PID4v.6 W HTRPTDSRT . N'terminal-Al-9-mers TableX-109P1D4v.6 [ SVHTRPTDSj 0.100 Each peptide is a portion of SEQ N' terminal-A0201-9-mers r _3 _ 1_____ 0 ID NO: 13; each start position Is Each peptide is a portion of SEQ [F-2j VSVHTRPTD I specified, the length of peptide is 9 ID NO: 13; each start position is I =1 L nVVHRiP 0 amino acids, and the end position specified, the length of peptide is = LTPDR for each peptide is the start 9 amino acids, and the end - position plus eIght position for each peptide Is the Table XXI-109P1D4v.6 Su corestart position plus eigh. C'terminal-B3501-1ners SDISSVVRV 0.001 = LSuisequenceSre Each peptide is a portion of SEQ SWRVNTTN KLLSGTYI 451 ID NO: 13; each start position Is = WRVNTTNC 0 FNSDISSW .511 specified, the length of peptde is LiL[L MTVGFNSD 10 amino acdds, and the end F4 cDl=.3 position for each peptide is the tLVRVNTTN NTTNCHKC start plus nine. CHKCLLSGT _ 17 TTNCHKCLL 0 297 LPosI I Subsequence llSjcore __ _ _ _S_____2I2V _fij _VPVSvHRPT_ 2.000j Table IX-109P1D4v.6 3 0LSGTYF [ ] VSVHIRPTDS o.500 N' terminal-Al-1(-mers 10 SSRVNTT 4 _ JL VHPTSR 0.010 Each peptide Is a portion of SEQ! FOL NSDISS 0111 VHRpTDSRT ID NO: 13; each start position is'SS F-5iII 000 specified, the length of pepid - III S0.0NT 83p V2JLPShTRPTD 0.001] 10 amino acids, and the end [1W111 RVNTTNCj .056J position for each peptide is the f LVNTTNCHKC g Table Vil09PD4vI sart position pl _ _ _ _ _ _ _ _ _ _ _ _ _ _ _ _ _ _ _ _ _ F [ P o s J [ S u u en I~w S V V R V N r rN 7 0 .0 0 7 [ Each peptide is a portion of SEQ 6 [NSDlS Vj 1 . NS 0 ID NO: 13; each start position is [ KC[LLsGTYIF 0.0[ specified, the length of peptide is 9 L amino adds, and the end FN I Ifj N hKCLLS R125 01 poito - D S Li E57 = NCHKCLLSG 001 for each peptide is the start E111FNDS R 10051 h position plus eight [2 1[~TVGFnSDIqS 1 ILTNCHKCLLS 0_00 Subeence Scr e CLLSgTYFA L r 2 CHKCLLSGT 0.000 NSDISSWR 15.6LNTTNcHK DSRVN LCLLSGT .MTV00NSD 1 VRVNTTNCH 23 LRVNTTNCHK DSvRN 0.200 1ImTvGRNsDis01 .------ NSDISSVVR 0001 E14L 'T 0.20 [SSVVRVNTj 91 HKCLLSGTY0000 F 6-1NTTNCHKCL 0.2 _j IISS KvRVNTT [16 ~0.2 _j N1NCKCSSY1 ~L~VRY=N 110.o151 Table XI-1 09P1 D4v.6 IGFNSDI025 TNCHkCLLSG ., N' terminal-A0201-10-mers L F7 HKCLLSGTY 0i VRVTNCHK 11(1010 Each peptide is a portion of SEQ ID TTNCHKCL .025 RN IK NO: 13; each start position is 0.015 20 CHKCILSGTY specified, the length of peptide is 10 3[ VGFNSDISS 0.013 [ VNTTnCHKCL 0 each peptide is the start position plus 18 TNCHKCLLS J IVGFNsISSVj. nine. F T FNSDiS 0.010 NCHKcLLSGT[ 0.0j . SuIseguence L2 KCLLSGTYl_ 0.0 WRnTTNCH .CLgTFA 1 ,~DISWV J0.010 -NTC LVGF jIV L NCHKCLLS .005 SDISsVNC 4N0.001N 0 E9 EC LS 1 0 j tsy ~ 1J YTNIIq-FNSDISSW |[0.003 HCSTiSWRvNTTNC E LVNN'-NCH-KC J 4 GFNSdlSSw ow-H6 NSDlsSWRV 0.418] 162 Table XI-109P1D4v.6 Table XIl-109PID4v.6 Table XIII-109P1D4v.6 N' terminal-A0201-1 0-mers N' terminal-A3-9-mers N'terminal-A3-10-mers Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ Each peptide Is a portion of SEQ NO: 13; each start position is ID NO: 13; each start position is ID NO: 13; each start position is specified, the length of peptide Is 10 specified, the length of peptide Is 9 specified, the length of peptide is amino acids, and the end position for amino acids, and the end position 10 amino acids, and the end each peptide is the start position plus for each peptide Is the start position for each peptide is the nine. I position plus eight. start position plus nine. Subsequence So Subequence ri Subsequence 16 L NTTNcHKC. 297 [2]iHKCLLSG1Y oj E ]GFNSdlSSW iL0.1 Ei VNTTnCHKCL 0.237 SDISSVVRV 0115 LVNTTnCHKCL 0.001] 9IS S,§VvRVNTT G.190 L FNSDISSV [ 021 HKCUS _.001 ='_ NCHLLsGT 0.1 1_ 9I ISSWRVNT ] SS =rVTTT =0000 LD-ISvVRVNT h Ln1INCHKCLLSG aLko[18 TN6)kCLL SG 0.000 L GFNSdISSW FNSDISSW SDISsVVRVN [ iiTVGFnSDISS I oi~LV.rNTTN f 21 H CUSGTYI _VGFSD03 Table XIV-109P1D4v.6 L ~=6 KLsGTlFVVNTC N' terminal-A1101-9-mers TH kL 0.001 DISSVVRVN F 0 I Each pepide isaportion of SEQ ID E r 7 - __cc__-__-661 EK NO: 13; each start position is TI'N1hKCLLS N0.000] 1 specified, the length of peptide is 9 1271 VVRVnTTNCH 010 CHKCLLSGT M -6.701 amino acids, and the end position for FNSi Reach peptide is the start position plus LNTable XI1-1I09PID4v.6 S enice. Score MTVGfNSDIS ][L N' terminal-A3-10-mers I S - s E a c h p e p tid e s a p o rt so n o fMSE QG F N S D j .0 1 5 _ [J~ ~l~ ___ IIID NO: 13; each start position is IiiiiIMTVGFNDI ]0.=015 = VVNtTNCHK specified, the length of peptide is ~ 3 CLLSGjd|_0012 2IE CHKCI'~!LSGTY if 0:0qj 10 amino acids, and the end [ii7 TTNCHKCLL 0|.0.0 ______________ position for each peptide is the -- b -- - -- - start position plus nine KCLLSGTL 0.0 Table J

-

Subsequence L]4 GFNS N' terminal-A3-9Mers- ______ -. ____ Each peptide is a portion of SEQ L --- C1C. LTIFA _6 16 1 NTTNCHKCL |[0.005 ID NO: 13; each start position is _KCLLsGTYIF 27 [ NSDISSRjO.004 specified, the length of peptide is 9 13 VRVNtTNCHK L 1 11 SVNT 0.003 1 ino acids, and the end position 5 ) 51KLL ] V.0IL012 j for each peptide Is the start ___ ___ ___ 0_030_1__F__ itionplus eight TFNSDIS_ .00__ POS I[ Subseqence I c RVNTtNCHKC o.o2Oj 7I } NCHKCLLSG ] 0.000 C23 LLSGTYF WRVnTTNCH 0.020 FNSDISSW] 0.000 4 L ~RVNTTNCHK ][11 FNSiSSWR1= I SID IS SWvRV IL0.0 IMVGFNSDI 0.203 F 2 TVGFnSDISS 10008 13 VRVNTTNCH F0.000| TTNCHKCLL f00 3 1~ MTVGfNSDIS [ 6I05] [ 2i- HKCLLSGTY 0.000| [ I~7KCLLSGT'i .27 11_ DISSvVRVNT 10005] 3~7 VGF-NSDISS 0_.000 j NSDISSWRTT1NhKCSI TNCHKCLLS .0005 1711.NTTNCHKCLL VGFNsDISSV 01 -10 SSWRVNlTT 0.000 SWRVNTTN 110050ISSVvRVNTT IS 0.000 | S VGFNSDIS 19 NCHKcLLSGT 0.002 I CHKCU-SGT | 0.000 SSSWRVNTT 1 1 CHKCILSGTY 0.001 8ET] DISSWRVN 0.000 163 Table XV-109P1 D4v.6 1 N' terminal-A24..9-mers- I N' terminal-A24-10)-mers N' terniinalA1101-1 0-mere I Each peptide is a portion of Each peptide Is a portion of SEQ Eac pelid Isa orton f TabII EQ I O1 v TahsatI O able sttoitionP1 is NO: 13; each start position is 0 position is specified, the length specified, the length of peptide is specified, the length of peptide is 10 of peptide is9I amino acids, and. 10I amino acids, and the end amino acids, and the end position forl the end position for each position for each peptide Is the each peptide Is the start position plus peptide Is the start position plus satposition plus nine. nine. Ieight.Ps Sb ec cr !7~~Lsubsequenoe ILucorel =no [ s ISVVT j01oo

F

7 '13 T~Hja~o i4 G FNSDISSVL mi[7 ISvRNT 010 V7 RVNIImCHK j~ 0.00 AE L ~L7?IF =9__v~N- jW12 = LKOLLSTTNCH jF626 _1 L9 V T 0.- .. - ____i J5=cLSG l0.120J _ _____ __ HCUS1Y F-fjLF- E -. [li 1VGFnSDISS 110.1001 DE,,7 LN TTWcHKCII 0.10 =_]D~WVIO01 [-6] NSDIsSWRV 0.100 Lii._F S~iSS1 1[. 0 5 L9[s w v' I 010 D [i _][ GFNsDSSv_D 07.100 fW] RVN tN0.C006~i LE! V1r NH CI 011 LJiJ~ D~RvN 0.0211 r 21 1VGFnSDISS 1[l- 1 TNhCHKCLLSj010L I NDSW 02 1=1 SVv1TCf 0. 00 3 [ff]GFINSP.SS! 0.100 -. ___ .0 55-1] 1 Fnrm 0 o _12jl F 3]1 VGFNsDISSV =.000] [F SiSS .1 NCHcLS j 7I~o ~ IKLS1 Table XVIII-1O9P1D4v.6 [ILs WR _Ii ~~CHcLGTL90~L~ N'rmial-7-9-mers; f?9iLP KCILSGT I .01L1~osv~I_.1 Each peptide is a portion of SEQi -- ~,HKCSGYI ~ ..J..r19.I specified, the length of peptide Is 5.655_ I[IRVTTNCH .II 0 9 amino acids, and the end F- L DISSvRVNT 0~.o0o0 1 position for each peptide Is the [1071 SSWrVNTTNW -- Fi ~sqecf L~~flI ISS VvV1 0.000 Each peptide is a portion of SEQl =62I RNUC.000 SDI 0. ID NO: 13; each start position is 1 16 qL NTTNC L. IJ40001 [1] SOI~~sWRVN 0j00j specified, the length of peptide is L1.l!!~i~~ _________________________________10 amino adds, and teend 17 L * n _L1 0 r -- position for each peptide is the []jj!rvGnsiI0.4o61 TableXVI-I9PID~.6 Istart position plus nine. J N' termlnal-A24-9-mers 2= L________ 04_7) Each peptide Is a portion of I -J~gec~~oe LIFNESDSSW 0.0 SEQ ID NO: 13; each start F 221 I F_6L_7TYIE [I]ISRVTIO1so position Is specified, the length F._1 YNtNCKqLL_[P27L ~ SVVN~ ~a~ of peptide Is 9 amino acids, and JF_71 P~ T' .0 e end position for each i m 14.000 4 I sviFvrS r V ;1.100o! peptide Is the start position plus 4 ________ 1V FSI 10l0 -eight IIhLV--1 0~I 15- FJ VNFMrPcH cJ0.00Iq Po[s jubsuence Scoe ! L _. 1 ~q ~ .-9 171J SSTrNTTJIO210 IL1 RVN!~TTNCHK 1 0050 I 3CLSf6I .000 -~L!! i.-GNSIS 000 11 SV~v4TTC 0.50 ri~[_TNHKCLS10.0201 KCFLLSGYI FLAI J!i~5~ L Lp~V .2 MTV _GFNSDI =7L361-5Sk00 164 Table XVIII-109P1D4v.6 Table XIX-1 09P1 D4v.6 Each peptide is a portion of SEQ N' terminal-87-9-mers N' terminal-87-10-mers ID NO: 13; each start position is Each peptide Is a portion of SEQ Each peptide is a portion of SEQ specified, the length of peptide Is ID NO: 13; each start position Is ID NO: 13; each start position is 10 amino acids, and the end specified, the length of peptide is specified, the length of peptide is position for each peptide Is the 9 amino acids, and the end 10 amino acids, and the end - start position Pus nine. _ position for each peptide Is the position for each peptide Is the Subsequence start position plus eight. start position plusnine. KCL sGT0lF PO j Subsequence Pos [ uIbsqn ]1ce_J NNcrKCe CiLL STF 0.020 VRVtTNCHK VNTTnCHKCL J[VGFNSDISS 0.020 PH - f0[ KCLT 0.00 CHKS§!11-1 T Table XX-109P1D4v.6 FI6IEach NCK SsaGportionof SEQ F 1[ SSWrVNTTN 50o. o D D I y- Lsi ID NO: 13; each start position is L6 -NSDisWRV HKCLLSGTY 0.002 specified, the length of peptide is 9 [7]L VGFNsDISSV 0.300 VVT .001 amino acids, and the end position -- 1- LRV CHKC for each peptide is the start L -- I.~ position plus eight 1 L CHKcLLSGT S P1D4v.6 s nce reTVGFnSDISS N 3tria-7-1 0-mers _=Pis ________ I________.__=2 Each peptide Is a portion of SEQ- NTNCHKCL_ 1 ID NO: 13; each start position Is LLSGT____I__lF .00 l MTVGfNSDIS [oioo specified, the length of peptide is L17 TTNCHKCLL |0 L 2-IL CLLSgTYIFA =0.100 10 amino acids, and the end I - FE1-L L~'K position for each peptide Is the I KC LSG I |10.800 2L I TNChKCLLS IIql start position plus nine. F9i ISSWRVT_|0.5001 F SVVRvNTTNC 0 100 [Pos Subsequence 1 0 [SSWRNTTj0.500 HKCSGTYI 0.040 (16]1 NTTNcHKCLL MTVGFNSDI |00 [ WRVnTTNCH o30 5 VTTnCHKCLJ5 00 FI SSW1j[0.400 L2 GFNSdISSW 0Io.020 51 SWRvNTNC L W T I50 F1 2 L-7 0.l0 IW 20R L _RVNNHKC_ KL: T8 YI TNCHkCLLSG 0 W12 VVRVnTTNCH = 1 TVGFNSDIS 0.100 SDISsVVRVN 010 L3 1LVGFNsDISV 8200[ DSSWRVN 0100 VRVNtTNCHK 0 00I] [87 DISSvVRVNT L TNHK10.150 =8L CLLS 0.100 19[NCHKcLLSGT V01 1= LYNTTNCHKC Table VIII-109PID4v.7 _SvN :_ VGFNSDISS d 10.100N' terminal-A1-9-mers [iI1 ISSWRNE 0 01001 Li1=1 GN~J~ 0.100 Each peptide Is a portion of SEQ [23J[CLLSgYFA I 0.100 2=0 L SRVNTTN L010 ID NO: 15; each start position is [ TVGFnSDISS 0.1[ CHKCLLSGT .0 specified, the length of peptide Is 9 6 _NS_:sSWRV=4 0_0FNSDISSV_ 030 amino acids, and the end position 2 LSCLSGTY 91 7 ]SDSSV for each peptide Is the start GFNSdISSW 104 RVNTTNCHK 020 P plsequence |eIF IF KCLLsGTY! F[. 020 {T] NSDISSVVR Fj0.015 C 11 _SLSPLLLVS [0.500 | SSVrVN'lTN [0.026jIJ NCHKLLSG I[.010 07SLSPLLL0075] i MTVGfNSDIS V0.020RVNTTNCH D7301 [ssLSTPLLL 0 T [NChKCLLS ~ I TNtkCLLG 10.1 q Table XXI-109P1D4v.6 i - _ SPLLVSV j 0.0 -FNSDISSWR N'termInal-83501-1 0-mers -l SSSSLSPLL_______ ] 7T SDISsVRVN 0.002 PLLLVSWR 0.020 SHCILSG1 LLLVSWIRV 0.920 1 165 Table VII-109P1D4v.7 Table IX-109P1D4v.7 Each peptide is a portion of SEQ N' terminai-A1-9-mers N' terminal-A1-10-mers ID NO: 15; each start position is Each peptide is a portion of SEQ Each peptide is a portion of SEQ ID specific a ngth of pepd is ID NO- 15; each start position is NO: 15; each start position Is position for each peptide Is the specified, the length of peptide is 9 specified, the length of peptide is 10 s p ositionf s ie. amino acids, and the end position amino acids, and the end position for jfl plu. nine. _ for each peptide is the start each peptide is the start position plus _ Pos Lubseq uence Scor position plus eight. _.nine. -L .. SLSPILLVSV 1599701 L ubseg [ ubsequence ]FUsSSSSL LLSW VN -EL VFiSS PLLLvSWRV [1J sSSSLSPL[ o15 ] FRVGIUISS L !9 ~VT vVR I 266 1 VLN PL20R LVSV RVNT 550 ___LLVW GFiSSSSS 0.001 [il SSSsPLLLV _lSSSSL MFR[W ~ gFUI o~ L SULsVW 0 2 F-LISSSSS 1- lSSsSLSPL 0.545 T LISSSSSL 0.010 TableX-109PID4v.7 1 1 S 0 =9 0ISSSSSLSP ~SSSN'stermsnal-A0201sLersL EK]F-G----:] ---j Each peptide is a portion of SEQ I i1[ 0-088 VGFUSSS[ .003 ID NO: 15; each start position is LLLVsWRVN 2 T]L1LFRVGFLllS 0.003 specified, the length of peptide is 9 7= UISsSSSLS [ .017 6PL 0:0_3 amino acids, and the end position 3 RGlSS 0.015 [7]G uss I for each peptide Is the start ;_____T]___ GFUSSSS 101 position plus eight. 8 IISSsSSLSP 0.003j .MFRVGFUI Lm eJE GFiSS I~ii RY.FYL[ ~oo]iP~l~s-e-uencie1 re D:-G ______ _ [F 1 VSWRV 006209, IfSSLLLVS 0. Table IX-109P1D4v.7 S 40.001 N'termina--l-mers ] ]LISSL__I93 [21][ VSrV T J[0.0 Each peptiSe is a portion of SEQ ID =3 SSLSPLLLV_6 D:12_GFUISSSS[-090 NO: 15; each start position is 1 5 L 17j515 SPLUVSVVRj =0.000 specified, the length of peptide is 10 1 S6 _LLLVSW 2 [ __FRVGfllSS 0000 amino acids, and the end position for r. - F~FLI Ir...-___ each peptide is the start position plus LVSWRV NTs.y mw MFRVgFUIS 0.00 nine. FUISSSSS L 343 FoiSubsequence j SSS1S0 SLSPL Table XlI-109P1D4v.7 SLSPLLVSV NVSWRVN N terminal-A3-9-mers I-4 ~L F SSSLSPL 0[19 Each peptide isa portion of SEQ 1=2 _____ ____________f ___L___S-S-L17E ID NO: 15; each start position Is 1=1 LSSSSPLu _ 0.075 1 12-I SSSLSPLLL 0.139 specified, the length of peptide is 9 SLSpLLVS[1 LSP LVSamino acids, and the end position 1=3 KOO 14 L-LS-PU V S E. 07=0for each peptide is the start F 716-[SPWVSWR U.V050W 19 L LVS)RVN 0.024 WRVN position plus eight. 000_SSSSsLSP L9 =LL 8 lSPSSLS C Subsequence score [uLLVSvVRT RVGFIS PLLLVSW2R 30.9001 1 T TLSPULVSW 0 0015] I ) YGFUISSS ii. .007 fLLLSyWy 00w VSWrVNTTN 005 MFRVGFI SLSPLLLVS 9IJ iSSSsSLSPL PLLLVSWR ISSSSSL 0.00 _ F~lsSSSSLi GFU I]..9 ISSS .'k ~ f6[ FUISSSSS 18 LL LysWRVN 1 010 FRVGFUIS LN 20 LVSWRVNT 0.015 271 YLVSVvRVNTT 0 1 0 0 ISSSSSLSP [ LLVSWRVN jfo93! RVGFIIISSS _._1_.. RVGFLIISS [ 0 ITaSsSSe N m I-10201-13] SPLLLVSW 007 N 'tSm isS S L S P- l q S S L S P L L L 166 Table Xl-109P1D4v.7 Table XIII-109P1D4v.7 Each peptide is a portion of SEQ N temiinal-A3-9-mers N' terminal-A3-10-mers ID NO: 15; each start position is Each peptide is a portion of SEQ Each peptide Is a portion of SEQ ID specified, the length of peptide is ID NO: 15; each start position is NO: 15; each start position is 10 amino acids, and the end specified, the length of peptide Is 9 specified, the length of pepdde is 10 position for each peptide is the amino acids, and the end position amino acids, and the end position for start position plus nine. for each peptide is the start each peptide Is the start position plus Pos Subsequence Score - position plus eight. I _ nine. _ 'I11 jSPUVVR 0 .0-6 0 P [S ue_ _SubseguenceFlsSSSSL .O6 FI fsssLsPLLL FRVGfUISS i90j 0 3 RVGFilSSS 0.006j SSSSSLSPL 1 VSWrVNTTN 4 L LSPLLVSV .04 -IISSSSSL 001 [N' te iSSSSS L VSvRVNTT 0011 MF VG U - --- 5 - -- §L - -- 1F S E SSSSPLL 03 Table XIV-1 09P1 D4v.7 T L V V V R N T TN ' term in alA 110- 9 - e P8_ ! L P W R V LPLL VS Each peptide Is a portion of SEQ 1 U7 IS SS0L _______IDNO,_15 each start poson Is [=L~ 0.001 FRVF-l specified, the length of peptide Is 9 LLVSvVRVNT 1 VGFUIISSS- [oad0 amino acids, and the end position SS PLLL for each peptide Is the start _______ 111____PE 0.0 7 L( GFLISSSS ]0000 position plus eight. iFFRygFULIIS - e- - 1 17 PLLLVSWR0.012e L1 SSSLSPLL i.000 N'trminal-A3-10-mers jiL ~ 1 k % - ~iJ L ~ L 38 L LVWRV S 0. 1 .SU L 0.000 _ Each peptide Is a portion of SEQ ID LLLVSWRV LL NO: 15; each start position is UISSS 0 E LLLVsWRVN 1 0.00 specified, the length of peptide is 10 M0=04RVGFUI [000 SLp L amino acids, and the end position for 003= each peptide is the start position plus PLLLVSW 2 FRVGfLISS 0.000 nine. 20 LVSWRVN6:00VGFLlSS Ps Sube S GFISSSS 0.001 21 VSWrVNTTN l S FLIIsSSSSL I 1 SLSPLLLVS .001 14 SLSPILLVSV 050J SSPL-L V Table XV-109P1 D4v.7 _19 _LVVRT 2 T FLl0SSSSS

.

N A24-9-mers 16SPLUVSVVR 8IISSSSSLS Each peptide Is aportionof SEQ =_________1 ID NO: 15; each start position is 1 P vSWRV _90 2 1 SSPLLL specified, the length of peptide is 9 0 ILVVvRVNTT 030 0 SSSSSLSPLamino acids, and the end position 18 L WS o0 for each peptide is the start 3~~~~~~ LfvFIss[~pj - _ [~ position plus eight. 3_ LVGFIlssSI LI LSPLLLVSV [ [0Ii subsequence Score - 7_ LISsSSSLS] 006 [ FRVGFLis UFSSS oss SSSSISPLLL 0.6 LLVSWRVN I0MFRVGFU 0 12 [SSSLsPLLLV 0.005 7 ISSSSSLSP SSSSLSPLL L7 -ISS~sSLSP 41O VS SSRVNTT _1SSSLPL 8 I SSSSLSP2_LLT S .003S1SSSL 10 SSlsLPLLGFUISSSSL100 TUILSPULVSW 0 Table XV-109P1D4v.7 R - 0'001- N'terminal-All110mr F1 RV FLIS j0240q 13 SSLSpLLLVS . L- - [n19__A -- _ni s - LLVSWRVN 0.20 _0__ MFRV 15J LSPLLLVSV 0.180 4 _VG.F S SPLLLVSW 0.180 16 7 Table XVI-109P1 D4v.7 ITable XVII-109P1 D4v.7 Each peptide is a portion of SEQ N' terminal-A24-9-mers N' terminal-A24-1 0-mers JID NO: 15; each start position is Each peptide is a portion of SEQ Eahppiei oto fSQ-specified, the length of peptide is 1I) NO: 15; each start position Is I)N1;Each sa portion SE 10 amino acids, arnd the end specified, the length of peptide Is 9 specified, the length of epide Iss~ posifieahpeptd ris the amino adds, and the end position 10 amino acids, and the endStrpoionpsnne for each peptide Is the start position for each peptide is the Ps _ubseqyene~~ position plus. eight lsnn.L~7LISsLP 40~ ~~~j~~~~~os 1 ubn~n Susqene[ooreos~SSSSLL 400 I[1 VY r~l O IK 1 IR~ US _~.1 f O S SSSS ISPLL f18 1. 11~yj0.1501 _PLLLvSMVj 10.0151 _____ 6___ -0SLPjqooj j LS~V~ 0.5001 tF~iLsss I.150 J ___________ j7J S~PLV~03~ TF I SLP L vI 0.1-144" Table XVlll-109P1D4v.7 t21[ _ LsPULVS F[.30 0 204 J EachV T 0.ptide is N' po~7rtio of QF-16 SPWVSVVRI .2001 LiiiyL~I.1 4=0 ID NO: 15; each start position is = ___ P YVJ=.0 [iIL± ! 11 0.100] specified, the length of peptide is 9 L-]AVvRVTIoio [=2 yui L~ amino adds, and the end position ljVFISSIomuoj ~~- ~ol fo each Peptide is the start - _ _ ~~~~psto plus_ eight IILLsV N11 1=7i PLLLVSW [------ = D] Suseuec -L. Lxsv-)o!= 2 Each peptide Is a portion of SEQ 21]I SSSLSP4LL iroit =] -211] Ls! -jj[0.020J ID NO: 15; each start position is - 7f LlSSSL~iA~ [iL. IJ.Vy~.J000 specfed, the length of peptide Is 4.0 107 1 SS0.020{~] 10 amino acids, and the end E TS -LP -EK ['7___F_________0_2 position for each peptide is the [-k.ii YTDFY1LJ 0]0 l~j][ IISSsSSLSP D501 strtpostion plus nine. - i.]MRGLIj .~ I2JFVfiS_] O [ j]FLIIsSSSSL 6.000' = LJJLSPLLLVSV 10.200 [IZiSssSPL1 4.8001 fi]L': y \C JIRV 0 Table X-t1~ . 11L SSSPL=J 4.0006-61N1 0.lOl0- N'teminal-830-9mr LSSSSPL [4.000J [W[VFHS.LO0] Each peptide is a portion of SEQ DD L LGF 1 -s. Eo.iooI ID NO: 15; each start position is 1-J-__FOR ELFij[s:P:La yLy o0 specified, the length of peptide is 9 []j]MFRgFUS l.50J L~hlL~sv~v~r0201 amino adds, and the end position for each peptide Is the start - ~ - -. .. ~ .- -position pluselIgh 189J LLLVsVV=RVNT 102101 7F1 _SSS2S21011 1.1isL K[I =1J!.JLSWPUVS= 10.101 E17]L FRVISJIOO2 ... t~L-~.J 0 1 -J L7L'Lsmv ]Fq7?J TabL-Is§SxiPn q-010Y L~ T5- 20 ii 7V~RVT 10' =5- ~ -- * - 3jSSSLL 00q FLVS sIwvvyjjoIN FL-5-i R1FLS qFIS 1.0. 7(LLLVSW 14.00 168 Table XX-109P1D4v.7 Table XXI-109P1D4v.7 Table X-109P1D4v.8 N' terminal-B3501-9-mers N' terminal-B3501-10-mers A0201-9-mers Each peptide is a portion of SEQ Each peptide Is a portion of SEQ Each peptide is a portion of SEQ ID NO: 15; each start position Is ID NO: 15; each start position Is ID NO: 17; each start position is specified, the length of peptide Is 9 specified, the length of peptide Is specified, the length of peptide Is 9 amino acids, and the end position . 10 amino acids, and the end amino acids, and the end position for each peptide is the start position for each peptide is the for each peptide is the start position plus eight start position plus nine.._ I -_,__ position plus eight S Subsequent Subsequence I Subsequence [T MFRVGFI FRVGfLlISS 2 FIPGLKKEI 6.599 F1971 LLVSVVRVN I =0100 F llsSSLSP 8 KEIVQPV 433 SLSPLLLVS 0 5ILGFLliSSS 0Io1p L PGLKKEITVlP-3zJ -20 SVVRVNT IPGLKKEIT 0.017 871i Lillss-Ls. 0o oo Table Vill-109P1D4v.8 K. K05I F6--'lFUIISSSSS -F5-0 - A1-9-mers GLKLV =4 i~ i 0.0 ILj _ _ _ETQ7 O. 4 GFLlSSS 00Each peptide is a portion of SEQ LK 0 IDNO 7;echstr pstinis 1 - [-iE] =FPLKEI0.009] F9 ISSSSLSP_ 0.05q specified, the length of peptide Is 9 LKKEITVQP ] EFGFUISSSS L.0 amino acids, and the end position _ for each peptide Is the aTable X-109P1D4v.8 F-2 ]LFLY 0.~10i - position plus eight Tale01-10- r 17 PLLLVSV 00 Pc e Each peptide Is a portion of SEQ - -- -I0TVQPT 04 ID NO: 17; each start position is Table -109PD4v.7 FiPGLKKE [0.1 - specified, the length of peptide Is N' terminal-83501-10-mers --- _10 amino acids, and the end Each peptide is a portion of SEQ IPGLKKEIT position for each peptide Is the ID NO: 15; each start position Is KiLWQ11P start position plus nine. specified, the length of peptide is TFGLKEl Subsequence ire 10 amino acids, and the end position for each peptide Is the L PGLKKE_=TV EI FPGIKKEIT J.947 start position plus nine. GLKKEITVQ ff000 [4 IPGLkKETV 110.7721 [ SubeuenceLKKITVQP K KltVQPTV_ . [9]I ISSSsSLSPL _.00 [2][ TFIPgLKKEI El §I Lii s~~SSPLLL 5.o9 Table IX-109P1D4v.8 1L KKVQPT l 0 SSSSsLSPLL 5 A1-10-mers F STFlpGKKE LsPU Each peptide Is aponofSEQ [I] GLKKeTVQPjI05iI ___________ ID NO: 17; each start position is___ _____ F lsSSSSL specified, the length of peptide Is KEITvQPTVE 0 [wSSSLsPLLLV 10 10 amino adids, and the end [ -PGLkEITVQO =21 VSV~rVNTN position for each peptide Is the_0 VSVMrVNTN start position plus nine. j SSLLLVS Pos |5-: Ssuc|Table XII-109PID4v.8 ~F"l =osVS[.50 I[ Susqence[ e -9m =67 SPLLIVSWVR 110.2001 F--- ______I I.9 1 139m FPL UVV §LLKK... l It A7 VQPTV |[ 0091 Each peptide Is a portion of SEQ i S P4ILLVS 10.20PGLkKEIT | 0I ID NO: 17; each start position is RVGFIllSSS FIPGIKKEIT 0 0 specified, the length of peptide is 9 II _1~ LLLV RVNJ0 100 TFIPgLKE I amino adds, and the end position _________________ 0.10 IFT1 __________ 0.051 for each peptideIs the start 1 L LV vVRVNTSTFIpGLKKE position plus eight S LVSVvR 0 F71- L(KETVQPT |O6 Pos Subsequence S[ore 0VGFU0ISSSS 1KEiTvQPTVE 0000 [ G LEITVQ [l.90 LlSsSSSL I1PGLKkEITVQ [0 LIPGL[l 04 RVgFLS_ 0 61 GLKKeiTVQP 0.000 8 1 KEITVQPTV F0.04 =PLLLvSVRV 0.0201 [_T)IGLKKET _ 0_0_ 169 Table XIl-109P1D4v.8 -- Table XViI-109P1 D4v.8 A3-9-mers Table XV-109P1D4v.8 A24-10-mers Each peptide is a portion of SEQ L A1101-10-mers Each peptide is a portion of ID NO: 17; each start position is Each peptide is a portion of SEQ SEQ ID NO: 17; each start specified, the length of peptide Is 9 ID NO: 17; each start position is position is specified, the length amino acids, and the end position specified, the length of peptide Is of peptide is 10 amino acids, for each peptide is the start 10 amino acids, and the end and the end position for each position plus eight position for each peptide is the peptide is the start position plus [SSubsequence *[ start poiplus nine. nine. j [7) KKEITVQPT Pose Subseqeneq S[ubsScore F___4 05700 _Errl- O004PGUKnvITo1oo 1= IF PGLKKEITV [4 EG IP KEITV IPGLE _ 1 6 _KKpltVJj [ i -rv]T 0.014 = TFIPGLKKE : =oo6 GL KKe:lTVQP F-o - LKK7iTVQPT 1 TFl pGLKKE=0 LKelVQ RTableXllf91D4v.8i8 KKEltVQPTV R [I STFlpGLKKE A3-10-mers 3_1 FIPGIKKE0. i v 1Q I Ech III1OP1Dv.8 ~ .Z..4L EI~QPTE 0 000 EL:IIKETvQ PYEL.0031 Each peptide is a portion of SEQ _ KEITvQPTVE F _[ PGLKkEIT VQF0002 1 ID NO: 17; each start position is 7 ~~ specified, the length of peptide is 7 LE__TV__QPT_ = - 10 amino acids, and the end [ 5 _PGLKkEITVQ Table XVilI-109P1D4v.8 position for each peptide is the B7-9-mers start position plus nine. Table XVI-109P1 D4v.8 Each peptide is a portion of SEQ Subsequence A24-9-mers _ ID NO: 17; each start position is E -- i specified, the length of peptide Is __LK_elTVQP Each peptide is a portion of SEQ 9 amino acids, and the end = 1~...i FIPGIKKEIT 1 ID NO: 17; each start position is position for each peptide is the 1 I iPG .2654j specifi, e the length of peptide Is start position plus eight. LLI[ TF~pG(KE ~9 amino acids, and the endre ST.0pGLKKE position for each peptide is the [ Po s Score IEltVQP 0 1 start position plus eight _ LIPGLKKET _.000 I [i FIPg LK 0.S u Po bsequence FI PGLKl 0] .40 LKKiTVQPT IPGLKKET 1.98-A0- KETQPV 0.2 L 1 KEITvQPTVE IPGLKKEIT 0.100 PGLKKEITV 0.020 1 PGL~kETVQE1TFIP V 0.09 IQ 0.010_ - - KEITVQPTV 00421 L KKEITVQPT 0.003 Table XIV-109P1D4v.8 KKETVQPT 0.036 L KEi 0.00_ Al 101-9-mers 4 1 PGLKKEITV 0.0151 I TFIPGLKKE 0.001 Each peptide is a portion of SEQ 5 GLKKEITVQ [.010 ID NO: 17; each start position LKKEVQP 0.002 Table XX-109P1D4v.8 specified, the length of peplide is 9 I B-0mr___ amino acids, and the end position for each peptide is the start Table XVi-109P1 D4v.8 Each peptide is a portion of SEQ position plus eight A24-1-mers ID NO: 17; each start position is specified, the length of peptide is Pos SubsequencOScore; Each peptide is a portion of 10 amino acids, and the end 8 [ KEIQPTV 0.3 SEQ ID NO: 17; each start position for each peptide is the -oF I stion Is specified, the length start position plus nine. ____ _ -. of peptide is10 amino acids, 5__ L GLKKEITVQ 0o.00_1 Iand the end position for each .. Sbseque scoe 3 IPGLKKEIT 0.00 peptide is the start position plus IPGLkKElW 4.000 1_ . Ti KE 0 00 - -..n ne. 3 F i FIPGIKKEIT .10.IO5 4L f.S'P i~ i ~ PKK0 -_TFJ__gLKK ___ 7L~ i KKEITVQPT 2 i.gLKKEITVQPT 0.010 L_. ULElQP ' FIPGIKKEIT ST1GKKE_ 170 Table XIX-1 09P1 D4v.8 Each peptide is a portion of SEQ Each peptide is a portion of SEQ B37-10-mers ID NO: 17; each start position is ID NO: 17; each start position is Each peptide is a portion of SEQ specified, the length of peptide Is specified, the length of peptide is ID NO: 17; each start position Is 9 amino acids, and the end 10 amino acids, and the end specified, the length of peptide is position for each peptide Is the position for each peptide Is the 10 amino acids, and the end - start position plus eight. j start position plus nine. position for each peptide is the I__Pos ScoLeSubseuee i Scor strposition!lu nne. 3os ' PL Subsequence 5e 00FPGLKKEI400 -- IPGwL V 4 L[IF]IG2KKe]TVQPJ 0 GK TQ .0 -- FIPGIKKEIT O0 F[8l1 KKEItVQPTV KETQPTV0.040 o LKKEITVQPT i9 " l(9 IlK-EITvQPTVE 11.001 ] LPC LKK<E T 70020 TFI L 1 5 PGLkEITVQ 0.001= |-[VQP 0 G PLl 0].03 [ ~ ~ ~ E KETQT8 KlVPTV ]0.0121 Table XX-109P1 D4v.8 GI O D STFIpGLKKE B519-mers 9 KKEIT=9 vQP 02 Table XM-109 L8 PGLKkEITVQ 0.002 B3501-10-mers 171 Tables XXII - XLIX' Table XXIl -i09P1D4v.1 Table XXI -109PID4v.1 Table XXII -109PID4v.1 I A1-9-mers A1-9-mers A1-9-mers Each peptide is a Each peptide is a Each peptide is a portion of SEQ ID NO: portion of SEQ ID NO: portion of SEQ ID NO: 3; each start position Is 3; each start position is 3; each start position is specified, the length of specified, the length of specified, the length of peptide is 9 amino peptide is 9 amino peptide is 9 amino acids, and the end acids, and the end acids, and the end position for each position for each position for each peptide is the start peptde is the start peptide is the start position plus eight position plus eight. position plus eight [ I [ - I 911 |LEEQTMKY 27 [1 HIRPVGQV 1 317 |REETPNBKL|1 5 TMQFKLVY [ MEENVLIGD 319 |EIPNHKkLV|9 570|FHN Y EEDTGEIFT R411 VESNQFLLE 14 1807| TSDYVKILV 90R RDREKLCA 514 SLDCRTQML F20 1HSGAQENY 109 EYEVAILPD 15 AKDNGVEPL 1418) LETAAYLDY 21 1321 ||NDNAPLFP 516 572 HliEYNFXVP j 4951SPNAKINY 1163 |ADPDVGIN 14612 EDDFTDS [594 |1VIDPDYSDN 21401 |DHEIPFRLR 1644 KAEDGGEVS 1 |SDPYSSD 21 5 EKEDKYL8FT 6] DKPVFVP 364 VDTVVLSE 2631 FF6REKQSY 1SYELVLEST 37011 L2ENlPLNT 738 KCDVTDLGL 720 TEDLFAIDQ 14 1674 ||PPSNCSY 797 NIEIAD1SS QEDSLFSV 1_ [7 IEAPIPN-9i 802 DVSSPTSDY 16LINELVR 1 [1681 VINGVNY 1 97 DSDGNRTL 851NSEWA'NP [3511 NyPSID!RY 6 TDVPL1RI 1TLLPQLE |1 741 | VIDLGL6RV 100 IERDEHCFY PLDNTFAC| 9311 DSPDLARHY LEDEIFLV 81CSSSSQPY LREEK-Y Table XXIII 109P1D4v.1 P816 19EF _ELLETAY[i A0201-9-mers 4ESAINKY Each peptide I a portion 5__ [1 H of SEQ ID NO: 3; each 3291 DGGLMPA 424 YESTEY 5 start position is VIDVNDVP4 specified, the length of __345 _____ __428 ___ peptide Is 9 amino acids, 991 VSDCGYEVT ITfDEDY [ and the end position for 221 VDGGFEQR [EKQESYIFY 5 each peptide is the start VTDTNDHP 645 ADGGRSR [5 position plus eight [251 EIEEVIP 688 SINPGTVF AIDA~gEN _GMNENRY114 |ILPDE!FRL (273 I IAIFNF17051TMAYY1 16 FLTAL1 354 SIDIRYVN 17PYSVSDDGY 416 |LLETL V3851 DKDAHN KIGDVPLIR 43 LKDLLSL 399 FDHEIEFR |7 148 IEENSAINS 333 GHL V 52LDREKEQKY 211 39TVKGLJ<KL 26 (567 SEVFTHNEY| 111278|1 IENAK1HF 14 4 LIGDLKDL [21 (727 DQETGN!TL [17 IEPDE NIARRLFHL_| 99KPDSPDLAR|[ 4 1 SLDCRIGML|9 172 Table X(Ill 109P1D4v.1 Table XXIII 109P1D4v.1 Table )(Il 109P1D4v.1 A0201-9-mers A0201-9-mers A0201-9-mers Each peptide is a portion Each peptide is a portion Each peptide is a portion of SEQ ID NO: 3; each of SEQ ID NO: 3; each of SEQ ID NO: 3; each start position is start position is start position Is specified, the length of specified, the length of specified, the length of peptide Is 9 amino acids, peptide is 9 amino acids, peptide Is 9 amino acids, and the end position for and the end position for and the end position for each peptide Is the start each peptide is the start each peptide is the start position plus eight. position plus eight. position plus eight. 2817 AVAGT4TVV |2 GVPPLTSNV 369 VLSENIPLNF3691 880 NLLLNEVTI 24 550 |LTSNVIVFV 2381 ALITDKD 18 [64I KLVYKIGDV 656 SAKVTINV 403 EIPFRLRPV 231| STAILVSV 23 658 |KVTINVDV 480 SPGQITKV ] 307| GUTIIEPL j715 VGGNIRDL 49 GPNAKNYL 375| PLNTK!AU | AIDQEIGN [ LDENQDFT 539[ | TLAKD.NGV 23|7 TNATLINEL 2067 TIDSQIGVI ~ [745 GLHRVLVKA 23 781| LINElRKS 2 693| TVVFQIAV 18 810 YVKILyAAV 826 VIFITAV 2733| ITLMECDV 8 813 |ILVAAVAGT 23 [ | GTYIFAVLL 19734 |TLMEKQDVT ~ 38 | VLIGDLLKD fJ12 |VLLACWVFH 19748 |RVLVKANDL j] 741 |VTDLGLHRV 22 | GAQEKWIYTI [Ti77GQPDSL~FSV I~ 816 AVAGIITV 135 |NAPLFPATV LFSVVVNL 9 IFAV ACV 2162 |AVDPVGI 178 TLINELVRK 76 RIEEDIGE 21 303| NATTGLITI 1814 LVAAVAGTI KIRFLIEDI 326 LVLASDGGL 822 ITVV FI 1 SAINSKYTL 25377 |NTKALTV 5 PLNSKjHI 301 HLNATIGLI 438 |5AADAGPPL 8 SKHHIQEL 1DIRYNPV 21 503| YLGPAPP 9 SVSDCYPV 360| IVNPVDTV 1542 AKDNGPPL Y19 FAVLLACH 536| YLFTLAK |8.PRHGIVGL 1LTAMQFKL 17 7431 DLGLHEVLV 216| FTIDSQTGV GARIDEEKL 17 820 GTITVVVI 818 VAGTIVVV 143 VINISIPEN 17 8251VVIFITAV 881 LLLNFVTIE 156 SKYTLEAAV 17 999 |1 V 903 | VTLDLEIDL 9165 DPDVGINGV 50D| SLIPNFSLT 914 QTMGKYN 1179 IKSQNIFGL 7 1271 FUED!NDN 3 LLSGTlFA 256| VSIPENAPV 234| ILQVSyTDT 4 LSGTYlFAV 18 0 TPNHK 7L 27 QLH-ATOADI 213 LLACVVFH-S 18327 VLASDSGLM ~ 298 RLFHL9A8T 51 3PNK9LTT VVLSENIPL 1 3341 LMPARAMVL 0KLCAGIPRD KIAUTVTD 337 |ARAMVLVNV 2 120 FRLVKIRFL 18 482| GQLTIVSA [40 MVLVNVTDV 20 121 RLVKIBFU | 493 ADSGPNAKI 347 |1DVNDNMPSI 201 VV18 [6HGTVGk1V[ 359 YVNPNDT ADIGENAKI | 685 VLPSTPGT1 1428 STKEYIKL 20 283 KIHFSESNL 16 LFSVVN_ 173 Table XXIII 109PID4v.1 Table XXIII I09P1D4v.1 Table XXIII 109P1D4v.1 A0201-9-mers A0201-9-mers A0201-9-mers Each peptide Is a portion Each peptide is a portion Each peptide is a portion of SEQ ID NO- 3; each of SEQ ID NO: 3; each of SEQ ID NO: 3; each start position is start position is start position is specified, the length of specified, the length of specified, the length of peptide is 9 amino acids, peptide Is 9 amino acids, peptide Is 9 amino acids, and the end position for and the end position for and the end position for each peptide Is the start each peptide is the start each peptide is the start position plus eight. position plus eight position plus eight fl SVVIVNLFV l88 [ |] LLNFVIIEE H16 9 61 lHIQELPLD f|H 7951 TPNTEADV 19341 DLARHYKSA 1970 NTFVACDSI 11 819 AGTITVV 17 1008| HTRPVGIQV 16 SSSSDPYSV 15 965 ELPLDNTFV 141 | GDLLKDLNL 9515 [ GYPVTIFEV|15 1006 SVHTREVGI 17 [58 |TAMQEKLV 44 [] LKDLNLSLI |~4 [21 DLLSGYF 1 [1 | 1SfPEfSAI [ DLNLSLIPN 146 1101 FAVLLACVV [j 16011 LPAAVDPDV [fj 665 VYKTGDVPL [| 42 DLLDLNLS [170| INGVQIIYEL 5I [06| CFYEVEVAi [6 F49J LSUPKSL 181 | SQNIFLDV 5 111 | EVAIL1DE 4 |[ AQFKLVYK 16 182 QNIFGLDV |5 113 AILPDEIFR $ 1671 YKTGDNPUI[6 2 RSSTA!LQV 15 115 |LPDElfRLV 14 83f ElFTTARI f263~ PVGTSVTQL 5 128 |LUEDINDNA 1 107 FYEVEAl 61 IHFSFSNLV 5 | PLFPAIVIN 14 [1jDEIFRLVKI 1 287] SFSNLVSNI f5s 138 |LFPATIlNI 14 [ NISIPNSA R1 1RAMVLVNVT 147| SIPENSAIN [F KPQijVQK 374 IPLNTKIAL | [598|TLPA8DPD | 2337] ALQVVTD [ 396 VTCFTDHE15 183 |NIFGLDVlE 19 NLVSN!ARR Ii 448 QSAMLIKV 1521EKDTYyMKV J~ 291 LVSNIARRL 16 45 AMLFKVKD 232 TAILQMSVT 30FHLNAITGL L6 [451 MLFIKyKDE 11248 VFKET~IEV ] F21YAIKLLAAD 5 LLGPDAPPE 2 KETEEVSI 433f AIKLLAADA i6 517 CRTGMLTVV 1530TIKEPLDRE J 435 K ~LLAG 590 GUT1VIDPD 15LLVLASDG 3 LLAADAGKP 6 4 VRPNSFD 2 ASDGGLMPA 5321 KEDKYLFTI 16 4 VKAEDGRV 15 MPARAVLV 553| NV1VFMSiL VSRSSSAKV 339AMV VTD 4 1587 | GTVGLITVT 6 ~ [88 STNPGTVVF 1544 NVTDVHIDNVIE41 5YGDNSAVTL 11703 INDTGMNAEV [S32NPVNDIVVL|[9 602 NSAVTLSIL 707 |MNAEVRYSI j 388 KDADHNGRV|E9 5SSAKVINV 17421 TDLGLHRVL 412 FSNQFLLET |R 667j NDNKPyFIV 16 767 |IVNLFVNES 145[VFTQSEVTV | 4 HDLFAIQET 16 769 NLFVNESVT IQLTKSAM | 4 54 |NDLGQEDSL 16 875 KHSPKNLLL 15 2KINYLLGPD 760| DSLFSIV 16 7 DSDGNRVTL 1 7 PDAPPFSL 4 |FVNESTNA 16 | TLDLPIDLE 15 5 DCRTGMLTV| 806 PTSDYYKIL 16 [ DLPIDLEEQ 15LADGVP [ 174 Table XXIII 109P1D4v.1 Table XXV- Table XXV A0201-9-mers 109P1D4v.1-A3-9-mers 1109P1D4v.1-A3-9-mes Each peptide is a portion Each peptide Is a Each peptide Is a of SEQ ID NO: 3; each portion of SEQ ID NO: portion of SEQ ID NO: start position Is 3; each start position Is 3; each start position Is specified, the length of specified, the length of specified, the length of peptide is 9 amino acids, peptide is 9 amino peptide is 9 amino and the end position for acids, and the end acids, and the end each peptide is the start position for each position for each position plus eight peptide is the start peptide Is the start position plus eight. position plus eight. 52SNVTVEVSI 1 0THNEYNFYV TLINELVRK 2360 PVDTV IE7J SNCSYELVL . 527 KLDREKEDK 748 RVLVKANDL 686][LPSTNPGTV14 172 |GVNYELIK 24 8261 FIIAV 0 SNPG'10FQV 0RLPVESNQ 4 17 |VEHSAQE1 706 |GMNAEMRYS 1827 VIITVR 116__PDgIFBLVK 19 714 SIVGGNTRD 839APLKQ 24 [189| VIETPEGDK 9 768]| VNLFVNESV 4AYLDYESTK 3 218 |V1EDGF[ 773 3NESVTNATL 674 IVEPSNCSY 23220 KVEDGGEPQ 784] ELVRKTEA 841 HL23AAQNK 384TVDKADH 812 KILVAVAG FVACDSISK 416 | FLLETMYL 878 PKNLLLNFV 112 VL2ACFH 2 FT AI LDA 95|DVDSDGNRV 1233 EALQVTD 22 [49 NSEG TK F QQE 518 RGMLIVK 535j KYIFTLAK .9[ IQLELDN GVIRPfISF 22 PLSN VF 662 NVVDVNDNK 228 VGLITVTD 19 TableXXIV 814 LVAAVATI 665DVNDNKPVF 109P1D4v.1 833 VVBCR APH 22 802 DVSSPISDY A0203-9- 910 DLEEQIMGK 22 [6 MIMMKKKK mersF916 5 SLTAQFK 21 DLLSGIF No Results L167 LiGDLL1K Found. 16 DVINGQN 21 60 AMQFKL_YK 298 RLEHLAT21 RIRE!HLCA Table XXV- 324 |KLLVLA9DG| 212 109P1D4v.1-A3-9-mers [379 KA9 TD |211 267 |SVIQLHjATD| Each peptide is a 1524 F31 331E 21 ~GMA18 portion of SEQ ID NO: 5 K l 3; each start position Is 1582 |NLERHG214 PLQSAMLF|18 specified, the length of 740DVILGLHR 1 487 KVsAM DS 58 peptide is 9 amIno ______ adds, and the end oLGLRVLVK2 ILAKD VP I position for each 812 KIVAA 1AG | 642 YV1 AEDGGR| peptide is the start AVAGTJJVV | 6 |AERGGEySR p8805J[NLLLNE7VT1| 658 KVIINyDV | 65 RV RSSSAK 31 81 |T[VF 435 113DGILrPKLT | 694 |VVVjLDT 11 AVLLAFVF 28 AP F |697 | 7 NVIGQLLK KMQLJYQK|5 Gl-RVYKA I 175 Table XXV- Table XXV I9P1D4v.1-A3-9-mers 109P1D4v.1-A3-9-mers 802DVSSPTSDY Each peptide is a Each peptide is a DVNDNKPVF_ portion of SEQ ID NO: portion of SEQ ID NO: 3; each start position is 3: each start position is DTNDNHPVF specified, the length of specified, the length of ENVLIGDLL 25 peptide is 9 amino peplide is 9 amino 109 EVEVAILPD acids, and the end acids, and the end position for each position for each DVDNPS peptide is the start peptide is the start 1002 EVPVSVHTR position plus eight. position plus eight. 150 ENSAINSKY I _ _ _ __ _ _ I [I8 VEPG 1832 AV1RCBQAP 8]238 |SVIDTNH 16D351VID 4 835RCQALK [242 TNDNHFK 8 7 KK KKHPK 277 | DIENAH 9 623 GVRPNISF |1F 10 1002 EV1VS 8L!R [2931 SNAR 6L [62710EVRYsVGG| 43 [LLDLNLSL jf 4IVLYNVIQVNJ [8 251 ETEIEVSIP| RENKLT 351 NVESIDRY 0PVGTSVTQL|2 95 KLCAGIERD 17354~ SilIRXVN DVDLLH|2 122 LVIR LIE 371 SE IP NTK 1 6 130 D D L |$ 17PLFPATVIN 1J380J IALITVTIDK [ 131 DINDNAPLF|[~ 163 AVDPDVGIN 1749SAMLFIj VK ~'17ELIKSQNIF |~ 177 |3EL4KSQF LLIPDAEPE 4 ETAYLDYE| 210 |EEI DTYVMK 17 546 |IGVEPLISNV ff!477 |ENNSPGIQL|j~ 257| SIEENAEVG 17 6081| SILDEDF 16 634 EKQESYTFY| 20QLHATDADI 17ERYTEYVKlf6 674 |IVPPSNCSY |~ 290J NLySNIARR 1770IAVQNDIGMNI1 729 |ETGNITLME |J 1 ALIVTDKD 71 YSIVGGNTR 71 DVPIRIEE 2 L36F AD 7 73 TLMEKCDVT 80 |DTGEIFTTG|2j 4QLKVMD 17DLGLHLV 1 16 5YLLGPDAPP [1I70LVISANDLGQ 1617DVGINGVQN|~ 4 AVLSLDE 1761 SLESVYJVN ETPEGDKMP 4VIPNJFD 7 SVVLFV 1255 EVSIPENAP 2 Z IEVBYSXVGG 7j80YVKILyAAV 16NA___HFSF 5DLQPLF 3DLRHYSA 16 2 EENK0HKL IIM 'M 1T 6 LNFA 161 38fETNHL 21 79 VNLVNVT 17 PNI 3AC[ DTVVLSENI 79 NLVESVTbl XV 142] STKEYAIKL ji 83 ILVR WVFQVIAV 21 1 IVVAT A26-9-mers 806 PTSDYVKIL T7IV 7! Each peptide is a 993 DCGYPVTF21 F05 GQVS IF E7 portion of SEQ ID NO: 2914| LVSNIARRL speifed the le gh f368 - VLE6P 2 55 F4][8 21TAQ 11 pfeth egho PREETpeptide Is 9 amino 39 |i]DHNGRVTCF [0o LacidsTaci the endTV L 1--- peptide Is the start TVFVSIDQ 1 LVQKELDR position plus eih. 5 |DVDSDGNRV 176 Table XXVI- Table XXVI- Table XXVI 109P1D4v.1 109P1D4v.1 109P1D4v.1 A26-9-mers A26-9-mers A26-9-mers Each peptide Is a Each peptide Is a Each peptide is a portion of SEQ ID NO' portion of SEQ ID NO: portion of SEQ ID NO: 3; each start position is 3; each start position Is 3; each start position is specified, the length of specified, the length of specified, the length of peptide is 9 amino peptide is 9 amino peptide is 9 amino acids, and the end acds, and the end acids, and the end position for each position for each position for each peptide is the start peptide is the start peptide Is the start position plus eight. position plus eight, position plus eight. 931 |DSPLARHY 20 [8971 DSDGNRVTL [8277 |DIGENAKIH1| EIFTTGARI 19 [2[ DLLSGTYF |TPNHKLLVL|1 218 KVKVEDGGF 1 117][DEIFRLVKI |7 340 MVLVNVTDV| 319 |ETPNHKLLV 19 213DYVMKVKV E 3631 PVNDTWLS|15 26|LVLASDGGL 19350 DNVPSIDIR TWLSENIP 15 533 EDKYLFTIL 19 72ENIPLNTKI 1 470 |FVTVSIPEN 715 |VGGNTRDL 19 431 EYAIKLLA 17 471 |VVSIPENN 748 |RVLVKAN~DL 19 578 YVPENLPRH|L7 549 |PLTSNVTVF 765 WIVNLFVN 19 [ GTVGLITVT |I 567 |SPVFTHNEY 809 DYVKILVAA 19 DTGMNAEVR 17 591 |LIVTDPDY [ 823 VVFIT DLGQPDSLF 17 VTLSILDEN 601 825 WVIFITAV 1ITWVVIFI EDGGRVSRS 15 VTLDLPIDL 1DGNRVTLDL 662NWDVNDNK 15 953 ETPLNSKHH 61 GTYIFAVLL 16 | PVFIVPPSN 11 |1AVLLACVF 8 16 CWFHSGAQ 16 ESVTATLI 33 EMPENVLIG 1 17 WFHSGAQE| 178461ELVRKSTEA] 39 LIGDLLKDL 18 79 EDTGEIFTT 16 832 AWCRQAP 57Il |LTTAMQFKL 8 163 |AVDPDVGIN 161 860ENRQMIMMK| 141 ATVINISIP 18 2 NIARRLFHL 16 877][SPKNLLLNF |15 142 |VINISIPE 18 529 |DREKEDKYL 886] VTEETKAD [15 168 |VGINGVQNY||18 [5 NVTVFVSII 16 902| RVTLDLPID |15 253 |EIEVSIPEN 18 | AVTLSILDE 16 958][ SKHHIIQEL | 356 DIRYIVNPV 18 |DDFTIDSQT 16 1011|PVGIQVSNT | 403 EIPFRLRPV |18| | KVTNWDV 16 458 DENDNAPVF18 659 VTINVVDVN16 Table XXVl-109P1D4 56 DQNDNSPVF181 | SWIVNLFV 1 v.1-B0702-9-mers 570 FTHNEYNFY18 771 FVNESVTNA|Each peptide Is a Efl I Iportion of SEQ ID NO: 688 STNPGTVVF[18 799| EIADVSSPT | 3; each start position is 694 WFQVIAVD 18 810 YVKILVV specified, the length of 6_94]_1 peptide is 9 amino 727 |DQETGNI |[18|820 [ | I[TWi[ |acids, and the end 763 |FSWVNLF [18] 826 WIFITAW | 16 position for each 821 |T F |[18 [9761| DSISKCSSS|peptide Is the start - position plus eight 824 | F |8 |T TFEVPVSV|16 890 |ETKADDVDS18j 211 EKDTYVMKV LP1 177 Table XXVII-109P1D4 Table XXVII-109P1D4 Table XXVII-109P1D4 v.1-B0702-9-mers v.1-B0702-9-mers v.1-B0702-9-mers Each peptide is a Each peptide is a Each peptide is a portion of SEQ ID NO: portion of SEQ ID NO: portion of SEQ ID NO: 3; each start position is 3; each start position Is 3; each start position Is specified, the length of specified, the length of specified, the length of peptide is 9 amino peptide is 9 amino peptide is 9 amino acids, and the end adds, and the end acids, and the end position for each position for each position for each peptide Is the start peptide is the start peptide Is the start position plus eight. position plus elghi position plus eight 362 NPVNDTVVL| 24 F262 APVGTSVTQ| 16 1599l YGDNSAVTL[ 13|6F APLFPATV1| 3 43 AADAGKPPLLl [7 |- SNCSYELVL| 13 3201 TPNHKLLVL [23 F93 ADSGPNAKl r6 742|TDLGLHRVL|H 374 | IPLNTKIAL 22 506 GPDAPPEFS| [6 7 731 |NESVTNATLH 409 9 RPVFSNFL AKDNGVPPL 806| PTSDYVKIL 6761 PPSNCSYEL 58 NPENRQMIM 1 AVAGTI 13 1792 APVTPNTEI 2 H875 KH9SPKNLLL| 839APHLKAQK| 44PPLNQSAML 21 ~IDSDGNRVTL| 899 [ DGNRVTLDL [ 496 GPNAKINYL 7LPIDLEEQT F 9KSASPQPAF| [404 IPFRLRPVF [954 ~1TPLNSKHHl| [6951 |fQPETPLNSK|I~ 52 IPNKSLTTA 1 1REEMPENVL 19601 HHIQELPL 1601 LPAAVDPDV 477 ENNSPGQL 258 IPENAPVGT 19 507 APPEFSL5 Table XXVIII-109P1D4 335 MPARAMVLV IVGGNTRDL v 1-B08-9-mers 463 APVFTQSFV 18FQlQPETPL 5 Each peptide Is a PI fl III1 portion of SEQ ID NO: 758 QPDSLFSW I01RPVGQVSN 15 3; each start position is 115 LPDEFRLV 100IPREHFY 4 specfied, the length of F261-4H peptide is 9 amino 226 |FPQRSSTA 154 INSKYTLPA and the end 352 |VPSIDIRYI7 PQRSSTAIL [4 position for each KPPLNQSAM 317 REETPNHKL peptide is the start 475 IPENNSPG 18 A ESLD position Pus eight. 480 SPGQLTKV 670 KPVFIVPPS F4f 46 |GPNAKNYL 548 | V 18 78 K 43 |LLKDLNLSL 68|LPSTNPGTV 1!LFSWIVNL '4] 320TPNHKLLVL f f690 |NPGTWVFQV 1 8741[KKH-SPKNLL|9 453 FIKVKDEND ~ 86] SPTSDYVKI 1SG1 YFAVL [ 514 |SLDCRTGML 18771| SPKNLLLNF 149[LSLIPNKSL [22~ |GAQEKNYTI 2 929IKPDSPDLAR 1861VYKTGDVPL |24 HPVFKETEI 2 1LPLDNTFVA 18GARIDRE 428 STKEYAIKL DPDVGINGV 1EDINDNAPL | SPKNLLLNF 24 249|HPVFETEl AAVDPDVGI|1 120 |FRLVKIRFL 547F|VPPLTSNVT 9 KSQNIFGL 26 |VMKVKVEDG 2 596 DPDYGDNSA jfJ12TPEGDKMPQ| [3375j| PLNTKIALI 795| TNTEADV ~~ 6 PVGTSVTQL [3 [5331| EDKYLFTIL| 6 1TPNPENRQM[7 3 EDKYLFIL 13 [8] LPRHGTVGL 178 Table XXVIl-109P1D4 Table XXVIll-109P1D41 Table XXVIII-109P1D4 v.1-B08-9-mers v.1-B08-9-mers v.1-B08-9-mers Each peptide is a Each peptide is a Each peptide is a portion of SEQ ID NO: portion of SEQ ID NO: portion of SEQ ID NO: 3; each start position is 3; each start position is 3; each start position is specified, the length of specified, the length of specified, the length of peptide is 9 amino peptide is 9 amino peptide is 9 amino acids, and the end acids, and the end acids, and the end position for each position for each position for each peptide is the start peptide is the start peptide is the start position plus eight position plus eight position plus eight 41GDLLKDLNL 124 KIRFLIEDI 248 VFKETEIEV | 66 VYKTGDVPL[ 218 |KVKVEDGGF 281 NAKHFSFS 294 NIARRLFHL [g 307 |GLTIKEPL 1283 KIHFSFSNL |f ] 955PLNSKHI NPVNDVVL 308UTIKEPLD 1_ GARDREKL 1 RPVFSNQFL 17 352 VPSIDIRYI 7 MEKCDVTDL 2 426| YESTKEYA7] SIDFRY6VN | 7RVLVKANDL | 66PPSNCSYEL jJ43EIPFRLRPV| f4 66MMKKKKKKK 21839 |APHLKAQK 438 AADAGKPPL14 867 MKKF6KKKKKK 1 SVHTRPVG 498 NAKINYLLG| [68 KKKKKKKKH 21152 | SAINSKYTL 539 ][TILAKDNGV|~4 K8K6 KKKK 176 YELIKSQNI 1 792 |[APVTPNTEl 873KKKHSPKNL 227PQRSSTAL 16 808 SDYVKILVA 14 87 KHSPKNLLL TIKEPLDRE NPENRQMM14 91 IDREKLCAG 313 EPLDREETP 16 880 NLLLNFVJ 11931 PEGDKM~PQL 20 0 PFRLRPVFS 1698SKH-HilQEL |] 845 QKNKQNSE 20 PPLNQSAML 870 KKKKS 1633 REKQESYTF Table XXIX-109P1D4 871KKKS KAQKNKQN F3 v.1-B1510-9-mers TFKPDSPDL 20 GDLLKDL Each peptide is a F92]9Ef portion of SEQ ID NO: 16 FLLET MYL DEIFRLVK 1 3; each start position is FDREKQESY 1KSQNIFG specified, the length of __63_1__ EA peptide Is 9 amino 784ELVRKSTEA 9DHNGRVTCF ads, and the end 1 ILPDEFRL AIKLLAADA position for each 122 LVKIRFE LAKDNGVPP eptide is the start SLMPARAMVL18 8 position plus eight 374 IPLNTKIAL VRRQAPH 1875 KHSPKNLL 451MLFIKVKDE 18 MIMMKKKK FHLNATGL 528LDREKEDKY PNKSLTT 9601 HHiQELPL | REKEDKYLF 119 IFRLVKIRF DHNGRVTCF| 656 SAKVTINVV AINSKYTLP ILPDEIFRL 666 VNDNKPVF1 INGVQNYEL 179 IKSQNIFGL 1 734 TLMEKCDVf 1 177 ELIKSQNIF 1475IVGGNTRDL|1 41 HLKAAQKNK LIVQKELDR 14TDLGLHRVL1 6|KLVYKTGDV 203 VQKELDREE 1DSDGNRVTL 72 |VPURIEED FPQRSSTAI 97LVSNARRL 179 Table XXIX-109P1D4 Table XXIX-109P1D4 Table XXX v.1-B1i510-9-mers v.1-B1510-9-mers 109P1D4v.1 Each peptide is a Each peptide is a B2705-9-mers portion of SEQ ID NO: portion of SEQ ID NO: Each peptide is a 3; each start position is 3; each start position is portion of SEQ ID NO: specified, the length of specified, the length of 3; each start position Is peptide is 9 amino peptide is 9 amino specified, the length of acids, and the end acids, and the end peptide is 9 amino position for each position for each adds, and the end peptide Is the start peptide Is the start position for each peptide position plus eight position plus eight is the start position plus ___ _ eight 40|TDHEIPFRL 1537GLITIKEPL ~ 762 LFSW1VNL 3 REETPNHKL 39 IGRVTCFTDH| 31 REEMPENVL 11322 NHKLLVLAS 12E Y 104EHCFYEVEV 31 334V 1861] NRQMIMMKK ] 120FRLVKIRFL 4IPFRRPVF 1 LRPVFSNQF 170INGVQNYEL 477 ENNSPGQL 125 IRPNISFDR | 3181 EETPNHKLL GPNAKINYL 2316 DREETPNHK 362 NPVNDTVVL 14 [497 PNAKINYLL VRCRQAPHL|~ 374 IPLNTKIAL 14LTVVKK 41 GDLLKDLNL 2 401 |DHEIPFRLR 529 DREKEDKYL 92 DREKLCAGI| 507 |PDAPPEFSL 71 THNEYNFYV 1 97 |KMPQLVQK|2 599 YGDNSAVTL 1YNFYVPENL REKQESYTF 777 TNATLINEL 1 2 NSAVTLSIL NRVTLDLPi |1 9 TFKPDSPDL 14 66 DVNDNKPVF 47 LNLSLIPNK | |GTYFAVLL 1676 PPSNCSYEL 304 ATTGLITIK 66 |VYKTGDVPL 13 678 SNCSYELVL ~520 GMLTVVKKL 10 FYEVEVAILl1 5 NDLGQPDSL 12~PRHGTVGLIl|J 193 PEGDKMPQL 874 KKHSPKNLL 623 GVRPNISF SNHPVFKETE 13 9iVTLDLPIDL F2 RVLVKANDL 320f| TPNHKLLVL 948 FQIQPETPL IRIEEDTGE 1 429 TKEYAIKLL1 SKHHIQEL 1 ELKSQNIF | 48 |AADAGKPPL [VHTRPVGQ RRLFHLNAT | 542 |AKDNGVPPL 13 l 1 REETPNHKL[] [83 |LPRHGTVGL 1 GPNAKINYL 688 STNPGTVF 13 Table XXX- 5 I A 727 |DQETGNITL 13109P1D4v.1- 1013| GQVSNTTF 7 B2705-9-mersGIFAVLL [F7LRVVAN6]~ Each peptide Is a ________ 773NESVTNATLII portion of SEQ ID NO: 31 REEMPENVL [806] PTSDYVKIL 1 3; each start position is 55 1KSLTTAMQF [5 Sspecified, the length of 114 ILPDEIFRL F--1 ____j peptide Is 9 amino________ 19 | A acids, and the end 119 IFRLVKIRF [E7 35 |~ PENVLGDLK | position for each peptide 290 NLVSNIARR | 7 88~1[ PENGARDRL I2 Is the start position plus 307 |GLITKEPL 17 [12|lAIKL |p 309h| ITIKEPLDR | 7 284][2IFNV [ FRLVKIRFL |6357 2IjHFSFSNLV I12________ 180 Table XXX- Table XXX- 1 Table XXX 109P1D4v.1- 109PID4v.1- 109P1D4v.1 B2705-9-mers 82705-9-mers B32705-9-mers Each peptide is a Each peptide is a Each peptide is a portion of SEQ ID NO: portion of SEQ ID NO portion of SEQ ID NO: 3; each start position is 3; each start position is 3; each start position is specified, the length of specified, the length of specified, the length of peplide is 9 amino peptide is 9 amino peptide is 9 amino acids, and the end acids, and the end acids, and the end position for each peptide position for each peptide position for each peptide Is the start position plus is the start positon plus is the start position plus eight. eight. eight 404 IPFRLRPVF 17 835 RCRQAPHLK F16 4161FLLETAAYL | |0[RPVSNQFL 839 APHLKQK 422AYLDYESTK[j 479 NSPGIQLTK |17 |ENRQMIMMK 428 STKEYAIKL | [518! RTGMLTVVKIE R |62]RQMIMMKKK 1 38 AADAGKPPL| 530 REKEDKYLF 866 MMKKKKKKK PLNQSAMLF 15 [64 |AEDGGRVSR 8 86.7MKKKKKKKK 449SAMLFKK |GRVSRSSSA 17 86 KKKKKKKKH 497 PNAKINYLL | 6501 RVSRSSSAK 7 871 |KKKKKHSPK 59 ETGMLTVVKK| 7 |77HRVLVKAND 7 [7 KHSPKNLLL V5241 KKLDREK | LFSWIVNL E7 940 |KSASPQPAF [542 AKDNGVPPL 780 |TLINELVRK 10091 TRPVGQVS FYVPENLPR 865 |MMKKKKKK 17 [E | DLLSGTYIF 662 NVDVNDNK [4H FQIQPETPL 17 23 AQEKNYTIR 688] STNPGTVF 964 | QELPLDNTF 17 49| LSLIPNKSL 727 DQETGNITL | AVLLACVVF 1 82 GEFTTGAR [ QEGNITLM 37[ NVLIGDLLK 1 8 GARIDREKL 744 LGL1RVLVK| 5 125 IRFLIEDIN 112| VAlPDEIF L 754 NDLGQPDSL 152 SAINSKYTL 113| AILPDEIFR 7551 DLGQPDSLF 179 IKSQNIFGL EFRLVKIR 15 79 ATLINELVR| 199 PQLIVQKEL 16149 PENSAINSK 15 820 GTITVVI 15 29REEKDTYVM 1 1681 VGINGVQNY 15863 QMIMMKKKK 15 21 VEDGGFPQR 201 LIVKELR 873 KKKHSPKNL 5 1276 UADIGENAKI [j]28DREEKDTYV 1584KKHSPKNLL 15 KHFSFSNL 16 263 PVGTSVTL 877 SPKNLLLNF 15 337ARAMVLVNV 29SNLVSNIAR 5 894DDVDSDGNR 350 DNVPSIDIR 169[[ARRLFHLNA 929 |KPDSPDLAR| 380 IALITVTK 13321 GGLMPARAM 13 936 ARHYKSASP|9 435 KLLAADAGK 368 | VVLSENIPL 15 958!! SKHHIIQEL |I CRTGMLTV 6 372 ENIPLNTKi ! 993 BCGYPVTTF15 55 P N 374 |IPLNTKIAL |9 1|VFHSGAQEK1 7131 YSIVGGNTR 16 391 DHNGRVTCF15 22 1GAQEKNYTi 742 |TDLGLHRVL | FTDHEIPFR |15 H26 KNYTIREEM| 777 |TNARNEL 16 1406 |FRLRPVFSN| 5 30f |REEMPENV| [ 827!| VIFITAVVR |K61 41 PVFSNQFLL 15 35 J PENVLIGDL 19 181 Table XXX- Table XXX- Table XXX 109P1D4v.1- 109P1D4v.1- 109PID4v.1 B2705-9-mers 82705-9-mers B2705-9-mers Each peptide is a Each peptide is a Each peptide is a portion of SEQ ID NO: portion of SEQ ID NO: portion of SEQ ID NO: 3; each start position Is 3; each start position is 3; each start position is specified, the length of specified, the length of specified, the length of peptide is 9 amino peptide is 9 amino peptide is 9 amino acids, and the end acids, and the end acids, and the end position for each peptide position for each peptide position for each peptide is the start position plus is the start position plus is the start position plus eight eight. eight. 43 L N 14 7 FSVV1VNLF 492 DADSGPNAK 57L1TAMQFKL| 1|04SSPTSDYVK|1 507 |PDAPPEFSL [9 60 AMQFKLVYK|1 836 |CRQAPHLKA|1 533 |EDKYLFTIL| KTGDVPL 4 841 HLKAAQKNK4 562 DQNDNSPVF 13 68 KTGDVPLIR 14 864[MIMMKKKKK|I4 569 |VFTHNEYNF 121 RLVKIRFLI 64 [897]|DSDGNRVTL| ~57 YVPENLPRH-I 130 EDINDNAPL 1 [903][ VTLDLPIDL | 583 |LPRHGTVGL|3 136 APLFPATV | 9 5 GTVGLTVT 17 |NGVQNYEL 70 95114QPETNS 6311FDREKQESY _ 172| GVQNYEUK |F4 [ ]PETPLNSKH| I63 DREKQEST H 212 KDTYVMKVK 14 15][ SGTYIFAVL 3 652 |SRSSSAKTII 218 KVKVEDGGF 3ENVGDLL 1 5 RSSSAKVTI 280 ENAHFSF 15 TAMQFKLVY 1 665 3DVNDNKPVF 291 LVSNIARRL FTTGARIDR 674| IVPPSNCSY 13 30 FHLNA1TGL TGARIDREK 676JjPPSNCSYEL 13 320 TPNHKLLVL ARIDREKLC 13 699 |(AVDNDTGM| 326 LVLASDGGL 94 EKLCAGIPR 1 (7151 IVGGNTRDL [ SDGGLMPAR 4GIPRDEHCF 17201 TRDLFAIDQ 13 371 SENIPLNT1 FYEVEVAIL 730 TGNITLMEK 400 DHEPFRL ISIPENSA 1 736 |MEKCDVTDL [ 1427 |ESTKEYAIK [[10 ENSAINSKY 13 773 |NESVTNATL 13 SKPPLNQSAM 1901 IETPEGDKM 792| APVTPNTE 1 HPPLNQSAML F 3PEGDKMPL 821| TITVVIF | 483] IQLTKVSAM 1 275 DADIGENAK [4 WATPNPENR| 3 1ADSGPNAK|147 IGENAKIHF [ 884 NFVTIEETK 522I LTVVKKLDR |14 LDREETPNH f 921 WVTTPTTFK( 527 4KLDREKEDK 1 33 LMPARAMVL 3 927 TFKPDSPDL 9 PLTSNVTVF 1351NVPSIDIRY 930 PDSPDLARH 599 YGDNSAVTL 14 3 NPVNDTVVL 1 960 HH1IQELPL ] 608 SILDENDDF QFLLETAAY | 972 |FVACDSISK | 618 IDSQTGVIR 14 424 LDYESTKEY13 1002EVPVSVHTR 627 PNISFDREK 14 429 TKEYAIKLL 13 71 VRYSIVGGN 45 DENDNAPVF Table XI-109PD4v. KCDVTDLGL|[ ENNSPGQL 1B2709-9-mers 182 Each peptide is a Table XXXI-109P1D4v.1 Table XXXJ-109P1 D4v.1 portion of SEQ ID NO: B2709-9-mers B2709-9-ners specified, the length of . Each peptide Is a Each peptide is a peiedhe ls9 anof portion of SEQ ID NO: portion of SEQ ID NO: aidds, and the end 3; each start position is 3; each start position Is position for each peptide specified, the length of specified, the length of poist for posetinc p peptide Is 9 amino peptide is 9 amino Is the start position plus acids, and the end acids, and the end position for each peptide position for each peptide is the start position plus is the start position plus 120 FRLVKIRFL eight. eight 834 VRCRQAPHL 2 337 ARAMVLVNV 21 76 RIEEDTGEI [3 136 APLFPATVI Fu IREEMPENV 02RDEHCFYEV 13 152SAINSKYTL 529 DREKEDKYL2 KETEIEVS 13 170 IINGVQNYEL 2 NRVTLDLP 283 KIHFSFSNL 1 193 IPEGDKMPQL 12 408 LRPVFSNQF 19 291 LVSNIARRL 13 195 GDKMPQUV 517 CRTGMLTVV ARRLFHLNA 1 199 PQLIVQKEL 584 PRHGTVGL NPVNDWVL 8 QRSSTAILQ 21 786 VRKSTEAPV 19VVLSENIPL 1 263 PVGTSVTQL 9 DREKLCAGI [18 374 IPLNTKIAL 13 IHFSFSNLV 4061FRLRPVFSN 300 FHLNATTGL 6 GTYFAVLL 17 410 318 EETPNHKLL 41GDLLDLNL 416 FLLETAAYL 1 LVLASDGGL 740 RVLVKANDL 496 GPNAKNYL13 333 GLMPARAMV RRLFHLNAT AKDNGVPPL 4 | TDHEIPFRL 2 520 GMLTVVKKL GVPPLTSNV 13 IPFRLRPVF [3071 GLITIKEPL 15575 YNFYVPENL 438 AAAGKPPL 409 RPVFSNQFL 15633 REKQESYTF H13 PPLNQSAML 1 649 GRVSRSSSA 15KVTINDV 477 ENNSPGQL 711VRYSIVGGN 57 GNTRDLFAI IQLTKVSAM REEMPENVL 14KCDVTDLGL 497 PNAKINYLL 55KSLTAMQF KKKHSPKNL 13 599YGDNSAVTL GARIDREKL KKHSPKNLL 13 623 GVIRPNISF 121 RLVKIRF TFKPDSPDL 3 IRPNISFDR 125 IRFLIEDIN 14 2 DLLSGTYIF 2 [6j SRSSSAKVT 12 209 REEKDTYVM 14 5 SGTYIFAVL 1 [678 SNCSYELVL 12 229 RSSTAILOV i 11 AVLLACWF 736 MEKCDVDL1 317REETPNHKL 4 22 GAQEKNYTI 7 TDLGLHRVL 332 GGLMPARAM 36 ENVLIGDLL 747 HRVLVKAND| 5 IRYVNPVN 14 49 LSLIPNKSL 1 754 NDLGQPDSL12 GRVTCFTDH 1467 YKTGDVPLI DSLFSVIV REKEDKYLF 75 IRIEEDTGE 12LFSVVNL | 653 RSSSAKVTI ARIDREKLC 2 805 SPTSDYVK 2 820 GTITVVVVI 99 GIPRDEHCF 819 AGTITVVV 875 KHSPKNLLL 14ILPDEIFRL VTDLPIDL 2 2 KNYTIREEM 1 EDINDNAPL 12 [ KSASPPAF 12 183 Table XXXI-109PID4v.1 Table XXXI-109P1D4v.1 Table XXXII-109P104 B2709-9-mers B2709-9-mers v.1-B4402-9-mers Each peptide is a Each peptide Is a Each peptide is a portion of SEQ ID NO: portion of SEQ ID NO: portion of SEQ ID NO: 3; each start position is 3; each start position is 3; each start position is specified, the length of specified, the length of specified, the length of peptide is 9 amino peptide is 9 amino peptide is 9 amino acids, and the end acids, and the end acids, and the end position for each peptide position for each peptide position for each is the start position plus is the start position plus peptide is the start eight eight position plus eight 2HHIQELPL 757GQPDSLFSV 1135PENVLIGDL LLKDLNLSL FSVIVNLF 7REETPNHKL 2 57LTAMQFL PTSDYVKIL NESVTNATL KVYKTGDV TITVVVV1 F 1 1REEMPENVL22 66 ViYKTGDVPL I822 ITVVVVIFI PEGDKMPQL EFTGARI 11 CRQAPHLKA 26YESTKEYA 106CFYEVEVA 1 NRQMIMMK KEDKYLFT 22 107 FYEVEVAIL NLLLNFVTI IEEDTGEIF 46 ISIPENSA DVDSGNRV 250KETEIEVSI 162] AVDPDVGI 1 DSDGNRV'L 14 LETAYLDY 176 YELKSQNI 8 DGNRVTLDL REKEDKYLF 179 IKSQNIFGL ARHYKSASP 1REKQESYTF 190 IETPEGDKM IASPQPAFQ MEKCDVTDL 2131 [TYMKK [8 FQIQPETPL 91 LEEQTMGKY2 [22 PQRSSTAHL 958 SKHHIQEL 1 YELIKSQNI 320 TPNHKL QELPLDNTF [ HEPFRLRP 334LMPARA SSSSDPYSV AVLLACF 340 MVLVNVTDV 995]| GYPVTTFEV 11 3 ENIPLNTKI 33 PSIDIRYV 11 999 TTFEVPVSV AEDGGRVSR [88 KDADHNGRV 1103G1QVSNTTF 1168STNPGTVVF [~ 428 STKEYAIKL KHSPKNLLL 457 KDENDNAPV 1 Table XXXII-109P1D4 GEIFTTGAR 7PDAPPEFSL v.1-B4402-9-mers EDINDNAPL 54 PPLTSNVTV Each peptide is a |_ISIPENSA _________portion of SEQ ID NO:. ~ SPNA 16 549 PLTSNVVF 3; each start position is 5 SAINSKYTL 16 569 VFTHNEYNF specified, the length of | ELIKSQNIF j 581 ENLPRG peptide Is 9 2 ADIGENAK 1 H acids, anid the end 583 LPRHG 1VGL position for each TKEYAIKLL 597 PDYGDNSAV peptideis the startGMLVKKL QTGVRPNI position pus eight F DNGVPPL 65KQESYTFYV li38EETPNHLL70 AEVRYSIVG| 676PPSNCSYEL 1[ EEMPENVL QTGNITLM IVGGNTRDL 1 QELPLDNTF 8DSDGNRVTL 720 TRDLFADQ 1 DEIFRLVKI 5 36 ENVLIGDLL ITLMEKCDV 11DENDNAPVF 2 KSLT 184 Table XXXI-109P1D41 Table XXXIIII-109P1D4 Table XXXIIII-109P1D4 v.1-B4402-9-mers _ v.1-B5101-9-mers v.1-B5101-9-mers Each peptide is a Each peptide is a Each peptide is a portion of SEQ ID NO: portion of SEQ ID NO: portion of SEQ ID NO: 3; each start position is 3; each start position is 3; each start position is specified, the length of specified, the length of specified, the length of peptide is 9 amino peptide Is 9 amino peptide is 9 amino acids, and the end acids, and the end acids, and the end position for each position for each position for each peptide is the start peptide is the start peptide is the start position plus eight position plus eight position plus eight EEDTGEIFT 303 NATTGLIT [6 106]| CFYEVEVAl 1114 ILPDEIFRL 158548 PPLTSNVTV 26 152][ SAINSKYTL I M5FRLVKIRFL 15 4]TPLNSKHHI 2 194 EGDKMPQL l F1 21EDINDNAP H1 115] LPDEIFRLV 24!463]APVFTQSFV|[lg Fi-j ENSAINSKY 16DPDVGINGV 24 583 |LPRHGTVGL| 168VGINGVQNY SAKVTINW 599 YGDNSAVTL IKSQNIFGL LPSTNPGTV 24 708NAEVRYSIV 205KELREEK 1 NPGTVVFQV 28240 GTITVWVVI 1 291LVSNIARRL 818 VAGTITWV 899 DGNRVTLDL 1 3 GITIKEPL FAVLLACW 52| IPNKSLTTA 362NPVNDVVL NAPLFPAV 88 GARIDREKL 18 374IPLNTKAL LPAAVDPDV 117 DEIFRLVKI J IPFRRPVF 5 FPQRSSTAI 138 LFPATVNI I 415 LLETAY TPNHKLLVL 336 PARAMVLVN 18 599 YGDNSAVTH 15 VPSIDIRYi 380 IALITVK 18 623 GVIRPNISF APVTPNTEI 3 [3891 DADHNGRVT LFSWVNL 805 SPTSYVK RPVFSNQFL 777TNATLNEL 1PATVNISI |PPLNQSAML 18061 PTSOYVKIL [1 6]AAVDPDVGI l 586 |HGTVGLITV ~ SGTITWI HPVFKETE 601 DNSAVTLSI 0NLLLNFVT (PLNTKIAL 760| DSLFSWV ] 9EEQTMGKYN 475 IPENNSPG814 LVVAGTI 9 SKIQEL 1SPGQLTKV 9661 LPLDNTFVA 69 PG1VVFQVI 9961 YPVTFEVP Table XXXMIl-109P1D4 7 PDSLFSW 171 NGVQNYELI :8] v.1-85101-9-mers 16AVAGTITV 2347 1DVNDNVPSI7 Each peptide Is a ______ _____ portion of SEQ ID NO: 6 NPVNDTWL|21 43AADAGKPPL1 3; each start position is 795TPNTEIADV | 4 |DAGKPPLNQ specified, the length of A T 91 TVVV |2 |iVPPLTSN E peptide is 9 aminoTGDVPLIRI | 822 | ITVVVVFI acids, and the end :69: F8-22 17U position for each D21T3YVMKV 20t80] NLLLNFVIl peptide is the start 335 MPARAMVLV 5 SGTYFAVL position plus eight 4:: 39 46GPNAKINYL jJ 139 FPATVINIS | 136 APLFPATV177 NATLUNELV 20 208~ |DREEKDTYV 16 G16A AKYI 2698 DPYSVSDCG| 20 232 |TAILQ VS VT 16 :G7:8: F20ff 185 Table XXXJIII-109P1D4 Table XXXIlII-109P1 D4 Table XXXIllI-109P1D4 v.1-B5101-.9-mers v.1-835101-9-mers v.1-B5101-9-mers Each peptide Is a Each peptide is a Each peptide is a portion of SEQ ID NO: portion of SEQ ID NO: portion of SEQ ID NO: 3; each start position is 3; each start position is 3; each start position is specified, the length of specified, the length of specified, the length of peptide is 9 amino peptide is 9 amino peptide Is 9 amino acds, and the end acds, and the end acids, and the end position for each position for each position for each peptide is the start peptide is the start pepide is the start position plus eight. Position plus eight. position plus eight 8RAMVLVNVT [ 800 LADVSSPTS 1 742 TDLG-LHRVL 14 404 IPFRLRPVF 18171 AVAGTITV 759| PDSLFSVI4 492DADSGPNAK16 1003|VPVSVHTRP 1 768 |VNLFVNESV 14 508 DAPPEFSLD 1630 IREEMPENV 14 895 DVDSDGNRV 14 516 DCRTGMLTV 1 72 VPLIRIEED 4897 DSDGNRVTL 520 GMLTVKKL 16 83 EIFTTGARI 1 PPSNCSYEL 156 SKYTLPAV 14 Table XXXIV-109P1D4 7 LGLHRVLVK 16 161 PAAVDPDVG 14 v.1-A1l-10-mens 79I EAPVTPNTE 6 182 QNIFGLDVI 14 Each peptide is a VE 1 poon of SEQ ID NO: 973 16C211S14 3; each start position is TTFEVPVSV 1258 IPENAPVGT specified, the length of 'K, JDWLSG-TY1115peptide is 10 amino [ MDLLSGTYI 276 ADIGENAKI acids, and the end 14 |LACVVFHSG 15I328 ILASDGGLMP 14 position for each peptide 34 |MPENVLIGD 15 4 |LMPARAMVL Is the start position plus 59 TAMQFKLVY 15 340 MVLVNVTDV 14 mne. 67 YKTGDVPLI 1 361 VNPVNDTVV [2 DREKLCAGI 15366 |DWLSEN LTAYLDY D73 1 IPENSAINS j ENIPLNTKI 14 423 E 28 176 YELIKSQNI 15 2AAYLDYEST 14 YDYESKEY 18FGLDVIETP 426 YESTKEYA 14 F9K1DEE KY 8MPQLIVQKE1 YAIKLLAAD DLG KY 2 NAPVGTSVT LAADAGKPP DA14 EK Y APVGTSVTQ VFTQSFVTV EDREEK Y 2 275 DADIGENA TQSFVTVSI 306 DSREEDT 313EPLDREETP ADSGPNAKI VPDYG S 356 DIRYVNPV APPEFSLDC 14 673 2VP Y SIVNPVNDTV 15 11TILAKDNGVFP 1P4SCSY| 1pJSAMLFIKVK j51LAKDNGVPP 1[i7JDIGMNAEVRY|1~ 17 CRTGMLTVV 15579 VPENLPRHG 1 807 TDYVKjLVA 532 9 w 1 985 2SPS~SC11 532 KEDKYLFT[ 15 PRHGTVGU SADPYVi 2 15521 SNVVFVSI 597 PDYGDNSAVA 14AVDPDV.GING2 DPYGNS 251NDFETEIEVSIPE |20 596 DPDGD NSA 15 610 1LOENDOFTI IiI56NPFH E 1 KAEDGGRVS [ 617 TIDSQTGV 14 SPV Y 707 MNAEVRYSI|E es6 VNDNKPVF F930 LA.RHY 727 DQETGNITL 51 6 5AVDNDTGM 14 115 EDFLVK PENSAI1SK 186 Table XXXJV-109P1D4 Table XXXV-109P1D4 Table XXXV-109P1D4 v.1-A1-10-mers J jv.1-A0201-10-mers v.1-A0201-10-mers Each peptide is a Each peptide is a portion Each peptide is a portion portion of SEQ ID NO: of SEQ ID NO: 3; each of SEQ ID NO: 3; each 3; each start position Is start position is start position is specified, the length of specified, the length of specified, the length of peptide Is 10 amino peptide is 10 amino peptide Is 10 amino acids, and the end acids, and the end acids, and the end position for each peptide position for each peptide position for each peptide is the start position plus is the start position plus is the start position plus nine. nine nine VIDTNDNHPV 1 VLGDLLKDL LIPNKSLTTA I |273FAIDADIGENA 18 113 AIlPDEIFRL 28 E AMQFKLVKT 20 45VIDVNDVPS 8YlFAVLACV AILQVSVTDT |2 29| TKEYAIKLLA 1819GINGVQNYEL 25~NLVSN!ARRL |I 71VIDLGL-IRVL 18 42DLLKDLNLSL 2 48STKEYAIKLL 20 S2EAPV4PNT 1LLKDLLSLI LAADAGKPPL 81DSDGNRTLD KSQNIFGL 24 IIDQNNSPV 0 19F8SGAQEKNY 17GLMPARAMVL 24 62GTVVFQVIAV 20 [J FYEVEVAILP AMVLVNVTDV 24 LGQPDSLFSV20 38VDKDAHNG 609ILDENDFTI 24 16 AAVAGIVV 0 FIDHEIPFRL 10SUPNSLTT 2 VVVIITAV [ 0DBEIPFBLRP 156SLTTAMQFKL 23[62IQELPLDN~T [2 797 EIADVSSP 1ILPDEFRLV 23 LVYKTGDVPL| ~JTLDLPIDLEE 1735LLVLASDGGL 231 CFYEVEVAIL |] IDLLKDLNL i 5 NLPRHGTVGL FLIEDINDNA | 4 LKDLNLSLIP 1VLPSTPGT SIPENAPVGT [9 DGINGQNY 1LMEKCDVTDL 2KHFSESNLV [19 1EGDKMPQLIV 1176VTNATLINEL 2335IDIRYIVNPV |9 ASDGGLMPAR 137PLFPAIVINI 360IVNPVNDV 9 SLDCRTMLT LMPARAMVLV2 373 NIPLNKIAL 19 F1VETHNEYNFY 1YVNPNDTV FTILADNGV 19 50GLITVTDPDY 1144SIPEN!NSPGI [| 65 SSAKVIINVV 19 81ADVSSPISDY 1674SIVGGNTRDL 22 767 IVNLFyNESV |9 812 KILVAVAGT 22 VAVATITV 19 Table XXXV-109P1D4 1813 ILV AGTI |9 TITVVVIFI |9 v.1-A0201-10-mers 817 AVAGTITVV 22 TIEETKADDV | Each peptide Is a on 882 LLNFVIIEET KTGDVLIRI 18 of SEQ ID NO: 3; each E1NSINS 1 ~jJVPVIG 8 start position is | EG specified, the length of TLPAMDPDV 21APVGTSVTQL| peptide Is 10 aminoNIFGLVIET SNIARLFHL acids, and the end 183E_[--11 position for each peptide 541|LAKDNGVPPL 21 2 LNATTLTI 18 is the start position plus GMNAEYRYSI 21 VLSENIPLNT 18 nine E 79 VTPNTEIADV 21IPLNTIALI |LLSGTYFAV |18 VAGTIIVVVV |2 HEIPFLRPV 18 |I SLF~yVN |9 TIREEMPENV|20 4~ NSPGIQLTKV 18 171F3 VMV] F8

J

187 Table XXXV-109P1D4 Table XXXV-109P1D4 Table XXXV-109P1 D4 v.1-A0201-10-mers v.1-A0201 -10-mers v.1-A0201-10-mers Each peptide is a portion Each peptide Is a portion Each peptide is a portion of SEQ ID NO' 3; each of SEQ ID NO: 3; each of SEQ ID NO: 3; each start position Is start position is start position Is specified, the length of specified, the length of specified, the length of peptide is 10 amino peplide is 10 amino peptide is 10 amino acids, and the end acids, and the end acids, and the end position for each peptide position for each peptide position for each peptide is the start position plus is the start position plus is the start position plus nine nine nine 482 GIQLTL<VSAM 18 MjPVFTQSFVTV 16 230 F SSTAILQVSV |J 549 PLTSNT 18 [ SLDCRTGMLT 16 265 GTSVTLHAT| 5 650 RVSRSSSAKV 18 519 TGMLTVKKL 16 275DADIGENAKl |[ AKV T NVVDV 18 540 ILAKDNGVPP 16 [328 LASDGGLMPA1 15 7 DVTDLLHRV8 559 SIIDQNDNSP 6 332 GGLMPARAM 1 780 TLINELVRKS 18 585 RHGTV UTV 16 346TDVNDWVPS LINELYRKST FTIDSTGVI 16 379 KIALI1VTDK 15 LVRKSEAPV 684LVLPSTNPGT 16 FTDHEPFRL 2VLLACVFHS 17 TNPGTVVFQV 16 35KLLAAAGKP| 131 LLACVFHSG 7 VIAVDDTGM 16 56VKDENDNAPV DNAPLPATV 1 FADQETGNI 1 AMDADSGPNA 15 7NISIPNSAI 7 7 DQETGNITL 2DADSGNAK PARAMVLVNV 17 742TDLGLRVLV 16 LDCRTGMLTV LNTKIALITV 17 44 LGLHRLVKA VPPLTSNVV 15 81ALITVIDKDA VIVNLEVNES 570 FTHNEYNFYV15 PLNQSAMLFI 7 DYVKILVAV 16 642 YVKAEGGRV5 66FTQSFTVSI 827 VHFTARC 6 665 DVNDNPVFI 5 95SGPNAKINYL 17 VVRCRQAPHL 6 66 VNDNKVFIV 3YLLGPAPPE 1SPKN NFV 16 6 STNPGIFQ15 04LLGPDPPEF 88 NLLLN IE GGNTRLFAI15 608 SIDE FT 881 LLLNFIEE 725 AIDQEGNIT 732 NITLMEKDV 81 VDSDGRVTL 741 VTDLGLHRVL 734 TLMEKCDvTD 1TMGKYWVTT 745 GLHRVLVKAN 825 VVVIFITAVV TFKPSPDL 76 NLFVNESVTN 98VTFEYPVSV 17 91SASPQPAFQI 819 AGTOVVVI15 ~IRIEEDTGEI D~ LLSGIlFA Is 8791 KNLLLAFVl ~ 1IFRLVKIRFL 16 GTYIFAVLLA Ls97NSKHHJIQEL f JJAINSK(YTLPA 16 21SGAQE NYTI WI982|SSSSSPYSV jj 12STAILQVSVT 146DLNLSLIPNK 1 994|CGYPVITFEV II VTDTNNHPV 16IDREKLCAGI 1HLNATGLIT VKIRFLIEDI 5 Table XXXVi-109P1D4 ETPNHLLVL L1151NSAINSKY'TL 151-020-1-mers 351NVPSlDIRYI 1 8 SQNIFQLDVI 1 SIDIRVNP 16KMPQLIVQKE 15 FLLETAAYLD 16 85 QRSSTALQV 188 Each peptide is a portion Table XXXVI-1 09P1 D4 Table XXXVI-1 09P1 D4 of SEQ ID NO: 3; each v.1-A0203-10-mers v.1-A0203-10-mers start position is Each peptide Is a portion Each peptide is a portion specified, the length of of SEQ ID NO: 3; each of SEQ ID NO: 3; each peptide Is 10 amino start position Is start position Is acds, and the end specified, the length of specified, the length of position for each peptide peptide is 10 amino peptide Is 10 amino is the start position plus adds, and the end ads, and the end nine position for each peptide position for each peptide is the start position plus is the start position plus INSKYTLPAA 19 nine nine 13 SIIQFLLETAA 1_ KEYAIKLLAA T29 FTEYAIL LLA I EDINDNAP 88SDYVKILVAA1 2 AG.KPPL!SQSA 113NDNAPLEPAT[] CEQAPHLKAA 1IVKDENDNA 1 NISIPESAI ~JSQGGLMPARA 1[4jPGIQLTEVSA 1!i GEPQRSSTAI [ 32YAIKLI4D 18A QITKVSAMDA 1!24iEVSIPENAP9 8YVKILVAAVA 1490 AMDADSGPNA 10i]GISVTOLHAT9 NSKYTLEAAV 1KIYLLPDA 10 VIQLHAIDAD 44NQFLLEIAAY 1753EDKYLFILA 10 71TDADIGENAK 9~ 31 EYAIKLLAAD T9PDYGNSA FSNLVSAR []DYVKILVAAV 17 66QESYTFYVKA 10 9JARRLFHLNAT 9~ 87RQAPHLKAAQ 1768GGRVSRSSSA 10 2JP1NHKLLVLAS[j DLSGTYFA 1PTVVFVIA 1 5 ADGGLMPAR W GfIlFAVLLA 1 JAMDNDTGMNA 10 8JDOGLMPARAM 9 111LACVVFHSGA Fo 76VGGNTRDLFA 10 7]N!PLNT1KIAL E 1LPNKSLTTA 101LFLHR7V LTVTDKDAD 80DIGEFIGA LENESNA 10 425 DYESTKEYA 8ARIDREKLCA 0 i1NELVRKSTEA 10I1AIKLLAADAG [ ~i]EHCFYEVEVA ~o72AEVTrPNEIA 1 G1 PPLNQSAM ji]FLIEDIN~DNA (fl87TSDYVKI!LVA 10IJKyKDENQNAP 12NDNAPLFPA [ 2 TVVVVIEITA |10 l~]GIQLTKYSAM E iN]l~ISIPENSA 1083 IIAVVRCRQA|E0Oj LTKVSADAD E 13A!NSKYILPA Ifl85RCRQAPIILKA|1 4! MDADSGENAK|E GGFPQRSSTA 6 QKNKQNSEWA19 INYLLGEDAP 23EIEVSIPENA [ ~ I]NEVTIEETKA 10 DKYLFq~ILAK~ |f VTSVTQLHA 97TEKPDSEDLA 1 DEDYGDNSAV| 2 STQLHATDA 933 PLARHYSA| 10 63 EYTFYYKAE9 ATDADIENA 8HKSASEQPA|10 MGBVSRSSAK 27SFSNLVSNIA 95ELPLDNIFVA 10 1692 GIVFQylAVII 0LLSGTYFAV |] 701 VRNDTGMNAE 30TENHKLLVLA 107~ TYIFAVLLAC 9[ 77 G§NTRDLFAI E FLASDGG PA 11AVFHGAQ GLHRVLVKAN 9 ENIPLNIKIA 52 IENKSLITAM 771 FNESVNAT | 31 ALITVTDKDA 1TEFTGAR 784 ELVRKSIEAP 9 49| FSNQFLLETA 10RDREKCAG PVTPNTEIAD 9 144 LYESTEYA 1HFYEVEVA[ VILVAVAG 3 R

I

189 Table XXXVI-1 09P1 D4 Table XXXVII-109P1D04 Table XXXVll-109P1D4 v.1-A0203-10-mers v.1-A3-10-mers v.1-A3-10-mers Each pepUde Is a portion Each peptide is a portion Each peptide Is a portion of SEQ iD NO: 3; each of SEQID NO- 3; each of SEQ ID NO- 3; each start position Is start position Is specified, start position is specified, specified, the length of the length of peptide is 10 the length of peptide is 10 peplide Is 10 amino amino acids, and the end amino acids, and the end acids, and the end position for each peptide position for each peptide position for each peptide is the start position plus is the start position plus Is the start position plus nine nine nine W_ iFTAV |[46 DLfLSLIPNK 21464 PVETQSEVTV [8 VwFJTAV 2 201 KVEDGGFPR2150450 LLGPDAEPEF 18 TAWRCBQAP 3 GLPARAMVL RTGMLVKK B1 84 KNKQNSEWAT 3 KL GKP[2 VIEPNLFDR 1 77QVAVDTM!G|2 KVIIN9y9DVN 18 FKPDSPDLAR QAH Q 838 21K| 674 IVEPSNSYE |8 3DARHYSAS 64 KLVYKT.DVP700 AVNDIGMNA| 9391YKSASPPAF PL1RIEDTG 769 NLFVNESVN [| :L]LDNTVAC REEDTGEF 202 VVF8F5W 18 Table1 DKMPQJVQK jj MIMMKKKK K v.1-A3-10-mens f3_6_0V D9 EI _ Each peptide Is a portion 1478 NN2PG0LTK 934 DLARH SAS of SEQ ID NO: 3; each [487 KVBAMADSG 20 4 DLLKDLNLSL start position is specified, __ _ the length of peptide Is 10GIERD CFY amino acids, and the end T523 VVKKLQREK 121 RLYKIBELIE position for each peptide [40 ILAKDfOVPP 20 17 DVGINGVQNY[ is the start position plus R nine 65-0R1 RSSK 20 27011 IA1A 7 77 ATLINLVRK 20 308 LIIKELDR DLHLK116 2 CVFH.SAQE 19 1PLREEPNH F 1 FITAW 28 11 LPQEIEFLVK [19 4031 EIIFRLRPVF RLPVFNQF AVDPDING 19 |3IKLLMDAG 17 D78 VFEED 209 REEKDTVMK 19 448| QSAMLEAKVK 17 A LDETK 25 417! LLTAYLDY |19 503 YLGPPPE|17 421 AALYET 25 DYFJA(fg AVL~yFi2I34D LFJA |5I9] MLIVVELDR 17 SLAPNKELTT 24 GL TVI2PDY 19 521TINGV |17 9 LII TK 617 TIDSQIGVIR 19 6GVPPLTSNVT17 817AVGTIW24 623 GRPSFD 9 NLERHgIVGL 17 W7EHSAQEK 673 PPSSCSY 6 ILDENDFI |17 206 ELDREEKDTY -GGNTDLF 1 635 |KQESYIYVK 7 32AWRCBQAPH 23 TLMEKVTD 191 7YVAEGGRV 17 QLVQELDR 2 65 LVKTVPL 198 693 | TVYF(LAVD |17 298 RLHLNATTG 218 KVVEDGGFP 6941 WEQV EVDN|7 7KlQREDKY HLjATIGLIT 8 750_ LV1ANLGQP 7 1 810 YVKilyAVA 1 LVLASDGLM 18 7651 WVNLEVNE | ILMAAAGT7 VLSD32LMP|18 803 VSSPTSDYVK| IMK j8G |[. 814 | LVAVATIT |7F 190 Table XXXVII-1 09P1 D4 Table XXXVII-1 09P1D04 ITable XXXVIl-109P1D04 v.1-A3-10-mers v.1-A3-10-mers v.1-A3-10-mers Each peptide is a portion Each peptide is a portion Each peptide is a portion of SEQ ID NO: 3; each of SEQ ID NO: 3; each of SEQ ID NO: 3; each start position Is specified, start position is specified, start position Is specified, the length of peptide is 10 the length of peptide Is 10 the length of peptide is 10 amino acids, and the end amino acids, and the end amino acids, and the end position for each peptide position for each peptide position for each peptide is the start position plus is the start position plus is the start position plus nine nine nine 8701 KK SPK|7 1 | IPENSANSK |] | FLIEDINDNA 11 9Q49 QPEIELNS 17 11561 SKXYT1.AAVD 1 142 TVINISIPEN |1 37NVLIGDLLKD 257 SEENAEVGT 53AINSKYLPA RI1RE6LCAG 1 267 SVTQLHTDA EKDTYVMKVK|I KLCAGBPRDE 12761 ADJGENKH 23311 AILQVSVTDT 1 5]EVAILPDEF 16 315DEEIENHK EVSIPENAPV 14 113 APD1 FRL 16 3KiLVLASDGG 63 PVTSVQL 4 ILVSMDT 16 341 VNVIVND 354 SIDIRYVNP 24DT1NNVFK NVIDVNDNVP 8 4 TVIDKFADHN 291 LVNI6RLF 347 DVDNMESD 395 RV1CF4HEI 4 340 MVLVNV5DVN 16 DIYlVNPVN MDADSHENAK 14 363 PVDTLSE 1 VLSENLNT 1 KINYLLGPDA [3P7 I IT LSNIELNTK 5 [PLSN VFV -8" ALTVIKDA 7KDENDPVF 1PVETHEYNF 14 4161 FILLET FYLD 16 514 SLDCRIMLT 15 AVTLSILDEN 4 423 YLDYESKEY 559 SIDQNSP 649 GRVSRSSSAK [436 LA 1KPP 6RPISEDREK 10EVYSVGGN 455 KVDENDNAP 644KADGVSR 15 725 AlDQE4GNIT 484 QLIKV 6MDA 1 671 PVEIVPSNC 1GLHRVLVKAN 526KKLDREDK 684 LVLPSIPGT 780TLINELRKS 665DVNDNVFI 16 761 SLESVYVNL 15 78 ELRKIEAP 685VLESTEGTV 16IVNLFESV PVTPNTEIAD 14 712RYSIVNTR 6859 PENRC9]MMK EADVPTS [722 DLEAIQETG L6 8621 RCMIMM!9KKK[& 83 T\&VVITA [48 |RVLVKAFDLG 5QMMM!KKK VR RQPHLK 414 764 |SVVNLFVN 16 HIQEETELNSK 15 [60 ENHQMMMKK 785 |LVKSIEAPV 6HIQELELDN 89KNLNEVT 14 812 KILVAAAGT 965 ELELD2IHFVA 15 [880 NLLLNEVTIE 833 VVBCRAPHL 6 1004 PVVHIPVG 15 LNEVTETK 902 RVILDLEIDL 1 1011 PVIQVSNTT 15 DVSDGRVT 684] 909 IDLEEQIMGK 1612 14VC FHS 1 904 TLLPJQLEE 1 FlSVDCQPVT 6 36 ENVLIGDLLK 14 906 DLEIDLEEQT 1M [381 VLGDLLKDL 5 51 LIENKSLTTA 14 [9671 PLNTEVACD1 E LLEDLNLSLI 15AMQELV|14 9971 TF1ACDSISK 4 555 KSLTT1MQFK 19TAMQFLYKl FVACDSKC| 14 18EERLYIRF 14KRFLEDIN 1 SISKCSSSSS 19 191 Table X)Vli-109P1D4 ^Table XXXVIll-109P1D4 Table XXXVII-109P1D4 v.1-A3-10-mers v.1-A26-10-mers v.1-A26-10-mers Each peptide is a portion Each peptide is a portion Each peptide Is a portion of SEQ ID NO- 3; each of SEQ ID NO: 3; each of SEQ ID NO: 3; each start position is specified, start position is specified, start position is specified, the length of peptide is 10 the length of peptide is 10 the length of peptide Is 10 amino acids, and the end amino acids, and the end amino acids, and the end position for each peptide position for each peptide position for each peptide is the start position plus is the start position plus is the start position plus nine nine nine [97 PVITFEVPVS 14T58 TAMQFKLVY20 761 SLFSWIVNL | 191 ETPEGDKMPQ V833 WRCRQAPHL ILB Table XXXill-109P1D4 213 DTYVMKVKVE 20 ETPLNSKHHI 18 v.1-A26-10-mers EVSIPENAPV EMPENVLIGD 17 Each peplide is a portion DVNDNVPSID 3AILPDEFRL of SEQ ID NO3,each:3:] VD-PSIlE2 start position is specified, 366DTWLSENIP 20 178 UKSQNIFGL the length of peptide is 10 4DSGPNAKINY 20 241 DTNDNHPVFK| amino 'adids, and the end r5 TVSIDN(]2APVGSVQ [D position for each peptide 55 F VSilDPQN APVTSVQL| is the start position plus 6293 SNIARRFHL1 nine __________ n737 EKCDVTDLGL 26 363 PVNDTVVLSE 17 DGG N776 VTNATLINEL 5 VVFVSIDQ E ETPNHLV 930 RVTLDLPIDL 632 DREKQESYTF17 ~i28 EVPIF 999 TFEVPVSVH 2C 714SIVGGNTRDL [ 11 EEVPVSR C 775[ SVTNATLINE EFRLVKIRF 142 TVINISIPEN 809 DYVKILVV 17 704 DTGMNAEVRY ETEIEVSIPE 9 TVVVVIFITA 17 188DVIETPEGDK DREETPNHKL WFHSGAQE 6 710EVRSVGGN 623 GVIRPNISFD 9 32EEMPENVLIG 16 1993EVEVAllPDE 2 665DVDNKVl NVLIGDLLD 16 350DNVPSIDIRY 24 TFQVVD VGDLLKDL 16 367 LSENIPL SWVNLFVN DEIFRLVKIR SDVTDLGlRV 802 DVSSPTSDYV 19GVQNYELIKS 6 401GTTWVVF 824 VVFITAV [ IO] EEKDTYVMKV 16 DIGENAKHF 3 DVDSDGNRVT 19 309[ ITIKEPDRE 428 STKEYAIKLL 23 97 |DPYSVSDCGY 19 FTDHEPFRL | ETKDDDS 23 H42 DLLKDLNLSL 4[il0PVFSNQFLLE(6 L7-1 DVPLIRIEED 65 LVKGDVPL 18 [522 1L RE |I 130EDINDNAPLF [I DTGEIFTTGA 1 529 |DREKEDKYLF| 403EPFRLRPVF 83 EIFTTGARID 1 531 EKEDKYLFTI 6 PVFTHNEYNF 22 291LVSNIARRLF 8 612 ENDDFTIDSQ IM 9 ETGNITLMEK |2412 ETAAYLDYES 18 662NWDVNDNKP 9 DLEEQTMGKY2 461 DNAPVFTQSF 74 DLGLHRVL 16 6 ELDREEKDTY21 574 EYNFYVPENL 1750 LVKANDLGQP 427 ESTKEYAIKL 21 598 DYGDNSAVTL 8 799 EIADVSSPTS SDNSAVLSIL |21 [6921 GTWFQVIAV ADVSSPTSDY||6 9 |TTFKPDSPDL|1 IVGGNTRDLF I8 [J nWvVIFIT |6 192 Table XXXVIII-109P1D4 |Table XXXIX-109P1D4 Table XX)IX-109P1D4 v.1-A26-1D-mers v.1-B=0702-10-mers v.1-B0702-10-mers Each peptide is a portion Each peptide is a portion Each peptide is a portion of SEQ ID NO: 3; each of SEQ ID NO: 3; each of SEQ ID NO: 3; each start position is specified, start position is specified, start position is specified, the length of peptide is 10 the length of peptide Is 10 the length of peptide is 10 amino acds, and the end amino acids, and the end amino acids, and the end position for each peptide position for each peptide position for each peptide Is the start position plus is the start position plus is the start position plus nine nine nine _ I _ _ _ _ I | [972 FVACDSISKC 16 547 VPPLTSNVTV F1 160LPAAVDPDVG I1006SVHTRPVGIQ 16 596 DPDYGDNSAV 18282| AKIHFSFSNL3 16761 PPSNCSYELVI 18 33EPLDREETPN 3 Table XXXIX-109P1D4 [56 TPNPENRQMI18 3331 GLMPARAMVLI13 v.1-80702-10-mers QPAFQIQPET18 362 NPVNDTVLS[3 Each peptide Is a portion 3VPVSHTRPV [ 437 |LAADAGKPPL[1 of SEQ IDNO3; each 1031[VVTV18F3113 start position is spedfied, 1139 FPATVINISI 17 SPGHQLTKVS the length of peptide is 10 []VELR TI17 54 ADGPL13 amino acds, and the end 579VEL PRHGT LAKDNGVPPL| position for each peptide 877SPKNLLLNFV 17 582 NLPRHGTVGL13 Is the start position plus 72 VPRIEEDT 598 DYGDNSAVTL13 nine 4 PPLNQSAMLF 6 601 |DNSAVTLSIL 1 PPEFSLDCRT 6 667 PSNCSYELVL 2 APVGTSVTQL 2 NPENRQMIMM 4SIVGGNTRDL TPEGDKMPQ907 LPIDLEEQTM 6 LEKCDVTDL1 1226 FPQRSSTAll TPLNSKHHIl 1 37 KCVTDLGL|3 EKPPLNQSAML 5LPDEIFRLVK 1 [3 ANDLGQPDSL 506GPDAPPEFSL 22APLFPAVIN RCRQAPHL 52 PNKSLTTAM MPARAMVLN KKHSPKNLLL E8i 409[RPVSNFLL KEDKYLFT9 KPDSPDLARH 1GPNAKINYLL 21 817AVAGTIVVV 805 SPTSDYVKIL 21 896 VDSDGNRVTL15 Table 34MPENVLIGDL 20 LSGYFAVL

XL

8MPQLIVQKEL 20 IGDL4DLNL 109P1 4 7____a ]__E v.11-13B 67 VPPSNCSYEL 65 LKTGDVPL14 10-mers 686 LPSTNPGTVV 119 IFRLVKIRFL 75 QPDSLFSVVI IEDINDNAPL4 No 20______ Results 100RPVGIQVSNT 319 ETPNHKLLVL Res Fuds [52 VPSIDIRYIV 361 VNPVNDTVVL Found. APVFTQSF IPFRLRPVFS Table [48 PPLTSNVTVF 1 SDGNRWL

XLI

583 LPRHGTVGLI 947 AFQQPETPL 109P1D4 6 1 1fl 9v.1 NPGTVFQVI 959 KHHQELPL 14 81510 792 9AP PNTEA 1 966 LPLDNTFVAC 10-mers 996~ |YPVTFEVPV 194 ~ DLLKDLNLSL I 0 TPNHKLLVLA 1 IPRDEHCFYE 3 No 374 |IPLNTKALI 18 113 APDEIFRL E 3 Rul 193 Found. Table XLIV-109P1D4 Table XLIV-109P1D4 v.1-B4402-10-mers [ v.1-B4402-10-mers Table Each peptide is a portion Each peptide Is a portion XLIl- of SEQ ID NO: 3; each of SEQ ID NO: 3; each 109P1D4 start position is specified, start position Is specified, v.1- the length of peptide is 10 the length of peptide is 10 B2705- amino acids, and the end amino acids, and the end 10-mers position for each peptide position for each peptide is the start position plus is the start position plus nine nine No Results Found. REKQESYFY 20 61 ELDREEKDTY I 110 VEVAILPE 19 j EEKDTYVMKV 15 Table EEMPENVLIG 1291 LVSNIARRLF xl0 78 EEDTGEIFTT 18 293 SNIARRLFHL v.11- 130 EDINDNAPLF 390 ADHNGRVTCF 1 B2709- HEIPFRLRPV18 403| EPFRLRPVF1 10-mers |AEVRYSIVGG [407| RLRPVFSNQF1 38| VLGDLLKDL 1427]| ESTKEYAIKL No 282 AKIHFSFSNL 430]| KEYAIKLLAA 17s] Found. 318 |EETPNHKLLV 17582 NLPRHGTVGL 3191 ETPNHKLLVL 18961 VDSDGNRVTL Table XUV-109P1D4 14141 NQFLLETAAY 17 941 |SASPQPAFQ 1 v.1-84402-10-mers 428 | STKEYAIKLL 7 952| PETPLNSKHH 5 Each popbde is a portion | SGPNAKINYL 4 5 | SGTYFAVLL 4 of SEQ ID NO: 3; each _________ 19FS EKN j start position is specified, 761 SLFSV4VNL 19 | the length of peptide isl1 117 DEIFRLVKIR | MPENVLIGDL 14 amino acids, and the end EIFRLVKIRF 108 YEVEVAILPD position for each peptide [FJ EESPN(~ 12JKE8 RET 11 Is the start position plus 252 TE P 312K D nine 262 APVGTSVQL 1 NVPSIIRY 4 333 GLMPARAMVL 16 351NVPSIDIRYI 317REETPNHKLL 24 373 NIPLNTKIAL 16 361VNPVNDVL 4 476] PENNSPGIQL 235 TGMLVVKKL 3 IPLN4ALI 532KEDKYLFTIL 645 AEDGGRVSRS 397 TCFTDHEIPF R14 912EEQTMGKYN ANDLGQPDSL 423 YLDYESTKEY |4 73 YELKSQNIF 22 790 TEAPVPNTE 16 PPLNQSAMLF9 NESVTNATLI 9 820 GTITVVVV1F KDENDNAPVF 35 PENVLUGDLL F~I90PDSPDLARHY [461J DNAPVFTQSF|[4 [ GEFTTGARI 1 FEVPVSVHTR DSGPNAKINY | 9IEDINDNAPL QEKNYTIREE 15 [04 LLGPDAPPEF | [1491 PENSAINSKY 2NLSLIPNKSL 51 [PEFSLDCRTG 13PEGDKMPQLI 214 NKSLTTAMQF 15 527 [KLDREKEDKY|[~ 31 REEMPENVL 20 IFRLVKIRFL 5 548 PPLTSNVTVF :41 9[AGIPRDEHCF 2~0J2 VKIRFLIEDI 5~s 590 |GLITVI-DPDY 14 113 AILPDElFRL 20 PLFPATVINI 59 DYGDNSAVTL 14 [2791 GENAKHFSF IETPEGDKMP 7LSILENDDF |14 371 SENIPLNTK KELDREEKDT 616 FTIDSQTGV 1] 194 Table XLIV-109P1D4 Table XLiV-1 09P1 D4 Table XLIV-109P1D4 v.1-B4402-10-mers J v.1-84402-10-mers L v.1-84402-10-mers Each peptide is a portion Each peptide is a portion Each peptide is a portion of SEQ ID NO: 3; each of SEQ ID NO: 3; each of SEQ ID NO: 3; each start position Is specified, start position is specified, start position is specified, the length of peptide is 10 the length of peptide is 10 the length of peptide is 10 amino acids, and the end amino acids, and the end amino acids, and the end position for each peptide position for each peptide position for each peptide is the start position plus is the start position plus is the start position plus nine nine nine 67 PSTNPGTVVF 531] EKEDKYLFTI F2 | FPQRSSTAL| 2 714]1 SIVGGNTRDL 566] NSPVFTHNEY 11 240| TDTNDNHPVF| I EKCDVTDLGL 14 5681 PVFTHNEYNF 13 250 KETEIEVSIP | 71VTDLGLHRVL 14 573 INEYNFYVPEN 13LFHLNATTGL [12 74NDLGQPDSLF| [4 574 | EYNFYVPENL tI30]FHLNATTGUI |I2 1LFSVIVNLF 6111 DENDDFTIDS 2 LNATTGUTI |1 VTNATUINEL |[ 6301 |SFDREKQESY [f[36]DREETPNHKL|[$2 :EADVSSPTSDY 636| QESYTFYVKA [ TVLSENIPL 85] SPTSDYVKIL 14 | FIVPPSNCSY 399 FTDHEIPFRL | 89AGTITVVVVI 14 715 |lVGGNTRDLF 1 417 ILLETAAYLDY |1 85AQKNKQNSEW 14 724 |FAIDQETGNI [i1426 IYESTKEYAIK 12 89PENRQMIMMK 14 (728 | QETGNITLME 3~ 528 LDREKEDKYL [12 SKKKKHSPKNL 14 [47 | HRVLVKANDL 13 541I LAKDNGVPPL |i9 SKNLLLNFVTI 14 [798]| TEIADVSSPT [3 561I IDQNDNSPVF [~ 898 SDGNRVTLDL 14 .[80411 SSPTSDYVKI [3 |9[PENLPRHGTV|12 97NSKHHIlQEL L~ 8731| KKKHSPKNLL 13 601 |DNSAVTLSIL 12 64QELPLDNTFV [4 874 KKH-SPKNLLL 13 SRSSSAKVTI 12 F SDCGYPVTTF [14 8761 HSPKNLLLNF 3 [64VDVNDNKPVF1 1012 VGlQVSNTTF [4 889 EETKADDVDS ( 677[ PSNCSYELVL lMDLLSGTYIF 13 902RVTLDLPIDL 1 | NPGTVVFQVI IILSGTYFAVL 1P 93 |J1YKSASPQPAF [3 |17 GGNTRDLFAI 2~ 1J[FAVLLACVVF [P 1947]| AFQQPETPL W3 72 IDQETGNITL 2~ 40[IGDLLKDLNL [f 953]| ETPLNSKHHI Ldi 736 |MEKCDVTDLG 56SLTTAMQFKL 963 |~J IQELPLDNTF [173NELVRKSTEA [9 87TGARIDREKL L3 [30 |[ IREEMPENVL P2 5 TPNPENRQMI [92 [105]| HCFYEVEVAI [ 21| DLLKDLNLSL [P1IEETKADDVD 2~ [135 | NAPLFPATVI |1 [58 | TAMQFKLVY 1291LEEQTMGKYN 2 178LIKSQNIFGL 13 KTGDVPURI 1 2YNWVPTF 1 MPQUVQKEL |3 75 | IRIEEDTGE T9TFKPDSPDL ~!IVEDGGFPQRsI 773 _ IEEDTGEIFT 11199 KIH~IIQELPL 9 254tf IEVSIPENAP (3 (93f| REKLCAGIPR [fJ90KCSSSSSDPY [j9 01 NLVSNIARRL [ GIPRDEHCFY 14151| QFLLETAAYL 13 111 | EVALPDEIF [2 Table I 443 |KPPLNQSAML 145| NISIPENSAI |F7 XLV 2DENDNAPVFT | NSAINSKYTL |2 8v819.D 91 FSLDCRTGML_ TPEGDKMPQLF B501 - 195 10-mers Table XLVI -1 09P1 D4v. 1 -DRB1 Table XLVI -109P1D4v.1-DRB1 0101- 15-mers 0101- 15-mers No Each peptide is a portion of SEQ Each peptide Is a portion of SEQ Results ID NO: 3; each start position is ID NO- 3; each start position is Found. specified, the length of peptide is specified, the length of peptide is 15 amino acids, and the end 15 amino acids, and the end position for each peptide is the position for each peptide is the Table XLVI -109P1D4v.1-DRB1 start position plus fourteen start position plus fourteen 0101- 15-mers Each peptide is a portion of SQ [41 GDLLKDLNLSLIPNK ||25 712]| RYSVGGNTRDLFAI ||24 ID NO: 3; each start position is _________________g5[ l LHVLKAD7G7P7 specified, the length of peptide is 62 QFKLVYKTGDVPLIR |251 74 |GLHRVLVKANDLGQP |41 15 amino acids, and the end 10411 EHCFYEVEVAILPDE |2f |760|[ DSLFSWIVNLFVNE ||24 position for each peptide Is the 176 | YELIKSQNIFGLDVI 251 822][ IWVVVIFITAVVRC |24 Start position plus fourteen VMKVKVEDGGFPQRS25 885 FVTIEETKADVDSD 80811 SDYVKILVAVAGTI 36 223 DGGFPQRSSTAILQV |51 900|| GNRVTLDLPIDLEEQ ||2 7 || TYFAVLLACWFHS ||34 [9 ARRLFHLNATTGLT |25 |919| |YNWVTTPTTFKPDSP||24 265||l GTSVTQLHATDADIG | 325| LLVLASDGGLMPARA g|5 975 |CDSISKCSSSSSDPY 124 48211 GlQLTKVSAMDADSG [3 3 5ARAMVLVNVTDVNDN |25 3 || LLSGTYIFAVLACV |2 498J1 NAKINYLLGPDAPPE |33 433 | AIKLLAADAGKPPLN ||25 45fl KDLNLSLIPNKSLTT |2 285]| HFSFSNLVSNIARRL |32 434 | IKLLAADAGKPPLNQ | [78fl EEDTGEIFTTGARID |23 173| VQNYELIKSQNIFGL |3 1 580| PENLPRHGW2GLITV ||25 1 IEDINDNAPLFPATV 23 4053 PFRLRPVFSNQFLLE |30 |61 NDDFTIDSQTGVIRP ||5| 151| NSAINSKYTLPAVD ||2 117]| DEIFRLVKIRFLIED 2E | 6401 TFYVKAEDGGRVSRS||251 116711 DVGINGVQNYELIKS |23 155||NSKYTLPAAVDPDVG| 28 730]| TGNITLMEKCDVTDL ||51 [81 | NAKIHFSFSNLVSNI ||3! 2971 RRLFHLNATTGLITI |28 764[ SVIVNLFVNESVTN |15' 289][ SNLVSNIARRLFHLN ||23 F710] EVRYSIVGGNTRDLF 1|28 811l| VKILVAAVAGTITV 25' 342|| LVNVTDVNDNVPSID |23 797 NTEIADVSSPTSDYV |28 [925] PTTFKPDSPDLARHY 25! [349][ NDNVPSIDIRYIVNP 23 882|| LLNFVTIEETKADDV 281 936 ] ARHYKSASPQPAFQ |25 [370]1 LSENIPLNTKIALIT 23[ 945 _____ _ | F E K8 NYTIREEMPENVLG 24 J3791| KIALITVTDKDADHN |23 F94]1 QPAFQIQPETPLNSK 128J [iEK1[__________ [109| EVEVAILPDEIFRLV 27 46 |[DLNLSLIPNKSLTTA||24 5311| EKEDKY'LFTILAK(DN l|3 413| SNQFLLETAYLDYE 2 7411 LIRIEEDTGEIFTTG |24 5341| DKYLFTILAKDNGVP ||23 8071| TSDYVKJLVAAVAGT 27 116|1 PDEIFRLVKIRFLIE 24 [547] VPPLTSNVTVFVSII ||31 F-9011 RIDREKLCAGIPRDE |2 145| NISIPENSAINSKYT 24 630| |SFDREKQESYTFYVK |23| 105|| HCFYEVEVAILPDE 26 |322| NHKLLVLASDGGLMP 24 [4 fj GGRVSRSSSAKVTIN|23 1l-4-11| ATVINISIPENSAIN |32411 KLLVLASDGGLMPAR|24 663 3 WDVNDNKPVFIVPP ||3| 1871 LDVIETPEGDKMPQL 26 329ASDGGLMPARAMVLVI|24 66911 Ni PVFIVPP Y |23| 288|| FSNLVSNIARRLFHL | ~ 331|][DGGLMPARAMVLVNV [24 679| |NCSYELVLPSTNPGT ||23| 430[ KEYAIKLLAADAGKP 26 358 RYIVNPVNDTVLSE [2 [6801 CSYELVLPSTNPGTV 231 431 EYAIKLLAADAGKPP 26 472|1 TVSIPENNSPGnQLT |24 7821 INELVRKSTEAPVTP ||23 538| FTILAKDNGVPPLTS ||26 478 NNSPGQLTNSAM6 [24 8121 KILVAAVAGTWVV |23| 5721HNEYNFYVPENLPRH j|6 488| |VSAMDADSGPNAKIN| [2 819 AGTTVVwIFITAV |1|3 596|| DPDYGDNSAVrLSIL |26 499|] AKINYLLGPDAPPEF 2 821 TITWVVIFITAVR ||23 7381 KCDVTDLGLHRVLVK|26 [586 1 HGTVGLTPOYG 8 [ VFIAVVRCRQ ||23] 823|1 TWWIFITAVVRCR 26 660 ] TINWDVNDNKPVFI |4 84 |AAQKNKQNSEWATPN||23 831| TAVVRCRQAPHLKAA26 670| KPVFIVPPSNCSYEL 2 916 |MGKYNWVTTPTFKP 23 _3]EMEVLGLLD 8VIAVDNDTGMNAEVR |24 963|| IQELPLDNTFVACDS|23 151I EMPENVUGDELKL 2 196 Table XLVI -109P1D4v.1-DRB1 Table XLVI -109P1D4v.1-DRB1 Table XLVI -109P1D4v.1-DRB1 0101- 15-mers 0101- 15-mers 0101-15-mers Each peptide is a portion of SEQ Each peptide is a portion of SEQ Each peptide is a portion of SEQ ID NO: 3; each start position is ID NO: 3; each start position is ID NO: 3; each start position is specified, the length of peptide is specified, the length of peptide is specified, the length of peptide is 15 amino acids, and the end 15 amino adds, and the end 15 amino acids, and the end position for each peptide Is the position for each peptide is the position for each peptide is the start position plus fourteen start position plus fourteen start position plus fourteen F6_j GTYIFAVLLACWFH 22 323 HKLLVLASDGGLMPA|20 319| ETPNHKLLVLASDGG |18 1261| RFLIEDINDNAPLFP |2 346 TDVNDNVPSIDIRYI |0 411|| VFSNQFLLETAAYLD |81 1321 INDNAPLFPATVNI ||2 425- DYESTKEYAIKLLAA ||20 [4 YLDYESTKEYAIKLL |1 1i78[ LIKSQNIFGLDVIET |45911 ENDNAPVFTQSFVTV ||2 450| AMLFIKVKDENDNAP |18 25i[ ETEIEVSIPENAPVG 42 463| APVFTQSFVTVSIPE ||2 6411 |FYVKAEDGGRVSRSS|8( 328f LASDGGLMPARAMVL| 22 470|| FVTVSIPENNSPGQ ||20 717| [GGNTRDLFAIDQETG |81 402|| HEIPFRLRPVFSNQF 22 522| LTVVKKLDREKEDKY 20 [50 [LVKANDLGQPDSLFS| 18 44211 GKPPLNQSAMLF2KV2 . 619|| DSQTGVIRPNISFDR |20 762| LFSVVIVNLFVNESV 18 462|| NAPVFTQSFVTVSIP |768|| VNLFVNESVNATLI 20 7651 WIVNLFVNESVTNA |1 455[LTKVSAMDADSGPNA 783| NELVRKSTEAPVTPN 20 778|| NATLINELVRKSTEA |18 502|| NYLLGPDAPPEFSLD| 22 883|| LNFVTIEETKADDVD 20 779|| ATLINELVRKSTEAP [18 510||PPEFSLDCRTGMLTV [22 944|| PQPAFQIQPETPLNS||20 8701 KKKKKKHSPKNLLLN |18 535|| KYLFTILAKDNGVPP [ 992|| SDCGYPVTTFEVPVS|20 918 |KYNWVTTPTTFKPDSj18 54-41 |DNGVPPLTSNVTVFV 63 1 FKLVYKTGDVPLIRI |19 98611 SDPYSVSDCGYPVTT||1 557|| FVSIIDQNDNSPVFT |[22 6 KLVYKTGDVPLlRIE |I|1 993| DCGYPVTTFEVPVSV|[1 615|| DFTIDSQTGVIRPNI |[22 122 LVKIRFLIEDINDNA |19 995 GYPVTTFEVPVSVHT ||1 683| ELVLPSTNPGTVVFQ| 22 182| QNIFGLDVIETPEGD 19 692|| GTVVFQVIAVDNDTG| 22 306|| TGLITIKEPLDREET |19 Table XLVII-109P1D4v.1 753 ] ANDLGQPDSLFSWI 22 352|| VPSIDIRYVNPVND |19 pDRBI 0301 - 15-mers o 756|| LGQPDSLFSWIVNL |22 365| NDTWLSENIPLNTK ||19 Ea pd s a porof 759j| PDSLFSWIVNLFVN 22 420|| TAAYLDYESTKEYA |19 position Is specified, the length 800]| IADVSSPTSDYVKIL 5001 KINYLLGPDAPPEFS 19 of peptide Is 15 amino acids, 815 VVAGTIVVIF 60 AVTLSILDENDDFTI 19 and the end position for each I1l =AVGI64AULEDDFT119 peptide is the start position plus 9391| YKSASPQPAFQIQPE |2 696||FQVIAVDNDTGMNAE 19 fourteen 947]| AFQIQPETPLNSKHH L 733] ITLMEKCDVTDLGLH |19 10011 FEVPVSVHTRPVG Q |22 8][ YIFAVLLACVFHSG |18 [0j IGDLLKDLNLSLIPN 38 60 AMQFKLVYKTGDVPL||21 14 1 LACWFHSGAQEKNY| 18 111| EVAJLPDEIFRLVK1 [|32 1081| YEVEVAILPDEIFRL [21 401| IGDLLKDLNLSLIPN [18 [90 GNRVLDLPIDLEEQ 3I1 1841 IFGLDVIETPEGDKM [21 50 f SLIPNKSLTTAMQFK [|1 [36| ENVLIGDLLKDLNLS 30 36311 PVNDTVVLSENIPLN |21 [54 11NKSLTTAMQFKLVYK ||18 [74] LIRIEEDTGEIFTTG ||29| 541J[ LAKDNGVPPLTSNVT ||21 F8 81|| TGEIFTTGARIDREK |18 97 |CAGIPRDEHCFYEVE 29 7221 DLFADQETGNITLM ||21| 133|| NDNAPLFPATVINIS ||8 125| IRFLIEDINDNAPLF I9 I43|[ VINISIPENSAINSK |20] 136|| APLFPATVINISIPE |1| 5021 |NYLLGPDAPPEFSLD129] 215||YVMKVKVEDGGFPQR [|0 170|| INGVQNYELIKSQNI |8 [89 3ADDVDSDGNRVTLDL 28 222][ EDGGFPQRSSTAILQ||20 2451 NHPVFKETEIEVSIP [|8 [361| NDTVVLSENIPLNTK |27 246 |j HPVFKETEIEVSIPE 1 257|| SIPENAPVGTSVTQL |18 605 VTLSILDENDDFTID ]|7 253_| EIEVSIPENAPVGTS 2 293 SNIARRLFHLNATTG ||8 671| PVFIVPPSNCSYELV ||7| 197 Table XLVil -109P1D4v.1- Table XLVII -109P1D4v.1- Table XLVIII - 109P1D4v.1 DRBI 0301 -15-mers DRBI 0301 - 15-mers DRBI 0401-15-mers Each peptide is a portion of Each peptide is a portion of Each peptide is a portion of SEQ SEQ ID NO: 3; each start SEQ ID NO: 3; each start 10 NO. 3; each start position Is position is specified, the length position Is specified, the length specified, the length of peptide Is of peptide is 15 amino acids, of peptide is 15 amino acids, 15 amino acids, and the end and the end position for each and the end position for each position for each peptide is the peptide Is the start position plus peptide is the start position plus start position plus fourteen fourteen fourteen 1 VQ 1I73||1 VQNYEU KSQNIFGL ||2 904 TLDLPIDLEEQTMGK |27| 2881 FSNLVSNIARRLFHL ||0 [28511 HFSFSNLVSNARRL [|28 4 I DLNLSLJPNKSLTTA [26| 13 SNQFLLETAAYLDYE |201 510|PPEFSLDCRTGMLTV|281 54] NKSLTTAMQFKLVYK [26| 341 IKLLAADAGKPPLNQ |20I 6131| NDDFTIDSQTGVIRP| 281 371 SENIPLNTKIAUTV |26 R580 PENLPRHGTVGLITV |20 [9161 MGKYNWVTTPTTFKP 8N1 525 VKKLDREKEDKYLFT 696FQVIAVDNDTGMNAE |20 401| IGDLLKDLNLSLIPN 16| 6-13 NDDFTIDSQTGVIRP [|26| 803| VSSPTSDYVKILVAA ||l 46 I DLNLSUIPNKSLTA ||6| 626 RPNISFDREKQESYT [26 |86]NRQMIMMKKKKKKKK|2 54 ||NKSLTTAMQFKLYK [|6| 2041 QKELDREEKDTYVMK 25| 908 PIDLEEQTMGKYNWV|JC 125|| IRFLIEDINDNAPLF 126| 275|| DADIGENAKIHFSFS |25| 928 FKPDSPDLARHYKSA20 1671| DVGINGVQNYELKS 1261 2891 SNLVSNARRLFHLN g|2 1j EHCFYEVEVAILPDE 19 354 | SIDIRYIVNPVNDTV |261 [401] DHEIPFRLRPVFSNQ||2 f1[091 EVEVAILPDEIFRLV |19 544 DNGVPPLTSNVTVFV|261 510]|PPEFSLDCRTGMLTV [ [117 DEFRLVKIRFUED |19| -555| TVFVSIIDQNDNSPV 26 F56]6 NSPVFTHNEYNFYVP|2 5 [182 QNIFGLDVIETPEGD |19 17041 DTGMNAEVRYSIVGG||26 662| NWDVNDNKPVFIVP |25 186| GLDVIETPEGDKMPQ 19 765|| WIVNLFVNESVTNA ||2 713| YSVGGNTRDLFAID ||5J 190 IETPEGDKMPQUVQ 19 779|| ATLINELVRKSTEAP 26 1161 PDEIFRLVKIRFLIE ||24 198 MPQLIVQKELDREEK 19 [7971 NTEIADVSSPTSDYV 26 167| DVGINGVQNYELIKS ||24 238 SVfDTNDNHPVFKET| 19 823 VVVVIFITAVRCR ||6 395| RVTCFTDHE2PFRLR |4 3051 TTGLITIKEPLDREE 19 827__VIFITAWRCRQAPH [2 721|| RDLFAIDQETGNITL ||24 331 |DGGLPARAMVLVNV 19 [893 ADDVDSDGNRVTLDL|26 3251 LLVLASDGGLMPARA] 23 15| QFLLETAAYLDYEST I|1 |9311 IQELPLDNTFVACDS 1|26| 6281 NISFDREKQESYTFY 23) 211 AAYLYESTKEYAIK |1 7 |Y6FAVLLACVVFHS 945| QPAFQIQPETPLNSK 23 52| LFKVKDENDNAPVF 1916 CVVFHSGAQEKNYT 22 161 PAAVDPDVGINGVQN||2 518| RTGMLTVKKLDREK [19 1104 EHCFYEVEVAILPDE [|22 81 VSAMDADSGPNAKIN 22 19|TGMLVKKLDREKE |19] [117j DEIFRLVKIRFLIED f|22 925 PTTFKPDSPDLARHY 567 SPVFTHNEYNFYWPE| 124 | KIRFUEDINDNAPL |2 970 NTFVADSISKCSSS 22| 588| TVGLTVTDPDYGDN 19| 297fl| RRLFHLNATTGUTI ||2 165) DPDVGINGVQNYEL| 21| 6821 YELVLPSTNPGTVVF |19| 413 | SNQFLLETAYLDYE || 3231 HKLLVLASDGGLMPA21| 712| RYSIVGGNTRDLFAI |1 9 467j TQSFVTVSIPENNSP ||2 05| PFRLRPVFSNQFLLE ||21| |730|| TGNITLMEKCDVTDL |9| [6281| NISFDREKQESYTFY |22 5381 FTILAKDNGVPPLTS 21| 746 LHRVLVKANDLGQPD| 19| 67011 KPVFIVPPSNCSYEL 22 698 1VIAVDNDTGMNAEVR 211 791 EAPVTPNTEIADVSS 19 r679|NCSYELVLPSTPGT 2 759| PDSLFSWIVNLFVN 21 831 TAWRCRQAPHLKAA191 721| RDLFAIDQETGNITL ||22 963| IQELPLDNTFVACDS |1 8l9APHLKAAQKNKQNSE19j 768 VNLFVNESVTNATU 22 63|| FKLVYKTGDVPURI ||20| |862 RQMIMMKKKKKKKKH |19| 80711 TSDYVKILVAAVAGT 22 1281 LIEDINDNAPLFPAT 20 1864 MIMMKKKKKKKKHSP |191 882 LLNFVTIEETKADDV |22 176 YELIKSQNIFGLDVI | [918 KYNWVTTPTTFKPDS 122.

198 Table XLVIII- 109P1D4v.1- Table XLVIII - 109P1D4v.1- Table XLVIII - 109P1D4v.1 DRB1 0401-15-mers F DRB1 0401-15-mers DRB1 0401-15-mers Each peptide Is a portion of SEQ Each peptide is a portion of SEQ Each peptide is a portion of SEQ ID NO: 3; each start position is ID NO: 3; each start position Is ID NO: 3; each start position Is specified, the length of peptide Is specified, the length of peptide is specified, the length of peptide Is 15 amino acids, and the end 15 amino acids, and the end 15 amino acids, and the end position for each peptide is the position for each peptide is the position for each peptide is the start position plus fourteen start position plus fourteen start position plus fourteen 925 PTTFKPDSPDLA RHY 22 1365] NDTVVLSENIPLNTK ||20 767 | IVNLFVNESVTNATL ||2 9361 ARHYKSASPQPAFi 22 [366j DTVVLSENIPLNTKI |01 [76-91 NLFVNESVTNATLIN |20 [969]| DNTFVACDSISKCSS 22f 377J NTKIALITVTDKDAD ||20 [778f NATLINELVRKSTEA |20 98| VTTFEVPVSVHTRPV 22 [379]1 KIALITVTDKDADHN |08 8001| IADVSSPTSDYVKIL ||20 6|| GTYIFAVLLACWFH |2CI 1393] NGRvTCFTDHEiPFR 1|01 [808]| SDYVKILVAAVAGTI 20 27|| NYTIREEMPENVLIG |2C| j405f| PFRLRPVFSNQFLLE ||0, 810]| YVKILVAVAGTITV 20 36 || ENVLIGDLLKDLNLS |2C| 421 If AAYLDYESTKEYAIK ||0 |811|| VKILVAAVAGTITVV 20 [37 71 NVLIGDLLKDLNLSL ||2C 47211 TVSIPENNSPGQLT |201 [812|f KILVAAVAGTITWV |2C| [41]1 GDLLKDLNLSLIPNK [20 [4821 GIQLTKVSAMDADSG||20I |8f1| VAAVAGTMNWVIF |2O 48 NLSLIPNKSLTTAMQ |20 [8 |VSAMDADSGPNAKIN|20| 819J[ AGTITVVVIFITAV 20 97 CAGPRDEHCFYEVE|20 [498] NAKINYIIGPDAPPE |10| 821fl TITVVVIFITAVVR |2O ri111 EVALPDEIFRLVKf ||20 5221 LTWKKLDREKEDKY |20 8221 |TVVVVIFITAWRC 120 112 I VALPDEIFRLVKIR ||20 |534| DKYLFILAKDNGVP ||| 8|APHLKAAQKNKQNSE||2C| 122|| LVKIRFLIEDINDNA |20 547 | VPPLTSNVTVFVSI [2 |879|| KNLLLNFVTIEETKA ||2C 135|| NAPLFPATVINISIP |20 5511 TSNVVFVSiiDQND ||0 880| NLLLNFvr IEETKAD 120 1401| PATVINISIPENSAI |201 558]1 VSIlDQNDNSPVFTH |20 [883|| LNFVTIEETKADDVD ||20 143f[ VINISIPENSAINSK 580|f PENLPRHGTVGLITV ||2 900] GNRVTLDLPIDLEEQ |20 57 |KYTLPMAAVDPDVGIN 120 606][ TLSILDENDDFTIDS |2 904| TLDLPIDLEEQTMGK |20 [181| SQNIFGLDVIETPEG [20 60 [TFYVKAEDGGRVSRS 20 906 DLPIDLEEQTMGKYN 20 184| IFGLDVIETPEGDKMJ 20 16481 |GGRVSRSSSAKVTIN ]20 9471 AFQQPETPLNSKHH ||20 231 1 STAILQVSVTDTNDN f20j 6581 KVTINWDVNDNKPV| f] 959| KHHIIQELPLDNTFV F20 232|| TAILQVSVTDTNDNH |20 [661 1 INWDVNDNKPVFIV ||20 196011 HHIIQELPLDNTFVA ||20 2341 ILQVSVTDTNDNHPV |20 1682 f YELVLPSTNPGTVVF ||0 975I| CDSISKCSSSSSDPY ||2 [245f| NHPVFKETEIEVSIP ||2 692| G1WFQVIAVDNDTG| 20| 995| GYPVTTFEVPVSVHT ||20 253]| EIEVSIPENAPVGTS |20 I VFQVIAVDNDTGMNA |20| [12 |VLLACVVFHSGAQEK| 18 265| GTSVTQLHATDADIG|20 [696] FQVIAVDNDTGMNAE20 13 ] LLACWFHSGAQEKN||18 281|| NAKJHFSFSNLVSNI 20 698|| VIAVDNDTGMNAEVR |20| 19| FHSGAQEKNYTIREE |18 289|| SNLVSNIARRLFHLN | 20| 712] RYSIVGGNTRDLFAI 20 51]| LIPNKSLTTAMQFKL ||18| 312|| KEPLDREETPNHKL 20| 720| TRIDLFAIDQETGNIT |20| 73f| PLIRIEEDTGEIFT |18 322||NHKLLVLASDGGLMP |20| 723] LFAIDQETGNITLME ||20 78J| EEDTGEIFTTGARID 18 323 HKLLVLASDGGLMPA| 20| 738]|IKCDVTDLGLHRVLVK |5 FTTGARIDREKLCAG 18 331||DGGLMPARAMVLVNV |20| I43|DLGLHRVLVKANDLG||201 113|| AILPDEFRLVKIRF 18 337I ARAMVLVNVTDVNDN|20| 747 |HRVLVKANDLGQPDS 120| 137fl PLFPATVINISIPEN 18 338 |RAMVLVNVTDVNDNV 20 753|1 ANDLGQPDSLFSVVI 20| [144 | INISIPENSAINSKY ||18 349|| NDNVPSIDIRYIVNP 20 759|| PDSLFSVVIVNLFVN [20 148|| IPENSAINSKYTLPA |18| 357| IRYVNPVNDTVVLS ||0| 762|| LFSWIVNLFVNESV |20| 196|DKMPQUVQKELDRE |[8 358|| RYIVNPVNDTWLSE |20 7 SVIVNLFVNESVTN |20| [201| LIVQKELDREEKDW |18| 199 Table XLVIII - 109P1 D4v.1- Table XLVII-109P1D4v.1- Table XLVIII - 109P1 D4v.1 DRB1 0401-15-mers DRB1 0401-15-mers | DRB1 0401-15-mens Each peptide is a portion of SEQ Each peptide Is a portion of SEQ Each peptide is a portion of SEQ ID NO: 3; each start position Is ID NO: 3; each start position is ID NO: 3; each start position is specified, the length of peptide is specified, the length of peptide is specified, the length of peptide is 15 amino acids, and the end 15 amino acids, and the end 15 amino acids, and the end position for each peptide is the position for each peptide Is the position for each pepUde is the start position plus fourteen start position plus fourteen start position plus fourteen 2201| KVEDGGFPQRSSTAI118| 775[ SVTNATLINELVRKS ||18 W693 |VTFQV1AVDNDTGM||6 228 | QRSSTAILQVSVTDT |18| 7961| PNTEIADVSSPTSDY |18 710 J[ EVRYSIVGGNTRDLF |16 258 IPENAPVGTSvTQLH [|18| 813 | ILVAAVAGTITVWV ||18| 760]| DSLFSWVNLFVNE |6I 1262 APVGTSVTQLHATDA |18| 833 WRCRQAPHLKAAQK 12|6]| WIFITAWRCRQAP 16 282| AKHFSFSNLVSNIA ] |838 QAPHLKAAQKNKQNS 18 [945] QPAFQIQPETPLNSK 16 293 SNIARRLFHLNATTG 18 |54 WATPNPENRQMIMMK 118 151J| NSAINSKYTLPAAVD ||1 298 RLFHLNATTGLMK |18| 876 | HSPKNLLLNFVTIEE 1 953][ ETPLNSKHHIlQELP ||15 3091| ITIKEPLDREETPNH 18 890 ETKADDVDSDGNRVT|1L8 1l| MDLLSGTYIFAVLLA ||14 341|| VLVNVTDVNDNVPSI |18| [90j LPIDLEEQTMGKYNW||18 9 | IFAVLLACWFHSGA ||14 346| TDVNDNVPSIDIRY |18 929 KPDSPDLARHYKSAS 1j FAVLLACVVFHSGAQ |14 3501| DNVPSIDIRYVNPV |18| |930|jPDSPDLARHYKSASP||18 11 AVLLACWFHSGAQE [14 363 PVNDTVVLSENIPLN |18 [962 |J IIQELPLDNTFVACD ||I 15 |ACWFHSGAQEKNYT||14 370| LSENIPLNTKIALIT [18 992|| SDCGYPVTTFEVPVS |18 44]| LKDLNLSLIPNKSLT ||1I 3851 VTDKDADHNGRVTCF [10-0e1| FEVPVSVHTRPVGIQ 18 63 FKLVYKTGDVPLIRI |14| 406|| FRLRPVFSNQFLLET ||18| 223 DGGFPQRSSTAILQV||17| [69| TGDVPLIRIEEDTGE |1 4401 DAGKPPLNQSAMLF M 18| 5][ SGTYFAVLLACVVF |16| 71 i DVPLIRIEEDTGEIF 1141 452| LFIKVKDENDNAPVF ||18| 60 [AMQFKLVYKTGDVPL||16| 7 |] II VPLIRIEEDTGEIFT ||14 460 NDNAPVFTQSFVTVS 118| [64J[ KLVYKTGDVPLIRIE |16| 74J| URIEEDTGEIFTTG | 464 PVFTQSFVTVSIPEN ||1 82 | GEIFTTGARIDREKL 16| 88J[ GARIDREKLCAGIPR | [87 KVSAMDADSGPNAK |18| 1j5 HCFYEVEVAILPDEI ||1 6|07| FYEVEVAILPDEIFR |14 [531 EKEDKYLFTILAKDN [|18 F36|| APLFPATVINISIPE | 16 109[ EVEVAILPDEIFRLV 14| 5561 VFVSIIDQNDNSPVF ||8 5182] QNIFGLDVIETPEGD |16 |][ PDEIFRLVKIRFLIE ||14| 568| PVFTHNEYNFYVPEN |18| 246][ HPVFKETEIEVSIPE |16 119[ IFRLVKIRFLIEDIN 14| 577 FYVPENLPRHGTVGL|[18 283|j KIHFSFSNLVSNIAR 16J [12611 RFLIEDINDNAPLFP ||14 [595|| TDPDYGDNSAVTLSI |18| 356] DIRYIVNPVNDTVVL 16 141|| ATVINISIPENSAIN 14 598 | DYGDNSAVTLSILDE |I18 40|RPVFSNQFLLETAAY 16| 145fl NISIPENSAINSKYT |1 609|| ILDENDDFTIDSQTG |18 4201 TAAYLDYESTKEYA |16| 161 ||PAAVDPDVGINGVQN 14 6181 IDSQTGVIRPNISFD 18| 423|| YLDYESTKEYAIKLL |1 6 170] INGVQNYELKSQNI |14 625 IRPNISFDREKQESY |18 450 | AMLFIKVKDENDNAP ||6 |175] NYELIKSQNIFGLDV 14 645 |AEDGGRVSRSSSAKV|8] |463|| APVFTQSFVTVSIPE 16| 176|| YELIKSQNIFGLDVI [|14 659 | VTINVVDVNDNKPVF |18| 535 [ KYLFTILAKDNGVPP 16| 1861 GLDVIETPEGDKMPQ||4! 689| TNPGVVFQVIAVDN 18 554|| VTVFVSIIDQNDNSP 16 [187| LDVIETPEGDKMPQL |14| 740||DVTDLGLHRVLVKAN 18| 572 jHNEYNFYVPENLPRH16| 195|GDKMPQLIVQKELDR 14 750||LVKANDLGQPDSLFS 18| j574 EYNFYVPENLPRHGT I6| 2001 QLIVQKELDREEKDT |14 756 LGQPDSLFSVVIVNL |18| I575 YNFYVPENLPRHGTV 116] 204 |QKELDREEKDTYVMK 14 761 1 SLFSVVNLFVNES 18 DPDYGDNSAVTLSIL 16] 213|DTYVMKVKVEDGGFP 14 770 | LFVNESVTNATUNE L1 6391 YTFYVKAEDGGRVSR[f|1 216 |VMKVKVEDGGFPQRS 14 200 Table XLVIII - 109P1D4v.1- Table XLVIII - 109P1D4v.1- I Table XLIX- 109P1D4v.1-DRB11 DRB1 0401-15-mers DRBI 0401-15-mers 1101-15-mers Each peptide is a portion of SEQ Each pepuide is a portion of SEQ Each peptide is a portion of SEQ ID NO: 3; each start position is ID NO: 3; each start position is ID NO: 3; each start position Is specified, the length of peptide is specified, the length of peptide is specified, the length of peptide is 15 amino acids, and the end 15 amino acids, and the end 15 amino acids, and the end position for each peptide is lhe position for each peptide is the position for each peptide is the start position plus fourteen start position plus fourteen start position plus fourteen 251 ETEIEVSIPENAPVG ||1 622 TGVIRPNISFDREKQ [14 [1161 PDEIFRLVKIRFLIE 25 255]| EVSIPENAPVGTSVT |41 [6[26 RPNISFDRQESYT ||1 [285 | HFSFSNLVSNIARRL |25 261| NAPVGTSVTQLHATD |14 [65611 SAKVTINWDVNDNK ||1 [050| TFEVPVSVHTRPVGI 25 288 | FSNLVSNIARRLFHL [1 660]1 TINVVDVNDNKPVFI ||14 60 ||AMQFKLVYKTGDVPL [24 296|| ARRLFHLNATTGLIT |1 [6631 WDVNDNKPVFIVPP 14 [518 RTGMLTVVKKLDREK[23] 299|| LFHLNATTGLITIKE ||14 669|| NKPVFIVPPSNCSYE [4 5191 TGMLTVVKKLDREKE| 23 305|| TTGUTIKEPLDREE 14 671[ PVFIVPPSNCSYELV 1 882]| LLNFVTIEETKADDV [23 324|KLLVLASDGGLMPAR|[1 [68111 SYELVLPSTNPGTW 14 289 | SNLVSNIARRLFHLN |22 325| LLVLASDGGLP R 14 68311 ELVLPSTNPGTVVFQ 14 636 IQESYTFYVKAEDGGR |22 339 |AMVLVNVTDVNDNVP [14 70811 NAEVRYSIVGGNTRD [1 73011 TGNITLMEKCDVTDL |22 340 MVLVNVrDVNDNVPS|14 171311 YSIVGGNTRDLFAID 14| 7791 ATLINELVRKSTEAP ||22 342 LVNVTDVNDNVPSID |14 j 730| TGNITLMEKCDVTDL 1 I002| EVPVSVHTRPVGIQVJ22 F367 TWLSENIPLNTKIA ||14 733j ITLMEKCDVTDLGLH [14| 1I2 VLLACVVFHSGAQEK [21 3571 II SENIPLNTKIALITV |14 74111 VTDLGLHRVLVKAND 1 37 l NVLIGDLLKDLNLSL |21 415||. QFLLETAAYLDYEST 14 f773|| NESVTNATLINELVR 14 34211 LVNVTDVNDNVPSID |21] 431 | EYAIKLLAADAGKPP [14 783 INELVRKSTEAPWPN 4 522| LTVVKKLDREKEOKY [21 433|| AIKLLAADAGKPPLN | 14 824]1 VVVVIFITAVVRCRQ 14 808 SDYVKILVAVAGTI |21i 434]1 IKLLAADAGKPPLNQ ||14| F8301 ITAVVRCRQAPHLKA 14 1861 |NRQMIMMKKKKKKKK |21 4 |3 KPPLNQSAMLFIVK |4| 86|NRQMIMMKKKKKKKK 14 11 AVLLACVVFHSGAQE |20 448[ QSAMLFIKVKDENDN |48 [88511 FVTIEETKADDVDSD 14 821| GEIFTTGARIDREKL 20 4i3| FIKVKDENDNAPVFT ||14| 913]|EQTMGKYNWVTTPTT |14 105| HCFYEVEVAILPDEI |20| 462|| NAPVFTQSFVTVSIP 114 9191 YNWVTTPTTFKPDSP 14 212]KDTYVMKVKVEDGGF 20 468] QSFVTVSIPENNSPG |14| [93211 SPOLARHYKSASPQP |14 26511 GTSVTOLHATDADIG|20| 4701 FVTVSIPENNSPGIQ ||14 970| NTFVACDSISKCSSS |14 r293| SNIARRLFHLNATTG |0 F4801 SPG[QLTKVS A 14 988 |PYSVSDCGYPVTFE4 479 |NSPGIQLTKVSAMDA |20| 502 INYLLGPDAPPEFSLD |14 1000| TFEVPVSVHTRPVGI|1 482 GIQLTKVSAMDADSG||0 518||RTGMLTVVKKLDREK |14 [00j EVPVSVHTRPVGQV|1 [6445||AEDGGRVSRSSSAKV||20 5191 TGMLTVVKKLDREKE |14 932] SPDLARHYKSASPQP||20| 52511 VKKLDREKEDKYLFT ||14 Table XLIX- 109PID4v.1-DRB1 [9721 FVACDSISKCSSSSS |20 Ii38I| FTILAKDNGVPPLTS |14 1101-15-mers 1361| APLFPATVINISIPE |19 | NVTVFVSIlDQNDNSI Each peptide Is a portion .[FGLDVIETPEGDKM ||19] 55 VVFSI 1-41 ID NO: 3; each start position Is [--1 FLVEPG---~ 5861 HGTVGLITVTDPDYG [14 specified, the length of peptide is F29[ ARRLFHLNATTGLIT |g19 5881 TVGLITVTDPDYGDN 1 15 amino acids, and the end 3 NHKLLVLASDGGLMP|9[ I]- 1 position for each peptide Is the I APVFTQSFvTvsIPE i 591 LITVTDPDYGDNSAV t4a poste46 plus fourteen 602|| NSAVTLSILDENDDF] ||146I0i1 TINVVDVNDNKPVF[l |19 604|( AVTLSILDENDDFTI 14 5 KYLFTILAKDNGVPP | 20 TRDLFAIDQETGNT ||9 607|| LSILDENDDFTIOSQ |4 827 VIFITAVVRCRQAPH-I ||2 821 TITVVVVFITAVVR |19] 201 Table XL1X- 109P1D4v.1-DRB1 Table XLIX - 109PD4v.1-DRB1 Each peptide is a 11015-mers 1101-15-mers portion of SEQ ID Each peptide is a portion of SEQ Each peptide is a portion of SEQ NO: 5; each start ID NO: 3; each start position is ID NO: 3; each start position is position is specified, specified, the length of peptide Is specified, the length of peptide Is the length of peptide 15 amino acids, and the end 15 amino acids, and the end Is 9 amino acids, position for each peptide Is the position for each peptide Is the and the end position start position us fourteen start position plus fourteen for each peptide is the start position F71 TYFAVLLACWFHS 8618 IDSQTGVIRPNISFD 16 plus e[ght 71 DVPLIRIEEDT|EF18 9 NCSYELVLPSTNPGT|16 STIECSEI II 126 RFLIEDINDNAPLFP 18 6891 TNPGTVVFQVAVDN 168 PTDSRTST 155 NSKYTLPAAVDPDVG |18 704 DTGMNAEVRYSIVGG 16 DSRTSIIEI 11 1]82 QNIFGLDVIETPEGD |18 710 EVRYSIVGGNTRDLF|16 HTRPTDSRT r213 DTYVMKVKVEDGGFP 738 KCDVTDLGLHRVLVK 16 3791 KIALITVTDKDADHN |1 768 VNLFVNESVTNATU 16 Table 431 EYAIKLUAADAGKPP 18 807 TSDYVKLVAAVAGT 16

XXIV

-- 109P1D4 485 LTKVSAMDADSGPNA|18 [9161 MGKYNWVTPTTFKP 16 v.2 C' SNAKNYLLGPDAPPE 18 936 ARHYKSASPQPAFQ16 Terminal 510 PPEFSLDCRTGMLTV |18 A0203-9 mers 5861 HGTVGLITVTDPDYG Table XXI-109P1D4 695 VFQVIAVDNDTGMNA f18' v.2 C' Terminal-Al _________ 9-mers No 760 DSLFSVWVVNLFVNE |p18 Results _____________________ 18EachpetdIsaFu. 764 SWIVNLFVNESVTN portion of SEQ ID 797 NTEIADVSSPTSDYV|18 NO: 5; each start NTEIA D VSSPTSD Y V ~ ~ position is specifed, T b e X - 0 p o 993 DCGYPVTTFEVPVSV I18 the length of peptide TableXXV-109PI04 104 EHCFYEVEVAILPDE |17 Is 9 amino acids, v.2 C' Terminal-A3 117 DEIFRLVIRFLIED ||17 and the end position 9-mers 210 EEKDTYVMKVKVEDG17 for each peptide s Each peptide isa 210EEKTYVKVIVED 17the start position portion of SEQ ID 246 HPVFKETEIEVSIPE 17 plus eight NO: 5; each start position Is specified, 380] ALTMKDNG 7l the length of peptide [49 SAMLFlKVKDENDNA PIDSRTT 16 Is 9 amino ads, and! 638 SYTFYVKAEDGGRVS|17 [HIRPTDSR the end position for _638 ____________17_ each peptide is the [670 IKPVFIVPPSNCSYEL 17 12 RSTIECS 10 start position plus [6931 TVVFQVIAVDNDTGM|17 10 DSRTSTIEl 8 eight 744 LGLHRVLVKANDLGQ 17 14 SLECEl8 819 AGTITVVW IFTAV 17 3 SVITRDS 925 PTTFKPDSPDLARHY| TableXXlIIl PVSVHTRPT 1 986 SDPYSVSDCGYPVTT17 C'Term ial020 1 V HIRPISR 138 LFPATVINISIPENS 16 9-mers 5 EPTP RT 173 VQNYELIKSQNIFGL 7 RPIDS9IST F3991 FTDHEIPFRLRPVFS ||1 8_ PTDSREl 450 AMLFKVKDENDNAP 16 4 STiElCSEl 8 467 TQSFVTVSIPENNSP| 16 500 KINYLL-GPDAPPEFS ||6TabeXXVI-109P1D4 15] VYFLL NDPS |61 v.2 C' Termlnal-A26 551T0 VIDQDS L1j 9msA 202 Each peptide is a Table XXVIII Each peptide is a portion of SEQ ID 109PID4v.2 portion of SEQ ID NO: 5; each start C'Terminal-B08 NO: 5; each start position is specified, 9-mers position is specified, the length of peptide Each pepide is a the length of pepde Is 9 amino adds, portion of SEQ iD is 9 amino acids, and and the end position NO:5; each start the end position for for each pepbde is position is specified each peptide is the the start position the length of peptid' start position plus plus eight is 9 amino acids, eight and the end position STIEICSEI for each peptide Is 11SRTSTIEIC 13 Iii~~I [18 the start position _____ USVHTRPTDS lus eight 4 VHTRPTDSR 12 E PTDSRTSTI TRPTDSRTS | RTSTIEICS 1 PTDSRTSTI 1 14STIEICSEI1 PVSVTRPT DSRTSTIE1 1 DSRTSTIEI 5 HTRPTDSRT ~o 4STIE1CSEI 1 G RPTDSRTST Ii DSRTS[R I HTRPTDSn TableXXVII Table XXXI 109P1D4v.2 Table XXIX 109PID4v.2 C'Terminal-0702 T9PD4v.2 C' Terminai-82709 9-mers C'Teminal-510- 9-mers Each peptde is a 9-mers Each peptide is a portion of SEQ ID portion of SEQ ID NO: 5;each start Each peptide is a NO: 5; each start position Is specified, portion of SEQ D position Is specified, the length of pepde NO: 5; each start the length of peptide is 9 amino acids position is is 9 amino acids, ane ends specified, the and the end position for each pepoitis length of peptide is for each peptide Is the start position 9 amino acids, and the start position plus eight j the end position for plus eight each peptide is the start position plus Each pepide is a 7eRPTDSRTST _eight portion of SEQ 10 (flfRPTOSRTO: 191 5; each start M[PVSVHTRPT 0 position Is specified, HTRPTDSRT [9 VHTRPTDSR 11the length of peptide 10 DRTSTEI 9[~]PVSVITRP [~Is 9 amino adds, . DSRTSTIEI 1PVSVHTR-PT4 and the end position 5 HTRPTDSRT for each peptide is Table )(X 6[JTRPTDSRTS 41 the start position 109P1D4v.2 plus eight _ C'Terminal-B08 Table X SRTSTIEIC 9-mr B 109PD4v.2 TRPTDSRTS Each peptlde is a C' Terminal-B2705 1 STIEICSE 1 portion of SEQ ID 9-mers NO' 5; each start position is specied, 10 DSRTST1EI the length of peptide Is 9 amino acids, and the end position Table XXXI for each peptide is 109P1D4v.2 the start position CTerminal-84402 plus eight 9-mers 203 Each peptide Is a Table XXXV Table XXXVII 1 portion of SEQ ID 1O9P1D4v.2 109P1D4v.2 C' NO: 5; each start C'Terminal-A0201-10- terminal-A26-10-mers position is mers Each peptide Is a specified, the Each peptide Is a portion of SEQ ID NO: length of peptide IS portion of SEQ ID NO: 5; each start position 9 amino acids, and 5; each start position is specified, the length the end position fr is specified, the length of pepude is 10 amino each peptide is the of peptide is 10 amino acids, and the end start position plus acids, and the end position for each eight position for each peptide is the start peptide is the start position plus nine 1| STIEICSEI 13 position plus nine [IPTDSRTSTl12 [ 1 RTSTIEICSE 13 10 DSRTSTI 1 RPTDSRTSTI 1 SVHTRPTDSR 10 TDSRTSTIElI 11 DSRTSTIEIC 12 Table E1 RTSTICSE PVVHRPD 1O9P1D4v.2 1 TSTIEICSEI HTRPTDS C'Termlnal-B5101 SVHTRTDSR PTDSRTS 10 9-mers E__R__ H9 Each peptide Is a HTRPTDSRTS portion of SEQ ID TRPTDARTST 6. Table XXXIX NO: 5; each start j VPVSVHTRPT]M 109PID4v.2 position Is specified, C'Terminal-B0702 the length of peptide 10-mers is 9 amIno acids, Table Each peptide is a and the end position XXXVI portion of SEQ ID NO: for each peptide Is 109PID4v.2 po rtpion the start position C7erminal- e n pus eight A0203-10- of peptide is 10 amino mers acids, and the end 1 |DSRTSTIEI 7 position for each RPTSRTST 13 No Results peptide Is the start Found. position plus nine SPTDSRTST= 14| STiEICSEI 12Table XXXVI WVPVSVHTRPT 18 1O9P1D4v.2 - C' [| RPTDSRTST Table XXXIV Terminal-A3-10-mers | TDSRTSTIEI | IO9P1D4v.2 Each peptide is a ______ C' Terminal-A1-10- portion of SEQ ID mers NO: 5; each start Table XL Each peptides a position Is specified, 109P1D4 portion of SEQ ID the length of peptide v.2 NO: 5; each start is 10 amino acids, CTerminal position is specified, and the end position 808-10 the length of peptide for each peptide Is mers Is 10 amIno acids, the start position plus and the end position nine No for each peptide Is Results the start position plus _ _ PIDSRund nie ~JSVITPTSR17 Found. ne2PVSVHIBPTD 5 I9|PTDSRTSTIE| 168|RPTDSRTSTI 1 |~HIRPTDERTS|10 6HTEPTDSRTS 1 204 Table Table Table XLVIII-1 09P1 D4v.2 XLI- XLV- C' Terminal-DRB1 0401 109P1D4 109P1D4 15-mers v.2 C' v.2 C' Each peptide is a portion of Terminal- Terminal- SEQ ID NO- 5; each start B1510- B35101- position is specified, the 10-mers 10-mers length of peptide is 15 amino acids, and the end position for No No each peptide is the start Results Results position plus fourteen Found. Found. 1]VTTFEVPVSVHTRPT||22 Table Table XLVI-109P1D4v.2 14]FEVPVSVHTRPTDSR|1Y8 XLII- C' Terminal-DRBI 0101 101 VHTRPTDSRTSTIE ]18 109P1D4 15-mers 3||TFEVPVSVHTRPTDS||14 v.2 C' Each peptide Is -a portion of [f TEVPVSVHTRPTDST [14] Tennin- SEQ ID NO: 5; each start EVPVSVHTRPTDSRT 82705- position is specified, the 9||SVHTRPTSRTSTIE 10-marslength of peptIdelIs 15 amino 1] SHTRPTDSRTSTIE [1 acids, and the end s 11 HTRPTDSRTSTIEIC ||1 No each peptide is the start |13| RPTDSRTSTIEICSE |1 Results position plus fourteen Found. Table XLIX-109P1D4v.2 | 3|TFEVPVSVHTRPTDS 1 C' Terminal-DRB1 1101 Table 9|SVHTRPTDSRTSTIE17 15-mers Xill- [1||VTFEVPVSVHTRPT16 Each peptide is a portion of 109P104 SEQ ID NO: 5; each start v.2 C' |6]VPVSVHTRPTDSRTS 16 position is specified, the Terminal- |1|I| HTRPTDSRTSTIEIC|1 length of peptide is 15 amino B2709- acids, and the end position 10-mers |4]FEVPVSVHTRPTDSR| 14 for each peplide Is the start ||PVSVHTRPTDSRTST|[4] position plus fourteen No |13| RPTDSRTSTIEICSE |14 Results [5|EVPVSVHTRPTDSRT [3] TFEVPVSVHTRPTDS 25 Found. [5]EVPVSVHTRPTDSR 15 Table XLVII-109PID4v.2 11|VTTFEVPVSVHTRPT 1] Table XLIV C' Terminal-DRB1 0301 109P1D4v.2 15-mers Term as-B42- Each peptide is a portion of 2 a rs SEQ ID NO: 5: each start mers Each peptide is a position Is specified, the portion of SEQ ID length of peptide is 15 amino Each peptide Is a NO: 5; each start acids, and the end position for portion of SEQ ID position is specified, each peptide Is the start NO: 5; each start the length of peptide position plus fourteen position is specified, is 10 amino acids, the length of peptide and the end position Is 9 amino acids, and for each peptide is [0 VHTRPTDSRTSTIE ||17 the end position for the start position plus S jEVPVSVHTRPTDSRT each tide Is the nine flHstart position plus TIPVSVHTRPTDSRTST [|1 eight E3]TFEVPVSVHTRPTDSj0 f5j RTDSRTSTI 1|VT]vTFEVPVSViTRPT UQQTyTSV TDSTCS1 QIFQVLCGL 24 TS S VUQIEQVL 3 20OK 22VLCGQQT Table XXV-1 09P1 D4 Table XXVI WVM lQ v.2 N' terminal-A3- 109P1D4v.2 N' GQI9-mers terminal-A26-9-mers Each peptide is a Each peptide is a 6TSVPGMDL portion of SEQ ID portion of SEQ ID 16LCG QTV NO: 5; each start NO: 5; each start position is specified, position is specified, QTVTSPGM the length of peptide the length of peptide 2 TSVPGMDLL 14 is 9 amino acids, and is 9 amino acids, and RTERQVU 3 the end position for the end position for each peptide is the each peptide is the UQIFQVLC | start position plus start position plus eight eight Table XXII-109P164 v.2 N' terminal- 18GLQQTS GMDLLSGTY 13 A0201___________ __ 9-mers QVLCGjQQ 26 SVPGMDLLS Each peptide is a~ VLQI.FVL 1MRTERQWVL I portion of SEQ ID 76WVjQEQV| NO: 5; each start 261 FV6DLS16TbeXVI position is specified, SVEG 16DLS Tabi-O the length of peptide VLCGLQQT v.2 N' terminal-B0702 is 9 amino acids, and 2 ISVEMD 1 9-mers the end position for each peptide is the 9L3FLC Each peptide is a start position plus 2 GMDLLSGTY portion of SEQ ID eight _ NO: 5; each start RTERQWVU| position is specified, QIEQVLCGL the length of pepide UQQTVTSV U9 QTVTSV| 1Is 9 amino acids, and QIFQVLCGL the end position for each peptide is the VUOIEQVL Table XXVI start position plus VLCGLQQT 109P1D4v.2 N' eight VUQFQV 2terminal-A26-9-mers 8 GUQQIVTS 19Each peptide is a VTSVPGMDL 16 portion of SEQ ID ______ 4 VTSVPGMDL NO: VPGMDLLSG LCGUQQTV position is specified, VUQIFQVL [ij~Jthe length of peptide QTVTSPGM is 9 amino ads, andMRTERQWV ~] TSVPGMDLL [14J the end position for TSVPGMDLL RTERQWVLI each peptide is the QIFQVLCGL 1 UFVLCstart position plus _RTERQWVU 9 IQF~LCIIIeight 2 TRVNIf9 1 ____________ 15VLCGUIQQT8 Table QIFQVLCGL 0 CGUQQTVT 109PD4 VTSVPGMDL QQVTSV v.2 N' ERQWVUQ QTVTSVPGM terminal- QVLCGUQQ A0203 Ir Table XXVII 9-mers QTVTSVPGM 9PD4v.2 N' WUQlFQV 15terminal-B08-9-mers No 2 TVTSVPGMD Results [8] VULQIFQVL 14 Found. TSVPGMDLL []RQWVQFj 206 Each peptide is a Table XXX-109P1D4 Each peptide is a portion of SEQ ID v.2 N' terminal-B2705 portion of SEQ ID NO: 5; each start 9-mers NO: 5; each start position is specified, Each p de Is position is specified, the length of peptide portion SEQ ID the length of peptide Is 9 amino acids, and NO: 5 each start is 9 amino acids, and the end position for position is specified, the end position fbr each peptide is the the length of peptide each peptide is the start position plus is 9 amino adds, adstart position plus eight the end position for eight :J each peptide Is the MRTERQ start position plus VQlFQVL SVUQFQVL eight TSVPGMDLL II QFQVLCGL MRTERQWVL E RQWVLIQI 1131 2J VTSVPGMDL 1121 EROWVLIQI 20 RQWVU__F I21TSVPGMDLL RQWV _F QIQVLCL 3 5f RQWVUIQIfl 18 1191 H1QIFQVLCGL 7 GMDLLSGT Table XXIX-109P1D41 ME v.2 N' terminal-B1510 VUQIFQVL 16 9-mners [2]GMDLLSGTY 153 TERQVUMQ I Each peptude is a [2JTSVPGMDLL||14j] RTERQWVUI[i portion of SEQ IDVTSVPGMDL NO: 5; each start iJ[i position Is specified, Table XXXI-109P1 D4 IFQVLCGUI the length of peptide v.2 N' terminal-B2709 is 9 amino acids, and 9-mers Table XXXII the end position for Each peptide Is a 109P1D4v.2 N' each peptide is the portion of SEQ ID terminal-85101 start position plus NO: 5; each start 9mers eight .

position is specified, Each peptide is a the length of peptide portion of SEQ ID TSVPGMDLL 15 is 9 amino acids, and NO: 5; each start the end position for position is specified, MRTERQWVL 3 each peptide Is the the length of peptide VQFQVL 3 start position plus is 9 amino acids, and 4 TSVPGMDL 13 eight the end position for each peptide is the QIFQVLCGL MRTERQWVL 21 start position plus 5] RQWVUQF eight ~QVTSVPGM 8 ERQWVUQI 1 RTERQWVU ERQWVQI 14 Table XXX-109P1D4 RQWVUQIF UQQTVTSV 14 v.2 N' terninal-B2705 VUQIFQVL 12 VPGMDLLSG|1 9-mers n QFQVLCGL 1MRTERQWVL[ Each peptide s TSVPGMDLL IFQVLCGL 12 portion of SEQ ID 91w~~~ j_____ NO: 5; each start WVU6FQ1 LCGQQTV 12 position Is specified, QVTSVPGM CGUQQTV 1 the length of peptide is 9 amino acids, and RTERQWVU 1 the end position for Table XXXII , VUFV II each peptide Is the 109P1D4v.2 N' start position plus terminal-84402-9- VUQFQVL 11 eight mers 1 QFQVLCGL |I0] ____________ QQTVTSVP |_]

[]PGMDLL.SGT

20 Table XXXIII Table XXXV-109PD4 Table XXXVII 109P1D4v.2 N' v.2-N' terminal-A0201- 109P1D4v.2 N' terminal-B5101- 10-ners terminal-A3-1 0-mers 9mers Each peptide is a Each peptide is a Each peptide Is a portion of SEQ ID NO: portion of SEQ ID NO: portion of SEQ ID 5; each start position 5; each start position NO: 5; each start Is specified, the length is specified, the length position Is specified, of peptide is 10 amino of peptide Is 10 amino the length of peptide acids, and the end acids, and the end is 9 amino acids, and position for each position for each the end posItion for peptide is the start peptide is the start each peptide Is the position plus nine osition plus nine start position plus eight 7 WVLIZIFQVL 16Q LIIFQLCG 12 |VTSVPGMDL__ VUQIEQVLC 128PGMDLLSGTY|12 |VTSVPGMDL U 9 LIQIFVLCG 112 2VTSVPGMDLL Ih17CGLIQQIVTS 1 Table XXXIV SVPGMLLSG 2RTERQWLIQ10 109P1 D4v.2- N' terminal-Al-10-mers Table Table XXXVIII Each peptide is a XXXVI- 109P1D4v.2 N' portion of SEQ ID NO: 109P1 D4 terminal-A26-10-mers 5; each start position v.2-N' Each peptide is a is specified, the length terminal- portion of SEQ ID NO: of peptides 10 amino A0203- 5; each start position is ads, and the end 10-mers specified, the length of position for each peptide is 10 amino peptide Is the start acids, and the end position plus nine Re position for each Foun.ts peptide is the start W._ position plus nine 2]RIERQWyLIQ I 25 TSVPGMQLLS Table XXXVII E V 28PMLLGY1 109P1D4v.2 N' I[ RWLQF~ P GM~'DLLSGTY 11 termin--A3 -1-mers TVTSVPGMDL Each peptide Is a WVUQIFQVL portion of SEQ ID NO: 26 SVPGMDLLSG 1 Table XXXV-109P1D4 5; each start position v.2-N' terminal-A0201- Is specified, the length 0IQFQVLCGL | 10-mers of peptide is 10 amino VTSVPGMDL.| Each peptide Is a apaodsi on othe end 1QVLCGLIQQT H por en of sQ ItiO peptide is the start QTVTSVPGMD|9 Is specified, the length position plus nine 2]RTERQWVUQ of peptide Is 10 amino PGMDLLSGTY| acids, and the end SVEG1fL8L position for each peptide Is the start WVLIQIFQVL |i Table XXXIX position plus nine 8VLQEQVLC | H 109PID4v.2 N' 14 QVLCGIQQT terminal-B0702-10mer 18GUQQIVTSV [ ~ ~ 11VL&GLIQQTV|E6 5VLCGLQQTV 18 GLHQQIYTSV| 10 IQIFQyLCGL 819 UQ ISVP|15 H QHFQVLCGU TVISVEMDL II1GMDLLEGTYI 7 208 Each peptide is a Table XLIII Table XLVI-109PID4v.2 portion of SEQ ID NO: 109P1D4v.2 N' terminal-DRBI 0101 5; each start position is N' terminal- 15-mers specified, the length of B2709- Each peptide is a portion of peptide is 10 amino 10mer . E ach s tart acids, and the end poSEQID NO: 5; each start position for each position is specified, the length peptide is the start No Results of peptide is 15 amino acids, position plus nine Found. and the end position for each peptide is the start position plus fourteen 2 VPGMDLLSGT 17 Table XLIV 7__________12 109PID4y.2N' I________ WVUQFQVL terminalB4402-1 mer [4] ERQWVUQIFQVLCG||26 24 VTSVPGMDLL 2 Each peptide is a 10| IQIFQVLCGLIQQTV 26 I IQIFQVLCGL 11 portion of SEQ ID NO: 5 RQV IQIFQVLCGL [|25 TVTSVPGMDL 15; each start position 13| FQVLCGLIQQTVsv [|24 LCGJ 9Is specified, the length 15 LGIQTFVG(3 LCGUQQTVT of peptide is 10 amino VLCGUQQTVTSVPG|2 1 MRTERQWVU acids, and the end 161 LCGUQQTVTSVPGM |2 TRWU I] position for each_______ TERQV Ql [ peptide is the tart 9| LIQIFQVLCGUQQT ||2 5 VLCGLIQQTV [ position plus nine 17||CGUQQTVTSVPGMD||2 18 GUIQQTVTSV [8 VLIQIFQVLCGLIQQ ||17 QQTVTSVPGM 8 3 TERQWVUQ 21 JGMDLLSGTYi 4 ERQWVLIQIF 15 Table XLVII-1 09P1 D4v.2 f1j IQFQVLCGL 14 N' terminal-DRBI 0301 Table XL 7 WVLIQIFQVL 15mers 109P1D4v.2 Each peptide is a portion of 'N'terminal- PMLST SEQ ID NO: 5; each start BO8-10mers VTSVPGMDLL position is specified, the length QFQVLCGU of peptide is 15 amino acids, and the end position for each NoRsut peptide is the start position Foud |Table XLV plus fourteen 109P1D4v.2 Table )XLI N' terminal 109P1D4v.2 85101- 5|] RQWVLIQFQVLCGL ||21 N' terminal- 10mer 21| QQTVTSVPGMDLLSG |21 B1510- 6|] QWVLQIFQVLCGLI |1 10mer No Results 1 FQVLCGUQQTVTSV [I| Found. I12|| IFQVLCGLIQQTVTS 14 No Results -N_2J| GMDLLSGTYFAVLL 13 Found. Table XLVI-109P1D4v.2 9| LIQIFQVLCGLIQQT I|1 N' terminal-DRBI 0101 I il TSVPGMDLSGTYIF 1 Table XUl 15-mers2 109PID4v.2 Each peptide is a portion of 27|1 VPGMDLLSGTYIFAV |12 N' terminal- SEQ ID NO: 5; each start |2| PGMDLLSGTYIFAVL ||1 B2705- position Is specified, the length El WNUQIFQVLCGUQ1 10mer of peplide is 15 amino acids, 7V and the end position for each |I||LCGUQQTVrSVPGM 11| peptide Is the start position 24 |VTSVPGMDLLSGTY i dplus fourteen 271 VPGMDLLSGTYFAV||34 teT XLV109R104j 21 Qq SVPMDLLSG 31 209 Each peptide is a portion of Table XXII-109P1D4 Table XXIII-109P1D4 SEQ ID NO: 5; each start v.3-A1-9-mers v.3-A0201-9-mers position is specified, the length Each peptide is a Each peptide is a of peptide is 15 amino acids, portion of SEQ ID NO: portion of SEQ ID NO: and the end position for each 7; each start position is 7; each start position Is peptide is the start position specified, the length of specified, the length of plus fourteen peptide is 9 amino peptide is 9 amino acids, and the end acids, and the end 13||FQVLCGLIQQTVTSV I26 position for each position for each IF LC peptide is the start peptide is the start 4|ERQWVLQI~FQVLCG||22] position plus eight position plus eight 10|| IQIFQVLCGLIQQTV ||22 6|| QWVLIQIFQVLCGLI |20 TSHGLPLGY SLTSTHGL | 9| LIQIFQVLCGLIQQT ||0 SAQASALCY 2ALHHSEPLV| 21|QQTVTSVPGMDLLSG||20 NCTQECJY 2GLCSVQGV| 27] VPGMDLLSGTYFFAV||20 S.SDGGLDH 19RLHPSDSI 3]1 TERQWVUQIFQVLC 18 DYDAGSLTS 3ALCHSEPP 11 QVLCGUQQTVTSVP 18 0 REGDGNSD 256SPLPQlAL [|| RQWVLIQIFQVLCGL 14 NSDPESTFI QGADGLCSV| 7l| WVUQlFQVLCGLIQ |14 [238FIPGLKK SALCYPPL i2| IFQVLCGUQQVS |141 176 PGYPQEEY SALCHPPL |9 16I| LCGLIQQTVTSVPGM |14 18 DEESTFIPG IALCHPPV |j 17|CGLIQQTVTSVPGMD 14 KSEGKVAGK 2 SALHPPL 29] GMDLLSGTYIFAVLL H|4 SSSDGGLGD ALHSEPSA 19 132 ASDNCTQEC 5 HTRPPMKEVH Table XLIX-109PID4v.2 N' 28svVGS 1 AISHSSPL FH Terminal-ORBI 1101 1 1 15-mers 1110 QSATSFY SHSSPLPQV ( Each peptide is a portion of 32 YMSERHP SQAQSVSL SEQ ID NO: 5; each start 310 PaDDSIVI AEITVPTV position is specified, the length PEEYFRA of peptide IsI15 amino acids, E1 4 i 1140 HLYISD ~ and the end position for each IHDACWMPA DACWMEASL peptide is the start position 7M8ERLHESD 4 1 STQHHPRV 7 plus fourteen |MEVRSCT 13 1 ALCHSEPVT |J 10| IQIFQVLCGLIQQTV [18 186|SLDHSS6SQ 13 HLPGSQES|_ 241 VTSVPGMDLLSGTYI |18 1 VQTIALCH F4PLEEA |1 411ERQWVUQIFQVLCG||16 VHTAC VQTEA| 171 CGUQQVVGD||15 SELPQVIAL | 239 ALCYSPLA 1 9|| U~CGQ QT ||14 272|SVSLQQGWV|16 LIQIFQVLCGLIQQT Table XXIl-109P1D4 274 SLQQGWVQG|16 2|jQQTVTSVPGMDLLSG||14 v.3-A0201-9-mers 3| SKVIELTT 16 6| QWVLIQIFQVLCGLi |1 Each peptide is a KVIP H 7] WVLIQIFQVLCGLIQ ||12| portion of SEQ ID NO: 16 13|QLCUQVTV|2 7; each start position is VAGKSQRRV|1 n131 FQVLCGLIQQ-TvTSV1 12 specified, the length of 66 GLGDHQAGS|9 18I| GUQQTVTSVPGMDL[|12 peptide Is 9 amino 271 VPGMDLLSGTYnFAV|12| acids, and the end TFIPGLKKA position for each 2 VALHRSQA |III 29| GMDLLSGTYILFAVL |12 peptide is the start 303 TMSERLHPS|III position plus eight HSQRRVIHL (I 2101 Table XXill-109P1D4 2 Table XXV-109P1D4 v.3-A0201-9-mers_ Results v.3-A3-9-mers Each peptide is a Each peptide is a portion of SEQ ID NO: portion of SEQ ID NO: 7; each start position is Table XXV-109P1D4 7; each start position is specified, the length of v.3-A3-9-mers specified, the length of peptide is 9 amino peptide is 9 amino acids, and the end Each peptide is a acids, and the end position for each portion of SEQ ID NO: position for each peptide is the start 7; each start position is peptide is the start position plus eight specified, the length of position plus eight peptide is 9 amino acids, and the end LGDHDAGSL 1 position for each SAQASALCY HDAGSLTST is the start IgrN SAI$Y 1 81FGLPLGYPQE GpositGo plus eight GKA QR 9PESTFPGL [ SVTRPMK 2 4 RVFHLPEG 6GKAAEIT VVRSCIEMK 24 FHGSE 141YGHSAC 14 WFHPQR GL_ F5 SLDHSSSSQ [LVQTA[H GL!EKA1E1T HVA~ J212EIOIE~ SHSPPVQTI 14 3ALRSQQS [22IVQIVE ALHRSAQS 14 EKVAGKQRR QAASALCH G27W81 VQGADGL 4 SLQQGWVQG 1ALHSEELS 312 DDSIKF3PL 4 1 iPLTFT ALHSEP | j STSHGLPLG KSEGKVAGK1 ALJAHSEELV E i~EL~iI~ ~QVIALHRSQ ~929ALOYSEELA fIQJ 11RPSSI [ SVSLQQWV 14 AASlMI1T T3 1 STE1PGLKK 145KSQRRMIFH|9J TJIVQPIVEE 3!J 4 CLYGUSDA 153HLEEGSQES|~ 131SDNCTQECL 13 17 SQ 18I9H FDEATESNR|E S2 ALCHSVT A 13 ALCHSEPLS VSALHH 1TILCSPP CHSPPEQV PLEQVLALH___ 17PVIQTALC13 I21 25 F LE4VI01 18 ~ i IL~~P13 1HHSPP1VQA 13GVGSASQ TIALCBPP 21CYSPPLAQA 13SiV_ LT SQQV P LPQV! 1RPeMKEVVR 17WVGALC1 2LQQGWV 3 y RTQTIALC 1728SVQGMQGS 1 8 SVDQGQGS 13Q 1 LHPSDDSIK13 221 F19AILH1771 39 HPSDD2IKV 1 17 VIELTETP1 31 VPLTFTP 13VIHBQA 1/ QPQKSGKTable XXVI-109P1D4 Table ~~RKG -~ 6 v.3-A2-9-mers XXIV- 81GLLGXEQE 16 Each peptide is a 109P1D4 83PLYPQEY 6 portion of SEQ ID NO: V.3- [1jSLDHSSSSQ 167; each start position is A0203-9- - ---- specified, the length of 1212V LBSPpeptide is 9 amino FALHSEESA 6 acids, and the end F30-9 0K1QR3T 15p245n o ec GKQRe pd pIs the sart v.3 L7YGHSDAC 15 position plus eIght 211 Table XXVI-109P1D4 Table XXVi-109P1D4 EVVRSCTPM 2 -A26-9-mers v.3-B0702-9-mers 31 DDSIKVIPL Each peptide is a Each peptide is a portion of SEQ ID NO: portion of SEQ ID NO: DACWMPASL 17 7; each start position Is 7; each start position is 315IKV1PLTTF specified, the length of specified, the length of L peptide is 9 amino peptide Is 9 amino acids, and the end acids, and the end 14TVQPTVEEA position for each position for each 256SPLPQVIAL 16 peptide Is the start peptide is the start 260 QVIALHRSQ 1 position plus eight position plus eight 1313 KVIPLT109 PESTFIPGL ] PPMKEVVRS DM EHPL 123 ITVQPTVEE 1 4RPPMKEVR14 R33F51 HL EEASDNCTQ | TSTSHGLPL | F9RATPS NCTQEC13Y |5PGLKKAE | 2ETQP -ECLYGHSD 2 D9 93CHSPPVTQT| 4 7 PTVEEASDN QVSALHHSP 217|HHSPPLVQA4 E3SAQASALCY F]DDSIKVIPL 13 WCQTCIALC 1527 SVSLQQGW1 ~ IPLTFTPR |I4 185VTQTIALC GWVQGADGL SQRRVTFHLI 19RE TTIL 15 SVDQGVQGS _________9 TPSNRTEGDIE3j 2S STTM l Table I-1 09P1D4 PESTFIPGL IE 1231 SflMIWIH [41v.3-830702-9-mers [F2 HHP2 SQA9j1 24 TMEWIHP Each peptide is a 271 PQPQ 1 portion of SEQ ID NO: 24 CYSPPLAQA|fIS EST 1GK7; each start position is 2 5 ISHSSPL | [1B1ESPK 14 specified, the length of 27SASVL13 PRVTQTIAL t peptide is 9 amino oSASSS| QTIALCHSP 14 acids, and the end TP2 ARS 881 PPQTIALS 141 position for each HTRPPMKEV|12 Fi~ R PTTAL1 peptide is the start 3112PRSE( 200 QTALCHSP 1 position plus eight HPQESE 8PPPQVSAL 4 5 ESSS 21 AAISHSSPL 232 PPSAQASAL 2S g 3 TFTPRQQA 2 SPLPQVIAL 23 [2JLPLGYPQEE g12 VTFHLPEGS 13PPVTQTIAL DPESTFIPG ESSSDGGLG 13 PPPQVSAL TSTSHGLPL PPLVQATAL CHSPPL 77STSHGLPLG 1 RPSRGDSPM C 3P QA 12 78TSHGLPLGY 13 F TPMKESTTM P V 128TVEEASDNC SPRVTQTIA 12 HSPPL EASNCTQE E] [71SPPPIQVSA 21 SALSPPL2 SDGLCSVDOG 4 PPL[AQAAI 23 SSSPP 2 3SVHTRPPMK 212 SPPLA A [3 SSLPQV [2 3 VVRSCTPMK ElHPSDDSIKV 1 LQAH ESTMEWI 12 SPPLSQAST Table XXVIII-109PD4 ]EGKVAGKSQ 151 SPPVTQTIA Ta17 V., 56EGSQESSSD 219SPPLVQATA DAGSLTSTSI2 21SPPSAQASA 212 Each peptide is a Table XXVIll-109P1D4 Table XXIX-109P1D4 portion of SEQ ID NO: v.3-B08-9-mers v.3-B1510-9-mers 7; each start position is f ZII specified, the length of Each peptide is a Each peptide Is a peptides 9 amino porton of SEQ ID NO: portion of SEQ ID NO: aidds, and the end 7; each start position Is 7; each start position is position for each specified, the length of specified, the length of peptide is the start peptide is 9 amino peptide Is 9 amino postide ps theight acids, and the end acids, and the end position for each position for each peptide is the start peptide is the start 312 DDSIKVIPL position plus eight position plus eight [256 SPLPQ VIAL 20 1 _ 114 IPGLKKE 2GWVQGADGL1E 30QOFYTMSERL 12 46 SQRRVTFHL 18 12 DDSIKVIPL |2 74 SLTSTSHGL 18 Table XXIX-109P1D4 lQESSSDGGL 208 S AL -- v.3-81510-9-mers IQS 16TSTSHGLPL E 281Each peptide is a :76:] ___E_ 220 PPLVQATAL portion of SEQ SHGLPLGYP 11 7 RPPMKEVVR .7; each start position Is 105 GNSDPESTF 115 PGLKKAAEI17id the length of 1471 116GK acids, and the end SSQAQASAL PPVTQTIAL 17 position for each 66 SALCHSPPL11 32_ 91 peptide is the start18PRQTA[] PP232ALposition plus eight 7SIKVPLT PPVTQTIAL QPQRKSEGK 130IHPQPQRKS 1P 44 GKSQRRVTF 16 217HHSPPLVQA SALCYSPPL 16SALCHSPPL 16 10QHHSPRVTQ 15QRRVTFHLE~ 1 SALHHSPPL 16 3CHSPPVTQT 1LGDHDAGSL 10 2SALCYSPPL 1625CHSPPPQV 1574 SLTSTSHGL 1 183 SPRVTQTLA 15 19 CHSPPLSQA SDNCTQECL EGKVAGKSQ 1 HHSPRVTQT AISHSSPL 10 TPSNRTEGD 14 26LHHSPPLVQ 14LHRISQASSK1 171DACWMPASL 1 2 HHSPPSAQA 14 ISHSSPL 14 SPLPQVIAL S H L 6IALHRSQAQ 14 []SQAQSSVSL D PMEE 9PMKEVVRSC GKQRVFTMKST [25-0 14QRVT F3 If HTPP [] 9PESTFIPGL T1 PPLAQAAAI 314 GHSDACWMP 1 LGYPQEEYF[] SQAQSSVSL LHH22 -I-SPPSAQ 1330RPSRGDSPM ~ I11PMKESTTME r2 53 SHSSPLPQV[1 TalXX-0PD1 fJSDNCTOECL 2j7 GWVQGADGL [fjIv3B2 09mD4 21 ALCHSPPPI 1 VHTRPPMKE Each peptide Is a RLHPSDDSI 1 FILPEGSQE portion of SEQ ID NO: TPRQQARPS 69DHDAGSLTS 127; each start position is 2QRKSEGKVA [DHSSSSQAQ slpepede t ino KSEGVAGK11 P~loSALacdds, and the end PESFIPGL 11 PPLVQATAL peptide Is a PRVTQTIAL 11 PPSAQASAL position plfs eagh 213 Table XXX-109P1D4 3PRQQARPSR v.3-B2705-9-mers 184PRVTQTIAL 14Each peptide is a F6TPMKW1 PRVQTIAL porin of SEQ T NO: ~] GKVAGKSQR 19 7; each start position Is HRSQAQSSV| 278GWVQGADGL specified, the length of RRVTFHLPE 16 IWHPQPQR is 9 io GWVQGADGL ________acids, and the end F-8 1 KVAGKSQRR 18 position for each 256 SPLPQVIAL 1 RPPMKEVVR peptide is the start 76 TSTSHGLPL 13 KSEGKVAGK position plus eight 166SALCHSPPL 13 44GKSQRRVTF LGYPQEF 3 SALHHSPPL 1 111 STFIPGLKK F92DRPS PPLVQATAL 13 35IKViPLTTF 17§]FTC R lYGH3 SALCYSPPL|Es3 ________ 137 QCLYG 13 1 RRVTFHE25 LPQVIALHR A250 SHSSPL |3 99NRTEGDGNS DDSIKVIPL 300QFYMSERL GNSDPESTF RLHPSDDS 13 )HRQA 1S 61 322-7 131QQR13____ 3H32RSRGDSPMEE 13GKSQRRVTF 27SQAQSSVSL 16VVRSCTPM_ 6 LGDHDAGSL 12] 12RS 1RSEGK SLTSTSHGL 12J 3301RSGDP 16 1-33 ___ 8TPMKESTTM 15KS99VANRTEGDGNS 1 93DRATPSNRT QESSSDGGL__ 1LALCHSPPV 1 E 5 9 Q12DGL1 [9PPIQVSALH is 7LGDHDAGSL 1225GLCSVDQGV 220O PPLVATA 1512___ 78TTSHGLPLGY2 ERLHPSDDS 9 5AAISSSPL PLGYPQEEY ARPSRGDSP 12 SPLPQVIAL YPQEEYFDR RPSRGDSPM PLQAHSNCQC 35QRKSEGKVA 2 SQYTMR NCTQECL1 QESSSDGGL __29 ____91_ H135NTEU 12 Ri] QFYTMSERL 5DACWMPASL LGYPQEEYF 38IPLTTFTPR LI10SSQAQASAL 1i1[]DRATPSNRT i AGSLTSTSH 196PPVQTIAL 12 1 GNSDPESTF 11 109PESTFIPGL PPHL PESTFIPGL 1 15PGLKKAAEI 4 1 PGLKKAAEIl1 1SALCHSPPL 1 21PPSQAAL 211AFVPV1 1PLSQASTQH 4 ~ VPSQSASQF~ YGHSDACWM 1_1 P 293 VQGATQ3 2 1ASTQHHSPR WI30JLHPSDDSIK 12J19 SSQQAAL 11 214SALHHSPPL ARP 238SALCYSPPL 208PPPQVSAL 38 ERLHPSDDS Table XXXI-109P1D4 2PPSAQASAL |H 307RLHPSDDS v.3-B2709-9-mers 1 2 PPLAQAAAI 1 RGDSPMEEH Each peptide Is a SHSSPLPQV STRPPMKEV portion of SEQ ID NO: 267 SQAQSSVSL 14VRSCTPMKE n7 each st r[ SATSQFYTM __________specified, the length ofE1 23 STTMEWIH peptide Is 9 amino [31 DDSIKVIPL 11 WIHPQPQRK acids, and the end PRQQARPSR Position for ec 45 KSQRRVF peptide is the start SSDGGLGDHIE3 position plus eight 214 Table XXXI Each peptide is a Table XXXIII 109P1D4v.3-B4402- portion of SEQ ID NO: 109P1D4v.3-B5101 9-mers 7; each start position is 9-mers Each peptide is a specified, the length of Each peptide is a portion of SEQ ID NO: peptide Is 9 amino portion of SEQ ID NO: 7; each start position acids, and the end 7; each start position Is is specified, the length position for each specified, the length of of peptide is 9 amino peptide is the start peptide is 9 amino acids, and the end position plus eight ads, and the end position for each [ position for each peptide is the start PPLAQAIl peptide Is the start position plus eight jVAGKSRV position plus eight PESTFIPGL__|T DACWMPASL 2 117 LKKAAEITV jJ 9 KESTTMLW2 IALCHSPPV 1QAQASALCH QESSSDEL 2 HPSDDSIKV IALCHSPPP 256SSPLPQVIAL 19 1 PGLKKAAE 21 S SALCY [1AEITVQPTV 1825SPQVA 2154HSSPL.PQV1 i [20ISHSSPL j620PPLVQATAL 20 (J ALH-RSQAQ 1 301PSDDSIKVI 1628PPPIQVSAL 1 22GADGLCSVD 14 2MElW1HPQP 15F31SALCYSPPL 1 jJDDSIKVIPL 4 4GKSQRRVTF 1516SALCHSPPL 18ESTTMElI3 __________ 116 25QIA 8 41 IGKAE1 84PRVTQTIAL 5 16PPVTQTIAL 15111SALHHSPPL 1 1 AETQ 89IEEYFDRATP Ii4 22PPSAQASAL 1 2JAE1QT1 SSQAQASALIPLTTFTPR18121AfVPV 3 ijJHSPPVTQTI jy 2LPLGYPQEE 1 95SPPVTQTIA 3 ________ 108 DPESTFIPG417 30PPPIQVSAL PESTIPG 22 TALHHSPPS 13 PPLVQATALPSDDS2KV QAQSSVSLQ 2PPSQAAL RPPMKEVVR SATSQFYT 24HSSPLPQVI 171DAGSLTSTS 1 3JQFYTMSERL 13 1KEVVRSCTP 1350 AASHSSPL 16J~ TPRQQARPS 13 [ SEGKVAGKS 1 28 QGADGLCSV I~]10MKESTTMEI[2 SSQRRVTFHL 13PMKEVR 15~ PQRKSEGKV 12] TSHGLPLGY TPMKESTTM~ LGYPQEEYF[2 LGYPQEEYF 13 61LGDHDAGSL __101NSDPESTFI 2 QEEYFDRATRATPSNRTE ~ 131 EASDNCTQE|[12 GNSYDESTi DNCTQECLI 1± 11SPPLSQAST|[2 10 NSDPESTF [i PPLSQASTQ I] fj SPRVTQTIA [2 1064 NSPSF13_______ 1EEASDNCTQ [~I12HSPRVTQTI 15A CHPP [2 SAQASALCY 14HSPPVTQTI 1 ]SPPPIQVSA|[2 6SERLHPSDD 21SPPLVQATA 120 PPQVSALH |{1 DDSIKVIPL_ 246 LAQAAISH js LPQVIALHR Table XXXIV Table XXXIIl DGLCSVDQG|1 109P1D4v.3-A1 109P1D4v.3-B5101 TRPPMKEV 14 9-mers LPEGSESS 1 SYPQEEYFDR14] 215 Each peptide is a Table XXXV-109P1D4 Table XXXV-109P1D4 portion of SEQ ID NO- v.3-A0201-10-mers v.3-A0201-10-mers 7; each start position is Each peptide is a portion Each peptide Is a portion specified, the length of of SEQ ID NO: 7; each of SEQ ID NO: 7; each peptide is 10 amino start position Is specified, start position is specified, acids, and the end the length of peptide is the length of peptide is position for each peptide 10 amino acids, and the 10 amino acids, and the is the start position plus end position for each end position for each nine peptide is the start peptide is the start position plus nine position plus nine [ 8 SISHGL LGY 16 13 r-PSAQASALCY 5 FHTRPPMKEW LCYSPPLAQA| [q DNCTQECLIY 21 [2011 PMKESITMEI [24411 SPPLAQAAAI JH SDGGLDHD 8STFIPLKKA 3 TMSERLHPSD SRIEGDGSDP 8 VQPVEEAI TTMEIWIHPQ |12 17NSDPESIFIPLI15 SLDHSSSSQA 1161 330[WHPQEQRKS 12 38KSEGKVAGKS WI ALCHSEPVTQ 6][ QPQRKSEGKV 12 32SDDSIKVIPL 1 jJSDDSIEVIPL [6 s]SQESSSDGGL|1 LELGYPEEY GSLTSISHGL 1 ASDNCQECL12 ~jVQGSATAQFY L6111LIYGHSDACW C ~ TQECLIYGH |t~ ~3JASDNCTQECL E11]ASALCIISPPL [s11CLIYGHSDAC SALCHSElPLSQ 1578ASTQHHSPRV Table XXXV-109P1D4 ASALCSPPL HHSPRVTQTI v.3-A0201-10-mers 35SIKVlELTTF 1514CH-SPPVTQTI 2 a pe a n HLPEGSQESS 1ALCHSPPQV 1 start position is specified, 19DPESTFJPGL 14 211LHHSPELVQA[2 the length of peptide is11 FIPGLKKAAE 14[51SPLPQyLALH [2 1amnas, and 1 IPGLKMAAEI 4 6 VIALHBISQAQ [2 peptide is the start 24VSALHIISPPL [1[ 7 SSVSLQQGWV 2 posItion plus nine ~ ~ ]ALHRSQAQSS [428QGWVQQADGL 1 ___________ ~LH-RSQAQSSV [425DGLCS2LDQGV|12 67GLGDH2AGSL 2427RSQAQSSVSL SVDQ28QGSA|2 17GLKKAAEITV 39LH-PSDQSIKV []30SQFYTMSERL |2 L~1TIALCIISPPV 21 35GDSPMEEHPL []33YTMSERLHPS |2 [7jSLQQGWVQGA [~ 2GLPLGYPQEE 1338RLHPSDDSIK [| | [4]KVAGKRQRRV [~ 6JSSSQAQASAL 1iJHPSDDSIKVI |2 2tjSPPPIQVSAL I18]SPRVTQTIAL 1 215 SALHHSPPLV IALCHSPPVT Table XXXVI 1 3AATQPTV sSPPVTQTIAL 109P1D4.3-A0203 E DACASL ALCHSEPLQ Each peptide Is a 216 Eportion of SEQ ID NO: LTSTSHGLPL SPPLVQATAL 7; each start position Is AAe V TAL13 specific, the length of 0 IALCHPPPI ALHHSPSAQ acids, and the end e53 ISHSSELPQV SPPSA [S AL Ff eac ssuvA ____peptde is the start F14VAHSP 41 S2PLPQV[AL SALCYSPPLA position plus nine 28 VQGADQLCSV ALCYSEPLAQ 216 Table XXXVI Table XXXVII Table XXXV1ll 109P1D4v.3-A0203 109P1D4v.3-A3 109P1D4v.3-A26 1 0-mers 10-mers 10-mers Each peptide Is a Each peptide is a portion Each peptide is a portion portion of SEQ ID NO: of SEQ ID NO: 7; each of SEQ ID NO: 7; each 7; each start position Is start position is start position is specified, the length of specified, the length of specified, the length of peptide is 10 amino peptide is 10 amino peptide is 10 amino acids, and the end acids, and the end acids, and the end position for each position for each peptide position for each peptide peptide is the start is the start position plus is the start position plus position plus nine nine nine 1243IYSPPLAQA PLEQALHR [20 EVVRSCTPMK [I51 [11 TEIPGLKKAA 19 i ALCHSPPLSQ 1 09 DPESTFIPGL 21 2 CYSPPLAQAA SVLQQGWVQ 19 STSHGLPLGY| 20 D1SSSSQA 8SIVIETF 9 GVQGSATSQF 20 19SSSSQAQASA 137RKSEGjKVAGK 1 05DGNSDPESTF||19~ 219 HSPPLVQATA 18 ALHHSPSAQ 1DNCTQECLIY|1 [n]LIHSPPSAQA 81j7JALQYSEELAQ ~8J6LTSTSHGLPL |I 231 HSPPSAQASA 1WVGALCS STFIPGLKKA |8 L241 YSPPLAQA 1AGSQVTF 3 SIKVIPLTTF 18 14F!PGLKKAAE 17~GLQDHQAGSL E9 91 EYFDRATPSN|16 SEPLAQAAI Y142FLYGHSDACW IVQPTVEEA 16 SLDHSSQA [17 SPPPQVSAL 16 Table XXXVII QVSALHSPP 261QVIALHRSQA 109PID4v.3-A3 2 EWIHPQPQR KVLTTFTP I1 Each peptide is a portion 6 ESTTMEWIH 15 of SEQ ID NO: 7; each KVAGKQRRV 6 TTMEWHPQ start position is ESTFIPSLKK EIWIHPQPQR 15 specific, the length of TREPMER EIVQPVEE peptide Is 10 amino 1 acids, and the end VVWSCIEMKE 15 SSPLPQVIAL | position for each peptide RVIFHLPEGS SDDSIKV1PL |i is the start position plus GLEKAAEIV VTFHLPEGSQ 1 nine A LWEVHF]RfHPEGSH ]22AHSELPQ ESTFIPGLKK 14 RLPSSIK GLSVGVQ 15 128PTVEEASDNC|1 EVRSIPMK 1 CTQECLlYGH | 86RVQTIALCH Table XXXVIII 3 LVQATALHHS| 14 QVA-1Q 24 109P1D4v.3-A26 |DSKVIPLTT| 261~~~ 0LjSA~l-mers 31 IKVITPL1 14 ~ KVPLIFTP 23 Each peptide is a portion |TTFTPRQQAR 1 9 A HSEEVTQ of SEQ ID NO: 7; each [ ESSSDGGLGD13 GVQGS_ SQstart position IsDHDAGSLTST 3 293 22~SQ specified, the length of [12 1VPVEA 216ALpHSEELVQ21 eptide Is 10 amino T PVEA [ ALRSAQSS acids, and the end 129 TVEEASDNCT 1 ZPVIQTALCH position for each peptide QTIALCHSPP 1181 is the start position plus 20 ~CSP13 F2 PLyQAILHH |20 nine QTIALCHSPP PLAQAAISH |2o SVDQGVQGS 13 217 Table XXXVIII Table XXXIX Table XLII 109P1D4v.3-A26 109P1D4v.3-B0702 109P1D4v.3 10-mers 10-mers B2705 10-mers Each peptide is a portion Each peptide is a of SEQ ID NO: 7; each portion of SEQ ID NO: start position is 7; each start position Is [o Results specified, the length of specified, the length of peptide is 10 amino peptide is 10 amino acids, and the end acids, and the end position for each peptide position for each peptide Table XLIII Is the start position plus Is the start position plus 109P1D4v.3 nine nine B2709 10-mers |6 SQFYTMSERL| [3| [JGDSPMEEHPL 14 J YTMSERLHPS [ | PPMKEVRSC9 MiIASDNCTQECL1o 9Table XXXIX | SSSQAQASAL|3 Table XLIV-109P1 D4 I09P1D4v.3-B0702 2| VSALHHSPPL 13 v.3-B4402-10-mers Each pepte Is aSDDSIKVIPL Each peptide is a portion portion of SEQ ID NO: 9 IPLTTFTPRQ 1 of SEQ ID NO: 7; each 7; eachstartpsition start position Is specified, secithe ntar of isV VS V HT RPP 12 the length of peptide is speie, e KSQRRVTFHL 12 10 amino acids, and the peptide and the nd LPEGSQESSS__ _ end position for each adds an theendLPESQESS [j~jpeptide is the start position for each peptide LPLGYPQEEY Ii position plus nine is the start position plus 1TP GDG 12 __SDACWMPASL 122 11 KESTTMEIWI SPRVTQTIAL PPQVSALHH AEITVQPTVE 19 SPPi F2QS]PPLVQATA 2 1 SPPPIQVSAL 96SPPVTQTIAL PPLAQAIS 1 25 SSPLPQVIAL 220SPPLVQATAL 22 25 SSPLPQVIAL AGKSQRRVTF 16 DPESTFIPGL SPLPQVALH 6SPPVTQTIAL [3SPPSAQASAL 2 :] SPPLVQATAL[6 [5 IPGLKKAEI Table XL 3 HPSDDSIKVI 1 1OI4v.3 HPSDDSIKV 109P1v.3- ASDNCTQEL 15 2 SPPLAQAAAI 1 10-mers 10SSSQAQASAL [5 8]YPQEEYFDRA [184 SPRVTQTIAL 1 QPQRKSEGKV No Results SPPSAQASAL 15 LTSTSHGLPL Found. GDSPMEEHPL ASALCHSPPL MEIWIHPQPQ 14 F ____661__ Table XLI ASALCYSPPL 15 19P1D4v.3- STSHGLPLGY SRPPMKEVVRS B1510 11 PESTFIPGLK J1 19TPMKESTTME 1 10-mers 166 ASALCHSPPL 14 PPSAQASALC HHSPRVTQT1 14 250 AAAISHSSPL[ CHSPPVTQTI | 4 26 RSQAQSSVSL ASALCYSPPL | 4 325TPRQQARPSR SPPLAQAAAI 114 SRPSRGDSPME I~ 32 SDDSIKVIPL [4] 218 Table XLIV-1 09P1 D4 Table Table XLVI-1 09P1 D4v.3 v.3-B4402-10-mers XLV- DRBI 0101-15-mers Each peptide Is a portion 109P1D4 Each peptide is a portion of SEQ of SEQ ID NO: 7; each v.3- ID NO: 7; each start position Is start position is specified, B5101- specified, the length of peptide is the length of peptide is 10-mers 15 amino acids, and the end 10 amino acids, and the position for each peptide is the end position for each No start position plus fourteen peptide is the start Results position plus nine Found. 55|| RVTFHLPEGSQESSS |2 13 270|LHRSQAQSSV=SLQQGd SSEGKVAGKSQ|9 [Table XLVI-1 09P1 D4v.3- F29]1 STTMELWQHPQ |o 46 KSQRRVTFL DRB1 0101-15-mers 1 ESTFIPGLKKA i 9 74 GSTTSI 13 Eac ptIis a portion of SEQ I1~ SFPLKET 1 LTSTSHGL ; each start position is 1 20 IPGLKKAAEIVQPT [9| LTSTSHGLPL 9 specked, the length of peptide is 326 LTTFTPRQQARPSRG ||1 F D P i 15 amino acids, and the end __PQEEYFDR T ||1II| DPESTFIPGL 13 position for each peptide is the 153| ED RAC PASD S S 18 91EADCQ start position plus fourteen 1 DACWMPSDSS [81 SEEASDNCTQE I 278||SVSLQQGVQGADGL |8| SASHSSPL j3 320|| SIKVPLTTFTPRQQ |30 2I]|GLCSVDQGVQGSATS |8| G SQF2ME] 5] QRRVTFHLPEGSQES 26 [|RQQARPSRGDSPMEE||18 F31Y51 T SiK L |146TF|| 13' CLIYGI-ISDACWMPAS 26| 3 TFEVPVSVHTRPPMK I SSKVIPLTF | 245|| ALCYSPPLAQAAIS |26| 117 KEWRSCTPMKESTT ||i7 QESSSDGG G 1281|| LQQGWVQGADGLCSV|| 25| 21 | RSCTPMKES 1TME 7W |1 GLGDH SL 33|| EWHPQPQRKSEGK ||24] 41|QRKSEGKVAGKSQRR|17 LPLGYPQEEY | I70||DGGLGDHDAGSLTST |24 42||RKSEGKVAGKSQRRV |17 89 QEEYFDRATP12 21 PIQVSALHHSPPLVQ 24] 45| EGKVAGKSQRRVTFH I|17 [9 DNCTQECLIY |1 2 HHSPPLVQATALHHS [24] 67| SSSDGGLGDHDAGSL 17 N QECLYGHSD 12 2 LPQVIALHRSQAQSS |24] 7811 AGSLTSTSHGLPLGY 171 47 SDACWMPASL2 267 VIALHRSQAQSSVSL 24 114| DPESTFIPGLKKAAE || 24 PSAQASALCY |I 283|QGWVQGADGLCSVDQ||24] 118 TFIPGLKKAEITVQ 17 2~ SHSSPLPQVI |1 318|| DDSIKVPLTFTPR 24] 189|| SPRVTQTIALCHSPP |17 306SERLHPSDDS]12 B_ KEWRSCTPM| 23 CTPMKESTTMEIW1H ||23] 201 SPPVTQTIALCSPP ||17 59 SQESSSDGGL 11 193| TQTIALCHSPPVTQT 23 - SPPLVQATALHHSPP I|17 102QTESSSDGL 205| TQTIALCHSPPPIQV |23 28 LVQATALHHSPPSAQ 17 TEGDGNSDPE 11 2S||QSSVSLQQGWVQGAD 1247| CYSPPLAQAAAISHS |17 ,05|DNDET1 327 TTFTPRQQARPSRGD 23| 253 AQAAAISHSSPLPQV |1 30j VEEASDNCTQ _4j FEVPVSVHTRPPMKE ||I 275|AQSSVSLQQGWVQGA |1 LYGHSDACW i Ii8]|PQPQRKSGKAGKS||22 j TSQFYTMSERLHPSD ||17 [2 VSALHHSPPL |1 1158 PASLDHSSSSQAQAS||I |309|| TMSERLHPSDDSIKV ||7 [6 RSQAQSSVSL| d 248|| YSPPLAQAAISHSS |22| | VTTFEVPVSVHTRPP [1 27 QSSVSLQQGWH 261 SSPLPQVIALHRSQA |22 | EVPVSVHTRPPMKEV |16 278 QGWVQGADGL EDQGVQGSATSQFYTM||2| 32| MEIWIHPQPQRKSEG ||16 107 ERLHPSDDSI | 1261 AAEITVQPTVEEASD 121| |50 GKSQRRVTFHLPEGS [|1 294| SVDQGVQGSATSQFY 21| |571 TFHLPEGSQESSSDG|I1 305 SQFYTMSERLHPSDD ||211 7 DAGSLTSTSHGLPLG 16 I PPMKEVVRSC 2 |79| GSLTSTSHGLPLGYP |J 219 I Table XLVI-1 09P1D4v.3- Table XLVI-1 09P1 D4v.3- Table XLVIl-1 09P1 D4v.3 DRB1 0101-15-mers DRB1 0101-15-mers DRB1 0301 15-mers Each peptide is a portion of SEQ Each peptide is a portion of SEQ Each peptide is a portion of ID NO: 7; each start position is ID NO: 7; each start position is SEQ ID NO: 7; each start specified, the length of peptide is specified, the length of peptide is position is specified, the length 15 amino acids, and the end 15 amino adds, and the end of peptide is 15 amino acids, position for each peptide is the position for each peptide Is the and the end position for each start position plus fourteen start position plus fourteen peptide is the start position plus

-

I Ifourteen 182|| TSTSHGLPLGYPQEE [|16 1| CTQECLIYGHSDACW ||15 87|| GLPLGYPQEEYFDRA [|1 [56WMPASLDHSSSSQAQ 15 IPGLKKAAEITVQPT [17 94|| QEEYFDRATPSNRTE [1 169 AQASALCHSPPLSQA |15 264] LPQViALHRSQAQSS 7I 9J EEYFDRATPSNRTEG [1 [i| SQASTQHHSPRVTQT ||15 F27 GLCSVDQGVQGSA|17 109|| GDGNSDPESTFIPGL |1 i86 QHHSPRVTQTIALCH 15 326||LTTFTPRQQARPSRG|17j 117|| STFIPGLKKAAEIV 16 [198|| LCHSPPVTQTIALCH ||15| 5_EVPVSVHTRPPMKEV||6i 128|| EITVQPTVEEASDNC 16 212 HSPPPlQVSALHHSP ||1 292|LCSVDQGVQGSATSQ||1 1141|| NCTQECLIYGHSDAC |1 217 IQVSALHHSPPLVQA |15| 301 TSQFYTMSERLHPSD| 16 154||ACWMPASLDHSSSSQ 16 229| VQATALHHSPPSAQA |15 78 AGSLTSTSHGLPLGY |14 155||CWMPASLDHSSSSQA|1 1241| AQASALCYSPPLAQA [5| 136| EEASDNCTQECLIYG||14 161| LDHSSSSQAQASALC |16J 265|| PQVIALHRSQAQSSV |15| 1|KEVRSCTPMKESTT3| 163 HSSSSQAQASALCHS |16 312 ERLHPSDDSIKV1PL |15 64|SQESSSGGLGDHDA |13| 168|| QAQASALCHSPPLSQ |1 |69||SDGGLGDHDAGSLTS||1 1187|| HHSPRVTQTIALCHS 16 Table XLVIlI-109P1D4v.3 126 AAEITVQPTVEEASD 13 192 VTQTIALCHSPPVTQ |RB1 030115-mers j1|132|QPTVEEASDNCTQEC| 13| Each peptide is a portion of |24| ASALCYSPPLAQAAA |13| 2041 VrQTIALCHSPPPIQ [6' SEQ ID NO: 7; each start ||PQVIALHRSQQSSV||13| 214|| PPPIQVSALHHSPPL 16 position is specified, the length 222]| LHHSPPLVQATALHH [|16 of peptide Is 15 amino acids, and the end position for each Table XLIX-1 09P1 D4v.3 22| PPLVQATALHHSPPS 16 peptide is the start position plus DRB11101-15-rners 233|1 ALHHSPPSAQASALC 161 fourteen Each peptide is a portion of SEQ 2I351 HHSPPSAQASALCYS ||1 ID NO: 7; each start position Is 240 SAQASALCYSPPLAQ |1 108_ EGDGNSDPESTFIPG| 26 specified, the length of peptide is 240 LSAQAA ASH LI 108 EGDPGYSPEEDR 15 amino ads, and the end 246| LCYSPPL |16 8|GLPLGYPQEEYFDRA|24| position for each peptide is the 249| SPPLAQAAAISHSSP |16 318| DDSIKVIPLTTFTPR ||20| start postpfteen 258|| ISHSSPLPQVIALHR 16 3] EWIHPQPQRKSEGK| |19 268| IALHRSQAQSSVSLQ |1 [17 STFIPGLKKAAEITV |19| 1 RPPMKEWRS 292 LCSVDQGVQGSATSQ|16 13||RPPMKEVVRSCTPMK |18| 26| LPQVIALHRSQAQSS ||26 30] QGSATSQFYTMSERL ||16 [7TFHLPEGSQESSSDG |I 289 ADGLCSVDQGVQGSA ||6| 323|| vIPLTrFTPRQQARP |16 70|DGGLGDHDAGSLTST |18 l VTFEVPVSVHTRPP 22 71|| PVSVHTRPPMKEWR |1 [116 ESTFIPGLKKAEIT 18 153 DACWMPASLDHSSSS 22 13 |RPPMKEVVRSCTPMK| 15 128 EITVQPTVEEASDNC |1 5 |[ EVPVSVHT__PMKEV 20 1161 MKEVVRSCTPMKEST |1I [296jDQGVQGSATSQFYTM||8 [8ilMKNEW CPMET]I 14711 KVAGKSQRRVTFHLP 15 31]| TMEIWHPQPQRKSE|I7 gf| CTPMKESTTMEIWIH ||20 56|| VTFHLPEGSQESSSD ||1 45]EGKVAGKSQRRVTFHI l3| EIWHPQPQRKSEGK ||20 721 GLGDHDAGSLTSTSH |15 47|KVAGKSQRRVTFHLP [17] [57J TFHLPEGSQESSSDG ||2 7511 DHDAGSLTSTSHGLP ||15 : 8 HGLPLGYPQEEYFDR IPGLKKAAE QPT 85_ SHGLPLGYPQEEYFD ||15 [104|SNRTEGDGNSDPEST |17 132 QPTVEEASDNCTQEC ||20 220 Table XLIX-109P1D4v.3 Table XLIX-109P1 D4v.3 Each peptide is a DRB1 1101-15-mers DRBI 1101-15-mers portion of SEQ 11 NO: 9; each star Each peptide is a portion of SEQ Each peptide is a portion of SEQ position is ID NO: 7; each start position is ID NO: 7; each start position is specified, the specified, the length of peptide is specified, the length of peptide Is length of peptide is 15 amino acids, and the end 15 amino acids, and the end 9 amino acds, and position for each peptide is the position for each peptide is the the end position for start position plus fourteen start position plus fourteen each peptide is the start position plus 158|PASLDHSSSSQAQAS 53 QRRVFHLPEGSQES| 14 eight 177| SPPLSQASTQHISPR ||20| 7 DGGLGDHDAGSLTST I4[Z 193| TQTIALCHSPPVQT |20| 78| AGSLTSTSHGLPLGY | W1HPQPQSQ|M 216| PIQVSALHHSPPLVQ 2 117 STFIPGLKKAAEITV 141 HEQPQSRR 265|| PQVIALHRSQAQSSV 20 126 AAEITVQPTVEEASD 14 QSQRRVTFH|] 283 |QGWVQGADGLCSVDQ|20 [28|| EITVQPTVEEASDNC I14 0 QT 292 |LCSVDQGVQGSATSQ|20 [44||QECLIYGHSDACWMP14 320|| SIKVIPLTTFTPRQQ 20 ACWMPASLDHSSSSQ 109P1D4v a 201 323|| VIPLTTFTPRQQARP |2 171 ASALCHSPPLSQAST 14 9-mers 56|| VTFHLPEGSQESSSD ||18 195| TiALCHSPPVTQTIA 14 Each peptide is a 72] GLGDHDAGSLTSTSH | 205| TQTIALCHSPPPQV |14 portion of SEQ ID 155 |CWMPASLDHSSSSQA |18| 0 7 TIALCHSPPPIQVSA 14 posin is specified, 156|WMPASLDHSSSSQAQ ,214 PPPQVSALHHSPPL 14 the length of peptide ________________________________________is 9 amino acds, 174| LCHSPPLSQASTQHH 1 19 VSALHHSPPLVQATA |14 and the end position 186|| QHHSPRVTQTIALCH 18 | SPPLVQATALHHSPP 14 for each peptide is 198|| LCHSPPVTQTIALCH [|8 i6 PPLVQATALHHSPPS 14 the start position 222| LHHSPPLVQATALHH ||| [231| ATALHHSPPSAQASA 14 lus eight 246|| LCYSPPLAQAAAISH 18 ASALCYSPPLAQAAA |14 IHPQEQSQ12 251|| PLAQAAAISHSSPLP 18 249 SPPLAQAAAISHSSP 114 .PQQSQRV 1 258| ISHSSPLPQVIALHR 8 255 AAFSHSSPLPQVLA 14 WPQPQS 263|| PLPQVIALHRSQAQS] [| SSPLPQVlALHRSQA |14J 269| ALHRSQAQSSVSLQQ| 18 267 VIALHRSQAQSSVSL 14 275||AQSSVSLQQGWVQGA 18 [76QSSVSLQQGWVQGAD|14 109P1D4v.4 286||VQGADGLCSVDQGVQ8 |278|SVSLQQGWVQGADGL 14 A0203 312| ERLHPSDDSIKVIPL 8 | QGVQGSATSQFYTM 14 94| QEEYFDRATPSNRTE 171 311 SERLHPSDDSIKVIP |14| 32 MEIWIHPQPQRKSEG16 318 DDSIKV1PLTTFTPR 14|u 89|| PLGYPQEEYFDRATP 16 95|| EEYFDRATPSNRTEG|16 0Te4 A Table XXV 116| ESTFIPGLKKAAEIT 16 9PD4As 109PID4v.4 146|| CLIYGHSDACWMPAS A3-9-mers 245]| ALCYSPPLAQAAAIS |16 305| SQFYTMSERUilPSDD 16 45|| EGKVAGKSQRRVTFH||15 3 |TFEVPVSVHTRPPMK 14 F29| STTMEIWIHPQPQRK |14 31|| TMElWIHPQPQRKSE 14 221 Each peptide is a Table XXViii Table XXXI portion of SEQ ID 109P1D4v.4-B08 109P1 D4v.4 NO: 9; each start 9-mers B2709-9-mers position is specified, Each peptide is a Each peptide Is a the length of portion of SEQ ID portion of SEQ ID peptide is 9 amino NO: 9; each start NO: 9; each start acids, and the end position is specified, position is position for each the length of peptide specified, the peptide Is the start is 9 amino acids, length of peptide is position plus eight and the end position 9 amino acids, and for each peptide is the end position for the start position each peptide Is the PQQRRVTF plus eight start position plus 2WIPPQ 4SQ 1 eight |IHPQPQSQR 2PQSQRRVTF| 8R |QSQRRVTFH| PQPQSQRRV 1]|HP Q | QSQRR| 7PQSQRRVTF| 9 1 8]| IWHPQPQS| Table XXVI Table XXIX 1 09P1 D4v.4-A26 109P1D4v.4 Table XXXII 9-mers B1510-9-mers 109P1D4v.4 Each peptide is a Each peptide is a B4402-9-mers portion of SEQ ID portion of SEQ ID Each peptide is a NO: 9; each start NO: 9; each start portion of SEQ ID position is position is specified, NO: 9; each start specified, the . the length of position is specified, length of peptide is peptide is 9 amino the length of 9 amino acids, and acids, and the end peptide is 9 amino the end position position for each acids, and the end for each peptide is peptide is the start position for each the start position position plus eight peptide is the start plus eight position plus eht jPQSQRRVTF 3||HPQPQSQR 7]|PQSQRRVTF| ~*JWIHPQPQSQ 7| ~PQSQRRVTFW[1 _|I__PQPQS FWIHP WPQS 4 Table XXX 109PID4v.4-82705 Table XXXII Table XXVII 9-mers 109P1D4v.4-B5101 109P1D4v.4-B0702 Each peptide is a 94mers 9-mers portion of SEQ ID Each peptide Is a Each peptide is a NO: 9; each start portion of SEQ ID portion of SEQ ID position Is specified, NO: 9; each start NO: 9; each start the length of peptide position Is specified, position Is specified, Is 9 amino acids, the length of peptide the length of peptide and the end posItion Is 9 amino acids, Is 9 amino acids, for each peptide is and the end position and the end position the start position for each peptide is for each peptde is plus eight the start position the start position plus eight plus eight 3] IHPQPQSQR| 18 ~J QQSQRVT 14]|HPQPQSQRR 14| QPQSQRRV|~ 6|QPQSQRRVT 5Q PQSQRRV| |HPQPQSQRR | HPQPQSQRR|~ 7|PQSQRRVTF|1QQ 222 Table XXXIV Each peptide is a Table 109P1D4v.4-A1 portion of SEQ ID

XL

10-mers NO: 9; each start 109P1D4 position is specified, v.4-B08 Each peptide is a the length of peptide 10-mers portion of SEQ ID Is 10 amino acids, NO: 9; each start and the end positionN position is specified, for each peptide is Ru the length of peptide the start position plus Results is 10 amIno acids, and the end position n for each peptide is the start position 3| PQ S 9Table XU plus nine 1 I91Dv4 7 QPQSQBBVTF|I B1510 1]|EWHEQPQS 12 10-mers 3|WjHPQPQSQR|4 [5| HEQPQSQRRVR ~Table XXXVII No Results 9|QSQRRVIFHL|I 109P1D4v.4-A26 Found. [5|PQPQSQERVTg ~ 10-mers Each peptide is a Table XLI Table xO(XV portion of SEQ ID 109P1D4v.4 109P1D4vA201 NO: 9; each start B2705 l O2m 1 position is specified, 10-mers 10-mers the length of peptide Each peptide is a is 10 amino acids, portion of SEQ ID NO: and the end position No Results 9; each start position for each peptide Is Found. is specified, the length the start position plus of peptide Is 10 amino nine acids, and the end Table XLIII position for each 109P1 D4v.4 peptide is the start 1 EIWIHPQPQS1 B2709 position plus nine 7]QPQSQRRVTF| 10-mers ____________ 9]|QSQRRVTFHL|8L lii 5HPQPQSQRR| 1N 9] QSQRRYTFHL | 1 Table XXXIX MOPDv.-00 Table X-IV ElWIHEQPQS 109P1D4 .4-B0702 109P1D4v.4-B4402 2 E 1WH~QQ 60-niers lo-mers Each peptide isa 10ersa portion of SEQ ID NO: Each pepide isa Table XXXVI 9; each start position portion of SEQ ID Poito NO 9 each start 109P1 D4v.4- is specified, the length psto sseiid th ent position is specified, A0203 of peptide is 10 amino the length of peptide 10-mers acids, and the end s 1 amino acids, Position for each and the end position No esutspeptide Is the start for each peptide is position plus nine the start position plus [1111111 nine Table )OO(VII IZI QPQSQRRVTF 19 109P1H4.4 gFHPQPQSQRR 17 7|QPQSQRRVTF A3-10-mers QSQRRVTFHL11 9 QSQRRVTFHL 223 Table XLV Each peptide is a _________ME___HP __P _ SQ---l portion of SEQ ID 109P1D4v.4- 4 TMEIWIHPQPQSQRR||20] NO- 11; each start 10-mers 5 IMEIWIHPQPQSQRRV||1 position is specified, 2l ST-TMEIWIHPQPQS-Q 1f4 the length of NEWIHPQPQSQ|14 peptide is 9 amino No Resul EIi HPQPQSQRRVT |1 acids, and the end Found. 1 N ESTTMEIWIHPQPQS|12] position for each 5 TTMEIWHPQPQSQR||2peptide is the start Table XLVI-109P1 D4v.4 8 WIHPQPQSQRRVTFH|12 DRBI 0101-15-mers 9 IHPQPQSQRRVTFHL||12 5]HTRPSQRR Each peptide is a portion of SEQ ID NO: 9; each start SVHTRESQR position is specified, the length Table XLIX-109P1D4v.4 of peptide is 15 amino acids, DRB1 1101-15-mers and the end position for each Each peptide is a portion of Table 1IV peptide Is the start position SEQ ID NO: 9; each start A0203-9 plus fourteen position is specified, the length of peptide Is 15 amino mers 2I S1TMEIHPQPQSQg a cids, and the end position for Q 1 each peptide is the start No Results 4]|TMEIWIHPQPQSQRR 19 position plus fourteen Found 5[|MEIWIHPQPQSQRRV 1 I1 PQSQRRVTFHLPEGS|16 2[] STTMEIWIHPQPQSQ |20 Table XXV 8]|WIHPQPQSQRRVTFHI|1 '1I|PQSQRRVTFHLPEGS 13 109P1D4v.5-A3 II||EIWIHPQPQSQRRVT|14 ||TMEWIHPQPSQRR IO| HPQPQSQRRVTFHLP|14| Each peptide is a F11I QPQs -- [WH s ] MEIWIHPQPQSQRRV 11 portion of SEQ ID 12||QPQSQRRVTFHLPEG||4] [9]HPQPQSQRRVTFHL |10 NO: 11; each start II| TTMEIWIHPQPQSQR||2 position is specified, the length of Table XXIl peptide is 9 amino Table XLVII-109P1 D4v.4 109P1D4v.5-A1 acids, and the end DRB1 0301-15-mers 9-mers position for each Each peptide is a portion of Each peptide is a peptide is the start SEQ ID NO: 9; each start portion of SEQ ID position plus eight position Is specified, the length NOI1; eachistart of peptide Is 15 amino acids, the l e d' of and the end position forpeptide is 9 amino RPQR F|9 peptide Is the start positionpetdIs9aioO L R F5 plus fourteen acids, and the end position for each peptide is the start Table XXV 6]|EWIHPQPQSQRRVT|1 position plus eight 109P1D4v.5-A26 4]|TMEIWIHPQPQSQRR 1 7H1 Each peptide is a 1H 5 portion of SEQ ID 2]|STTMEIWIHPQPQSQ|Ii0 2|VSVHTRESQ|] NO: 11; each start 8|PQRRV .FH| position is specified, LU the length of Table XLVIII-109P1 D4v.4 peptide is 9 amino i DRB1 0401-15-mers . Table XXIIll acids, and the end Each peptide is a portion of 109P1D4v.5 position for each SEQ ID NO: 9; each start A0201-9-mers peptde Is the start position is specified, the position plus eight length of peptide is 15 amino acids, and the end position 33 for each peptide is the start position plus fourteen 1]|PVSVHTRPS Table XXVI Each peptide is a 109P1D4v.5-A26 portion of SEQ ID Table XXXII 9-mers NO: 11; each start 109P1D4v.5 Eh opposition is specified, B4402-9-mers portion of SEQ ID the length of Each peptide is a NO: 11; each start peptide Is 9 amIno portion of SEQ ID position is specified, acison the end NO: 11; each start the length of tide is the start position Is specified, peptide is 9 amino position plus eight the length of acids, and the end peptide is 9 amino position for each acids, and the end peptide is the start 4] VHTRPSQRR position for each position plus eight peptide is the start 7 RPSQRRVTF| position plus eight ~] HTRPQRRV ~5 HTRPSQRRV E 5 RRRPS VTF 9 6 PSQRRVT| ]RPSQRRVTF 15 | QR3SVHTRPSQR El Table XXX Table XXVII 109P1D4v.5 TableX II 109P1 D4v.5 B2705-9-mers 109P1 D4v.5 B0702-9-mers Each peptide is a B5101-9-mers Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 11; each start portion of SEQ ID NO: 11; each start position is specified, NO: 11; each start position is specified, the length of . the length of peptide is 9 amino posit specified, peptide is 9 amino acids, and the end the lengthio position acids and the end position for each peptide is the start position for each peptide is the start position plus eight pptide Is the start sition plus eight ________isthestar position plus eight PS RRT IZ S 7r7]|RPSQRRVTF 18 7 R |VHTRPSQRR 7RPSQRRVTF| |HTRPSQRR 3 SVHTRPSQR HTRPSQRRV 11 6 TRPSQRRVT| |TRPSQRRVT 6 P1D4v.5 8PSQRRVTFH B08-9-mers Table XXXIV Each peptide Is a Table XXXI 109IO D4v.5-A1 portion of SEQ ID 109P1D4v.5 1O-mers NO: 11; each start B2709-9-mers Each peptide is a position is specified,Each portion of SEQ ID specifiedh peptide Is a NO 1 ac tr the length of NO:11; each start peptide is 9 amino Nof EQ ID position is specified, acids, and the end NO 's ec the length of peptide position for each the length of is 10 amino acids, peptide is the start peptide is 9 amino and the end position position plus eight acids, and the end for each peptide Is position for each the startstion plus 7]RPSQRRVTF 21 peptide is the start [S-V~ff-RIP Q~j 0 psition us eight 3|SVH-TRPSQR| 0-6|HR QRV| 6 HIJRPS QRRVTW 7 RPSQRRVTF 13 3 VSVHTRPSQR|I Table TRPSQRRVT 1B9P1D4v.5 | TRPSQRRV| 1 B1~ ~ ~ 51P!mesSS Q RR 1 225 Table XXXV Each peptide is a 109PID4v.5 portion of SEQ ID Table XLIl A0201-10-mers NO: 11; each start 109PID4v.5 Each peptide Is position is specified, B2705-10 the length of peptide mers NO:11; each start is 10 amino acids, is: sp;eacifiedt and te end position position is specified, pd s No Results the length of peptide the start position plus Found. is 10 amino acids, nine and the end position ninl e-111 for each peptide is _Table XLIl the start p position plus |PVSVHTRPSQ 1 50910 nine I4|SVHTRPSQRR |H mers VHTRSQTRPSQRRVTF 6 HTRPSQRRVT[ No Results HTRPSQRRVT 10PSQRRVTF Found. [PSQRRVI'FHL 12riVSVHTRPSQR|[* ]SVHTRESQRR [6 Table XLIV 109PID4v.5-B44O2 Table XXXIX 10-mers Table 109P1D4v.5 XXXVI B0702-10-mers Each peptide is a 109P1D4v.5 portion of SEQ ID A0203-10- Each peptide is a NO: 11; each start mers portion of SEQ ID position is specified, NO: 11; each start the length of peptide position is specified, is 10 amino acids, No Results the length of peptide and the end position Found. is 10 amino acids, for each peptide Is and the end position the start position plus for each peptide is nine Table XXXVIlI the start position plus 109P1D4v.5-A3 nine 10-mers DJTRPSQRRVTF| Each peptide Is a 112_____ prino EQ 8]|RPSQRRVTF-HPQRVFL NO:11; each start 1]VPVSVHTRPS potion is specifed, Ta 09P1 DLV. the length of peptde 6 HTRPSQRR 1 Tl Dv5 is 10 amino adds, 9]PSQRRVTFHL B5101-10 and the end position 7]|TRPSQRRVTF mers for each peptide is the start position plus Table XL 109P1D4v.5 Found. B08-10 SVTREQRR[15ers Table XLVI-109P1D4v.5 j PV.SVHIBPSQ 13 DRB1 0101-15-mers TRPSQEVTF13 No Results Each peptide Is a portion of SVSVHTRPSQRg Found. SEQ ID NO: 11; each start - -PS -R -1position is specified, the Table XLI length of peptide is 15 amino 109PD4v5 acids, and the end position for Table XXXV1l B1510-10- each peptide Is the start 109P1D4v.5-A26-10- mers position plus fourteen mers No ResultsIFEVPVSVHTRPSQRR Found. 3 TFEVPVSVHTRPSQR 17 226 Table XLVI-1 09P1 D4v.5 Table XXIII DRB1 0101-15-mers Table XLIX-109P1D4v.5 109P1D4v.6 Each peptide is a portion of DRB11101-15-mers C' termi 0201 SEQ ID NO: 11; each start Each peptide is a portion of position is specified, the SEQ ID NO: 11; each start Each peptide Is a length of peptide is 15 amino position is specified, the portion of SEQ ID acids, and the end position for length of peptide is 15 amino NO: 13; each start each peptide is the start acids, and the end position for position is position plus fourteen each peptide Is the start specified, the position plus fourteen length of peptide Is 9 amino acids, and 1|VTTFEVPVSVHTRPS||16] the end position for 13||RPSQRRVTFHLPEGS 16 3]|TFEVPVSVHTRPSQR||25 each peptide Is the ||PVSVHTRPSQRRVTF[|4 5||EVPVSVHTRPSQRRV|15 start position plus I||] VHTRPSQRRVTFHLP||1 1TFEVPVSVHTRPS|13| eight 12||TRPSQRRVTFHLPEG||4 [4]FEVPVSVHTRPSQRR1 []ASVHTRETDS| 1 3||RPSQRRVTFHLPEGS lVHTRPIDSR| Table XLVIl-109P1D4v.5 DRBI 0301-15-mers Table XXIl 109P1D4v.6 Table X(XIV Each peptide Is a portion of C' teninal-A1 109P1D4v.6 SEQ ID NO: 11; each start 9-mers C' terminal position is specified, the A0203 length of peptide is 15 amino Each peptide is a 9-ers acids, and the end position for portion of SEQ ID each peptide is the start NO: 13; each start position plus fourteen position is No Results specified, the F length of peptide is [5]|EVPVSVHTRPSQRR 16 9 amino acids, and 1I|VHTRPSQRRVTFHLP 16 the end position for Table XXV each peptide is the 109P1 D4v.6 7||PVSVHTRPSQRRVTF|1 start position plus C' terminal-A3 3] TFEVPVSVHTRPSQR 10 eight 9-mers [II VTTFEVPVSVHTRPS 9 Each peptide is a VSVHTRPSQRRVTFH||RPTD8T 10 portion of SEQ ID "I' NO: 13; each start 9]|SVHTRPSQRRVTFHL|[8 |VSVHTRETD position is 1[|TRPSQRRVTFHLPEG||8] specified, the XXIII011 length of peptide is Table IIll 9 amino acids, and Table XLVIll-109P1D4v.5 IO9P1D4v.6 the end position for DRB1 0401-15-mers C' terminal-A0201 each peptide is the Each peptide is a portion of 9 start position plus SEQ ID NO: 11; each start Each peptide Is a eight position is specified, the portion of SEQ ID length of peptide is 15 amino NO: 13; each start SVTREIDS15 acids, and the end position position is for each peptide is the start specified, the 1 |PVSVHTRPT 1 position plus fourteen length of peptide Is|VHIR_ SR| 9 amino acids, and 4 VHI QSR9 the end position for 5|HTBPTQSRT[] ijVTTFEVPVSVHTRPS each peptide Is the Sj|EVPVSVHTRPSQRRV start position plus Table XXVI [4] FEVPVSVHTRPSQRR R|8 1 09P1D4v.6 OITEVPSVH 14C'terminal TFEVPVSVTRPSQR(14 9HTRPTQSRT A29-mers 8||VSVHTRPSQRRVTFH||2 _|VVIRT[ 9]|SVHTRPSQRRVTFHL||12| VVIP ~ 227 Each peptide is a Table XXXI portion of SEQ ID Table XXIX 1 09P1D4v.6 po~on ' terminal-B2]709 NO: 13; each start 109P1ID4v.6 9Cters position is C' terminal 9-mers specified, the B1510-9-mers Each peptide is a length of peptide Is Each peptide IS portion of SEQ ID 9 amino acids, and portion of SEQ ID NO: 13; each start the end position for NO: 13; each start position is each peptide is the posieon is specified, the start position plusi length of peptide eight specified, the is 9 amino acids, eight ~length of peptide Isadth n amino acids, and and the end 9 amn ad, n position for eac 3 SVHTRPTDS 11 ~the end position for ~iei h tr 1 3 SVHTRPT 0 each peptide Is the s ett start position plus 5|HTRPTDSRT 10 eight 2VSVHTRPTD VSVHTRPTD 2 |VHTRPTDSR|I 5 HTRPTDSRT| Table XXVII 1] PVSVHTRPT 4 f ] VH-TRPTDSR| 109P1D4v.6 5|HTRPTDSRT4 C' terminal-B0702 TableXXIl 9-mers Table XXX109PD4v.6 Each peptide Is a Table XXX Cterminal-]4 portion of SEQ ID 0i9P1D4v.6 9-mers NO: 13; each start C' terminal-B2705 position is 9-mers Each peptide is a specified, the Each peptide is a portion of SEQ ID length of peptide is portion of SEQ ID NO: 13; each start 9 amino acids, and NO: 13; each start position is the end position for position is specified, the each peptide is the specified, the length of peptide start position plus length of peptide is is 9 amino ads, eight 9 amino acids, and and the end the end position for position for each -________ each peptide is the peptide isthestart 1|i PVSVHTRPT| 10start position plus sition us eight 5|HTRPTDSRT| 9 eight VHTRPTDSR4 3 SVHTRPTDSI1 4|VHTRPTDSR|12 1]|PVSVHTRPT| Table XXVEI I|HTRPTDSRT [5_ 5HTRPTDSRT|3 109P1 D4v.6 2VSV RPTD C' terminal-808 Table XXXI RIVHTRPTDSR 9-niers -109P1D4v.6 Each peptide is a C' terminal-B2709 portion of SEQ ID 9-mers Table XXXII NO: 13; each start E109P1D4v.6 position ise portion of SEQ ID 'terminal-85101 length of peptide Is NO: 13; each start 9 amino acids, and position is the end position for specified, the each peptide is the length of peptide start position plus is 9 amino acids, eight and the end position for each peptide is the start SVHTRPTDS position plus eight 5HTRPTDSRT|7] 228 Each peptide is a Table Each peptide is a portion of SEQ ID XXXVI portion of SEQ ID NO: 13; each start 109PID4v.6 NO- 13; each start position Is C' terminal- position is specified, specified, the A0203 the length of peptide length of peptide 10-mers is 10 amino acids, is 9 amino acids, and the end position and the end for each peptide is position for each No Results the start position plus peptide Is the start Found, nine sition plus eight I1 Table XXXVII 1] VPVSVHTRPT 18 ~J VSVI-ITRPTD 4 I9P1D4v.6 _____ SVHTRPTD Cterminal-A3VTRPTDSRT 10-mers |HTRPTDSRT| Each peptide is a Table portion of SEQ ID AL Table XXXIV NO: 13; each start 109P1D4 109PDv position Is specified, teinal 09P1 D4v.6 the length of peptide B08 C terminal-Al Is 10 amino acids, 10 1 0-mers and the end position [II] Each peptide is a for each peptide is portion of SEQ ID the start position plus No NO: 13; each start nine Results position is specified, Found. the length of .1. peptide Is 10 amino 4]SVHTRPIDSR 17___ acids, and the end 12|PSHIPTD Table position for each I- - XLI peptide is the start 109P1D4 position plus nine Table X)OVIII v.6-C' 109P1 D4v.6 terminal C' terminal-A26 B1510 3|VSVHTRPTDSS | 10-mers 10-mers |SVHTRPIDSR 2 Each peptide is a portion of SEQ ID Table XXXV NO: 13; each start Results 109P1 D4v.6 position is specified, C' termiaA02011 the length of peptide 1 -mers is 10 amino acids, and the end position Table Each peptide is a for each peptide is XLII portion of SEQ ID the start position plus 109P1D4 NO: 13; each start nine v.6-C' position is specified, terminal the length of B2705 peptide is 10 amino 4]|SVHTRPTDSR| 1 -mers acids, and the end 2|PVSVHTRPTD|1 position for each peptide Is the start No position plus nine Table XXXIX Results 109P1D4v.6 Found. C' terminal-80702 | SVHTRETDSR 8 10-mers Table Xll 1|PVVHRP9 109P1D4v.6 E|PVSVHIRPTD C' terminal VHRPDRB2709 j~j VHTRPIDSRT 229 No Results Each peptide is a portion of Each peptide is a SEQ ID NO: 13; each start portion of SEQ ID position is specified, the NO- 13; each start length of peptide Is 15 amino position is specified, Table XLIV acids, and the end position the length of peptide 109P1D4v.6 for each peptide is the start is 9 amino acids, C' termina]-B4402 position plus fourteen and the end position 10-mers for each peptide is Each peptide is a the start position portion of SEQ ID 5||EVPVSVHTRPTDSRT plus eight NO: 13; each start 3|TFEVPVSVHTRPTDS |10 position Is specified, |VTFEVPVSVHTRPTj9[ NSDISSYVR 1 the length of N________ peptide Is 10 amino |2HESCLLSGTY 1 acids, and the end Table XLVIII-109P1 D4v.6 |MIVGFNSDI| position for each C' terminal-DRB1 0401 peptide is the start 15-mers 1TNCHKCLL| position plus nine Each peptide Is a portion of 18 TNCHKCLLS ] SEQ ID NO: 13; each start PVSVHTRPTD position is specified, the Table XXIIl 3 length of peptide is 15 amino 109P1D4v.6 SVHTRPTDSR|} acids, and the end position N' terminal-A0201 VPVS-VH-TRPT2 for each peptide is the start 9-mers position plus fourteen Each peptide is a Table XLV I portion of SEQ IDa 109P1D4v.6 VTTFEVPVSVHTRPT 22 NO: 13; each start C' terminal- -iFEVPVSVHTRPTDSR||18 position Is specified, B5101 the length of peptide 10-mers 3] TFEVPVSVHTRPTDS |14 is 9 amino acids, 5| EVPVSVHTRPTDSRT 14] and the end position for each peptide Is Nothe start position Found. |Table XIX-109P1D4v.6 plus eight C' terminal-DRB1i 1101 Table XLVI-109PID4v.6 15-mers C' terminal-DRB1 0101 Each peptide is a portion of 15-mers SEQ ID NO: 13; each start 4 GFNSDISSV 18 Each peptide Is a portion of pos n of peid 15 aCLLSGTYIF 17 SEQ ID NO: 13; each start acidsand the end posion 1 MTVGFNSDI 15 position Is specified, the fo achpepands the startosition fen eac pepid ion s thu start :1]TTNCHECLL|1 length of peptide Is 15 amn positon ls outen10SVRLTI acids, and the end position 10SSVVRYNTTI for each peptide is the start FNSDISS 12 posItion plus fourteen 3 TFEVPVSVHTRPTDS|2 16NTTNCHKCL 12 5TEVPVSVHT RPTDSRT||15| |DISS VRVN 11 3|TFEVPVS TRPTDS|17| 1 VTFEVPVSVHTRPT|13] Q|KCLLSGYl|1 i1VTTFEVPVSVHTRPT |16] -~ ] FEVPVSVHTRPTDSR||14] Table XXII I|EVPVSVHTRPTDSRT 8] 19P1D4v.6 Table XXIV N' terminall-Al 109P1 D4v.6 9-mers N' terminal TableXLVlI-109P1 D4v.6 A0203 C' terminal-DRBI 0301 9-mers 15-mers _ No Results Found.

Table XXV Table XXVII 109P1D4v.6 109P1D4v.6 Table XXIX N' terminal N' terminal-B0702 109P1D4v.6 A3-9-mers 9-mers N' terminal-B1i510 Each peptide is a Each peptide is a 9-mers portion of SEQ ID portion of SEQ ID Each peptide is a NO: 13; each start NO: 13; each start portion of SEQ ID position is specified, position is specified, NO: 13; each start the length of peptide the length of peptide position is specified, is 9 amino acids, and is 9 amino acids, the length of peptide the end position for and the end position is 9 amino acids, each peptide is the for each peptide is and the end position start position plus the start position for each peptide is eight plus eight the start position -7 1 1 Iplus eight SRVNTNCHK 2ISSWVRVNT 12 SVVRVNN 20 NTNCHKCL 1 1TTNCHKCLL 1 CLSGIIIF 17 TTNCHKCLL 10 NTNCHKC 10 12 VN 14C FNSDISSW 2CHKCLLSGT 10 NSDISSV.VR 13 SDISSWRV 9jSSWVNT DISSVVVN 1KCLLSGTYI CLLSGTY Il 1HKCLLSGTY MVGFNSDI DISSRVN 10SSVVRVNTT E TableXVI |CLLSGIF Table DW6 Table17fl1O9P1D4v.6 N 9PnD4v.6 |GFNSDISSV N terminal-B2705 N' terminal-A26 9-mers |CHKCLLSGT 9-mers Each peptide is a Each peptide is a portion of SEQ ID Table XXVIII portion of SEQ ID NO: 13; each start 109P1D4v.6 NO: 13; each start position is specified, N' tetrminang0 is peie the length of peptide 9-mers is 9 amino acids, and Is 9 amino a rds, and Each peptide is a the end position for the end position for portion of SEQ ID each peptide is the each peptide Is the NO: 13; each start start position plus start position plus position is specified, eight eight the length of peptide is 9 amino acids, and [ DISSVVRVN ft7] the end position for VRVNTTNCH2 ____________each peptide is the 14RN F 51 1NTTNCHKCL start position plus [231RVNTN TTNCHKCLL eight 3| G 15 SSVVRVNTTN 6 NSDISSVVR 1 MTVGFNSDI H [ SSVRVNTT [2 KCSGTI 2]HKCLLSGTY E~ 2lCLLSGTYIF 12|i]HKCLLSGTY [~ 2]TVGFNSDIS j16NTTNCHKCL 11|lMTVGFNSDI I] VV] WRVNTTNC 7TTNCHKCLLI0 7|TTNCHKCLL I SSDISSVRV g TNCHKCLLS |NTTNCHKCL 17pJ SSSRVN 20 CHKCLLSGT 10 SRVNTTNCH 0 V RVNTTNC Table XXX __41 IO19P1D4v.6 CLSGTYlF EMVGFNSDId N' terminal-B2709 KCLLSGTYI 79-mers 231 Each peptide is a Each peptide is a portion of SEQ ID portion of SEQ ID _VGFNSDSSV NO: 13; each start NO: 13; each start position Is specified, position Is specified, M NSDISSVVRV the length of peptide the length of peptide 23CLLSGIYIFA 16 is 9 amino adds, and is 9 amino acds, DISSVVRVNT the end position for and the end position each peptide Is the for each peptide Is ISSWBVNTT start position plus the start position NTTNCHKCLL eight plus eight GFNSDISSW VNTTNCHKCL IGFNSDISSV ~j[]KCLLSGTYI 1NTHKCLG SDISWRVMTVGFNSDI 1 1J CKLLG 9 SKCLLSGYI FNSDISSW 13 Table XXXVI CLLSGTYF SDiSSWRV 13109PID4v.6 VRVNTTNCH 11DISSVVRVN N' terminal-A0203 6NTTNCHKCL 11[ VGFNSDISS| 10ch-mers ___________Each peptide is a TTNCHKCLL [ GFNSDISSV portion of SEQ ID MTVGFNSDI NTTNCHKCL|8 NO- 13; each start FNSDISSW 9T17TNCHKCLL position is specified, ] [1 the length of peptide is 10 amino acids, Table XXXII Table XXXIV and the end position 109P1D4v.6 109PID4v.6 for each peptide is N' terminal N' terminal-Al the start position B4402-9-mers 10-mers plus nine Each peptide is a Each peptide Is a I portion of SEQ ID portion of SEQ ID NO: |CLLSGTYIFAl1 NO: 13; each start 13; each start position position Is specified, is specified, the length the length of peptide of peptide is 10 amino Table XXXVlI is 9 amino acids, acids, and the end 109P1D4v.6 and the end position position for each N' terminal-A3 for each peptide Is peptide is the start 10-mers the start position tion plus nine Each peptideIs a plus eight __ portion of SEQ ID NO: NSDISSWYRV| 13; each start position -F is specified, the length NTNCHKCL| 20 CHKCLLSGTY of peptide Is 10 amino 17 TTNCHKCLLS acids, and the end 21 HCLLS1Y 1 __position for each |~]CLLSGTYIF| 9|161N1NCHI CLL 8she i~] ~NCHCLL i11 -' -peptide Is the start ________Lil position plus nine | G I TableXV MIVGFNSDI~ I OPD4v.6 _ | N' termina-A 201 2 VVRVNIINCH| 10-mers SyRVNITNC|Ih I Table XXXIll Each peptide is a 14RVNTNCHKC 1N9PI D4v.6 portion of SEQ ID NO: 5 FNSDISSWR| N' termial-51 011 13; each start position8DISRN 9-mers isNiSVYRVNT| of peptide Is 10 amino TVGFNSDISS acids, and the end |CHICLLGTY 2 position for each peptide is the start 23 C.LSGTYFA 12 position plus nine 13|VRNTINCHK a 232 Table XXXVII Each peptide is a 109P1D4v.6 portion of SEQ ID NO: N' terminal-A3 13; each start position Results 10-mers is specified, the length IFn of peptide is 10 amino Each peptide is a acids, and the end portion of SEQ ID NO: position for each Table 13; each start position peptide is the start XLiIl Is specified, the en position plus nine 109P1D4 of peptide is 10 amIno rv.6 N' adds, and the end terminal position for each ]DISSVVRVNT 11 B2709 pepide is the stat fl] NBI2W7 1 0r position plus nine NSDISVVRV 9 ISSVVRVNT1T |2 KCU.SGIYIF fo15VNTTNCHKCLR s 16 NTTNCHKCLL Found. Table XXXVIII 22 KCLLSGTYIF 109P1D4v.6 GFNSDISSV Table XLIV-109P1D4 N' termlnal-A26 1(NCHKCLLSGT F v.6 N' terminal 10-mers HKCLLSGTYR B34402-10-mers portion o E ID O- CLLSGTYIFA Each peptide is a 13; each start position VGFNSDISSV 13; each start position Is specified, the length is specified, the length of peptide is 10 amino -of peptide is 10 amino acids, and the end Table acids, and the end position for each acidstin for enc peptide is the start 109PID4' peptide is the start position plus nine v.6 N' position plus nine terminal ___ 17. BOB__ __ _ NTTNCHKCLL 10-mers KCLLSGTY F I 1]SVVRVNTTNC 15VNTCHKCL| TVGFNSISS No 16 NTTNCHKCLL DISSVVRVNT Results 20 CHKCLLSGTY 1 .. L11Found. IEl MTVGFNSDIS HKCLLSGTYl| O CHKCLLSG1Y Table SDISSVRVN 7_] RVNTNCHKC|1

XLI

SVGFNSDISSV 1 109P1D4 Table n7SDISSVRVN 10 v.6 N'D terminal 1 0P1 D4 12VRVNTTNCH10 B1510- v.6 N' TTNCHKCLLS| L. 10-mers terminal VNTTNCHKCL|] B5101 ______ 7~710-mers Table XXXIX Results 109P1D4v.6 N' terminal-B0702 Results 10-mers Found.

XLII

109P1D4 Table XV-109P1D4. v.6 N' iN' termnal-DRB1 0101 terminal 15-mers B2705 10-mers 233 Each peptide is a portion of Table XLVIII-109P1 04v.6 Table XXII SEQ ID NO: 13; each start N' terminal-DRB1 0401 109P1D4v.7 position is specified, the 15-mers N' terminal-Al length of peptide.is 15 amino Each peptide Is a portion of 9-mers acids, and the end position for SEQ ID NO: 13; each start Each peptide Is a each peptide Is the stalt position Is specified, the portion of SEQ ID position plus fourteen length of peptide Is 15 amino NO: 15; each start acids, and the end position for position Is specified, NCHKCLLSG1YIA each peptide Is the start the length of 1 K[6 sition lus fourteen peptide is 9 amino 2]TVGFNSDISSWRVN |25 acids, and the end F91 ISS WRVNTTNCHKC [22 _______ position for each 9||SSWRVNTNCHKC16 [2jTVGFNSDISSWRVN||8J peptide is the start 1 |SSWRVNTTNCHKCL |16 6||NSDISSVVRVNTTNC|26 [position plus eight 20 |CHKCLLSGTYIFAVL| |16 9] ISSWRVNTTNCHKCl|20 121| HKCLLSGTYFAVLL ||6| 10||SSWRVNTTNC HKC S1SPLLLVS1 2| KCLLSGTYIFAVLLV |16 HKCLLSGTYFAVLL |4 1| TNCHKCLLSGTYIFA|| 22 KCLLSGTYFAVLLV] [ ME I 11 6| NSDISSWRVNTTNC 2 SFSSSSLSL Table XLIX-1 09P1 D4v.6 Table XLVII-109P1D4v.6 N' terminal-DRB1 1101 Table XXIIl N' terminal-DRB1 0301 15-mers 109P1D4v.7 15-mers Each peptide Is a portion of N' terminal-A0201 Each peptide is a portion of SEQ ID NO: 13; each start 9-mers SEQ ID NO: 13; each start position is specified, the Each peptide is a position is specified, the length of peptide is 15 amino portion of SEQ ID length of peptide Is 15 amino acids, and the end position for NO: 15; each start acids, and the end position for each peptide is the start position is specified, each peptide is the start position plus fourteen the length of peptide position plus fourteen is 9 amino acids, and the end position TVGFNSDISSVVRVN 16NSDISSWRVNTTNC |22 for each peptide is 2|1TGFNS[SSV |1 9 ISSVVRVNTTNCHKC||12 the start position 6]|NSDISSVVRVNTTNC||19 21|| HKCLLSGTYIFAVLL ||12 plus eight 14||RVNTTNCHKCLLSGT [16 2||TVGFNSDISSWRVN| 11 2HKCLLSGTYIFAVL [30________ 21| ISSWRV1THKCL ||13 i14IRVNTTNCHKCLLSGT| 11 I1|1LLLVSyVRV 9| 1SSVVRVNTTNCISSSSL | 10|SSWRVNTTNCHKCL||12 Table XXII- |LSPLLLVSV2 20|CHKCLLSGTYIFAVL 112| 109P1D4v.7 |SSLSPLLLV2 12VVRVNTTNCHKCLLS||11| N' terminal-Al 14|SLSPLLLVS| I 9-mars 2| KCLLSG1YIFAVLLV a pSPLLLVSW 19 11Each peptide is a 18|TNCHKCLLSGTYFA ||10 portion of SEQ ID 6SSSSSLSPL NO: 15; each start LLVSVVRVN Table XLVIII-109P1D4v.6 positon Is specified, FLISSSSS N' termlnal-DRB31 0401 the length of ________ 't erm peptide is 9 amino acids, and the end Table XXIV Each peptide is a portion of position for each 109P1D4v.7 SEQ ID NO: 13; each start peptide Is the start N' terminal position is specified, the position plus eight A0203 length of peptide is 15 amino 9-mers acids, and the end position for each peptide is the start SSLSPLLLV position plus fourteen SSSLSP No Results I -- Found.

234 Table XXVII Table XXVIII Table XXV 109P1D4v.7 109P1D4v.7 109P1 D4v.7 N' terminal-B0702 N' terminal-B08 N' terminal-A3 9-mers 9-mers 9-mers Each peptide is a Each peptide is a Each peptide is a portion of SEQ ID portion of SEQ ID portion of SEQ ID NO: 15; each start NO: 15; each start NO: 15; each start position Is specified, position is specified, position is specified, the length of peptide the length of peptide the length of peptide is 9 amino acids, is 9 amino acids, is 9 amino acids, and the end position and the end position and the end position for each peptide is for each peptide is for each peptide is the start position the start position the start position plus eight plus eight plus eight 16SPLLLVSW9 LLVSWRVN 7PLLLVSWR [gSSSLSPLLL 1 |SLSPLLLVS SSSSSLSPL 13 Table XXIX | FL-ISSS 9 SSSSLSPLL N'ter nal B510 ] RVGFLISS 16 1MFRVGFLII 9-mers 7 LISSSSSL 1SSLSPLLLV 11 Each peptide is a 18|LLLVSRV 16LVSWRVNT portion of SEQ ID LVSWRVNT LSSSSSL NO: 15; each start Mn position is specified, |LLVS VN 1LLLVSWRV [ the length of peptide | IISSSSSLS 13 is 9 amino acids, Tal Xand the end position Table XXVIII for each peptide Is Table XXVI 109P1D4v.7 the start position 109P1 D4v.7 N' terminal-B08 plus eight N' terminal-A26 9-mers 9-mers Each peptide is a Each peptide is a portion of SEQ ID H portion of SEQ ID NO: 15; each start 12SSSLSPLLL NO: 15; each start position is specified, 10SSSSSLSPL ] position is specified, the length of peptide the length of peptide is 9 amino acids, is 9 amino acids, and the end position |LLLVSWRV and the end position for each peptide is for each peptide is the start position the start position plus eight Table XXX plus eight 109PID4v.7 N' terminal-B2705 9LISSSSSL 9-mers | LISSSSSL 11MFRVGFL 1Each peptide Is a RVGFLISS 1SSSLSPLLL 1f SEQD 10 SSSSSPL15 0 ssss~sP 12NO, 15; each start |SSSSSLSPL SSSSposition is specified, SVGFLIISSS 11SSSSLSPLL the length of peptide SSSSLSPLL TIs 9 amino acids, 21 VSVRVN1 11and the end position 12|SSSLSPLLL 10S6SPLLLVSW|10 for each peptide is |LVSWRVNT| 18|LLLVSWRV| the start position 14 SLSPLLLVS| plus eight 17|PLLLVSVVR| 1PLLLVSWR 6 FLIISSSSS 7 | LISSSSSL 16 235 Table XXX Table XXXII Each peptide is a 109P1D4v.7 109P1D4v.7 portion of SEQ ID N' terminal-B2705 N' terminal-B4402 NO: 15; each start 9-mers 9-mers position is specified, Each peptide is a Each peptide Is a the length of peptide portion of SEQ ID portion of SEQ ID is 1t0 amino ads, NO: 15; each start NO: 15; each start and the end position position is specified, position is specified, for each peptide is the length of peptide the length of peptide the start position plus Is 9 amino acids, is 9 amino acids, and the end position and the end position Ii for each peptide is for each peptide Is [-7 |FSLS PLL the start position the start position 2SSSSPLLV| 1 plus eight plus eight 1 I Z [ ,___ __ ], 13SSLSPLLLVS 13 A FRVGFLIIS 15 SSSLSPLLL [6] 10 SSSSSLSPLL| 10 SSSSSLSPL LIISSSSL1 SSPLLLVSV SSSSLSPLL 3SSSSSLSPL 13 SSSLSPLLL SSSSLSPLL XXXV 12 IO19P1D4v.7 |RVGFUISS 11MFRVGFUI N' terminal 4 VGFLIISSS 10 14 SLSPLLLVS 8 A0201-10-mers MFRVGFI9 Each peptide Is a [~j FUISSSTable XXXIII portion of SEQ ID ]FUISS 109PID4v.7 NO: 15; each start N'1teminal-51 01 position is specified, Tablemml-B101the length of peptide Table XXXI 9-mers is 10 amino adds, 109PlD4v.7 Each peptide is a and the end position N'termmal-B270 portion of SEQ ID for each peptide is the 9-mers NO: 15; each start start position plus Each peptide Is a position is specified, nine portion of SEQ ID the length of NO: 15; each start peptide is 9 amino position is specified, acids, and the end |SLSPLLLVSV|[ the length of peptide position for each | FUIS9SSSL | is 9 amino acids, peptide is the start 25 and the end position position plus eight P for each peptide is LLLVSRVN18 the start position __________ _ -T:11 hlus eightoSPLLLVSW 5 LLVSV ERVNT 18LLLVSWRV 1712 SSSLSLLLV 18LLLVSWRV 131MFRVGFI 32 LVSWEVNTT| 7 UIISSSSSL 115LSPLLLVSV 13[jISSSSSLSPL|E6 |1SSSSLSPtL1 ______!~ LSPLLLVSVV 16] 13|SSLSPLLLV 1Table XXXIV FRVGFUIS 1091 D4v.7 Table H ~ N' terminal-Al IXXXVI 0|SSSSSLSPL 10-mers 109PID4v.7 12 SSSLSPLLL11 N' terminal A0203-10 nSPLLLVSW 1 mers | MFRVGFLIl 15LSPLLLVSVNo Results Found.

236 Table XXXVII Table XXXIX No Results 109P1D4v.7 109P1D4v.7 Found. N' terminal-A3 N' terminal-B0702 10-mers 10-mers Table XLIII Each peptide Is a Each peptide is a 109P1D4v.7 portion of SEQ ID portion of SEQ ID N' terminal NO: 15; each start NO: 15; each start B2709 position is specified, position is specified, 10-mers the length of peptide the length of peptide ------ _ is 10 amino acids, is 10 amino acids, and the end position and the end position No Results for each peptide is the for each peptide is the Found. start position plus start position plus nine nine Table XLIV 109P1D4v.7 14SLSPLLLVSV 125 ISSSSSLSPL 14 N' terminal-B4402 3 RVGFLRSSS 19 SSSSLSPLLL 10-mers FLISSSL SSSSSLSPLLportion of SEQ ID HPLLLV7SVRV 7 SPLLLVSWR NO: 15; each start 16SPLLLVSWR SLSPLLLVSV 11 position is specified, 9 LLLVS-WRVNlFISSS the length of peptide 8ii~ L R F~] SSSL 1 Is 10 amino acids, [flFITSSSILSP SSSLSPLLLV and the end position 77 ] 5 ~ SLPLLLVVF for each peptide is E-,LL-SWVNT the start position plus LISSSSLS1E LLVSWRVNT nine LVSWRVNT2 LVSWRVNTT9 I1iSSLSPLLLVS LSPLLLVSW 8 1 SSSSLSPLLL []FLISSSSSL ~ Table XXXVIII Table XL 10SSSSSLSPLL 13 109P1D4v.7 109PID4v.7 ISSSSSLSPL N' terminal N' terminal A26-10-mers B08 Each peptide is a 1 0-mers Table XLV portion of SEQ ID 109P1D4v.7 NO: 15; each start No Results N' terminal position is specified, Found. B5101 the length of peptide 10-mers is 10 amino acids, and the end position Table XLI for each peptide is the 1 09P1D4v.7 No Results start position plus N' terminal nine B1510 1 0-mers Table XLVI-1 09P1 D4v.7 RVGFLIISSS N' terminal-DRBI 0101 20 VSWVN1 15No Results I 5-mers oud. Each peptide is a portion of F± lSSSSLSEQ ID NO: 15; each start 9 ISSSSSLSPL 1l position Is specified, the Table XLIl length of peptide is 15 amino iHSL 109P1D4v.7 acids, and the end position for FRVGFISS N' terminal- each peptide Is the start i SSS B2705 position plus fourteen S ISSSSSLS lg 9mIg RVGFLIISSSSSLSP 3 237 Table XLVI-109P1D4v.7 XLVIII-109P1D4v.7 Table XXII N' terminal-DRB1 0101 N' terminal-DRBI 0401 109PiD4v.8-A1 15-mers 15-mers 9-mers Each peptide is a portion of Each peptide is a portion of Each peptide is a SEQ ID NO: 15; each start SEQ ID NO: 15; each start portion of SEQ ID position is specified, the position is specified, the NO: 17; each start length of peptide is 15 amino length of peptide is 15 amino position Is acids, and the end position for acids, and the end position for specified, the each peptide Is the start each peptide is the start length of peptide position plus fourteen position plus fourteen Is 9 amino acids, and the end _ _position for each 1| MFRVGFLiISSSSSL |[]| RVGFLIISSSSSLSP [28 peptide is the start 4| VGFLIISSSSSLSPL [|2 17| PLLLVSVVRVNTTNC 26 position plus eight 121 SSSLSPLLLVSVVRV 241 1 MFRVGFLIISSSSSL [|1oI 15||LSPLLLVSWRVNTT||2 4]| VGFLIISSSSSLSPL ||20 KKEITVQPT|1 5|| GFLIISSSSSLSPLL 22 5| GFLIISSSSSLSPLL |i2 TFIPGLKKE[ 6] FLIISSSSSLSPLLL ||2 12 SSSLSPLLLVSWRV||20 9] ISSSSSLSPLLLVSV|2 15| LSPLLLVSWRVNT TablX8 20]|LVSWRVNTTNCHKC | 18||LLLVSWRVNTTNCH|20 A0201-9-mers 2] FRVGFLIISSSSSLS ||21 20|LVSWRVNTTNCHKC||20 Each peptide Is a II |SSLSPLLLVSWRVN||17 1l| FRVGFLIISSSSSLS 18portion of SEQ ID _______________ IISS118!LL NO: 17; each start 6 FLSSSSSLSPLLL position is Table XLVII-109P1D4v.7 16| SPLLLVSVVRVNTTN 14 specified, the N' terminal-DRB1 0301 21 |VSWRVNTTNCHKCL |14 length of peptide is 15-mers 9 amino acids, and Eachpepide s aporlon f 1the end position E ID NO 15 eac tart Table XLIX-109P1D4v.7 for each peptide is position is specified, the N' terinaRB1 1101 the start ition length of peptide Is 15 amino _________s__ adds, and the end position for Each peptide Is a portion of t each peptide is the start SEQ ID NO: 15; each start |FIPGLeKEI 2 position plus fourteen position is specified, the length of peptide is 15 amIno 8| KEITVQPTV 16 VGFLIISSSSSLSPL acids, and the end position for 5| GLKKEptVQ 14 SVGFLlSSSSSLSPL each peptide is the start 1PGLKKTV2 17] PLLLVSVVRVNTTNC||20| position plus fourteen 15| LSPLLLVSWRVNTT 115| Table XXIV 5|| GFLIISSSSSLSPLL ||1 3] RVGFLISSSSSLSP ||2 109P1D4v.8 6|| FIISSSSSLSPLLL |1 17 PLLLVSVVRVNTTNC |221 A0203-9 1I SSSLSPLLLVSWRV|| 13 1 MFRVGFLIISSSSSL 18 mers 9|| ISSSSSLSPLLLVSV 12| 1I LSPLLLVSWRVNTT L 16 SPLLLVSWRVNTTN||2 2|| FRVGFLIISSSSSLS ||13| Noun 20j LVSWRVNTTNCHKC| 12| 5 GFLIISSSSSLSPLL ||13= 21|VSVVRVNTTNCHKC i 1 18| LLLVSWRVNNCH |13j Table XXV [11 RVGFLIISSSSSLSP |[] 6| FLIISSSSSLSPLLL ||121 109P1D4v.8 81| IISSSSSLSPLLLVS ||11 12|SSSLSPLLLVSWRV A3-9-mers [18|LLLVSWRVNTTNCH||1 20| LVSWRVNTTNCHKC |121 [|] MFRVGFLISS SL ||10 [16||SPLLLVSWRVNTTN |11|, [7| LIISSSSSLSPLLLV I|10 239 Each peptide is a Table XXVII Table XXIX portion of SEQ ID 109P1D4v.8 109P1D4v.8 NO: 17; each start B0702-9-mers B1510-9-mers position is Each peptide is a Each peptide Is a specified, the portion of SEQ ID portion of SEQ ID length of peptide is NO 17; each start NO: 17; each 9 amino acids, and position is start position is the end position specified, the specified, the for each peptide Is length of peptide length of peptide the start position is 9 amino acids, is 9 amino acids, plus eight and the end and the end Im position for each position for each GLKKEITVQ| peptide is the start peptide is the position plus eight start position plus KMTVQTV 1 eight IJFIEGLKKEl| 10KlWQPT| SLKKEIVPVQ []|TFIPGLKKE|] 1 TFIPGLK KE 8 Table XXVIll 2FIPGLKKEl| 109P1D4v.8 3||PGLKKEIT| Table XXVI 608-9-ners 61LKKEITVQP|j 109P1D4v.8 Each peptide is a A26-9-mers portion of SEQ ID Each peptide Is a NO: 17; each start Ta9 DXX portion of SEQ ID position is 109PD4v.8 NO: 17; each start specified, the B2705-9-mers position is length of peptide is Each peptide is a specified, the 9 amino acids, and portion of SEQ ID length of peptide the end position NO: 17; each start Is 9 amino acids, for each peptide is position Is and the end the start position specified, the position for each plus eight length of peptide Is peptide is the start 9 amino acids, and position lus eight the end position 3 IPGLKKEIT 18 for each peptide is 5M GLKKEITV the start position [ TFIPGLKKE 11 FIPGLKKEI 13 plus eight jjFIPGLKKEI lLKIVP1 ~ LKIV ~~ HJLKKEITVQP 5 PGLKKEITV 10ITVQ SKEITVQPTV [|FIPGLKKE 1 Table XX | [KEITVQPTV9 Table XXVII 109P1D4v.8 (]TFIPGLKKE 8 109P1D4v.8 B1510-9-mers |PGLKKEITV[ B0702-9-ners Each peptide is a Each peptide Is a portion of SEQ ID portion of SEQ ID NO: 17; each Table XXXI NO: 17; each start start position Is 109P1D4v.8 position Is specified, the B2709-9-mers specified, the length of peptide length of peptide is 9 amino acids, Is 9 amino acids, and the end and the end position for each position for each peptide Is the peptide is the start start position plus position plus eight eight IPGLKKEIT 5 GLKKEITVQ z39 Each peptide is a Table XXXIV Each peptide is a portion of SEQ ID 109P1D4v.8 portion of SEQ ID NO: 17; each start Al-10-mers NO: 17; each start position is Eposition is specified, specified, the portion of SEQ ID the length of peptide length of peptide NO: 17; each start is 10 amino acids, is 9 amino acids, position Is specified, and the end position and the end the length of for each peptide is position for each peptide is 10 amino the start position peptide is the start acids, and the end plus nine position plus eight position for each peptide is the start O]GLKKEITVQP 1 KEITVQPTV position plus nine PGLKKEITV 10 RFIEGLEIT 10 2 FIPGLKKEl8] STFIPGLKKE| 1 1K!EIVQP 10Table XXXVIll Table XXXII 109P1D4v.8 109PID4v.8 Table XXXV A26-10-mers B4402-9-mers 109P1D4v.8 Each peptide is a Each peptide is a A0201-10-mers portion of SEQ ID portion of SEQ ID Each peptide is a NO: 17; each start NO: 17; each start portion of SEQ ID position is position is NO: 17; each start specified, the length specified, the position is specified, of peptide is 10 length of peptide the length of peptide amino acids, and is 9 amino acids, is 10 amino acids, the end position for and the end and the end position each peptide is the position for each for each peptide is start position plus peptide is the start the start position nine sition plus eight plus nine [ STFIPGLKKE|18 KEITVQP FIPGLKKEIT 15 [|FIPGLKKEIl12 41 IPGLKKEITV|1 Table XXXIX |TFIPGLKKE 1TFIPGLKKEI 1 09P1 e4v.8 IN HiollB0702-1O-mers ] KKEIT.QPW| Each peptide is a Table XXXII STFIPGLKKE portion of SEQ ID 109P1D4v.8 GLKKEriVQP| NO: 17; each start B5101-9-mers I11LGKKEIT position is specified, Each peptide is a LKKEIIVQPT the length of portion of SEQ ID peptide is 10 amino NO: 17; each start Table acids, and the end position is XXXVI position for each specfied, the 109P1D4v.8 peptide is the start length of peptide A0203-1 0- position plus nine is 9 amino acids, mers and the end m position for each IPGLIKKEITV1 peptide Is the start No Results FIPGLKKEIT| position plus eight Fud E LKKEITVQPT| 4 PGKKETV 2 Ir e~I~ 1 8KKEITVQPTV| |PGLKEle T1 V II FIPGLKKE 3-1 0-mers Table XL IPGLKKEIT 13 109PID4v.8 |KTQPV| B08-1 0 8 KE1VQPV 13mers; 240 Table XLVIII-1 09P1 D4v.8 Table XLV DRB1 0401-15-mers 109P1D4v.8 Each peptide is a portion of 85101-10- SEQ ID NO: 17; each start Table XU mers position is specified, the 19P1D4v.8 length of peptide Is 15 amino B1510-10- No Results acids, and the end position mers Found. for each peptide Is the start position plus fourteen Table XLVI-109P1D4v.8 oun. DB0101-15-mers El STFIPGLKKEITVQP I Each peptide is a portion of [ IPGLKKEITVQPTVE|gg Table XUI -SEQ ID NO: 17; each start 5][ESTFIPGLKKEITVQ l6 109P1D4v.8 position Is specified, the 13_KKEITVQPTVEE B2705-1 0- length of peptide Is 15 amino _ B751 acids, and the end position [ SDPESTFIPGU(KEI 12 mers for each peptide Is the start F311 DPESTFIPGLKKEIT 1 Its11 L position plus fourteen |PGLKKEITVQPVEE| 92 No Results Found. 9 IPGLKKEITVQPTVE| |GLKKEITVQPVEEA| 121 Table XLl 13 KKEITVQPTVEEASD 2 Table XLIX-109P1D4v.81 109P1D4v.8 5 ESTFIPGLKKEITVQ [91 DRB1 1101-15-mers B2709-10- DPESTFIPGLKKEIT 17 Each peptide is a portion mers STFIPGLKKEITVQP of SEQ ID NO: 17; each _____________EA start position is specified, LKKEITVQPTVEEAS the length of peptide is 15 amino adds, and the end Table XLVII-109PID4v.8 position for each peptide is DRB1 0301-15-mers the start position plus TablePXLIV Each peptide is a portion of fourTn 109P1D4v.8 SEQ ID NO: 17; each start |STFIPGLKKEITVQP|[21 B4402-10-mers position is specified, the |]ESTFIPGLKKEITVQ ||8 Each peptide is a length of peptide Is 15 amino j IPGLKKEI1VQPTVE 112 portion of SEQ ID acids, and the end position NO: 17; each start for each peptide is the start position is specified, position plus fourteen the length of peptide is 10 amino acids, and the end 51 ESTFIPGLKKElWQ|I7 position for each 61 STFIPGLKKEITVQP i peptide Is the sW :v§J KKIVQ1EES 7 position plus nine KKEITVQPTVEED 9] IPGLKKEITVQPTVE|12 9KEIVQPTVE 17 ]NSDPESTFIPGLKKE TFIPGLKKE 16 241 Table L: Protein Characteristics of 109P1D4 109PID4 var.1 Bioinformatic URL on World Wide Web Outcome Program ORF ORF finder 846-3911 bp (includes stop codon) Protein length 1021aa Transmembrane TM Pred .ch.embnet.org/ 3 TM helices (aa3-aa23, aa756 region aa776, aa816-aa834), N terminus intracellular HMMTop .enzim.hu/hmmtop/ no TM, N terminus extracellular Sosui .genome.ad.jp/SOSui/ 3 TM helices (2-24aa, 756-778aa, 810-832aa), N terminus extra cellular TMHMM .cbs.dtu.dk/servicesifMHMM ITM helix (813-835aa), N terminus extracellular Signal Peptide Signal P .cbs.dtu.dk/services/SignalP/ yes pl p1/MW tool .expasy.ch/tools/ p 1 4.81 Molecular weight p1/MW tool .expasy.ch/tools/ 112.7 kDa Localization PSORT psortnibb.ac.jp/ Plasma membrane PSORT 11 psortnibb.ac.jp/ 67% endoplasmic reticulum Motifs Pfam .sanger.ac.uk/Pfam/ Cadherin domain Prints .biochem.ucl.ac.uk/ Cadherin domain, DNA topoiso Merase 4B, sonic hedgehog Blocks .blocks.fhcrc.org/ Cadherin domain, ribosomal protein L I0E, ribulose biphos phate carboxylase (large chain), ornithine decarboxylase antizyme protein phosphatase 2C subfamily Table U. Exon boundaries of transcript 109Pi D4 v.1 Exon Start End Length 1 1 1385 1385 2 1386 4603 3218 Table LI(a). Nucleotide sequence of transcdpt variant 109PI D4 v.2 (SEQ ID NO: 237) cccctttctc cccctcggtt aagtccctcc ccctcgccat tcaaaagggc tggctcggca 60 ctggctcctt gcagtcggcg aactgtcggg gcgggaggag ccgtgagcag tagctgcact 120 cagctgcccg cgcggcaaag aggaaggcaa gccaaacaga gtgcgcagag tggcagtgcc 180 agcggcgaca caggcagcac aggcagcccg ggctgcctga atagcctcag aaacaacctc 240 agcgactccg gctgctctgc ggactgcgag ctgtggcggt agagcccgct. acagcagtcg 300 cagtctccgt ggagcgggcg gaagcctttt ttctcccttt cgtttacctc ttcattctac 360 tctaaaggca tcgttattag gaaaatcctg ttgcgaataa gaaggattcc acagatcaca 420 taccggagag gttttgcctc agctgctctc aactttgtaa tcttgtgaag aagctgacaa 480 gcttggctga ttgcagagca ctatgaggac tgaacgacag tgggttttaa ttcagatatt 540 tcaagtgttg tgcgggttaa tacaacaaac tgtaacaagt gtacctggta tggacttgtt 600 gtccgggacg tacattttcg cggtcctgct agcatgcgtg gtgttccact ctggcgccca 660 ggagaaaaac tacaccatcc gagaagaaat gccagaaaac gtcctgatag gcgacttgtt 720 gaaagacctt aacttgtcgc tgattccaaa caagtccttg acaactgcta tgcagttcaa 780 gctagtgtac aagaccggag atgtgccact gattcgaatt gaagaggata ctggtgagat 840 cttcactact ggcgctcgca ttgatcgtga gaaattatgt gctggtatcc caagggatga 900 gcattgcttt tatgaagtgg aggttgccat tttgccggat gaaatattta gactggttaa 960 gatacgtttt ctgatagaag atataaatga taatgcacca ttgttcccag caacagttat 1020 caacatatca attccagaga actcggctat aaactctaaa tatactctcc cagcggctgt 1080 tgatcctgac gtaggaataa acggagttca aaactacgaa ctaattaaga gtcaaaacat 1140 ttttggcctc gatgtcattg aaacaccaga aggagacaag atgccacaac tgattgttca 1200 aaaggagtta gatagggaag agaaggatac ctacgtgatg aaagtaaagg ttgaagatgg 1260 242 tggctttcct caaagatcca gtactgctat tttgcaagtg agtgttactg atacaaatga 1320 caaccaccca gtctttaagg agacagagat tgaagtcagt ataccagaaa atgctcctgt 1380 aggcacttca gtgacacagc tccatgccac agatgctgac ataggtgaaa atgccaagat 1440 ccacttctct ttcagcaatc tagtctccaa cattgccagg agattatttc acctcaatgc 1500 caccactgga cttatcacaa tcaaagaacc actggatagg gaagaaacac caaaccacaa 1560 gttactggtt ttggcaagtg atggtggatt gatgccagca agagcaatgg tgctggtaaa 1620 tgttacagat gtcaatgata atgtcccatc cattgacata agatacatcg tcaatcctgt 1680 caatgacaca gttgttcttt cagaaaatat tccactcaac accaaaattg ctctcataac 1740 tgtgacggat aaggatgcgg accataatgg cagggtgaca tgcttcacag atcatgaaat 1800 ccctttcaga ttaaggccag tattcagtaa tcagttcctc ctggagactg cagcatatct 1860 tgactatgag tccacaaaag aatatgccat taaattactg gctgcagatg ctggcaaacc 1920 tcctttgaat cagtcagcaa tgctcttcat caaagtgaaa gatgaaaatg acaatgctcc 1980 agttttcacc cagtctttcg taactgtttc tattcctgag aataactctc ctggcatcca 2040 gttgacgaaa gtaagtgcaa tggatgcaga cagtgggcct aatgctaaga tcaattacct 2100 gctaggccct gatgctccac ctgaattcag cctggattgt cgtacaggca tgctgactgt 2160 agtgaagaaa ctagatagag aaaaagagga taaatattta ttcacaattc tggcaaaaga 2220 taacggggta ccacccttaa ccagcaatgt cacagtcttt gtaagcatta ttgatcagaa 2280 tgacaatagc ccagttttca ctcacaatga atacaacttc tatgtcccag aaaaccttcc 2340 aaggcatggt acagtaggac taatcactgt aactgatcct gattatggag acaattctgc 2400 agttacgctc tccattttag atgagaatga tgacttcacc attgattcac aaactggtgt 2460 catccgacca aatatttcat ttgatagaga aaaacaagaa tcttacactt tctatgtaaa 2520 ggctgaggat ggtggtagag tatcacgttc ttcaagtgcc aaagtaacca taaatgtggt 2580 tgatgtcaat gacaacaaac cagttttcat tgtccctcct tccaactgtt cttatgaatt 2640 ggttctaccg tccactaatc caggcacagt ggtctttcag gtaattgctg ttgacaatga 2700 cactggcatg aatgcagagg ttcgttacag cattgtagga ggaaacacaa gagatctgtt 2760 tgcaatcgac caagaaacag gcaacataac attgatggag aaatgtgatg ttacagacct 2820 tggtttacac agagtgttgg tcaaagctaa tgacttagga cagcctgatt ctctcttcag 2880 tgttgtaatt gtcaatctgt tcgtgaatga gtcggtgacc aatgctacac tgattaatga 2940 actggtgcgc aaaagcactg aagcaccagt gaccccaaat actgagatag ctgatgtatc 3000 ctcaccaact agtgactatg tcaagatcct ggttgcagct gttgctggca ccataactgt 3060 cgttgtagtt attttcatca ctgctgtagt aagatgtcgc caggcaccac accttaaggc 3120 tgctcagaaa aacaagcaga attctgaatg ggctacccca aacccagaaa acaggcagat 3180 gataatgatg aagaaaaaga aaaagaagaa gaagcattcc cctaagaact tgctgcttaa 3240 ttttgtcact attgaagaaa ctaaggcaga tgatgttgac agtgatggaa acagagtcac 3300 actagacctt cctattgatc tagaagagca aacaatggga aagtacaatt gggtaactac 3360 acctactact ttcaagcccg acagccctga tttggcccga cactacaaat ctgcctctcc 3420 acagcctgcc ttccaaattc agcctgaaac tcccctgaat tcgaagcacc acatcatcca 3480 agaactgcct ctcgataaca cctttgtggc ctgtgactct atctccaagt gttcctcaag 3540 cagttcagat ccctacagcg tttctgactg tggctatcca gtgacgacct tcgaggtacc 3600 tgtgtccgta cacaccagac cgactgattc caggacatca actattgaaa tctgcagtga 3660 gatataactt tctaggaaca acaaaattcc attccccttc caaaaaattt caatgattgt 3720 gatttcaaaa ttaggctaag atcattaatt ttgtaatcta gatttcccat tataaaagca 3780 agcaaaaatc atcttaaaaa tgatgtccta gtgaaccttg tgctttcttt agctgtaatc 3840 tggcaatgga aatttaaaat ttatggaaga gacagtgcag cacaataaca gagtactctc 3900 atgctgtttc tctgtttgct ctgaatcaac agccatgatg taatataagg ctgtcttggt 3960 gtatacactt atggttaata tatcagtcat gaaacatgca attacttgcc ctgtctgatt 4020 gttgaataat taaaacatta tctccaggag tttggaagtg agctgaacta gccaaactac 4080 tctctgaaag gtatccaggg caagagacat ttttaagacc ccaaacaaac aaaaaacaaa 4140 accaaaacac tctggttcag tgttttgaaa atattcacta acataatatt gctgagaaaa 4200 tcatttttat tacccaccac tctgcttaaa agttgagtgg gccgggcgcg gtggctcacg 4260 cctgtaatcc cagcactttg ggaggccgag gcgggtggat cacgaggtca ggagattgag 4320 accatcctgg ctaacacggt gaaaccccat ctccactaaa aatacaaaaa attagcctgg 4380 cgtggtggcg ggcgcctgta gtcccagcta ctcgggaggc tgaggcagga gaatagcgtg 4440 aacccgggag gcggagcttg cagtgagccg agatggcgcc actgcactcc agcctgggtg 4500 acagagcaag actctgtctc aaaaagaaaa aaatgttcaa tgatagaaaa taattttact 4560 aggtttttat gttgattgta ctcatgctgt tccactcctt ttaattatta aaaagttatt 4620 tttggctggg tgtggtggct cacacctgta atcccagcac tttgggaggc cgaggtgggt 4680 ggatcacctg aggtcaggag ttcaagacca gtctggccaa cat 4723 243 Table UIll(a). Nucleotide sequence alignment of 109P1D4 v.1 (SEQ ID NO: 238) and 109P1D4 v.2 (SEQ ID NO: 239) Score = 5920 bits (3079), Expect = 0.0ldentities = 3079/3079 (100%) Strand = Plus ! Plus V.1 800 agtgttgtgcgggttaatacaacaaactgtaacaagtgtacctggtatggacttgttgtc 859 V.2 544 agtgttgtgcgggttaatacaacaaactgtaacaagtgtacctggtatggacttgttgtc 603 V.1 860 cgggacgtacattttcgcggtcctgctagcatgcgtggtgttccactctggcgcccagga 919 11l1lllll1lll1l1lllll1llll111llllilllllllil1lllilll1l1l lil V.2 604 cgggacgtacattttcgcggtcctgctagcatgcgtggtgttccactctggcgcccagga 663 V.1 920 gaaaaactacaccatccgagaagaaatgccagaaaacgtcctgataggcgacttgttgaa 979 V.2 664 gaaaaactacaccatccgagaagaaatgccagaaaacgtcctgataggcgacttgttgaa 723 V.1 980 agaccttaacttgtcgctgattccaaacaagtccttgacaactgctatgcagttcaagct 1039 I l l I |||l ll I II1 11 1 1 111 lill1111l1lilll 1i11I ll l 1 l1 I I I1II l1|| V.2 724 agaccttaacttgtcgctgattccaaacaagtccttgacaactgctatgcagttcaagct 783 V.1 1040 agtgtacaagaccggagatgtgccactgattcgaattgaagaggatactggtgagatctt 1099 I1l1ill1 illi II Illil11i | IllI11 1I I l ll l Il l lIllil1IlI I I I V.2 784 agtgtacaagaccggagatgtgccactgattcgaattgaagaggatactggtgagatctt 843 V.1 1100 cactactggcgctcgcattgatcgtgagaaattatgtgctggtatcccaagggatgagca 1159 |||| |lil I I||I1 lill 11 I I111 l IilI 11111111 | l i i ||I11 ll111 l 1 ||1 V.2 844 cactactggcgctcgcattgatcgtgagaaattatgtgctggtatcccaagggatgagca 903 V.1 1160 ttgcttttatgaagtggaggttgccattttgccggatgaaatatttagactggttaagat 1219 I l111ilI111 lil I ll Iillii1 IlI 11 1 1 1 11 l li | l i1 11 1 I||| V.2 : 904 ttgcttttatgaagtggaggttgccattttgccggatgaaatatttagactggttaagat 963 V.1 : 1220 acgttttctgatagaagatataaatgataatgcaccattgttcccagcaacagttatcaa 1279 lill 11 11 i l l i I 11 I|iI l lIl lI l II I lll11 11 11 11 1 11 lilil1111 V.2 : 964 acgttttctgatagaagatataaatgataatgcaccattgttcccagcaacagttatcaa 1023 V.1 : 1280 catatcaattccagagaactcggctataaactctaaatatactctcccagcggctgttga 1339 1111|11I11I111111111I111111lI I lll Illlll lillll Il1i11il111I1l111I1l V.2 : 1024 catatcaattccagagaactcggctataaactctaaatatactctcccagcggctgttga 1083 V.1 : 1340 tcctgacgtaggaataaacggagttcaaaactacgaactaattaagagtcaaaacatttt 1399 |l1I I II1I 1I II II II1 I II 111111111111111111I1111111111111 I iiI i I V.2 : 1084 tcctgacgtaggaataaacggagttcaaaactacgaactaattaagagtcaaaacatttt 1143 V.1 : 1400 tggcctcgatgtcattgaaacaccagaaggagacaagatgccacaactgattgttcaaaa 1459 l l lillI1lllllll ll 1i l ll llll llllllllil li llll Il 1 1 lill V.2 : 1144 tggcctcgatgtcattgaaacaccagaaggagacaagatgccacaactgattgttcaaaa 1203 V.1 : 1460 ggagttagatagggaagagaaggatacctacgtgatgaaagtaaaggttgaagatggtgg 1519 11l l Il l l 11i | | || lllll 1 i lil11 ill11 ilill1l1 Ilil111I l11 ||1 V.2 : 1204 ggagttagatagggaagagaaggatacctacgtgatgaaagtaaaggttgaagatggtgg 1263 V.1 : 1520 ctttcctcaaagatccagtactgctattttgcaagtgagtgttactgatacaaatgacaa 1579 V.2 : 1264 ctttcctcaaagatccagtactgctattttgcaagtgagtgttactgatacaaatgacaa 1323 244 V.1 1580 ccacccagtctttaaggagacagagattgaagtcagtataccagaaaatgctcctgtagg 1639 V.2 1324 ccacccagtctttaaggagacagagattgaagtcagtataccagaaaatgctcctgtagg 1383 V.1 1640 cacttcagtgacacagctccatgccacagatgctgacataggtgaaaatgccaagatcca 1699 I llill il||| |||I1 I l li|lI I II|||1 |||1 | || |||| ||||| |||i V.2 1384 cacttcagtgacacagctccatgccacagatgctgacataggtgaaaatgccaagatcca 1443 V.1 1700 cttctctttcagcaatctagtctccaacattgccaggagattatttcacctcaatgccac 1759 lil||||| ||||||| 1I1l1ll|i||||||| l ||I |||| ||||||1 ||||||||111 V.2 1444 cttctctttcagcaatctagtctccaacattgccaggagattatttcacctcaatgccac 1503 V.1 1760 cactggacttatcacaatcaaagaaccactggatagggaagaaacaccaaaccacaagtt 1819 V.2 1504 cactggacttatcacaatcaaagaaccactggatagggaagaaacaccaaaccacaagtt 1563 V.1 1820 actggttttggcaagtgatggtggattgatgccagcaagagcaatggtgctggtaaatgt 1879 ||||||| |||||li ll 1|| 1|| 1|| iii|l|| i1 1||||||||||1 11 ||1 || V.2 : 1564 actggttttggcaagtgatggtggattgatgccagcaagagcaatggtgctggtaaatgt 1623 V.1 : 1880 tacagatgtcaatgataatgtcccatccattgacataagatacatcgtcaatcctgtcaa 1939 V.2 : 1624 tacagatgtcaatgataatgtcccatccattgacataagatacatcgtcaatcctgtcaa 1683 V.1 : 1940 tgacacagttgttctttcagaaaatattccactcaacaccaaaattgctctcataactgt 1999 V.2 : 1684 tgacacagttgttctttcagaaaatattccactcaacaccaaaattgctctcataactgt 1743 V.1 : 2000 gacggataaggatgcggaccataatggcagggtgacatgcttcacagatcatgaaatccc 2059 ||||ilIilI I|I|||||||||||I!||i||||||l| |||||||||||IIlif lll V.2 : 1744 gacggataaggatgcggaccataatggcagggtgacatgcttcacagatcatgaaatccc 1803 V.1 : 2060 tttcagattaaggccagtattcagtaatcagttcctcctggagactgcagcatatcttga 2119 V.2 1804 tttcagattaaggccagtattcagtaatcagttcctcctggagactgcagcatatcttga 1863 V.1 2120 ctatgagtccacaaaagaatatgccattaaattactggctgcagatgctggcaaacctcc 2179 V.2 1864 ctatgagtccacaaaagaatatgccattaaattactggctgcagatgctggcaaacctcc 1923 V.1 2180 tttgaatcagtcagcaatgctcttcatcaaagtgaaagatgaaaatgacaatgctccagt 2239 |||||1|||||||I I1I I||1|1||||||||||||||||||||||1||1|1||11|1|1 V.2 1924 tttgaatcagtcagcaatgctcttcatcaaagtgaaagatgaaaatgacaatgctccagt 1983 V.1 : 2240 tttcacccagtctttcgtaactgtttctattcctgagaataactctcctggcatccagtt 2299 V.2 : 1984 tttcacccagtctttcgtaactgtttctattcctgagaataactctcctggcatccagtt 2043 V.1 : 2300 gacgaaagtaagtgcaatggatgcagacagtgggcctaatgctaagatcaattacctgct 2359 1il11 llil11 ||1 |||||||1 ||11 ||||l |||11 |11 |||1|11 |jil ||ii ||||||I V.2 : 2044 gacgaaagtaagtgcaatggatgcagacagtgggcctaatgctaagatcaattacctgct 2103 V.1 : 2360 aggccctgatgctccacctgaattcagcctggattgtcgtacaggcatgctgactgtagt 2419 lVll : 10l4 l ll|||||l i1|||||||11 |1 ||||11 1|| 11||| 1il 11| 1 1 2l1 3 V.2 :2104 aggccctgatgctccacctgaattcagcctggattgtcgtacaggcatgctgactgtagt 2163 245 V.1 2420 gaagaaactagatagagaaaaagaggataaatatttattcacaattctggcaaaagataa 2479 1111I1I111l I 11l 11I l i ll I lil 1 111 lil11ll I Ilil lil I I I I I1lill V.2 2164 gaagaaactagatagagaaaaagaggataaatatttattcacaattctggcaaaagataa 2223 V.1 2480 cggggtaccacccttaaccagcaatgtcacagtctttgtaagcattattgatcagaatga 2539 I lililli I1 l11 I 11ll11ill1 ill11111ll11111llll11l1l l1lill11I1ll1 ll11 V.2 2224 cggggtaccacccttaaccagcaatgtcacagtctttgtaagcattattgatcagaatga 2283 V.1 2540 caatagcccagttttcactcacaatgaatacaacttctatgtcccagaaaaccttccaag 2599 111111I1li11111l1111 |I1 ill1 II i lIllil lilllil 111 i1 l ii i I lll V.2 2284 caatagcccagttttcactcacaatgaatacaacttctatgtcccagaaaaccttccaag 2343 V.1 2600 gcatggtacagtaggactaatcactgtaactgatcctgattatggagacaattctgcagt 2659 |11 1 li l i I 111 iI i liI lli I lilIiI i| 1IlI lill lillill I lili V.2 2344 gcatggtacagtaggactaatcactgtaactgatcctgattatggagacaattctgcagt 2403 V.1 2660 tacgctctccattttagatgagaatgatgacttcaccattgattcacaaactggtgtcat 2719 i ll I II Il 1 I I I lili I I l i ll111 li ll li I lli il lill1 | V.2 2404 tacgctctccattttagatgagaatgatgacttcaccattgattcacaaactggtgtcat 2463 V.1 2720 ccgaccaaatatttcatttgatagagaaaaacaagaatcttacactttctatgtaaaggc 2779 iIII II IIIi il l l l ill l iiI||1 l1111I111l il1I lill l I1I|1I1illlll I lil| V.2 2464 ccgaccaaatatttcatttgatagagaaaaacaagaatcttacactttctatgtaaaggc 2523 V.1 2780 tgaggatggtggtagagtatcacgttcttcaagtgccaaagtaaccataaatgtggttga 2839 V.2 2524 tgaggatggtggtagagtatcacgttcttcaagtgccaaagtaaccataaatgtggttga 2583 V.1 2840 tgtcaatgacaacaaaccagttttcattgtccctccttccaactgttcttatgaattggt 2899 V.2 2584 tgtcaatgacaacaaaccagttttcattgtccctccttccaactgttcttatgaattggt 2643 V.1 2900 tctaccgtccactaatccaggcacagtggtctttcaggtaattgctgttgacaatgacac 2959 ill 1 11 111 iIl iIl111 l I i I lilil I I||||ili11 lill I lI I lli I V.2 : 2644 tctaccgtccactaatccaggcacagtggtctttcaggtaattgctgttgacaatgacac 2703 V.1 : 2960 tggcatgaatgcagaggttcgttacagcattgtaggaggaaacacaagagatctgtttgc 3019 111I11111111|Il1111 ll1111111|11 1 i l i | | l l I lil11111111 il lil| V.2 : 2704 tggcatgaatgcagaggttcgttacagcattgtaggaggaaacacaagagatctgtttgc 2763 V.1 : 3020 aatcgaccaagaaacaggcaacataacattgatggagaaatgtgatgttacagaccttgg 3079 V.2 : 2764 aatcgaccaagaaacaggcaacataacattgatggagaaatgtgatgttacagaccttgg 2823 V.1 : 3080 tttacacagagtgttggtcaaagctaatgacttaggacagcctgattctctcttcagtgt 3139 V.2 : 2824 tttacacagagtgttggtcaaagctaatgacttaggacagcctgattctctcttcagtgt 2883 V.1 : 3140 tgtaattgtcaatctgttcgtgaatgagtcggtgaccaatgctacactgattaatgaact 3199 I1ll111||1 I I 1 lIIII I I I I l I II IIII I lIil lI llilililililil II V.2 : 2884 tgtaattgtcaatctgttcgtgaatgagtcggtgaccaatgctacactgattaatgaact 2943 V.1 : 3200 ggtgcgcaaaagcactgaagcaccagtgaccccaaatactgagatagtgatgtatcctc 3259 V.2 : 2944 ggtgcgcaaaagcactgaagcaccagtgaccccaaatactgagatagtgatgtatcctc 3003 246 V.1 3260 accaactagtgactatgtcaagatcctggttgcagctgttgctggcaccataactgtcgt 3319 V.2 3004 accaactagtgactatgtcaagatcctggttgcagctgttgctggcaccataactgtcgt 3063 V.1 3320 tgtagttattttcatcactgtgtagtaagatgtcgccaggcaccacaccttaaggctgc 3379 1i Iil 11111I 1111il 1ll 11ll 1l1ll 1ll 1I||||1 11 11 |||1 11111il I1ll lill V.2 3064 tgtagttattttcatcactgctgtagtaagatgtcgccaggcaccacaccttaaggctgc 3123 V.1 3380 tcagaaaaacaagcagaattctgaatgggctaccccaaacccagaaaacaggcagatgat 3439 1|1I1l 1 1111I 111il ll 1li |lill |lili 1111 ||||111il111I lli 111| |1 11i V.2 3124 tcagaaaaacaagcagaattctgaatgggctaccccaaacccagaaaacaggcagatgat 3183 V.1 3440 aatgatgaagaaaaagaaaaagaagaagaagcattcccctaagaacttgctgcttaattt 3499 i i l l 1 1 | 1 l i l l il | | 1 1 i l I I l | I l i l I I I l l I l I l l l i l l i l l i V.2 3184 aatgatgaagaaaaagaaaaagaagaagaagcattcccctaagaacttgctgcttaattt 3243 V.1 3500 tgtcactattgaagaaactaaggcagatgatgttgacagtgatggaaacagagtcacact 3559 111i I I|||I liliI l I l l l iIl i I|I 1 1lli111 1 1 11 1 11 |! I1lil1l -V.2 3244 tgtcactattgaagaaactaaggcagatgatgttgacagtgatggaaacagagtcacact 3303 V.1 3560 agaccttcctattgatctagaagagcaaacaatgggaaagtacaattgggtaactacacc 3619 111111I II || 1 liIi I I I 11 11 111|11|111|||1 11 III IIIIIIIIIIIIiiIiIIlII V.2 3304 agaccttcctattgatctagaagagcaaacaatgggaaagtacaattgggtaactacacc 3363 V.1 3620 tactactttcaagcccgacagccctgatttggcccgacactacaaatctgcctctccaca 3679 V.2 : 3364 tactactttcaagcccgacagccctgatttggcccgacactacaaatctgcctctccaca 3423 V.1 : 3680 gcctgccttccaaattcagcctgaaactcccctgaattcgaagcaccacatcatccaaga 3739 V.2 : 3424 gcctgccttccaaattcagcctgaaactcccctgaattcgaagcaccacatcatccaaga 3483 V.1 : 3740 actgcctctcgataacacctttgtggcctgtgactctatctccaagtgttcctcaagcag 3799 l1111 lil1ll1l1llll1lillllllillll 11111111|1|||lilllllllll1lllli V.2- : 3484 actgcctctcgataacacctttgtggcctgtgactctatctccaagtgttcctcaagcag 3543 V.1 : 3800 ttcagatccctacagcgtttctgactgtggctatccagtgacgaccttcgaggtacctgt 3859 l11l1l111l1lillllilll1llllllllllll1l1lllll1llll1llll1lllllil V.2 : 3544 ttcagatccctacagcgtttctgactgtggctatccagtgacgaccttcgaggtacctgt 3603 V.1 : 3860 gtccgtacacaccagaccg 3878 V.2 : 3604 gtccgtacacaccagaccg 3622 Table UV(a). Peptide sequences of protein coded by 109P1 D4 v.2 (SEQ ID NO: 240) MRTERQWVLI QIFQVLCGLI QQTVTSVPGM DLLSGTYIFA VLLACVVFHS GAQEKNYTIR 60 EEMPENVLIG DLLKDLNLSL IPNKSLTTAM QFKLVYKTGD VPLIRIEEDT GEIFTTGARI 120 DREKLCAGIP RDEHCFYEVE VAILPDEIFR LVKIRFLIED INDNAPLFPA TVINISIPEN 180 SAINSKYTLP AAVDPDVGIN GVQNYELIKS QNIFGLDVIE TPEGDKMPQL IVQKELDREE 240 KDTYVMKVKV EDGGFPQRSS TAILQVSVTD TNDNHPVFKE TEIEVSIPEN APVGTSVTQL 300 HATDADIGEN AKIHFSFSNL VSNIARRLFH LNATTGLITI KEPLDREETP NHKLLVLASD 360 GGLMPARAMV LVNVTDVNDN VPSIDIRYIV NPVNDTVVLS ENIPLNTKIA LITVTDKDAD 420 HNGRVTCFTD HEIPFRLRPV FSNQFLLETA AYLDYESTKE YAIKLLAADA GKPPLNQSAM 480 LFIKVKDEND NAPVFTQSFV TVSIPENNSP GIQLTKVSAM DADSGPNAKI NYLLGPDAPP 540 EFSLDCRTGM LTVVKKLDRE KEDKYLFTIL AKDNGVPPLT SNVTVFVSII DQNDNSPVFT 600 247 HNEYNFYVPE NLPRHGTVGL ITVTDPDYGD NSAVTLSILD ENDDFTIDSQ TGVIRPNISF 660 DREKQESYTF YVKAEDGGRV SRSSSAKVTI NVVDVNDNKP VFIVPPSNCS YELVLPSTNP 720 GTVVFQVIAV DNDTGMNAEV RYSIVGGNTR DLFAIDQETG NITLMEKCDV TDLGLHRVLV 780 KANDLGQPDS LFSVVIVNLF VNESVTNATL INELVRKSTE APVTPNTEIA DVSSPTSDYV 840 KILVAAVAGT ITVVVVIFIT AVVRCRQAPH LKAAQKNKQN SEWATPNPEN RQMIMMKKKK 900 KKKKHSPKNL LLNFVTIEET KADDVDSDGN RVTLDLPIDL EEQTMGKYNW VTTPTTFKPD 960 SPDLARHYKS ASPQPAFQIQ PETPLNSKHH IIQELPLDNT FVACDSISKC SSSSSDPYSV 1020 SDCGYPVTTF EVPVSVHTRP TDSRTSTIEI CSEI 1054 Table LV(a). Amino acid sequence alignment of 109P1D4 v.1 (SEQ ID NO: 241) and 109P1D4 v.2 (SEQ ID NO: 242) Score = 2006 bits (5197), Expect = 0.01dentities = 1012/1017 (99%), Positives = 1013/1017 (99%) V.1 1 MDLLSGTYIFAVLLACVVFHSGAQEKNYTIREEMPENVLIGDLLKDLNLSLIPNKSLTTA 60 MDLLSGTYIFAVLLACVVFHSGAQEKNYTIREEMPENVLIGDLLKDLNLSLIPNKSLTTA V.2 30 MDLLSGTYIFAVLLACVVFHSGAQEKNYTIREEMPENVLIGDLLKDLNLSLIPNKSLTTA 89 V.1 61 MQFKLVYKTGDVPLIRIEEDTGEIFrTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIF 120 MQFKLVYKTGDVPLIRIEEDTGEIFTTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIF V.2 90 MQFKLVYKTGDVPLIRIEEDTGEIFTTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIF 149 V.1 121 RLVKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIK 180 RLVKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIK V.2 150 RLVKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIK 209 V.1 181 SQNIFGLDVIETPEGDKMPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVT 240 SQNIFGLDVIETPEGDKMPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVT V.2 210 SQNIFGLDVIETEGDKMPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVT 269 V.1 241 DTNDNHPVFKETEIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSFSNLVSNIARRLF 300 DTNDNHPVFKETEIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSFSNLVSNIARRLF V.2 270 DTNDNHPVFKETEIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSFSNLVSNIARRLF 329 V.1 301 HLNATTGLITIKEPLDREETPNHKLLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYI 360 HLNATTGLITIKEPLDREETPNHKLLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYI V.2 330 HLNATTGLITIKEPLDREETPNHKLLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYI 389 V.1 361 VNPVNDTVVLSENIPLNTKIALITVTDKDADHNGRVTCFTDHEIPFRLRPVFSNQFLLET 420 VNPVNDTVVLSENIPLNTKIALITVTDKDADHNGRVTCFTDHEIPFRLRPVFSNQFLLET V.2 390 VNPVNDTVVLSENIPLNTKIALITVTDKDADHNGRVTCFTDHEIPFRLRPVFSNQFLLET 449 V.1 421 AAYLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDENDNAPVFTQSFVTVSIPENNS 480 AAYLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDENDNAPVFTQSFVTVSI PENNS V.2 450 AAYLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDENDNAPVFTQSFVTVSIPENNS 509 V.1 481 PGIQLTKVSAMDADSGPNAKINYLLGPDAPPEFSLDCRTGMLTVVKKLDREKEDKYLEI 540 PGIQLTKVSAMDADSGPNAKINYLLGPDAPPEFSLDCRTGMLTVVKKLDREKEDKYLErI V.2 510 PGIQLTKVSAMDADSGPNAKINYLLGPDAPPEFSLDCRTGMLTVVKKLDREKEDKYLFTI 569 V.1 541 LAKDNGVPPLTSNVTVEVSIIDQNDNSPVErHNEYNFYVPENLPRHGTVGLITVTDPDYG 600 LAKDNGVPPLTSNVTVFVSIIDQNDNSPVFrHNEYNFYVPENLPRHGTVGLITVTDPDYG V.2 570 LAKDNGVPPLTSNVTVFVSIIDQNDNSPVFTHNEYNFYVPENLPRHGTVGLITVTDPDYG 629 V.1 601 DNSAVTLSILDENDDrrIDSTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVT 660 DNSAVTLSILDENDDFTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVT V.2 630 DNSAVTLSILDENDDPIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVT 689 V.1 661 INVVDVNDNKPVFIVPPSNCSYELVLPSTNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNT 720 INVVDVNDNKPVFIVPPSNCSYELVLPSTNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNT V.2 690 INVVDVNDNKPVFIVPPSNCSYELVLPSTNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNT 749 V.1 721 RDLFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPDSLFSVVIVNLFVNESVTNAT 780 RDLFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPDSLFSVVIVNLFVNESVTNAT V.2 750 RDLFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPDSLFSVVIVNLFVNESVTNAT 809 V.1 781 LINELVRKSTEAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVRCRQAP 840 LINELVRKSTEAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVRCRQAP V.2 810 LINELVRKSTEAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVRCRQAP 869 248 V.1 841 HLKAAQKNKQNSEWATPNPENRQMIMMKKKKKKKKHSPKNLLLNFVTIEETKADDVDSDG 900 HLKAAQKNKQNSEWATPNPENRQMIMMKKKKKKKKHSPKNLLLNFVTIEETKADDVDSDG V.2 870 HLKAAQKNKQNSEWATPNPENRQMIMMKKKKKKKKHSPKNLLLNFVTIEETKADDVDSDG 929 V.1 901 NRVTLDLPIDLEEQTMGKYNWVTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLNSKH 960 NRVTLDLPIDLEEQTMGKYNWVTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLNSKH V.2 930 NRVTLDLPIDLEEQTMGKYNWVTTPTTFKPDSPDfARHYKSASPQPAFQIQPETPLNSKH 989 V.1 961 HIIQELPLDNTFVACDSISKCSSSSSDPYSVSDCGYPVTTFEVPVSVHTRPVGIQVS 1017 HIIQELPLDNTFVACDSISKCSSSSSDPYSVSDCGYPVTTFEVPVSVHTRP + S V.2 990 HIIQELPLDNTFVACDSISKCSSSSSDPYSVSDCGYPVTTFEVPVSVHTRPTDSRTS 1046 Table 111(b). Nucleotide sequence of transcript variant 109P1 D4 v.3 (SEQ ID NO: 243) ctggtggtcc agtacctcca aagatatgga atacactcct gaaatatcct gaaaactttt 60 ttttttcaga atcctttaat aagcagttat gtcaatctga aagttgctta cttgtacttt 120 atattaatag ctattcttgt ttttcttatc caaagaaaaa tcctctaatc cccttttcac 180 atgatagttg ttaccatgtt taggcattag tcacatcaac ccctctcctc tcccaaactt 240 ctcttcttca aatcaaactt tattagtccc tcctttataa tgattccttg cctcgtttta 300 tccagatcaa ttttttttca ctttgatgcc cagagctgaa gaaatggact actgtataaa 360 ttattcattg ccaagagaat aattgcattt taaacccata ttataacaaa gaataatgat 420 tatattttgt gatttgtaac aaataccctt tattttccct taactattga attaaatatt 480 ttaattattt gtattctctt taactatctt ggtatattaa agtattatct tttatatatt 540 tatcaatggt ggacactttt ataggtactc tgtgtcattt ttgatactgt aggtatctta 600 tttcatttat ctttattctt aatgtacgaa ttcataatat ttgattcaga acaaatttat 660 cactaattaa cagagtgtca attatgctaa catctcattt actgatttta atttaaaaca 720 gtttttgtta acatgcatgt ttagggttgg cttcttaata atttcttctt cctcttctct 780 ctctcctctt cttttggtca gtgttgtgcg ggttaataca acaaactgta acaagtgtac 840 ctggtatgga cttgttgtcc gggacgtaca ttttcgcggt cctgctagca tgcgtggtgt 900 tccactctgg cgcccaggag aaaaactaca ccatccgaga agaaatgcca gaaaacgtcc 960 tgataggcga cttgttgaaa gaccttaact tgtcgctgat tccaaacaag tccttgacaa 1020 ctgctatgca gttcaagcta gtgtacaaga ccggagatgt gccactgatt cgaattgaag 1080 aggatactgg tgagatcttc actactggcg ctcgcattga tcgtgagaaa ttatgtgctg 1140 gtatcccaag ggatgagcat tgcttttatg aagtggaggt tgccattttg ccggatgaaa 1200 tatttagact ggttaagata cgttttctga tagaagatat aaatgataat gcaccattgt 1260 tcccagcaac agttatcaac atatcaattc cagagaactc ggctataaac tctaaatata 1320 ctctcccagc ggctgttgat cctgacgtag gaataaacgg agttcaaaac tacgaactaa 1380 ttaagagtca aaacattttt ggcctcgatg tcattgaaac accagaagga gacaagatgc 1440 cacaactgat tgttcaaaag gagttagata gggaagagaa ggatacctac gtgatgaaag 1500 taaaggttga agatggtggc tttcctcaaa gatccagtac tgctattttg caagtgagtg 1560 ttactgatac aaatgacaac cacccagtct ttaaggagac agagattgaa gtcagtatac 1620 cagaaaatgc tcctgtaggc acttcagtga cacagctcca tgccacagat gctgacatag 1680 gtgaaaatgc caagatccac ttctctttca gcaatctagt ctccaacatt gccaggagat 1740 tatttcacct caatgccacc actggactta tcacaatcaa agaaccactg gatagggaag 1800 aaacaccaaa ccacaagtta ctggttttgg caagtgatgg tggattgatg ccagcaagag 1860 caatggtgct ggtaaatgtt acagatgtca atgataatgt cccatccatt gacataagat 1920 acatcgtcaa tcctgtcaat gacacagttg ttctttcaga aaatattcca ctcaacacca 1980 aaattgctct cataactgtg acggataagg atgcggacca taatggcagg gtgacatgct 2040 tcacagatca tgaaatccct ttcagattaa ggccagtatt cagtaatcag ttcctcctgg 2100 agactgcagc atatcttgac tatgagtcca caaaagaata tgccattaaa ttactggctg 2160 cagatgctgg caaacctcct ttgaatcagt cagcaatgct cttcatcaaa gtgaaagatg 2220 aaaatgacaa tgctccagtt ttcacccagt ctttcgtaac tgtttctatt cctgagaata 2280 actctcctgg catccagttg acgaaagtaa gtgcaatgga tgcagacagt gggcctaatg 2340 ctaagatcaa ttacctgcta ggccctgatg ctccacctga attcagcctg gattgtcgta 2400 caggcatgct gactgtagtg aagaaactag atagagaaaa agaggataaa tatttattca 2460 caattctggc aaaagataac ggggtaccac ccttaaccag caatgtcaca gtctttgtaa 2520 gcattattga tcagaatgac aatagcccag ttttcactca caatgaatac aacttctatg 2580 tcccagaaaa ccttccaagg catggtacag taggactaat cactgtaact gatcctgatt 2640 atggagacaa ttctgcagtt acgctctcca ttttagatga gaatgatgac ttcaccattg 2700 attcacaaac tggtgtcatc cgaccaaata tttcatttga tagagaaaaa caagaatctt 2760 acactttcta tgtaaaggct gaggatggtg gtagagtatc acgttcttca agtgccaaag 2820 taaccataaa tgtggttgat gtcaatgaca acaaaccagt tttcattgtc cctccttcca 2880 249 actgttctta tgaattggtt ctaccgtcca ctaatccagg cacagtggtc tttcaggtaa 2940 ttgctgttga caatgacact ggcatgaatg cagaggttcg ttacagcatt gtaggaggaa 3000 acacaagaga tctgtttgca atcgaccaag aaacaggcaa cataacattg atggagaaat 3060 gtgatgttac agaccttggt ttacacagag tgttggtcaa agctaatgac ttaggacagc 3120 ctgattctct cttcagtgtt gtaattgtca atctgttcgt gaatgagtcg gtgaccaatg 3180 ctacactgat taatgaactg gtgcgcaaaa gcactgaagc accagtgacc ccaaatactg 3240 agatagctga tgtatcctca ccaactagtg actatgtcaa gatcctggtt gcagctgttg 3300 ctggcaccat aactgtcgtt gtagttattt tcatcactgc tgtagtaaga tgtcgccagg 3360 caccacacct taaggctgct cagaaaaaca agcagaattc tgaatgggct accccaaacc 3420 cagaaaacag gcagatgata atgatgaaga aaaagaaaaa gaagaagaag cattccccta 3480 agaacttgct gcttaatttt gtcactattg aagaaactaa ggcagatgat gttgacagtg 3540 atggaaacag agtcacacta gaccttccta ttgatctaga agagcaaaca atgggaaagt 3600 acaattgggt aactacacct actactttca agcccgacag ccctgatttg gcccgacact 3660 acaaatctgc ctctccacag cctgccttcc aaattcagcc tgaaactccc ctgaattcga 3720 agcaccacat catccaagaa ctgcctctcg ataacacctt tgtggcctgt gactctatct 3780 ccaagtgttc ctcaagcagt tcagatccct acagcgtttc tgactgtggc tatccagtga 3840 cgaccttcga ggtacctgtg tccgtacaca ccagaccgcc aatgaaggag gttgtgcgat 3900 cttgcacccc catgaaagag tctacaacta tggagatctg gattcatccc caaccacagc 3960 ggaaatctga agggaaagtg gcaggaaagt cccagcggcg tgtcacattt cacctgccag 4020 aaggctctca ggaaagcagc agtgatggtg gactgggaga ccatgatgca ggcagcctta 4080 ccagcacatc tcatggcctg ccccttggct atcctcagga ggagtacttt gatcgtgcta 4140 cacccagcaa tcgcactgaa ggggatggca actccgatcc tgaatctact ttcatacctg 4200 gactaaagaa agctgcagaa ataactgttc aaccaactgt ggaagaggcc tctgacaact 4260 gcactcaaga atgtctcatc tatggccatt ctgatgcctg ctggatgccg gcatctctgg 4320 atcattccag ctcttcgcaa gcacaggcct ctgctctatg ccacagccca ccactgtcac 4380 aggcctctac tcagcaccac agcccacgag tgacacagac cattgctctc tgccacagcc 4440 ctccagtgac acagaccatc gcattgtgcc acagcccacc accgatacag gtgtctgctc 4500 tccaccacag tcctcctcta gtgcaggcta ctgcacttca ccacagccca ccatcagcac 4560 aggcctcagc cctctgctac agccctcctt tagcacaggc tgctgcaatc agccacagct 4620 ctcctctgcc acaggttatt gccctccatc gtagtcaggc ccaatcatca gtcagtttgc 4680 agcaaggttg ggtgcaaggt gctgatgggc tatgctctgt tgatcaggga gtgcaaggta 4740 gtgcaacatc tcagttttac accatgtctg aaagacttca tcccagtgat gattcaatta 4800 aagtcattcc tttgacaacc ttcactccac gccaacaggc cagaccgtcc agaggtgatt 4860 cccccattat ggaagaacat cccttgtaaa gctaaaatag ttacttcaaa ttttcagaaa 4920 agatgtatat agtcaaaatt taagatacaa ttccaatgag tattctgatt atcagatttg 4980 taaataacta tgtaaataga aacagatacc agaataaatc tacagctaga cccttagtca 5040 atagttaacc aaaaaattgc aatttgttta attcagaatg tgtatttaaa aagaaaagga 5100 atttaacaat ttgcatcccc ttgtacagta aggcttatca tgacagagcg cactatttct 5160 gatgtacagt attttttgtt gtttttatca tcatgtgcaa tattactgat ttgtttccat 5220 gctgattgtg tggaaccagt atgtagcaaa tggaaagcct agaaatatct tattttctaa 5280 gtttaccttt agtttaccta aacttttgtt cagataacgt taaaaggtat acgtactcta 5340 gccttttttt gggctttctt tttgattttt gtttgttgtt ttcagttttt ttgttgttgt 5400 tagtgagtct cccttcaaaa tacgcagtag gtagtgtaaa tactgcttgt ttgtgtctct 5460 ctgctgtcat gttttctacc ttattccaat actatattgt tgataaaatt tgtatataca 5520 ttttcaataa agaatatgta taaactgtac agatctagat ctacaaccta tttctctact 5580 ctttagtaga gttcgagaca cagaagtgca ataactgccc taattaagca actatttgtt 5640 aaaaagggcc tctttttact ttaatagttt agtgtaaagt acatcagaaa taaagctgta 5700 tctgccattt taagcctgta gtccattatt acttgggtct ttacttctgg gaatttgtat 5760 gtaacagcct agaaaattaa aaggaggtgg atgcatccaa agcacgagtc acttaaaata 5820 tcgacggtaa actactattt tgtagagaaa ctcaggaaga tttaaatgtt gatttgacag 5880 ctcaataggc tgttaccaaa gggtgttcag taaaaataac aaatacatgt aactgtagat 5940 aaaaccatat actaaatcta taagactaag ggatttttgt tattctagct caacttactg 6000 aagaaaacca ctaataacaa caagaatatc aggaaggaac ttttcaagaa atgtaattat 6060 aaatctacat caaacagaat tttaaggaaa aatgcagagg gagaaataag gcacatgact 6120 gcttcttgca gtcaacaaga aataccaata acacacacag aacaaaaacc atcaaaatct 6180 catatatgaa ataaaatata ttcttctaag caaagaaaca gtactattca tagaaaacat 6240 tagttttctt ctgttgtctg ttatttcctt cttgtatcct cttaactggc cattatcttg 6300 tatgtgcaca ttttataaat gtacagaaac atcaccaact taattttctt ccatagcaaa 6360 actgagaaaa taccttgttt cagtataaca ctaaaccaag agacaattga tgtttaatgg 6420 gggcggttgg ggtggggggg ggagtcaata tctcctattg attaacttag acatagattt 6480 tgtaatgtat aacttgatat ttaatttatg attaaactgt gtgtaaattt tgtaacataa 6540 actgtggtaa ttgcataatt tcattggtga ggatttccac tgaatattga gaaagtttct 6600 250 tttcatgtgc ccagcaggtt aagtagcgtt ttcagaatat acattattcc catccattgt 6660 aaagttcctt aagtcatatt tgactgggcg tgcagaataa cttcttaact tttaactatc 6720 agagtttgat taataaaatt aattaatgtt ttttctcctt cgtgttgtta atgttccaag 6780 ggatttggag catactggtt ttccaggtgc atgtgaatcc cgaaggactg atgatatttg 6840 aatgtttatt aaattattat catacaaatg tgttgatatt gtggctattg ttgatgttga 6900 aaattttaaa cttggggaag attaagaaaa gaaccaatag tgacaaaaat cagtgcttcc 6960 agtagatttt agaacattct ttgcctcaaa aaacctgcaa agatgatgtg agattttttc 7020 ttgtgtttta attattttca cattttctct ctgcaaaact ttagttttct gatgatctac 7080 acacacacac acacacacac gtgcacacac acacacattt aaatgatata aaaagaagag 7140 gttgaaagat tattaaataa cttatcaggc atctcaatgg ttactatcta tgttagtgaa 7200 aatcaaatag gactcaaagt tggatatttg ggatttttct tctgacagta taatttattg 7260 agttactagg gaggttctta aatcctcata tctggaaact tgtgacgttt tgacaccttt 7320 cctatagatg atataggaat gaaccaatac gcttttatta ccctttctaa ctctgatttt 7380 ataatcagac ttagattgtg tttagaatat taaatgactg ggcaccctct tcttggtttt 7440 taccagagag gctttgaatg gaagcaggct gagagtagcc aaagaggcaa ggggtattag 7500 cccagttatt ctcccctatg ccttccttct ctttctaagc gtccactagg tctggccttg 7560 gaaacctgtt acttctaggg cttcagatct gatgatatct ttttcatcac attacaagtt 7620 atttctctga ctgaatagac agtggtatag gttgacacag cacacaagtg gctattgtga 7680 tgtatgatgt atgtagtcct acaactgcaa aacgtcttac tgaaccaaca atcaaaaaat 7740 ggttctgttt taaaaaggat tttgtttgat ttgaaattaa aacttcaagc tgaatgactt 7800 atatgagaat aatacgttca atcaaagtag ttattctatt ttgtgtccat attccattag 7860 attgtgatta ttaattttct agctatggta ttactatatc acacttgtga gtatgtattc 7920 aaatactaag tatcttatat gctacgtgca tacacattct tttcttaaac tttacctgtg 7980 ttttaactaa tattgtgtca gtgtattaaa aattagcttt tacatatgat atctacaatg 8040 taataaattt agagagtaat tttgtgtatt cttatttact taacatttta cttttaatta 8100 tgtaaatttg gttagaaaat aataataaat ggttagtgct attgtgtaat ggtagcagtt 8160 acaaagagcc tctgccttcc caaactaata tttatcacac atggtcatta aatgggaaaa 8220 aaatagacta aacaaatcac aaattgttca gttcttaaaa tgtaattatg tcacacacac 8280 aaaaaatcct tttcaatcct gagaaaatta aaggcgtttt actcacatgg ctatttcaac 8340 attagttttt tttgtttgtt tctttttcat ggtattactg aaggtgtgta tactccctaa 8400 tacacattta tgaaaatcta cttgtttagg cttttattta tactcttctg atttatattt 8460 tttattataa ttattatttc ttatctttct tcttttatat tttttggaaa ccaaatttat 8520 agttagttta ggtaaacttt ttattatgac cattagaaac tattttgaat gcttccaact 8580 ggctcaattg gccgggaaaa catgggagca agagaagctg aaatatattt ctgcaagaac 8640 ctttctatat tatgtgccaa ttaccacacc agatcaattt tatgcagagg ccttaaaata 8700 ttctttcaca gtagctttct tacactaacc gtcatgtgct tttagtaaat atgattttta 8760 aaagcagttc aagttgacaa cagcagaaac agtaacaaaa aaatctgctc agaaaaatgt 8820 atgtgcacaa ataaaaaaaa ttaatggcaa ttgtttagtg attgtaagtg atacttttta 8880 aagagtaaac tgtgtgaaat ttatactatc cctgcttaaa atattaagat ttttatgaaa 8940 tatgtattta tgtttgtatt gtgggaagat tcctcctctg tgatatcata cagcatctga 9000 aagtgaacag tatcccaaag cagttccaac catgctttgg aagtaagaag gttgactatt 9060 gtatggccaa ggatggcagt atgtaatcca gaagcaaact tgtattaatt gttctatttc 9120 aggttctgta ttgcatgttt tcttattaat atatattaat aaaagttatg agaaat 9176 Table Lil1(b). Nucleotide sequence alignment of 109P1D4 v.1 (SEQ ID NO: 244) and 109P1D4 v.3 (SEQ ID NO: 245) Score =7456 bIts (3878), Expect = 0.01dentitles = 387878 (100%) Strand = Plus I Plus V.1 1 ctggtggtccagtacctccaaagatatggaatacactcctgaaatatcctgaaaactttt 60 I|||||1I |1 I II I | I il li i i li | |III I I II111llI I|I I Ill | V.3 1 ctggtggtccagtacctccaaagatatggaatacactcctgaaatatcctgaaaactttt 60 V.1 61 ttttttcagaatcctttaataagcagttatgtcaatctgaaagttgcttacttgtacttt 120 V.3 61 ttttttcagaatcctttaataagcagttatgtcaatctgaaagttgcttacttgtacttt 120 V.1 121 atattaatagctattcttgtttttcttatccaaagaaaaatcctctaatccccttttcac 180 lii 11I 111|| lii l i 11 111 111 I I11I11I1II11 | 1 |1I||1 1 Il111I| V.3 121 atattaatagctattcttgtttttcttatccaaagaaaaatcctctaatccccttttcac 180 V.1 181 atgatagttgttaccatgtttaggcattagtcacatcaacccctctcctctcccaaactt 240 1I IIi IllII11 II I I iii I1111111 111111 Ill II Iil 111 I 11 Ii1il 251 v.3 181 atgatagttgttaccatgtttaggcattagtcacatcaacccctctcctctcccaaactt 240 V.1 241 ctcttcttcaaatcaaactttattagtccctcctttataatgattccttgcctcgtttta 300 I li 11 I l 111i 11 II1 l11 lillllll1 lli111I1ll il Il I I|i l|| l lI Ilil V.3 241 ctcttcttcaaatcaaactttattagtccctcctttataatgattccttgcctcgtttta 300 V.1 301 tccagatcaattttttttcactttgatgcccagagctgaagaaatggactactgtataaa 360 |I I II 1 11 ||Illlilllil ll lill| Il li il Ili11 Ill1 ll1 ll11 il V.3 301 tccagatcaattttttttcactttgatgcccagagctgaagaaatggactactgtataaa 360 V.1 361 ttattcattgccaagagaataattgcattttaaacccatattataacaaagaataatgat 420 11II I l I II I l1 1111 11 i i i 1 l I 111lili I illlII V.3 361 ttattcattgccaagagaataattgcattttaaacccatattataacaaagaataatgat 420 V.1 421 tatattttgtgatttgtaacaaataccctttattttcccttaactattgaattaaatatt 480 V.3 421 tatattttgtgatttgtaacaaataccctttattttcccttaactattgaattaaatatt 480 V.1 481 ttaattatttgtattctctttaactatcttggtatattaaagtattatcttttatatatt 540 1illliillllllllllllllIIIlillil11111 illIlllIllllllli1 V.3 481 ttaattatttgtattctctttaactatcttggtatattaaagtattatcttttatatatt 540 V.1 541 tatcaatggtggacacttttataggtactctgtgtcatttttgatactgtaggtatctta 600 I||11 II I l11I li ll i ll l l l lIlll 11 1 1 11 1 1 li lilil lil111 I llllil V.3 541 tatcaatggtggacacttttataggtactctgtgtcatttttgatactgtaggtatctta 600 V.1 601 tttcatttatctttattcttaatgtacgaattcataatatttgattcagaacaaatttat 660 lil1llilllllllI1111111111111 1|1111111111lllllllllll1liI V.3 601 tttcatttatctttattcttaatgtacgaattcataatatttgattcagaacaaatttat 660 V.1 661 cactaattaacagagtgtcaattatgctaacatctcatttactgattttaatttaaaaca 720 l Ill |li l liI ll1 I1 li ll111 1 ll lill I 1 ll I 11 1 | I11 I llilillil Ill V.3 661 cactaattaacagagtgtcaattatgctaacatctcatttactgattttaatttaaaaca 720 V.1 721 gtttttgttaacatgcatgtttagggttggcttcttaataatttcttcttcctcttctct 780 V.3 : 721 gtttttgttaacatgcatgtttagggttggcttcttaataatttcttcttcctcttctct 780 V.1 : 781 ctctcctcttcttttggtcagtgttgtgcgggttaatacaacaaactgtaacaagtgtac 840 ||I III Il il l | II II|I I I II iI| i111111 lII 1I l11|1111111li11 V.3 : 781 ctctcctcttcttttggtcagtgttgtgcgggttaatacaacaaactgtaacaagtgtac 840 V.1 : 841 ctggtatggacttgttgtccgggacgtacattttcgcggtcctgctagcatgcgtggtgt 900 1I|II I1I1I |IlllllI1111111 lI li11||1111||1|1 V.3 : 841 ctggtatggacttgttgtccgggacgtacattttcgcggtcctgctagcatgcgtggtgt 900 V.1 : 901 tccactctggcgcccaggagaaaaactacaccatccgagaagaaatgccagaaaacgtcc 960 V.3 : 901 tccactctggcgcccaggagaaaaactacaccatccgagaagaaatgccagaaaacgtcc 960 V.1 : 961 tgataggcgacttgttgaaagaccttaacttgtcgctgattccaaacaagtccttgacaa 1020 lil lll llilil l1 ll l 11 l ll llll li lllll l11 ll lll ll lli V.3 : 961 tgataggcgacttgttgaaagaccttaacttgtcgctgattccaaacaagtccttgacaa 1020 V.1 : 1021 ctgctatgcagttcaagctagtgtacaagaccggagatgtgccactgattcgaattgaag 1080 252 11ilI I11 I II ll Ii11ii 11 1 l i i 1 11 1 I 1 II li I1 ||1 i I I l l V.3 1021 ctgctatgcagttcaagctagtgtacaagaccggagatgtgccactgattcgaattgaag 1080 V.1 1081 aggatactggtgagatcttcactactggcgctcgcattgatcgtgagaaattatgtgctg 1140 l il11lIlI1 I ll111l iIi i111111111||||1l1lliIl I1ll11||||I I V.3 1081 aggatactggtgagatcttcactactggcgctcgcattgatcgtgagaaattatgtgctg 1140 V.1 1141 gtatcccaagggatgagcattgcttttatgaagtggaggttgccattttgccggatgaaa 1200 11111! I||I|I |1i 1 I11111||l l lll i ili 1 ll l l ll 1illl 11l IlII V.3 1141 gtatcccaagggatgagcattgcttttatgaagtggaggttgccattttgccggatgaaa 1200 V.1 1201 tatttagactggttaagatacgttttctgatagaagatataaatgataatgcaccattgt 1260 V.3 : 1201 tatttagactggttaagatacgttttctgatagaagatataaatgataatgcaccattgt 1260 V.1 : 1261 tcccagcaacagttatcaacatatcaattccagagaactcggctataaactctaaatata 1320 V.3 : 1261 tcccagcaacagttatcaacatatcaattccagagaactcggctataaactctaaatata 1320 V.1 : 1321 ctctcccagcggctgttgatcctgacgtaggaataaacggagttcaaaactacgaactaa 1380 ||1lli1l111! I Il lII1I ll 1lillIllllllli lili 1111ll111111||11 V.3 : 1321 ctctcccagcggctgttgatcctgacgtaggaataaacggagttcaaaactacgaactaa 1380 V.1 : 1381 ttaagagtcaaaacatttttggcctcgatgtcattgaaacaccagaaggagacaagatgc 1440 lilllillllll lilllllllll111ll1lll1llllll1111111111111111111 I V.3 : 1381 ttaagagtcaaaacatttttggcctcgatgtcattgaaacaccagaaggagacaagatgc 1440 V.1 : 1441 cacaactgattgttcaaaaggagttagatagggaagagaaggatacctacgtgatgaaag 1500 I il iI l 1 111 l l1 Il li lll11llllli1 ll Iii I I||11 11 illll V.3 : 1441 cacaactgattgttcaaaaggagttagatagggaagagaaggatacctacgtgatgaaag 1500 V.1 : 1501 taaaggttgaagatggtggctttcctcaaagatccagtactgctattttgcaagtgagtg 1560 V.3 1501 taaaggttgaagatggtggctttcctcaaagatccagtactgctattttgcaagtgagtg 1560 V.1 1561 ttactgatacaaatgacaaccacccagtctttaaggagacagagattgaagtcagtatac 1620 V.3 1561 ttactgatacaaatgacaaccacccagtctttaaggagacagagattgaagtcagtatac 1620 V.1 1621 cagaaaatgctcctgtaggcacttcagtgacacagctccatgccacagatgctgacatag 1680 I ll l I I|111I Il lII II l II111I lI llil 1111lil1I1 II11 i11 V.3 1621 cagaaaatgctcctgtaggcacttcagtgacacagctccatgccacagatgctgacatag 1680 V.1 1681 gtgaaaatgccaagatccacttctctttcagcaatctagtctccaacattgccaggagat 1740 |11II111111I1II11I111|11111111111|1||11IIIIl!I!lIIIlilIll V.3 1681 gtgaaaatgccaagatccacttctctttcagcaatctagtctccaacattgcaggagat 1740 V.1 : 1741 tatttcacctcaatgccaccactggacttatcacaatcaaagaaccactggatagggaag 1800 lillilllll1 lil ll ll l l ll ll ll ll l l ll ll11 11 1 1 1 li i i V.3 : 1741 tatttcacctcaatgccaccactggacttatcacaatcaaagaaccactggatagggaag 1800 V.1 : 1801 aaacaccaaaccacaagttactggttttggcaagtgatggtggattgatgccagcaagag 1860 lill3 l:ll ll llll llli i 1111 lll lllllll ll1 11 11111 111 V.3 :1801 aaacaccaaaccacaagttactggttttggcaagtgatggtggattgatgccagcaagag 1860 253 V.1 1861 caatggtgctggtaaatgttacagatgtcaatgataatgtcccatccattgacataagat 1920 |||||11|| | 1111 ||111111 I I l l| 1 l111|| 1I l lil lii | |i lill V.3 1861 caatggtgctggtaaatgttacagatgtcaatgataatgtcccatccattgacataagat 1920 V.1 1921 acatcgtcaatcctgtcaatgacacagttgttctttcagaaaatattccactcaacacca 1980 lilili ll llllill llllllll11 11 i lilll llI lllilll ll11111 11 i V.3 : 1921 acatcgtcaatcctgtcaatgacacagttgttctttcagaaaatattccactcaacacca 1980 V.1 : 1981 aaattgctctcataactgtgacggataaggatgcggaccataatggcagggtgacatgct 2040 111l 1ll 111lll iil ll lll ll ll I illlll 11llllllll lililll1111 |111I V.3 : 1981 aaattgctctcataactgtgacggataaggatgcggaccataatggcagggtgacatgct 2040 V.1 : 2041 tcacagatcatgaaatccctttcagattaaggccagtattcagtaatcagttcctcctgg 2100 l ii lilii I llil Ill I Il I I11I lil Ilii I11|||lill I||li1 I I I1I||1I| V.3 : 2041 tcacagatcatgaaatccctttcagattaaggccagtattcagtaatcagttcctcctgg 2100 V.1 : 2101 agactgcagcatatcttgactatgagtccacaaaagaatatgccattaaattactggctg 2160 V.3 : 2101 agactgcagcatatcttgactatgagtccacaaaagaatatgccattaaattactggctg 2160 V.1 : 2161 cagatgctggcaaacctcctttgaatcagtcagcaatgctcttcatcaaagtgaaagatg 2220 i I|||||||||||lill I||||||||||| 1| i 1111i l||||il lii 11IIl 1|I V.3 : 2161 cagatgctggcaaacctcctttgaatcagtcagcaatgctcttcatcaaagtgaaagatg 2220 V.1 : 2221 aaaatgacaatgctccagttttcacccagtctttcgtaactgtttctattcctgagaata 2280 11ill1l1l1l11l1111l1liIIlIllllllllllillllllll II~~I Illl V.3 : 2221 aaaatgacaatgctccagttttcacccagtctttcgtaactgtttctattcctgagaata 2280 V.1 : 2281 actctcctggcatccagttgacgaaagtaagtgcaatggatgcagacagtgggcctaatg 2340 I llllllll lilll1l111111|11111111||11111111111|111 Il Illlli V.3 2281 actctcctggcatccagttgacgaaagtaagtgcaatggatgcagacagtgggcctaatg 2340 V.1 2341 ctaagatcaattacctgctaggccctgatgctccacctgaattcagcctggattgtcgta 2400 V.3 2341 ctaagatcaattacctgctaggccctgatgctccacctgaattcagcctggattgtcgta 2400 V.1 2401 caggcatgctgactgtagtgaagaaactagatagagaaaaagaggataaatatttattca 2460 1 I1i il llI l 11iIl|| 111|| ilI | | l111 l 1111|il11ilill| V.3 2401 caggcatgctgactgtagtgaagaaactagatagagaaaaagaggataaatatttattca 2460 V.1 : 2461 caattctggcaaaagataacggggtaccacccttaaccagcaatgtcacagtctttgtaa 2520 lill llll llll lll lllllllllllllllllll lll ll l lli Illlil l V.3 : 2461 caattctggcaaaagataacggggtaccacccttaaccagcaatgtcacagtctttgtaa 2520 V.1 : 2521 gcattattgatcagaatgacaatagcccagttttcactcacaatgaatacaacttctatg 2580 1ill1l11 lllI lI lll111 11ll11lll llll lllllll 1 1 lllllll lllllII V.3 : 2521 gcattattgatcagaatgacaatagcccagttttcactcacaatgaatacaacttctatg 2580 V.1 : 2581 tcccagaaaaccttccaaggcatggtacagtaggactaatcactgtaactgatcctgatt 2640 lIllllllllllllIIliiilllIllIIIllllIII111III|||I111111|11lillllil V.3 : 2581 tcccagaaaaccttccaaggcatggtacagtaggactaatcactgtaactgatcctgatt 2640 V.1 : 2641 atggagacaattctgcagttacgctctccattttagatgagaatgatgacttcaccattg 2700 V.3 : 2641 atggagacaattctgcagttacgctctccattttagatgagaatgatgacttcaccattg 2700 254 V.1 2701 attcacaaactggtgtcatccgaccaaatatttcatttgatagagaaaaacaagaatctt 2760 llil II lillilIll lI I 1111111111 1 il l l li lilil Ii 11 lli11I 111 V.3 2701 attcacaaactggtgtcatccgaccaaatatttcatttgatagagaaaaacaagaatctt 2760 V.1 2761 acactttctatgtaaaggctgaggatggtggtagagtatcacgttcttcaagtgccaaag 2820 li11l|1lillllli11|1I lllil 11 l|ill 111|11111111111 ill11111 V.3 2761 acactttctatgtaaaggctgaggatggtggtagagtatcacgttcttcaagtgccaaag 2820 V.1 2821 taaccataaatgtggttgatgtcaatgacaacaaaccagttttcattgtccctccttcca 2880 lii I l l lli || ||lI|lI liIIll I11 1 1 1 11 1 1 1 1 111 |||1 |1111 ||I lillli V.3 2821 taaccataaatgtggttgatgtcaatgacaacaaaccagttttcattgtccctccttcca 2880 V.1 2881 actgttcttatgaattggttctaccgtccactaatccaggcacagtggtctttcaggtaa 2940 I i i 1 I I 1 I11I1||| 1 l I| |1 i i 11 l i i II IlI i il I1 I||11 I I V.3 2881 actgttcttatgaattggttctaccgtccactaatccaggcacagtggtctttcaggtaa 2940 V.1 2941 ttgctgttgacaatgacactggcatgaatgcagaggttcgttacagcattgtaggaggaa 3000 llllll lllll llll lllllllll 11 11lllll l ll i ll 11 1Illll lllll I V.3 2941 ttgctgttgacaatgacactggcatgaatgcagaggttcgttacagcattgtaggaggaa 3000 V.1 3001 acacaagagatctgtttgcaatcgaccaagaaacaggcaacataacattgatggagaaat 3060 ||Il I I l i 11 1111 il Il ill Ill I 11l ill 1 I I I 11 l 11il i11 I I V.3 3001 acacaagagatctgtttgcaatcgaccaagaaacaggcaacataacattgatggagaaat 3060 V.1 3061 gtgatgttacagaccttggtttacacagagtgttggtcaaagctaatgacttaggaagc 3120 li 11 1 li I i l1ii I111111111 1 I I|1 |Il|| l | | 111I 111I li i V.3 3061 gtgatgttacagaccttggtttacacagagtgttggtcaaagctaatgacttaggacagc 3120 V.1 3121 ctgattctctcttcagtgttgtaattgtcaatctgttcgtgaatgagtcggtgaccaatg 3180 111I11I11 II I li I I1111111111 1111I 111I1I II11 I1 i 1 I 111I I ii I 1||1 I I II V.3 3121 ctgattctctcttcagtgttgtaattgtcaatctgttcgtgaatgagtcggtgaccaatg 3180 V.1 : 3181 ctacactgattaatgaactggtgcgcaaaagcactgaagcaccagtgaccccaaatactg 3240 I 1IIlllllI ll|1l Ill illlIl lll l11l lII i III 11 l l Illi V.3 : 3181 ctacactgattaatgaactggtgcgcaaaagcactgaagcaccagtgaccccaaatactg 3240 V.1 : 3241 agatagctgatgtatcctcaccaactagtgactatgtcaagatcctggttgcagctgttg 3300 Sli 111111111i|1111Illl1I111i 111i I||||Ii l IIii 1111Ili V.3 : 3241 agatagctgatgtatcctcaccaactagtgactatgtcaagatcctggttgcagctgttg 3300 V.1 : 3301 ctggcaccataactgtcgttgtagttattttcatcactgctgtagtaagatgtcgccagg 3360 I li I lil I111ll| 111il 1111I111li 111lil l Ili 1I 111ll 1l 111llillilli V.3 : 3301 ctggcaccataactgtcgttgtagttattttcatcactgctgtagtaagatgtcgccagg 3360 V.1 : 3361 caccacaccttaaggctgctcagaaaaacaagcagaattctgaatgggctaccccaaacc 3420 V.3 : 3361 caccacaccttaaggctgctcagaaaaacaagcagaattctgaatgggctaccccaaacc 3420 V.1 : 3421 cagaaaacaggcagatgataatgatgaagaaaaagaaaaagaagaagaagcattccccta 3480 II 1 li lI i |l i 1111 lii l II Ill I I ll1 lilllll 11ll 1I|1|1|| V.3 : 3421 cagaaaacaggcagatgataatgatgaagaaaaagaaaaagaagaagaagcattccccta 3480 V.1 : 3481 agaacttgctgcttaattttgtcactattgaagaaactaaggcagatgatgttgacagtg 3540 V. : 34l lll i11 il II lIl lilil Illii11111111111311 l 1101111 1 V.3 : 3481 agaacttgctgcttaattttgtcactattgaagaaactaaggcagatgatgttgacagtg 3540 255 V.1 : 3541 atggaaacagagtcacactagaccttcctattgatctagaagagcaaacaatgggaaagt 3600 111111l I 1I1lli 1I|| ji ll illl l li lll il lIlI 11 111 I i l i Illi11 V.3 : 3541 atggaaacagagtcacactagaccttcctattgatctagaagagcaaacaatgggaaagt 3600 V.1 : 3601 acaattgggtaactacacctactactttcaagcccgacagccctgatttggcccgacact 3660 ti I ||I I ||li l I I1 lll il I I llil11 11 1 11 11l 11ll 1||11 1 l IlII V.3 : 3601 acaattgggtaactacacctactactttcaagcccgacagccctgatttggcccgacact 3660 V.1 : 3661 acaaatctgcctctccacagcctgccttccaaattcagcctgaaactcccctgaattcga 3720 I l i II l II I I 11| 11 ||| 1I1 1I I Il I I llilll11 i I l111 11 V.3 : 3661 acaaatctgcctctccacagcctgccttccaaattcagcctgaaactcccctgaattcga 3720 V.1 : 3721 agcaccacatcatccaagaactgcctctcgataacacctttgtggcctgtgactctatct 3780 lilII 1 III I II Iiill lllll ilil11i1ll ||lil 111l Ill111|11 1 V.3 : 3721 agcaccacatcatccaagaactgcctctcgataacacctttgtggcctgtgactctatct 3780 V.1 : 3781 ccaagtgttcctcaagcagttcagatccctacagcgtttctgactgtggctatccagtga 3840 I lilII 1I l I I lil ili lillllli1111 I lIlli||lill1111111 l1 V.3 : 3781 ccaagtgttcctcaagcagttcagatccctacagcgtttctgactgtggctatccagtga 3840 V.1 : 3841 cgaccttcgaggtacctgtgtccgtacacaccagaccg 3878 V.3 : 3841 cgaccttcgaggtacctgtgtccgtacacaccagaccg 3878 Table LIV(b). Peptide sequences of protein coded by 109P1D4 v.3 (SEQ ID NO: 246) MDLLSGTYIF AVLLACVVFH SGAQEKNYTI REEMPENVLI GDLLKDLNLS LIPNKSLTTA 60 MQFKLVYKTG DVPLIRIEED TGEIFTTGAR IDREKLCAGI PRDEHCFYEV EVAILPDEIF 120 RLVKIRFLIE DINDNAPLFP ATVINISIPE NSAINSKYTL PAAVDPDVGI NGVQNYELIK 180 SQNIFGLDVI ETPEGDKMPQ LIVQKELDRE EKDTYVMKVK VEDGGFPQRS STAILQVSVT 240 DTNDNHPVFK ETEIEVSIPE NAPVGTSVTQ LHATDADIGE NAKIHFSFSN LVSNIARRLF 300 HLNATTGLIT IKEPLDREET PNHKLLVLAS DGGLMPARAM VLVNVTDVND NVPSIDIRYI 360 VNPVNDTVVL SENIPLNTKI ALITVTDKDA DHNGRVTCFT DHEIPFRLRP VFSNQFLLET 420 AAYLDYESTK EYAIKLLAAD AGKPPLNQSA MLFIKVKDEN DNAPVFTQSF VTVSIPENNS 480 PGIQLTKVSA MDADSGPNAK INYLLGPDAP PEFSLDCRTG MLTVVKKLDR EKEDKYLFTI 540 LAKDNGVPPL TSNVTVFVSI IDQNDNSPVF THNEYNFYVP ENLPRHGTVG LITVTDPDYG 600 DNSAVTLSIL DENDDFTIDS QTGVIRPNIS FDREKQESYT FYVKAEDGGR VSRSSSAKVT 660 INVVDVNDNK PVFIVPPSNC SYELVLPSTN PGTVVFQVIA VDNDTGMNAE VRYSIVGGNT 720 RDLFAIDQET GNITLMEKCD VTDLGLHRVL VKANDLGQPD SLFSVVIVNL FVNESVTNAT 780 LINELVRKST EAPVTPNTEI ADVSSPTSDY VKILVAAVAG TITVVVVIFI TAVVRCRQAP 840 HLKAAQKNKQ NSEWATPNPE NRQMIMMKKK KKKKKHSPKN LLLNFVTIEE TKADDVDSDG 900 NRVTLDLPID LEEQTMGKYN WVTTPTTFKP DSPDLARHYK SASPQPAFQI QPETPLNSKH 960 HIIQELPLDN TFVACDSISK CSSSSSDPYS VSDCGYPVTT FEVPVSVHTR PPMKEVVRSC 1020 TPMKESTTME IWIHPQPQRK SEGKVAGKSQ RRVTFHLPEG SQESSSDGGL GDHDAGSLTS 1080 TSHGLPLGYP QEEYFDRATP SNRTEGDGNS DPESTFIPGL KKAAEITVQP TVEEASDNCT 1140 QECLIYGHSD ACWMPASLDH SSSSQAQASA LCHSPPLSQA STQHHSPRVT QTIALCHSPP 1200 VTQTIALCHS PPPIQVSALH HSPPLVQATA LHHSPPSAQA SALCYSPPLA QAAAISHSSP 1260 LPQVIALHRS QAQSSVSLQQ GWVQGADGLC SVDQGVQGSA TSQFYTMSER LHPSDDSIKV 1320 IPLTTFTPRQ QARPSRGDSP IMEEHPL 1347 Table LV(b). Amino acid sequence alignment of 109PID4 v.1 (SEQ ID NO: 247) and 109PID4 v.3 (SEQ ID NO: 248) Score 2005 bits (5195), Expect = 0.0ldentities = 1011/1011 (100%), Positives = 101111011 (100%) V.1 1 MDLLSGTYIFAVLLACVVFHSGAQEKNYTIREEMPENVLIGDLLKDLNLSLIPNKSLTTA 60 MDLLSGTYIFAVLLACVVFHSGAQEKNYTIREEMPENVLIGDLLDLNLSLIPNKSLTTA V.3 1 MDLLSGTYIFAVLLACVVFHSGAQEKNYTIREEMPENVLIGDLLKDLNLSLIPNKSLTTA 60 V.1 61 MQFKLVYKTGDVPLIRIEEDTGEIETTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIF 120 256 MQFKLVYKTGDVPLIRIEEDTGEIFTTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIF V.3 : 61 MQFKLVYKTGDVPLIRIEEDTGEIFTTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIF 120 V.1 : 121 RLVKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIK 180 RLVKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIK V.3 : 121 RLVKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIK 180 V.1 : 181 SQNIFGLDVIETPEGDIAPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVT 240 SQNIFGLDVIETPEGDKMPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVT V.3 : 181 SQNIFGLDVIETPEGDKMPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILOVSVT 240 V.1 : 241 DTNDNHPVFKETEIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSFSNLVSNIARRLF 300 DTNDNHPVFKETEIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSFSNLVSNIARRLF V.3 : 241 DTNDNHPVFKETEIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSFSNLVSNIARRLF 300 V.1 : 301 HLNATTGLITIKEPLDREETPNALLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYI 360 HLNATTGLITIKEPLDREETPNHKLLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYI V.3 : 301 HLNATTGLITIKEPLDREETPNHKLLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYI 360 V.1 : 361 VNPVNDTVVLSENIPLNTKIALITVTDKDADHNGRVTCrDHEIPFRLRPVFSNQLLET 420 VNPVNDTVVLSENIPLNTKIALITVTDKDADHNGRVTCFTDHEIPFRLRPVFSNQFLLET V.3 : 361 VNPVNDTVVLSENIPLNTKIALITVTDKDADHNGRVTCFTDHEIPFRLRPVFSNOFLLET 420 V.1 : 421 AAYLDYESTKEYAIKLLAADAGKPPLNQSAHLFIKVKDENDNAPVFRQSFVTVSIPENNS 480 AAYLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDENDNAPVETQSFVTVSIPENNS V.3 : 421 AAYLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDENDNAPVFrQSFVTVSIPENNS 480 V.1 481 PGIQLTVSADADSGPNAKINYLLGPDAPPEFSLDCRTGMLTVVKKLDREKEDKYLNI 540 PGIQLTKVSAMDADSGPNAKINYLLGPDAPPEFSLDCRTGMLTVVKKLDREKEDKYLFTI V.3 481 PGIQLTKVSAMDADSGPNAKINYLLGPDAPPEFSLDCRTGMLTVVKKLDREKEDKYLFTI 540 V.1 541 LAKDNGVPPLTSNVTVVSIIDQNDNSPVFTHNEYNFYVPENLPRHGTVGLITVTDPDYG 600 LAKDNGVPPLTSNVTVFVSIIDQNDNSPVFTHNEYNFYVPENLPRHGTVGLITVTDPDYG V.3 541 LAKDNGVPPLTSNVTVFVSIIDQNDNSPVFTHNEYNFYVPENLPRHGTVGLITVTDPDYG 600 V.1 601 DNSAVTLSILDENDDFTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAVT 660 DNSAVTLSILDENDDFTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVT V.3 : 601 DNSAVTLSILDENDDFTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVT 660 V.1 : 661 INVVDVNDNKPVFIVPPSNCSYELVLPSTNPGTVVFQVIAVDNDTDNAVRYSIVGGNT 720 INVVDVNDNKPVFIVPPSNCSYELVLPSTNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNT V.3 : 661 INVVDVNDNKPVFIVPPSNCSYELVLPSTNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNT 720 V.1 : 721 RDLFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPDSLFSVVIVNLFVNESVTNAT 780 RDLFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPDSLFSVVIVNLFVNESVTNAT V.3 : 721 RDLFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPDSLFSVVIVNLFVNESVTNAT 780 V.1 : 781 LINELVRKSTEAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVWIFITAVVRCRQAP 840 LINELVRKSTEAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVRCRQAP V.3 : 781 LINELVRKSTEAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVRCRQAP 840 V.1 : 841 HLKAAQKNKQNSEWATPNPENRQMIMMKKKKKKKKHSPKNLLLNFVTIEETKADDVDSDG 900 Table Ul(c). Nucleotide sequence of transcript variant 109PI D4 v.4 (SEQ ID NO: 249) ctggtggtcc agtacctcca aagatatgga atacactcct gaaatatcct gaaaactttt 60 ttttttcaga atcctttaat aagcagttat gtcaatctga aagttgctta cttgtacttt 120 atattaatag ctattcttgt ttttcttatc caaagaaaaa tcctctaatc cccttttcac 180 atgatagttg ttaccatgtt taggcattag tcacatcaac ccctctcctc tcccaaactt 240 ctcttcttca aatcaaactt tattagtccc tcctttataa tgattccttg cctcgtttta 300 tccagatcaa ttttttttca ctttgatgcc cagagctgaa gaaatggact actgtataaa 360 ttattcattg ccaagagaat aattgcattt taaacccata ttataacaaa gaataatgat 420 tatattttgt gatttgtaac aaataccctt tattttccct taactattga attaaatatt 480 ttaattattt gtattctctt taactatctt ggtatattaa agtattatct tttatatatt 540 tatcaatggt ggacactttt ataggtactc tgtgtcattt ttgatactgt aggtatctta 600 tttcatttat ctttattctt aatgtacgaa ttcataatat ttgattcaga acaaatttat 660 cactaattaa cagagtgtca attatgctaa catctcattt actgatttta atttaaaaca 720 gtttttgtta acatgcatgt ttagggttgg cttcttaata atttcttctt cctcttctct 780 257 ctctcctctt cttttggtca gtgttgtgcg ggttaataca acaaactgta acaagtgtac 840 ctggtatgga cttgttgtcc gggacgtaca ttttcgcggt cctgctagca tgcgtggtgt 900 tccactctgg cgcccaggag aaaaactaca ccatccgaga agaaatgcca gaaaacgtcc 960 tgataggcga cttgttgaaa gaccttaact tgtcgctgat tccaaacaag tccttgacaa 1020 ctgctatgca gttcaagcta gtgtacaaga ccggagatgt gccactgatt cgaattgaag 1080 aggatactgg tgagatcttc actactggcg ctcgcattga tcgtgagaaa ttatgtgctg 1140 gtatcccaag ggatgagcat tgcttttatg aagtggaggt tgccattttg ccggatgaaa 1200 tatttagact ggttaagata cgttttctga tagaagatat aaatgataat gcaccattgt 1260 tcccagcaac agttatcaac atatcaattc cagagaactc ggctataaac tctaaatata 1320 ctctcccagc ggctgttgat cctgacgtag gaataaacgg agttcaaaac tacgaactaa 1380 ttaagagtca aaacattttt ggcctcgatg tcattgaaac accagaagga gacaagatgc 1440 cacaactgat tgttcaaaag gagttagata gggaagagaa ggatacctac gtgatgaaag 1500 taaaggttga agatggtggc tttcctcaaa gatccagtac tgctattttg caagtgagtg 1560 ttactgatac aaatgacaac cacccagtct ttaaggagac agagattgaa gtcagtatac 1620 cagaaaatgc tcctgtaggc acttcagtga cacagctcca tgccacagat gctgacatag 1680 gtgaaaatgc caagatccac ttctctttca gcaatctagt ctccaacatt gccaggagat 1740 tatttcacct caatgccacc actggactta tcacaatcaa agaaccactg gatagggaag 1800 aaacaccaaa ccacaagtta ctggttttgg caagtgatgg tggattgatg ccagcaagag 1860 caatggtgct ggtaaatgtt acagatgtca atgataatgt cccatccatt gacataagat 1920 acatcgtcaa tcctgtcaat gacacagttg ttctttcaga aaatattcca ctcaacacca 1980 aaattgctct cataactgtg acggataagg atgcggacca taatggcagg gtgacatgct 2040 tcacagatca tgaaatccct ttcagattaa ggccagtatt cagtaatcag ttcctcctgg 2100 agactgcagc atatcttgac tatgagtcca caaaagaata tgccattaaa ttactggctg 2160 cagatgctgg caaacctcct ttgaatcagt cagcaatgct cttcatcaaa gtgaaagatg 2220 aaaatgacaa tgctccagtt ttcacccagt ctttcgtaac tgtttctatt cctgagaata 2280 actctcctgg catccagttg acgaaagtaa gtgcaatgga tgcagacagt gggcctaatg 2340 ctaagatcaa ttacctgcta ggccctgatg ctccacctga attcagcctg gattgtcgta 2400 caggcatgct gactgtagtg aagaaactag atagagaaaa agaggataaa tatttattca 2460 caattctggc aaaagataac ggggtaccac ccttaaccag caatgtcaca gtctttgtaa 2520 gcattattga tcagaatgac aatagcccag ttttcactca caatgaatac aacttctatg 2580 tcccagaaaa ccttccaagg catggtacag taggactaat cactgtaact gatcctgatt 2640 atggagacaa ttctgcagtt acgctctcca ttttagatga gaatgatgac ttcaccattg 2700 attcacaaac tggtgtcatc cgaccaaata tttcatttga tagagaaaaa caagaatctt 2760 acactttcta tgtaaaggct gaggatggtg gtagagtatc acgttcttca agtgccaaag 2820 taaccataaa tgtggttgat gtcaatgaca acaaaccagt tttcattgtc cctccttcca 2880 actgttctta tgaattggtt ctaccgtcca ctaatccagg cacagtggtc tttcaggtaa 2940 ttgctgttga caatgacact ggcatgaatg cagaggttcg ttacagcatt gtaggaggaa 3000 acacaagaga tctgtttgca atcgaccaag aaacaggcaa cataacattg atggagaaat 3060 gtgatgttac agaccttggt ttacacagag tgttggtcaa agctaatgac ttaggacagc 3120 ctgattctct cttcagtgtt gtaattgtca atctgttcgt gaatgagtcg gtgaccaatg 3180 ctacactgat taatgaactg gtgcgcaaaa gcactgaagc accagtgacc ccaaatactg 3240 agatagctga tgtatcctca ccaactagtg actatgtcaa gatcctggtt gcagctgttg 3300 ctggcaccat aactgtcgtt gtagttattt tcatcactgc tgtagtaaga tgtcgccagg 3360 caccacacct taaggctgct cagaaaaaca agcagaattc tgaatgggct accccaaacc 3420 cagaaaacag gcagatgata atgatgaaga aaaagaaaaa gaagaagaag cattccccta 3480 agaacttgct gcttaatttt gtcactattg aagaaactaa ggcagatgat gttgacagtg 3540 atggaaacag agtcacacta gaccttccta ttgatctaga agagcaaaca atgggaaagt 3600 acaattgggt aactacacct actactttca agcccgacag ccctgatttg gcccgacact 3660 acaaatctgc ctctccacag cctgccttcc aaattcagcc tgaaactccc ctgaattcga 3720 agcaccacat catccaagaa ctgcctctcg ataacacctt tgtggcctgt gactctatct 3780 ccaagtgttc ctcaagcagt tcagatccct acagcgtttc tgactgtggc tatccagtga 3840 cgaccttcga ggtacctgtg tccgtacaca ccagaccgcc aatgaaggag gttgtgcgat 3900 cttgcacccc catgaaagag tctacaacta tggagatctg gattcatccc caaccacagt 3960 cccagcggcg tgtcacattt cacctgccag aaggctctca ggaaagcagc agtgatggtg 4020 gactgggaga ccatgatgca ggcagcctta ccagcacatc tcatggcctg ccccttggct 4080 atcctcagga ggagtacttt gatcgtgcta cacccagcaa tcgcactgaa ggggatggca 4140 actccgatcc tgaatctact ttcatacctg gactaaagaa agctgcagaa ataactgttc 4200 aaccaactgt ggaagaggcc tctgacaact gcactcaaga atgtctcatc tatggccatt 4260 ctgatgcctg ctggatgccg gcatctctgg atcattccag ctcttcgcaa gcacaggcct 4320 ctgctctatg ccacagccca ccactgtcac aggcctctac tcagcaccac agcccacgag 4380 tgacacagac cattgctctc tgccacagcc ctccagtgac acagaccatc gcattgtgcc 4440 acagcccacc accgatacag gtgtctgctc tccaccacag tcctcctcta gtgcaggcta 4500 258 ctgcacttca ccacagccca ccatcagcac aggcctcagc cctctgctac agccctcctt 4560 tagcacaggc tgctgcaatc agccacagct ctcctctgcc acaggttatt gccctccatc 4620 gtagtcaggc ccaatcatca gtcagtttgc agcaaggttg ggtgcaaggt gctgatgggc 4680 tatgctctgt tgatcaggga gtgcaaggta gtgcaacatc tcagttttac accatgtctg 4740 aaagacttca tcccagtgat gattcaatta aagtcattcc tttgacaacc ttcactccac 4800 gccaacaggc cagaccgtcc agaggtgatt cccccattat ggaagaacat cccttgtaaa 4860 gctaaaatag ttacttcaaa ttttcagaaa agatgtatat agtcaaaatt taagatacaa 4920 ttccaatgag tattctgatt atcagatttg taaataacta tgtaaataga aacagatacc 4980 agaataaatc tacagctaga cccttagtca atagttaacc aaaaaattgc aatttgttta 5040 attcagaatg tgtatttaaa aagaaaagga atttaacaat ttgcatcccc ttgtacagta 5100 aggcttatca tgacagagcg cactatttct gatgtacagt attttttgtt gtttttatca 5160 tcatgtgcaa tattactgat ttgtttccat gctgattgtg tggaaccagt atgtagcaaa 5220 tggaaagcct agaaatatct tattttctaa gtttaccttt agtttaccta aacttttgtt 5280 cagataacgt taaaaggtat acgtactcta gccttttttt gggctttctt tttgattttt 5340 gtttgttgtt ttcagttttt ttgttgttgt tagtgagtct cccttcaaaa tacgcagtag 5400 gtagtgtaaa tactgcttgt ttgtgtctct ctgctgtcat gttttctacc ttattccaat 5460 actatattgt tgataaaatt tgtatataca ttttcaataa agaatatgta taaactgtac 5520 agatctagat ctacaaccta tttctctact ctttagtaga gttcgagaca cagaagtgca 5580 ataactgccc taattaagca actatttgtt aaaaagggcc tctttttact ttaatagttt 5640 agtgtaaagt acatcagaaa taaagctgta tctgccattt taagcctgta gtccattatt 5700 acttgggtct ttacttctgg gaatttgtat gtaacagcct agaaaattaa aaggaggtgg 5760 atgcatccaa agcacgagtc acttaaaata tcgacggtaa actactattt tgtagagaaa 5820 ctcaggaaga tttaaatgtt gatttgacag ctcaataggc tgttaccaaa gggtgttcag 5880 taaaaataac aaatacatgt aactgtagat aaaaccatat actaaatcta taagactaag 5940 ggatttttgt tattctagct caacttactg aagaaaacca ctaataacaa caagaatatc 6000 aggaaggaac ttttcaagaa atgtaattat aaatctacat caaacagaat tttaaggaaa 6060 aatgcagagg gagaaataag gcacatgact gcttcttgca gtcaacaaga aataccaata 6120 acacacacag aacaaaaacc atcaaaatct catatatgaa ataaaatata ttcttctaag 6180 caaagaaaca gtactattca tagaaaacat tagttttctt ctgttgtctg ttatttcctt 6240 cttgtatcct cttaactggc cattatcttg tatgtgcaca ttttataaat gtacagaaac 6300 atcaccaact taattttctt ccatagcaaa actgagaaaa taccttgttt cagtataaca 6360 ctaaaccaag agacaattga tgtttaatgg gggcggttgg ggtggggggg ggagtcaata 6420 tctcctattg attaacttag acatagattt tgtaatgtat aacttgatat ttaatttatg 6480 attaaactgt gtgtaaattt tgtaacataa actgtggtaa ttgcataatt tcattggtga 6540 ggatttccac tgaatattga gaaagtttct tttcatgtgc ccagcaggtt aagtagcgtt 6600 ttcagaatat acattattcc catccattgt aaagttcctt aagtcatatt tgactgggcg 6660 tgcagaataa cttcttaact tttaactatc agagtttgat taataaaatt aattaatgtt 6720 ttttctcctt cgtgttgtta atgttccaag ggatttggag catactggtt ttccaggtgc 6780 atgtgaatcc cgaaggactg atgatatttg aatgtttatt aaattattat catacaaatg 6840 tgttgatatt gtggctattg ttgatgttga aaattttaaa cttggggaag attaagaaaa 6900 gaaccaatag tgacaaaaat cagtgcttcc agtagatttt agaacattct ttgcctcaaa 6960 aaacctgcaa agatgatgtg agattttttc ttgtgtttta attattttca cattttctct 7020 ctgcaaaact ttagttttct gatgatctac acacacacac acacacacac gtgcacacac 7080 acacacattt aaatgatata aaaagaagag gttgaaagat tattaaataa cttatcaggc 7140 atctcaatgg ttactatcta tgttagtgaa aatcaaatag gactcaaagt tggatatttg 7200 ggatttttct tctgacagta taatttattg agttactagg gaggttctta aatcctcata 7260 tctggaaact tgtgacgttt tgacaccttt cctatagatg atataggaat gaaccaatac 7320 gcttttatta ccctttctaa ctctgatttt ataatcagac ttagattgtg tttagaatat 7380 taaatgactg ggcaccctct tcttggtttt taccagagag gctttgaatg gaagcaggct 7440 gagagtagcc aaagaggcaa ggggtattag cccagttatt ctcccctatg ccttccttct 7500 ctttctaagc gtccactagg tctggccttg gaaacctgtt acttctaggg cttcagatct 7560 gatgatatct ttttcatcac attacaagtt atttctctga ctgaatagac agtggtatag 7620 gttgacacag cacacaagtg gctattgtga tgtatgatgt atgtagtcct acaactgcaa 7680 aacgtcttac tgaaccaaca atcaaaaaat ggttctgttt taaaaaggat tttgtttgat 7740 ttgaaattaa aacttcaagc tgaatgactt atatgagaat aatacgttca atcaaagtag 7800 ttattctatt ttgtgtccat attccattag attgtgatta ttaattttct agctatggta 7860 ttactatatc acacttgtga gtatgtattc aaatactaag tatcttatat gctacgtgca 7920 tacacattct tttcttaaac tttacctgtg ttttaactaa tattgtgtca gtgtattaaa 7980 aattagcttt tacatatgat atctacaatg taataaattt agagagtaat tttgtgtatt 8040 cttatttact taacatttta cttttaatta tgtaaatttg gttagaaaat aataataaat 8100 ggttagtgct attgtgtaat ggtagcagtt acaaagagcc tctgccttcc caaactaata 8160 tttatcacac atggtcatta aatgggaaaa aaatagacta aacaaatcac aaattgttca 8220 259 gttcttaaaa tgtaattatg tcacacacac aaaaaatcct tttcaatcct gagaaaatta 8280 aaggcgtttt actcacatgg ctatttcaac attagttttt tttgtttgtt tctttttcat 8340 ggtattactg aaggtgtgta tactccctaa tacacattta tgaaaatcta cttgtttagg 8400 cttttattta tactcttctg atttatattt tttattataa ttattatttc ttatctttct 8460 tcttttatat tttttggaaa ccaaatttat agttagttta ggtaaacttt ttattatgac 8520 cattagaaac tattttgaat gcttccaact ggctcaattg gccgggaaaa catgggagca 8580 agagaagctg aaatatattt ctgcaagaac ctttctatat tatgtgccaa ttaccacacc 8640 agatcaattt tatgcagagg ccttaaaata ttctttcaca gtagctttct tacactaacc 8700 gtcatgtgct tttagtaaat atgattttta aaagcagttc aagttgacaa cagcagaaac 8760 agtaacaaaa aaatctgctc agaaaaatgt atgtgcacaa ataaaaaaaa ttaatggcaa 8820 ttgtttagtg attgtaagtg atacttttta aagagtaaac tgtgtgaaat ttatactatc 8880 cctgcttaaa atattaagat ttttatgaaa tatgtattta tgtttgtatt gtgggaagat 8940 tcctcctctg tgatatcata cagcatctga aagtgaacag tatcccaaag cagttccaac 9000 catgctttgg aagtaagaag gttgactatt gtatggccaa ggatggcagt atgtaatcca 9060 gaagcaaact tgtattaatt gttctatttc aggttctgta ttgcatgttt tcttattaat 9120 atatattaat aaaagttatg agaaat 9146 Table UIll(c). Nucleotide sequence alignment of 109P1D4 v.1 (SEQ ID NO: 250) and 109P1 D4 v.4 (SEQ ID NO: 251) Score 7456 bits (3878), Expect = 0.0ldentities = 3878/3878 (100%) Strand = Plus / Plus V.1 1 ctggtggtccagtacctccaaagatatggaatacactcctgaaatatcctgaaaactttt 60 V.4 1 ctggtggtccagtacctccaaagatatggaatacactcctgaaatatcctgaaaactttt 60 V.1 61 ttttttcagaatcctttaataagcagttatgtcaatctgaaagttgcttacttgtacttt 120 V.4 61 ttttttcagaatcctttaataagcagttatgtcaatctgaaagttgcttacttgtacttt 120 V.1 121 atattaatagctattcttgtttttcttatccaaagaaaaatcctctaatccccttttcac 180 V.4 121 atattaatagctattcttgtttttcttatccaaagaaaaatcctctaatccccttttcac 180 V.1 181 atgatagttgttaccatgtttaggcattagtcacatcaacccctctcctctcccaaactt 240 lilllllllllllill111lll11llI illll11ll11lllIllllllllilllil1lillil V.4 : 181 atgatagttgttaccatgtttaggcattagtcacatcaacccctctcctctcccaaactt 240 V.1 241 ctcttcttcaaatcaaactttattagtccctcctttataatgattccttgcctcgtttta 300 V.4 241 ctcttcttcaaatcaaactttattagtccctcctttataatgattccttgcctcgtttta 300 V.1 301 tccagatcaattttttttcactttgatgcccagagctgaagaaatggactactgtataaa 360 V.4 301 tccagatcaattttttttcactttgatgcccagagctgaagaaatggactactgtataaa 360 V.1 361 ttattcattgccaagagaataattgcattttaaacccatattataacaaagaataatgat 420 lilliIlllllllIIlll1lll1ll1l1l11lll1ll1111l1lllllilllllllilli| V.4 : 361 ttattcattgccaagagaataattgcattttaaacccatattataacaaagaataatgat 420 V.1 : 421 tatattttgtgatttgtaacaaataccctttattttcccttaactattgaattaaatatt 480 lillilllllllllllll11lll11l1l11l1lllll111li1ll1ll11lli1 1illill V.4 : 421 tatattttgtgatttgtaacaaataccctttattttcccttaactattgaattaaatatt 480 V.1 : 481 ttaattatttgtattctctttaactatcttggtatattaaagtattatcttttatatatt 540 V. : 481 ttaattatttgtattctctttaactatcttggtatattaaagtattatcttttatatatt 540 V.1 : 541 tatcaatggtggacacttttataggtactctgtgtcatttttgatactgtaggtatctta 600 260 V.4 541 tatcaatggtggacacttttataggtactctgtgtcatttttgatactgtaggtatctta 600 V.1 601 tttcatttatctttattcttaatgtacgaattcataatatttgattcagaacaaatttat 660 lIill lllll l ll lliilIll l l ll lillllll 1 1 1 11 1 1 1 1 lllllllll V.4 601 tttcatttatctttattcttaatgtacgaattcataatatttgattcagaacaaatttat 660 V.1 661 cactaattaacagagtgtcaattatgctaacatctcatttactgattttaatttaaaaca 720 t lill lll l l ll l l l ll l l l ll l i l ll l lilllll11 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 li V.4 661 cactaattaacagagtgtcaattatgctaacatctcatttactgattttaatttaaaaca 720 V.1 721 gtttttgttaacatgcatgtttagggttggcttcttaataatttcttcttcctcttctct 780 V.4 721 gtttttgttaacatgcatgtttagggttggcttcttaataatttcttcttcctcttctct 780 V.1 781 ctctcctcttcttttggtcagtgttgtgcgggttaatacaacaaactgtaacaagtgtac 840 IIlillI1lillI1 i ll lll llll l lIIi llII l tII 1lI I Il 11 Il I|| V.4 781 ctctcctcttcttttggtcagtgttgtgcgggttaatacaacaaactgtaacaagtgtac 840 V.1 841 ctggtatggacttgttgtcgggacgtacattttcgcggtcctgctagcatgcgtggtgt 900 lili I ili l I II li illllI Ililll l I 11 1 111lilI i li iIl 1 V.4 841 ctggtatggacttgttgtccgggacgtacattttcgcggtcctgctagcatgcgtggtgt 900 V.1 901 tccactctggcgcccaggagaaaaactacaccatccgagaagaaatgccagaaaacgtcc 960 lil1l I I I II il I 1||| I l 111illli I l il||l I IllillI llliIIlill I1 V.4 : 901 tccactctggcgcccaggagaaaaactacaccatccgagaagaaatgccagaaaacgtcc 960 V.1 : 961 tgataggcgacttgttgaaagaccttaacttgtcgctgattccaaacaagtccttgacaa 1020 V.4 : 961 tgataggcgacttgttgaaagaccttaacttgtcgctgattccaaacaagtccttgacaa 1020 V.1 : 1021 ctgctatgcagttcaagctagtgtacaagaccggagatgtgccactgattcgaattgaag 1080 11I111111 I 1I I II I 1 l IIIi I11l I111 111111111 111111111 I I II III III I I IH V.4 : 1021 ctgctatgcagttcaagctagtgtacaagaccggagatgtgccactgattcgaattgaag 1080 V.1 : 1081 aggatactggtgagatcttcactactggcgctcgcattgatcgtgagaaattatgtgctg 1140 lii 111 lii l111|I111111ll1ll11l111|1il1 I1li11I1ll11I1lil11I1ll1| V.4 1081 aggatactggtgagatcttcactactggcgctcgcattgatcgtgagaaattatgtgctg 1140 V.1 1141 gtatcccaagggatgagcattgcttttatgaagtggaggttgccattttgccggatgaaa 1200 t l I I I lllII li I IIIl lilli11 |li 1 il111 ll11 ilil111 l1 I11111 llil I V.4 1141 gtatcccaagggatgagcattgcttttatgaagtggaggttgccattttgccggatgaaa 1200 V.1 1201 tatttagactggttaagatacgttttctgatagaagatataaatgataatgcaccattgt 1260 11II1II1il1 lll1llIlillllllll11lllllllilllllllllllllllllll V.4 1201 tatttagactggttaagatacgttttctgatagaagatataaatgataatgcaccattgt 1260 V.1 1261 tcccagcaacagttatcaacatatcaattccagagaactcggctataaactctaaatata 1320 I il11I IlI i IIIl I||||||111111l 11 l I 11l1lill11I1ll lil l 11ll1l1 V.4 1261 tcccagcaacagttatcaacatatcaattccagagaactcggctataaactctaaatata 1320 V.1 1321 ctctcccagcggctgttgatcctgacgtaggaataaacggagttcaaaactacgaactaa 1380 il||lill11111ll111lllllllllllllllllllli11111lilllllll1illi V.4 1321 ctctcccagcggctgttgatcctgacgtaggaataaacggagttcaaaactacgaactaa 1380 V.1 1381 ttaagagtcaaaacatttttggcctcgatgtcattgaaacaccagaaggagacaagatgc 1440 261 V.4 1381 ttaagagtcaaaacatttttggcctcgatgtcattgaaacaccagaaggagacaagatgc 1440 V.1 1441 cacaactgattgttcaaaaggagttagatagggaagagaaggatacctacgtgatgaaag 1500 V.4 1441 cacaactgattgttcaaaaggagttagatagggaagagaaggatacctacgtgatgaaag 1500 V.1 1501 taaaggttgaagatggtggctttcctcaaagatccagtactgctattttgcaagtgagtg 1560 lil l l l l ll ll l | |Ilillll ii1 1 1 11 1 1 1 1 11 1 il ili ll I l I I lI lilI|||||| V.4 1501 taaaggttgaagatggtggctttcctcaaagatccagtactgctattttgcaagtgagtg 1560 V.1 1561 ttactgatacaaatgacaaccacccagtctttaaggagacagagattgaagtcagtatac 1620 V.4 1561 ttactgatacaaatgacaaccacccagtctttaaggagacagagattgaagtcagtatac 1620 V.1 1621 cagaaaatgctcctgtaggcacttcagtgacacagctccatgccacagatgctgacatag 1680 V.4 1621 cagaaaatgctcctgtaggcacttcagtgacacagctccatgccacagatgctgacatag 1680 V.1 1681 gtgaaaatgccaagatccacttctctttcagcaatctagtctccaacattgccaggagat 1740 ||||||| |||| i l l 11||1|||1 |||||1 ||||1 |1 |1111 |||||||||||||||||| V.4 1681 gtgaaaatgccaagatccacttctctttcagcaatctagtctccaacattgccaggagat 1740 V.1 1741 tatttcacctcaatgccaccactggacttatcacaatcaaagaaccactggatagggaag 1800 V.4 1741 tatttcacctcaatgccaccactggacttatcacaatcaaagaaccactggatagggaag 1800 V.1 1801 aaacaccaaaccacaagttactggttttggcaagtgatggtggattgatgccagcaagag 1860 V.4 1801 aaacaccaaaccacaagttactggttttggcaagtgatggtggattgatgccagcaagag 1860 V.1 1861 caatggtgctggtaaatgttacagatgtcaatgataatgtcccatccattgacataagat 1920 V.4 1861 caatggtgctggtaaatgttacagatgtcaatgataatgtcccatccattgacataagat 1920 V.1 1921 acatcgtcaatcctgtcaatgacacagttgttctttcagaaaatattccactcaacacca 1980 V.4 1921 acatcgtcaatcctgtcaatgacacagttgttctttcagaaaatattccactcaacacca 1980 V.1 1981 aaattgctctcataactgtgacggataaggatgcggaccataatggcagggtgacatgct 2040 V.4 1981 aaattgctctcataactgtgacggataaggatgcggaccataatggcagggtgacatgct 2040 V.1 2041 tcacagatcatgaaatccctttcagattaaggccagtattcagtaatcagttcctcctgg 2100 V.4 2041 tcacagatcatgaaatccctttcagattaaggccagtattcagtaatcagttcctcctgg 2100 V.1 2101 agactgcagcatatcttgactatgagtccacaaaagaatatgccattaaattactggctg 2160 V.4 2101 agactgcagcatatcttgactatgagtccacaaaagaatatgccattaaattactggctg 2160 V.1 2161 cagatgctggcaaacctcctttgaatcagtcagcaatgctcttcatcaaagtgaaagatg 2220 V.4 2161 cagatgctggcaaacctcctttgaatcagtcagcaatgctcttcatcaaagtgaaagatg 2220 262 V.1 2221 aaaatgacaatgctccagttttcacccagtctttcgtaactgtttctattcctgagaata 2280 lillll Ilillllllllll lll l il illl ll llll11ll 11l 1l l i i ll ||||||| V.4 2221 aaaatgacaatgctccagttttcacccagtctttcgtaactgtttctattcctgagaata 2280 V.1 2281 actctcctggcatccagttgacgaaagtaagtgcaatggatgcagacagtgggcctaatg 2340 V.4 2281 actctcctggcatccagttgacgaaagtaagtgcaatggatgcagacagtgggcctaatg 2340 V.1 2341 ctaagatcaattacctgctaggccctgatgctccacctgaattcagcctggattgtcgta 2400 I Il li l IIll lil I| lil i i I l l lilli11 1 I||||||| 11 | 1 ||il| V.4 2341 ctaagatcaattacctgctaggccctgatgctccacctgaattcagcctggattgtcgta 2400 V.1 2401 caggcatgctgactgtagtgaagaaactagatagagaaaaagaggataaatatttattca 2460 111I111lJllIII|||||||||il l III|I|||||||||||||||||||||li1 Il|| V.4 2401 caggcatgctgactgtagtgaagaaactagatagagaaaaagaggataaatatttattca 2460 V.1 2461 caattctggcaaaagataacggggtaccacccttaaccagcaatgtcacagtctttgtaa 2520 V.4 2461 caattctggcaaaagataacggggtaccacccttaaccagcaatgtcacagtctttgtaa 2520 V.1 2521 gcattattgatcagaatgacaatagcccagttttcactcacaatgaatacaacttctatg 2580 I1111 ll1I I llllll l 1l 11lill 11 I lilli 1lilli11l ll||||||| 1111 I ll111 V.4 2521 gcattattgatcagaatgacaatagcccagttttcactcacaatgaatacaacttctatg 2580 V.1 2581 tcccagaaaaccttccaaggcatggtacagtaggactaatcactgtaactgatcctgatt 2640 11il1111 llll1l111llIIlIlll l I lllll lll lllillI I||||l|i| V.4 2581 tcccagaaaaccttccaaggcatggtacagtaggactaatcactgtaactgatcctgatt 2640 V.1 2641 atggagacaattctgcagttacgctctccattttagatgagaatgatgacttcaccattg 2700 lillllllllllllllllllillllll11 ll1 111ll11l ll l l1ll.lllll l V.4 2641 atggagacaattctgcagttacgctctccattttagatgagaatgatgacttcaccattg 2700 V.1 2701 attcacaaactggtgtcatccgaccaaatatttcatttgatagagaaaaacaagaatctt 2760 V.4 2701 attcacaaactggtgtcatccgaccaaatatttcatttgatagagaaaaacaagaatctt 2760 V.1 2761 acactttctatgtaaaggctgaggatggtggtagagtatcacgttcttcaagtgccaaag 2820 11I111l1l111111111111 11111111 11I1I11lilli1lil|i11I11 111i|1||||1 V.4 2761 acactttctatgtaaaggctgaggatggtggtagagtatcacgttcttcaagtgccaaag 2820 V.1 2821 taaccataaatgtggttgatgtcaatgacaacaaaccagttttcattgtccctccttcca 2880 lilillli1lllllIllllllllllllllllIl11IlIIIIll1llllI1i V.4 : 2821 taaccataaatgtggttgatgtcaatgacaacaaaccagttttcattgtccctccttcca 2880 V.1 : 2881 actgttcttatgaattggttctaccgtccactaatccaggcacagtggtctttcaggtaa 2940 lii lilll 11i1ll111I11il1111l111I 1111I1111l1l11111l1Il 11ilIl|11 V.4 : 2881 actgttcttatgaattggttctaccgtccactaatccaggcacagtggtctttcaggtaa 2940 V.1 : 2941 ttgctgttgacaatgacactggcatgaatgcagaggttcgttacagcattgtaggaggaa 3000 lilllilllllll11l1 Il111l1l1ll11l1l1 1l1l1l111l1lll11l11|1||1|1 V.4 : 2941 ttgctgttgacaatgacactggcatgaatgcagaggttcgttacagcattgtaggaggaa 3000 V.1 : 3001 acacaagagatctgtttgcaatcgaccaagaaacaggcaacataacattgatggagaaat 3060 1All lliillll111lll l l llll III 1111111111111111 3llI V.4 :3001 acacaagagatctgtttgcaatcgaccaagaaacaggcaacataacattgatggagaaat 3060 263 V.1 3061 gtgatgttacagaccttggtttacacagagtgttggtcaaagctaatgacttaggacagc 3120 lI I I I 11 I l1llli IIIlll1I1llil I | 1 11i Il 11111 lI l I Il1Ilil l V.4 3061 gtgatgttacagaccttggtttacacagagtgttggtcaaagctaatgacttaggacagc 3120 V.1 3121 ctgattctctcttcagtgttgtaattgtcaatctgttcgtgaatgagtcggtgaccaatg 3180 ||lI I|1 Ii1111 1111Il11 I I1I I ll|1il IIIl IIIi I I II| l llIlIll1 V.4 3121 ctgattctctcttcagtgttgtaattgtcaatctgttcgtgaatgagtcggtgaccaatg 3180 V.1 3181 ctacactgattaatgaactggtgcgcaaaagcactgaagcaccagtgaccccaaatactg 3240 Illi 111 I 11111 1111 l iI11 i | I lI | l I l1 1lill I11111111 I l 1 l l V.4 3181 ctacactgattaatgaactggtgcgcaaaagcactgaagcaccagtgaccccaaatactg 3240 V.1 3241 agatagctgatgtatcctcaccaactagtgactatgtcaagatcctggttgcagctgttg 3300 V.4 3241 agatagctgatgtatcctcaccaactagtgactatgtcaagatcctggttgcagctgttg 3300 V.1 3301 ctggcaccataactgtcgttgtagttattttcatcactgctgtagtaagatgtcgccagg 3360 V.4 3301 ctggcaccataactgtcgttgtagttattttcatcactgctgtagtaagatgtcgccagg 3360 V.1 3361 caccacaccttaaggctgctcagaaaaacaagcagaattctgaatgggctaccccaaacc 3420 11|111111111111|1|11||1111111l1ili|111I llil|||ll li11lill V.4 3361 caccacaccttaaggctgctcagaaaaacaagcagaattctgaatgggctaccccaaacc 3420 V.1 3421 cagaaaacaggcagatgataatgatgaagaaaaagaaaaagaagaagaagcattccccta 3480 |lill I11l1l1l1lll11111I1I111111l11 1 il11 illIII II l 11 I11 1I1 V.4 3421 cagaaaacaggcagatgataatgatgaagaaaaagaaaaagaagaagaagcattccccta 3480 V.1 3481 agaacttgctgcttaattttgtcactattgaagaaactaaggcagatgatgttgacagtg 3540 V.4 3481 agaacttgctgcttaattttgtcactattgaagaaactaaggcagatgatgttgacagtg 3540 V.1 3541 atggaaacagagtcacactagaccttcctattgatctagaagagcaaacaatgggaaagt 3600 I1ll111l111111I1 ll1 ll jIll lij iI 11 l||1 i lllllil||I I I ll lillilili V.4 3541 atggaaacagagtcacactagaccttcctattgatctagaagagcaaacaatgggaaagt 3600 V.1 3601 acaattgggtaactacacctactactttcaagcccgacagccctgatttggcccgacact 3660 11ll1ll1lilll1llllllll11111l1l1l1l111l1l111111lilllllllllll1li V.4 3601 acaattgggtaactacacctactactttcaagcccgacagccctgatttggcccgacact 3660 V.1 3661 acaaatctgcctctccacagcctgccttccaaattcagcctgaaactcccctgaattcga 3720 1111l||| i1l1ll ll111ll lill1111I| 11||I 111 111i11i1I| Il i I V.4 3661 acaaatctgcctctccacagcctgccttccaaattcagcctgaaactcccctgaattcga 3720 V.1 3721 agcaccacatcatccaagaactgcctctcgataacacctttgtggcctgtgactctatct 3780 111I|| 1Il 11I11 I I 11ll11 I1lli1i1I ll 111 lIIl i I I 1l l lili I1 lill V.4 3721 agcaccacatcatccaagaactgcctctcgataacacctttgtggcctgtgactctatct 3780 V.1 3781 ccaagtgttcctcaagcagttcagatccctacagcgtttctgactgtggctatccagtga 3840 lilllll11ll1l111l1ll1ill1ll1111lll1lll11ll1l11ll1lilll111l111l V.4 3781 ccaagtgttcctcaagcagttcagatccctacagcgtttctgactgtggctatccagtga 3840 V.1 : 3841 cgaccttcgaggtacctgtgtccgtacacaccagaccg 3878 VAl 1llil1 llil lll lllllllllll l lll i 3878 V.4 :3841 cgaccttcgaggtacctgtgtccgtacacaccagaccg 3878 264 Table UV(c). Peptide sequences of protein coded by 109P1D4 v.4 (SEQ ID NO: 252) MDLLSGTYIF AVLLACVVFH SGAQEKNYTI REEMPENVLI GDLLKDLNLS LIPNKSLTTA 60 MQFKLVYKTG DVPLIRIEED TGEIFTTGAR IDREKLCAGI PRDEHCFYEV EVAILPDEIF 120 RLVKIRFLIE DINDNAPLFP ATVINISIPE NSAINSKYTL PAAVDPDVGI NGVQNYELIK 180 SQNIFGLDVI ETPEGDKMPQ LIVQKELDRE EKDTYVMKVK VEDGGFPQRS STAILQVSVT 240 DTNDNHPVFK ETEIEVSIPE NAPVGTSVTQ LHATDADIGE NAKIHFSFSN LVSNIARRLF 300 HLNATTGLIT IKEPLDREET PNHKLLVLAS DGGLMPARAM VLVNVTDVND NVPSIDIRYI 360 VNPVNDTVVL SENIPLNTKI ALITVTDKDA DHNGRVTCFT DHEIPFRLRP VFSNQFLLET 420 AAYLDYESTK EYAIKLLAAD AGKPPLNQSA MLFIKVKDEN DNAPVFTQSF VTVSIPENNS 480 PGIQLTKVSA MDADSGPNAK INYLLGPDAP PEFSLDCRTG MLTVVKKLDR EKEDKYLFTI 540 LAKDNGVPPL TSNVTVFVSI IDQNDNSPVF THNEYNFYVP ENLPRHGTVG LITVTDPDYG 600 DNSAVTLSIL DENDDFTIDS QTGVIRPNIS FDREKQESYT FYVKAEDGGR VSRSSSAKVT 660 INVVDVNDNK PVFIVPPSNC SYELVLPSTN PGTVVFQVIA VDNDTGMNAE VRYSIVGGNT 720 RDLFAIDQET GNITLMEKCD VTDLGLHRVL VKANDLGQPD SLFSVVIVNL FVNESVTNAT 780 LINELVRKST EAPVTPNTEI ADVSSPTSDY VKILVAAVAG TITVVVVIFI TAVVRCRQAP 840 HLKAAQKNKQ NSEWATPNPE NRQMIMMKKK KKKKKHSPKN LLLNFVTIEE TKADDVDSDG 900 NRVTLDLPID LEEQTMGKYN WVTTPTTFKP DSPDLARHYK SASPQPAFQI QPETPLNSKH 960 HIIQELPLDN TFVACDSISK CSSSSSDPYS VSDCGYPVTT FEVPVSVHTR PPMKEVVRSC 1020 TPMKESTTME IWIHPQPQSQ RRVTFHLPEG SQESSSDGGL GDHDAGSLTS TSHGLPLGYP 1080 QEEYFDRATP SNRTEGDGNS DPESTFIPGL KKAAEITVQP TVEEASDNCT QECLIYGHSD 1140 ACWMPASLDH SSSSQAQASA LCHSPPLSQA STQHHSPRVT QTIALCHSPP VTQTIALCHS 1200 PPPIQVSALH HSPPLVQATA LHHSPPSAQA SALCYSPPLA QAAAISHSSP LPQVIALHRS 1260 QAQSSVSLQQ GWVQGADGLC SVDQGVQGSA TSQFYTMSER LHPSDDSIKV IPLTTFTPRQ 1320 QARPSRGDSP IMEEHPL 1337 Table LV(c). Amino acid sequence alignment of 109P1D4 v.1 (SEQ ID NO: 253) and 109P1D4 v.4 (SEQ ID NO: 254) Score = 2005 bits (5195), Expect = 0.0ldentities = 1011/1011 (100%), Positives = 1011/1011 (100%) V.1 :1 MDLLSGTYIFAVLLACVVFHSGAQEKNYTIREEMPENVLIGDLLKDLNLSLIPNKSLTTA 60 MDLLSGTYIFAVLLACVVFHSGAQEKNYTIREEMPENVLIGDLLKDLNLSLIPNKSLTTA V.4 1 MDLLSGTYIFAVLLACVVFHSGAQEKNYTIREEMPENVLIGDLLKDLNLSLIPNKSLTTA 60 V.1 61 MQFKLVYKTGDVPLIRIEEDTGEIFTTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIF 120 MQFKLVYKTGDVPLIRIEEDTGEIFrTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIF V.4 61 MQFKLVYKTGDVPLIRIEE DTGEIrTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIF 120 V.1 121 RLVKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIK 180 RLVKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIK V.4 121 RLVKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIK 180 V.1 181 SQNIFGLDVIETPEGDKMPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVT 240 SQNIFGLDVIETPEGDKMPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVT V.4 181 SQNIFGLDVIETPEGDKMPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILOVSVT 240 V.1 241 DTNDNHPVFKETEIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSFSNLVSNIARRLF 300 DTNDNHPVFKETEIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSFSNLVSNIARRLF V.4 241 DTNDNHPVFKETEIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSFSNLVSNIARRLF 300 V.1 301 HLNATTGLITIKEPLDREETPNHKLLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYI 360 HLNATTGLITIKEPLDREETPNHKLLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYI V.4 301 HLNATTGLITIKEPLDREETPNHKLLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYI 360 V.1 361 VNPVNDTVVLSENIPLNTKIALITVTDKDADHNGRVTCFTDHEIPFRLRPVFSNQFLLET 420 VNPVNDTVVLSENIPLNTKIALITVTDKDADHNGRVTCFTDHEIPFRLRPVFSNQFLLET V.4 : 361 VNPVNDTVVLSENIPLNTKIALITVTDKDADHNGRVTCNrDHEIPFRLRPVFSNQFLLET 420 V.1 : 421 AAYLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDENDNAPVSTSFVTVSIPENNS 480 AAYLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDENDNAPVFTQSFVTVSIPENNS V.4 : 421 AAYLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDENDNAPVFTQSFVTVSIPENNS 480 V.1 : 481 PGIQLTKVSAMDADSGPNAKINYLLGPDAPPEFSLDCRTGMLTVVKKLDREKEDKYLnI 540 PGIOLTKVSAMDADSGPNAKINYLLGPDAPPEFSLDCRTGMLTVVKKLDREKEDKYLyI 265 V.4 481 PGIQLTKVSAMDADSGPNAKINYLLGPDAPPEFSLDCRTGMLTVVKKLDREKEDKYLFTI 540 V.1 541 LAKDNGVPPLTSNVTVFVSIIDQNDNSPVFTHNEYNFYvpENLPRHGTVGLITVTDPDYG 600 LAKDNGVPPLTSNVTVFVSIIDQNDNSPVrTHNEYNFYVPENLPRHGTVGLITVTDPDYG V.4 541 LAKDNGVPPLTSNVTVFVSIIDQNDNSPVFTHNEYNFYVPENLPRHGTVGLITVTDPDYG 600 V.1 601 DNSAVTLSILDENDDTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVT 660 DNSAVTLSILDENDDFTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVT V.4 601 DNSAVTLSILDENDDFTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVT 660 V.1 : 661 INVVDVNDNKPVFIVPPSNCSYELVLPSTNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNT 720 INVVDVNDNKPVFIVPPSNCSYELVLPSTNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNT V.4 : 661 INVVDVNDNKPVFIVPPSNCSYELVLPSTNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNT 720 V.1 : 721 RDLFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPDSLFSVVIVNLFVNESVTNAT 780 RDLFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPDSLFSVVIVNLFVNESVTNAT V.4 : 721 RDLFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPDSLFSVVIVNLFVNESVTNAT 780 V.1 : 781 LINELVRKSTEAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVRCRQAP 840 LINELVRKSTEAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVRCRQAP V.4 : 781 LINELVRKSTEAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVRCRQAP 840 V.1 : 841 HLKAAQKNKQNSEWATPNPENRQMIMMKKKKKKKKHSPKNLLLNFVTIEETKADDVDSDG 900 HLKAAQKNKQNSEWATPNPENRQMIMKKKKKKHSPKNLLLNFVTIEETKADDVDSDG V.4 : 841 HLKAAQKNKQNSEWATPNPENRQMIMMKKKKKKKKHSPKNLLLNFVTIEETKADDVDSDG 900 V.1 : 901 NRVTLDLPIDLEEQTMGKYNWVTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLNSKH 960 NRVTLDLPIDLEEQTMGKYNWVTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLNSKH V.4 : 901 NRVTLDLPIDLEEQTMGKYNWVTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLNSKH 960 V.1 : 961 HIIQELPLDNTFVACDSISKCSSSSSDPYSVSDCGYPVTTFEVPVSVHTRP 1011 HIIQELPLDNTFVACDSISKCSSSSSDPYSVSDCGYPVTTFEVPVSVHTRP V.4 : 961 HIIQELPLDNTFVACDSISKCSSSSSDPYSVSDCGYPVTTFEVPVSVHTRP 1011 Table Ul(d). Nucleotide sequence of transcdpt vadant 109P1D4v.5 (SEQ ID NO: 255) ctggtggtcc agtacctcca aagatatgga atacactcct gaaatatcct gaaaactttt 60 ttttttcaga atcctttaat aagcagttat gtcaatctga aagttgctta cttgtacttt 120 atattaatag ctattcttgt ttttcttatc caaagaaaaa tcctctaatc cccttttcac 180 atgatagttg ttaccatgtt taggcattag tcacatcaac ccctctcctc tcccaaactt 240 ctcttcttca aatcaaactt tattagtccc tcctttataa tgattccttg cctcgtttta 300 tccagatcaa ttttttttca ctttgatgcc cagagctgaa gaaatggact actgtataaa 360 ttattcattg ccaagagaat aattgcattt taaacccata ttataacaaa gaataatgat 420 tatattttgt gatttgtaac aaataccctt tattttccct taactattga attaaatatt 480 ttaattattt gtattctctt taactatctt ggtatattaa agtattatct tttatatatt 540 tatcaatggt ggacactttt ataggtactc tgtgtcattt ttgatactgt aggtatctta 600 tttcatttat ctttattctt aatgtacgaa ttcataatat ttgattcaga acaaatttat 660 cactaattaa cagagtgtca attatgctaa catctcattt actgatttta atttaaaaca 720 gtttttgtta acatgcatgt ttagggttgg cttcttaata atttcttctt cctcttctct 780 ctctcctctt cttttggtca gtgttgtgcg ggttaataca acaaactgta acaagtgtac 840 ctggtatgga cttgttgtcc gggacgtaca ttttcgcggt cctgctagca tgcgtggtgt 900 tccactctgg cgcccaggag aaaaactaca ccatccgaga agaaatgcca gaaaacgtcc 960 tgataggcga cttgttgaaa gaccttaact tgtcgctgat tccaaacaag tccttgacaa 1020 ctgctatgca gttcaagcta gtgtacaaga ccggagatgt gccactgatt cgaattgaag 1080 aggatactgg tgagatcttc actactggcg ctcgcattga tcgtgagaaa ttatgtgctg 1140 gtatcccaag ggatgagcat tgcttttatg aagtggaggt tgccattttg ccggatgaaa 1200 tatttagact ggttaagata cgttttctga tagaagatat aaatgataat gcaccattgt 1260 tcccagcaac agttatcaac atatcaattc cagagaactc ggctataaac tctaaatata 1320 ctctcccagc ggctgttgat cctgacgtag gaataaacgg agttcaaaac tacgaactaa 1380 ttaagagtca aaacattttt ggcctcgatg tcattgaaac accagaagga gacaagatgc 1440 cacaactgat tgttcaaaag gagttagata gggaagagaa ggatacctac gtgatgaaag 1500 taaaggttga agatggtggc tttcctcaaa gatccagtac tgctattttg caagtgagtg 1560 ttactgatac aaatgacaac cacccagtct ttaaggagac agagattgaa gtcagtatac 1620 cagaaaatgc tcctgtaggc acttcagtga cacagctcca tgccacagat gctgacatag 1680 gtgaaaatgc caagatccac ttctctttca gcaatctagt ctccaacatt gccaggagat 1740 tatttcacct caatgccacc actggactta tcacaatcaa agaaccactg gatagggaag 1800 266 aaacaccaaa ccacaagtta ctggttttgg caagtgatgg tggattgatg ccagcaagag 1860 caatggtgct ggtaaatgtt acagatgtca atgataatgt cccatccatt gacataagat 1920 acatcgtcaa tcctgtcaat gacacagttg ttctttcaga aaatattcca ctcaacacca 1980 aaattgctct cataactgtg acggataagg atgcggacca taatggcagg gtgacatgct 2040 tcacagatca tgaaatccct ttcagattaa ggccagtatt cagtaatcag ttcctcctgg 2100 agactgcagc atatcttgac tatgagtcca caaaagaata tgccattaaa ttactggctg 2160 cagatgctgg caaacctcct ttgaatcagt cagcaatgct cttcatcaaa gtgaaagatg 2220 aaaatgacaa tgctccagtt ttcacccagt ctttcgtaac tgtttctatt cctgagaata 2280 actctcctgg catccagttg acgaaagtaa gtgcaatgga tgcagacagt gggcctaatg 2340 ctaagatcaa ttacctgcta ggccctgatg ctccacctga attcagcctg gattgtcgta 2400 caggcatgct gactgtagtg aagaaactag atagagaaaa agaggataaa tatttattca 2460 caattctggc aaaagataac ggggtaccac ccttaaccag caatgtcaca gtctttgtaa 2520 gcattattga tcagaatgac aatagcccag ttttcactca caatgaatac aacttctatg 2580 tcccagaaaa ccttccaagg catggtacag taggactaat cactgtaact gatcctgatt 2640 atggagacaa ttctgcagtt acgctctcca ttttagatga gaatgatgac ttcaccattg 2700 attcacaaac tggtgtcatc cgaccaaata tttcatttga tagagaaaaa caagaatctt 2760 acactttcta tgtaaaggct gaggatggtg gtagagtatc acgttcttca agtgccaaag 2820 taaccataaa tgtggttgat gtcaatgaca acaaaccagt tttcattgtc cctccttcca 2880 actgttctta tgaattggtt ctaccgtcca ctaatccagg cacagtggtc tttcaggtaa 2940 ttgctgttga caatgacact ggcatgaatg cagaggttcg ttacagcatt gtaggaggaa 3000 acacaagaga tctgtttgca atcgaccaag aaacaggcaa cataacattg atggagaaat 3060 gtgatgttac agaccttggt ttacacagag tgttggtcaa agctaatgac ttaggacagc 3120 ctgattctct cttcagtgtt gtaattgtca atctgttcgt gaatgagtcg gtgaccaatg 3180 ctacactgat taatgaactg gtgcgcaaaa gcactgaagc accagtgacc ccaaatactg 3240 agatagctga tgtatcctca ccaactagtg actatgtcaa gatcctggtt gcagctgttg 3300 ctggcaccat aactgtcgtt gtagttattt tcatcactgc tgtagtaaga tgtcgccagg 3360 caccacacct taaggctgct cagaaaaaca agcagaattc tgaatgggct accccaaacc 3420 cagaaaacag gcagatgata atgatgaaga aaaagaaaaa gaagaagaag cattccccta 3480 agaacttgct gcttaatttt gtcactattg aagaaactaa ggcagatgat gttgacagtg 3540 atggaaacag agtcacacta gaccttccta ttgatctaga agagcaaaca atgggaaagt 3600 acaattgggt aactacacct actactttca agcccgacag ccctgatttg gcccgacact 3660 acaaatctgc ctctccacag cctgccttcc aaattcagcc tgaaactccc ctgaattcga 3720 agcaccacat catccaagaa ctgcctctcg ataacacctt tgtggcctgt gactctatct 3780 ccaagtgttc ctcaagcagt tcagatccct acagcgtttc tgactgtggc tatccagtga 3840 cgaccttcga ggtacctgtg tccgtacaca ccagaccgtc ccagcggcgt gtcacatttc 3900 acctgccaga aggctctcag gaaagcagca gtgatggtgg actgggagac catgatgcag 3960 gcagccttac cagcacatct catggcctgc cccttggcta tcctcaggag gagtactttg 4020 atcgtgctac acccagcaat cgcactgaag gggatggcaa ctccgatcct gaatctactt 4080 tcatacctgg actaaagaaa gctgcagaaa taactgttca accaactgtg gaagaggcct 4140 ctgacaactg cactcaagaa tgtctcatct atggccattc tgatgcctgc tggatgccgg 4200 catctctgga tcattccagc tcttcgcaag cacaggcctc tgctctatgc cacagcccac 4260 cactgtcaca ggcctctact cagcaccaca gcccacgagt gacacagacc attgctctct 4320 gccacagccc tccagtgaca cagaccatcg cattgtgcca cagcccacca ccgatacagg 4380 tgtctgctct ccaccacagt cctcctctag tgcaggctac tgcacttcac cacagcccac 4440 catcagcaca ggcctcagcc ctctgctaca gccctccttt agcacaggct gctgcaatca 4500 gccacagctc tcctctgcca caggttattg ccctccatcg tagtcaggcc caatcatcag 4560 tcagtttgca gcaaggttgg gtgcaaggtg ctgatgggct atgctctgtt gatcagggag 4620 tgcaaggtag tgcaacatct cagttttaca ccatgtctga aagacttcat cccagtgatg 4680 attcaattaa agtcattcct ttgacaacct tcactccacg ccaacaggcc agaccgtcca 4740 gaggtgattc ccccattatg gaagaacatc ccttgtaaag ctaaaatagt tacttcaaat 4800 tttcagaaaa gatgtatata gtcaaaattt aagatacaat tccaatgagt attctgatta 4860 tcagatttgt aaataactat gtaaatagaa acagatacca gaataaatct acagctagac 4920 ccttagtcaa tagttaacca aaaaattgca atttgtttaa ttcagaatgt gtatttaaaa 4980 agaaaaggaa tttaacaatt tgcatcccct tgtacagtaa ggcttatcat gacagagcgc 5040 actatttctg atgtacagta ttttttgttg tttttatcat catgtgcaat attactgatt 5100 tgtttccatg ctgattgtgt ggaaccagta tgtagcaaat ggaaagccta gaaatatctt 5160 attttctaag tttaccttta gtttacctaa acttttgttc agataacgtt aaaaggtata 5220 cgtactctag cctttttttg ggctttcttt ttgatttttg tttgttgttt tcagtttttt 5280 tgttgttgtt agtgagtctc ccttcaaaat acgcagtagg tagtgtaaat actgcttgtt 5340 tgtgtctctc tgctgtcatg ttttctacct tattccaata ctatattgtt gataaaattt 5400 gtatatacat tttcaataaa gaatatgtat aaactgtaca gatctagatc tacaacctat 5460 ttctctactc tttagtagag ttcgagacac agaagtgcaa taactgccct aattaagcaa 5520 267 ctatttgtta aaaagggcct ctttttactt taatagttta gtgtaaagta catcagaaat 5580 aaagctgtat ctgccatttt aagcctgtag tccattatta cttgggtctt tacttctggg 5640 aatttgtatg taacagccta gaaaattaaa aggaggtgga tgcatccaaa gcacgagtca 5700 cttaaaatat cgacggtaaa ctactatttt gtagagaaac tcaggaagat ttaaatgttg 5760 atttgacagc tcaataggct gttaccaaag ggtgttcagt aaaaataaca aatacatgta 5820 actgtagata aaaccatata ctaaatctat aagactaagg gatttttgtt attctagctc 5880 aacttactga agaaaaccac taataacaac aagaatatca ggaaggaact tttcaagaaa 5940 tgtaattata aatctacatc aaacagaatt ttaaggaaaa atgcagaggg agaaataagg 6000 cacatgactg cttcttgcag tcaacaagaa ataccaataa cacacacaga acaaaaacca 6060 tcaaaatctc atatatgaaa taaaatatat tcttctaagc aaagaaacag tactattcat 6120 agaaaacatt agttttcttc tgttgtctgt tatttccttc ttgtatcctc ttaactggcc 6180 attatcttgt atgtgcacat tttataaatg tacagaaaca tcaccaactt aattttcttc 6240 catagcaaaa ctgagaaaat accttgtttc agtataacac taaaccaaga gacaattgat 6300 gtttaatggg ggcggttggg gtgggggggg gagtcaatat ctcctattga ttaacttaga 6360 catagatttt gtaatgtata acttgatatt taatttatga ttaaactgtg tgtaaatttt 6420 gtaacataaa ctgtggtaat tgcataattt cattggtgag gatttccact gaatattgag 6480 aaagtttctt ttcatgtgcc cagcaggtta agtagcgttt tcagaatata cattattccc 6540 atccattgta aagttcctta agtcatattt gactgggcgt gcagaataac ttcttaactt 6600 ttaactatca gagtttgatt aataaaatta attaatgttt tttctccttc gtgttgttaa 6660 tgttccaagg gatttggagc atactggttt tccaggtgca tgtgaatccc gaaggactga 6720 tgatatttga atgtttatta aattattatc atacaaatgt gttgatattg tggctattgt 6780 tgatgttgaa aattttaaac ttggggaaga ttaagaaaag aaccaatagt gacaaaaatc 6840 agtgcttcca gtagatttta gaacattctt tgcctcaaaa aacctgcaaa gatgatgtga 6900 gattttttct tgtgttttaa ttattttcac attttctctc tgcaaaactt tagttttctg 6960 atgatctaca cacacacaca cacacacacg tgcacacaca cacacattta aatgatataa 7020 aaagaagagg ttgaaagatt attaaataac ttatcaggca tctcaatggt tactatctat 7080 gttagtgaaa atcaaatagg actcaaagtt ggatatttgg gatttttctt ctgacagtat 7140 aatttattga gttactaggg aggttcttaa atcctcatat ctggaaactt gtgacgtttt 7200 gacacctttc ctatagatga tataggaatg aaccaatacg cttttattac cctttctaac 7260 tctgatttta taatcagact tagattgtgt ttagaatatt aaatgactgg gcaccctctt 7320 cttggttttt accagagagg ctttgaatgg aagcaggctg agagtagcca aagaggcaag 7380 gggtattagc ccagttattc tcccctatgc cttccttctc tttctaagcg tccactaggt 7440 ctggccttgg aaacctgtta cttctagggc ttcagatctg atgatatctt tttcatcaca 7500 ttacaagtta tttctctgac tgaatagaca gtggtatagg ttgacacagc acacaagtgg 7560 ctattgtgat gtatgatgta tgtagtccta caactgcaaa acgtcttact gaaccaacaa 7620 tcaaaaaatg gttctgtttt aaaaaggatt ttgtttgatt tgaaattaaa acttcaagct 7680 gaatgactta tatgagaata atacgttcaa tcaaagtagt tattctattt tgtgtccata 7740 ttccattaga ttgtgattat taattttcta gctatggtat tactatatca cacttgtgag 7800 tatgtattca aatactaagt atcttatatg ctacgtgcat acacattctt ttcttaaact 7860 ttacctgtgt tttaactaat attgtgtcag tgtattaaaa attagctttt acatatgata 7920 tctacaatgt aataaattta gagagtaatt ttgtgtattc ttatttactt aacattttac 7980 ttttaattat gtaaatttgg ttagaaaata ataataaatg gttagtgcta ttgtgtaatg 8040 gtagcagtta caaagagcct ctgccttccc aaactaatat ttatcacaca tggtcattaa 8100 atgggaaaaa aatagactaa acaaatcaca aattgttcag ttcttaaaat gtaattatgt 8160 cacacacaca aaaaatcctt ttcaatcctg agaaaattaa aggcgtttta ctcacatggc 8220 tatttcaaca ttagtttttt ttgtttgttt ctttttcatg gtattactga aggtgtgtat 8280 actccctaat acacatttat gaaaatctac ttgtttaggc ttttatttat actcttctga 8340 tttatatttt ttattataat tattatttct tatctttctt cttttatatt ttttggaaac 8400 caaatttata gttagtttag gtaaactttt tattatgacc attagaaact attttgaatg 8460 cttccaactg gctcaattgg ccgggaaaac atgggagcaa gagaagctga aatatatttc 8520 tgcaagaacc tttctatatt atgtgccaat taccacacca gatcaatttt atgcagaggc 8580 cttaaaatat tctttcacag tagctttctt acactaaccg tcatgtgctt ttagtaaata 8640 tgatttttaa aagcagttca agttgacaac agcagaaaca gtaacaaaaa aatctgctca 8700 gaaaaatgta tgtgcacaaa taaaaaaaat taatggcaat tgtttagtga ttgtaagtga 8760 tactttttaa agagtaaact gtgtgaaatt tatactatcc ctgcttaaaa tattaagatt 8820 tttatgaaat atgtatttat gtttgtattg tgggaagatt cctcctctgt gatatcatac 8880 agcatctgaa agtgaacagt atcccaaagc agttccaacc atgctttgga agtaagaagg 8940 ttgactattg tatggccaag gatggcagta tgtaatccag aagcaaactt gtattaattg 9000 ttctatttca ggttctgtat tgcatgtttt cttattaata tatattaata aaagttatga 9060 gaaat 9065 268 Table Lil(d). Nucleotide sequence alignment of 109P1D4 v.1 (SEQ ID NO: 256) and 109P1D4 v.5 (SEQ ID NO: 257) Score = 7456 bits (3878), Expect = 0.01dentities = 387813878 (100%) Strand = Plus / Plus V.1 1 ctggtggtccagtacctccaaagatatggaatacactcctgaaatatcctgaaaactttt 60 I 11l11ll lill I1I11|1111111 111i 11|| ll 1IIlllllIll||I lIll V.5 1 ctggtggtccagtacctccaaagatatggaatacactcctgaaatatcctgaaaactttt 60 V.1 61 ttttttcagaatcctttaataagcagttatgtcaatctgaaagttgcttacttgtacttt 120 lill11 I ililll11|11 1 1 1 11ll| |Ill 11il 111111 11 l i11111 l1 V.5 61 ttttttcagaatcctttaataagcagttatgtcaatctgaaagttgcttacttgtacttt 120 V.1 121 atattaatagctattcttgtttttcttatccaaagaaaaatcctctaatccccttttcac 180 1i11 l||11l111|111111111|||1 I ill 1ill1i1|||I ll1ilil 11 I il11 V.5 121 atattaatagctattcttgtttttcttatccaaagaaaaatcctctaatccccttttcac 180 V.1 181 atgatagttgttaccatgtttaggcattagtcacatcaacccctctcctctcccaaactt 240 llil11 lil I I l1illl1lil 11111111 111l1l1ll I I I lI.l 111I1 ll lilI V.5 181 atgatagttgttaccatgtttaggcattagtcacatcaacccctctcctctcccaaactt 240 V.1 241 ctcttcttcaaatcaaactttattagtccctcctttataatgattccttgcctcgtttta 300 II I II I I III I l llIIIII I lII lIII I I I I I III l l ll l ll l I lill li1||||ii l V.5 241 ctcttcttcaaatcaaactttattagtccctcctttataatgattccttgcctcgtttta 300 V.1 301 tccagatcaattttttttcactttatgcccagagctgaagaaatggactactgtataaa 360 1I 1 I 1l1lillill1 lil I 11 l i ll 1lill 1111i l I1I||lill I 1 illll V.5 301 tccagatcaattttttttcactttgatgcccagagctgaagaaatggactactgtataaa 360 V.1 361 ttattcattgccaagagaataattgcattttaaacccatattataacaaagaataatgat 420 |I1 ll 111I1||1|||111|l 11 i111I1111111ll1111111111lil1111|11ll V.5 361 ttattcattgccaagagaataattgcattttaaacccatattataacaaagaataatgat 420 V.1 421 tatattttgtgatttgtaacaaataccctttattttcccttaactattgaattaaatatt 480 1l1l III IIlIIII llI I I lii 11|Ill i I 11 Ill111111i11I1l i11111li V.5 421 tatattttgtgatttgtaacaaataccctttattttcccttaactattgaattaaatatt 480 V.1 481 ttaattatttgtattctctttaactatcttggtatattaaagtattatcttttatatatt 540 lillllllllllll11 lllll11 ll llllll ll111|11l liill1ll1l1 l1 lllI V.5 481 ttaattatttgtattctctttaactatcttggtatattaaagtattatcttttatatatt 540 V.1 541 tatcaatggtggacacttttataggtactctgtgtcatttttgatactgtaggtatctta 600 I IlII I III I I|i l l Iil 111111 1illlll I I I II III||| 111 I I Ill V.5 541 tatcaatggtggacacttttataggtactctgtgtcatttttgatactgtaggtatctta 600 V.1 601 tttcatttatctttattcttaatgtacgaattcataatatttgattcagaacaaatttat 660 lill|11 1 11111 11 l l l l l i llll111 llllllllllIII lllI I llI i1111 V.5 601 tttcatttatctttattcttaatgtacgaattcataatatttgattcagaacaaatttat 660 V.1 661 cactaattaacagagtgtcaattatgctaacatctcatttactgattttaatttaaaaca 720 ||lill11 1111111llll1 I 111Il|||1lil I il I 1111111l11111Ill11ill11il V.5 661 cactaattaacagagtgtcaattatgctaacatctcatttactgattttaatttaaaaca 720 V.1 : 721 gtttttgttaacatgcatgtttagggttggcttcttaataatttcttcttcctcttctct 780 I IIIIIIIII 1l|1111il II111111111||11111IlI11lil1111 V.5 : 721 gtttttgttaacatgcatgtttagggttggcttcttaataatttcttcttcctcttctct 780 V.1 : 781 ctctcctcttcttttggtcagtgttgtgcgggttaatacaacaaactgtaacaagtgtac 840 269 V.5 : 781 ctctcctcttcttttggtcagtgttgtgcgggttaatacaacaaactgtaacaagtgtac 840 V.1 : 841 ctggtatggacttgttgtccgggacgtacattttcgcggtcctgctagcatgcgtggtgt 900 lI l lll i 1 1 1 lilll l ll llill l ll l lllllllllll1 llilli1 V.5 : 841 ctggtatggacttgttgtccgggacgtacattttcgcggtcctgctagcatgcgtggtgt 900 V.1 : 901 tccactctggcgcccaggagaaaaactacaccatccgagaagaaatgccagaaaacgtcc 960 lil i I I I lI I ||II I 1 11 1 1111|1li lll ll 1!l 1111I| |||11 lilli V.5 : 901 tccactctggcgcccaggagaaaaactacaccatccgagaagaaatgccagaaaacgtcc 960 V.1 : 961 tgataggcgacttgttgaaagaccttaacttgtcgctgattccaaacaagtccttgacaa 1020 lilllll Illill ll 1 IIl|||| i11I I li iII11II l llI11 lili V.5 : 961 tgataggcgacttgttgaaagaccttaacttgtcgctgattccaaacaagtccttgacaa 1020 V.1 : 1021 ctgctatgcagttcaagctagtgtacaagaccggagatgtgccactgattcgaattgaag 1080 ||| 11 11 111111111Il11|1111111 1111111111111111 |1 1 llllli V.5 : 1021 ctgctatgcagttcaagctagtgtacaagaccggagatgtgccactgattcgaattgaag 1080 V.1 : 1081 aggatactggtgagatcttcactactggcgctcgcattgatcgtgagaaattatgtgctg 1140 I l li|| I||l i I I11 11111il 111| liilllll11111111l1ill11il1I1I1Il V.5 : 1081 aggatactggtgagatcttcactactggcgctcgcattgatcgtgagaaattatgtgctg 1140 V.1 : 1141 gtatcccaagggatgagcattgcttttatgaagtggaggttgccattttgccggatgaaa 1200 I ii I I I I I i I I I I 11l i iI II ~ii i I III Ii ii I 11 I l1 1 1 V.5 : 1141 gtatcccaagggatgagcattgcttttatgaagtggaggttgccattttgccggatgaaa 1200 V.1 : 1201 tatttagactggttaagatacgttttctgatagaagatataaatgataatgcaccattgt 1260 lll i ll lllll I1 1liilliii il111 Il llll l ll llllllll lli V.5 : 1201 tatttagactggttaagatacgttttctgatagaagatataaatgataatgcaccattgt 1260 V.1 : 1261 tcccagcaacagttatcaacatatcaattccagagaactcggctataaactctaaatata 1320 V.5 : 1261 tcccagcaacagttatcaacatatcaattccagagaactcggctataaactctaaatata 1320 V.1 : 1321 ctctcccagcggctgttgatcctgacgtaggaatsaacggagttcaaaactacgaactaa 1380 V.5 : 1321 ctctcccagcggctgttgatcctgacgtaggaataaacggagttcaaaactacgaactaa 1380 V.1 : 1381 ttaagagtcaaaacatttttggcctcgatgtcattgaaacaccagaaggagacaagatgc 1440 V.5 : 1381 ttaagagtcaaaacatttttggcctcgatgtcattgaaacaccagaaggagacaagatgc 1440 V.1 : 1441 cacaactgattgttcaaaaggagttagatagggaagagaaggatacctacgtgatgaaag 1500 V.5 : 1441 cacaactgattgttcaaaaggagttagatagggaagagaaggatacctacgtgatgaaag 1500 V.1 : 1501 taaaggttgaagatggtggctttcctcaaagatccagtactgctattttgcaagtgagtg 1560 l ll I I i ll llllllll lill l llllilll Illlllllilllll1111 l V.5 : 1501 taaaggttgaagatggtggctttcctcaaagatccagtactgctattttgcaagtgagtg 1560 V.1 : 1561 ttactgatacaaatgacaaccacccagtctttaaggagacagagattgaagtcagtatac 1620 V.5ll ll l I ll ill lllllll 111 li llllll l l illlllllll l l lll 1620 V.5 :1561 ttactgatacaaatgacaaccacccagtctttaaggagacagagattgaagtcagtatac 1620 270 V.1 : 1621 cagaaaatgctcctgtaggcacttcagtgacacagctccatgccacagatgctgacatag 1680 |||||||||111il I i lillI 111 1l I|| Ill I I I 1 |||I lil1 l ilI|||||||| V.5 : 1621 cagaaaatgctcctgtaggcacttcagtgacacagctccatgccacagatgctgacatag 1680 V.1 : 1681 gtgaaaatgccaagatccacttctctttcagcaatctagtctccaacattgccaggagat 1740 11 11 1 i 1 11 1 11 l ll l l I lllllli11l l Il 11 1 11i I 1||11lil lii i11 V.5 : 1681 gtgaaaatgccaagatccacttctctttcagcaatctagtctccaacattgccaggagat 1740 V.1 : 1741 tatttcacctcaatgccaccactggacttatcacaatcaaagaaccactggatagggaag 1800 Il IiI tlIIl| I| I III | 1 lI|| i 1 11 It||1I IIII lI ItttIl.1I l i l iI l V.5 : 1741 tatttcacctcaatgccaccactggacttatcacaatcaaagaaccactggatagggaag 1800 V.1 : 1801 aaacaccaaaccacaagttactggttttggcaagtgatggtggattgatgccagcaagag 1860 1111|11ll1l1111l1l1l1l1l I lilli|||I1ll II I 111 II I||11|||||lIl V.5 : 1801 aaacaccaaaccacaagttactggttttggcaagtgatggtggattgatgccagcaagag 1860 V.1 : 1861 caatggtgctggtaaatgttacagatgtcaatgataatgtcccatccattgacataagat 1920 |||I ll lil111ll ll l I ll|1111I1ll11 I11 llil1 lill l ll111111l1lil 1illi V.5 : 1861 caatggtgctggtaaatgttacagatgtcaatgataatgtcccatccattgacataagat 1920 V.1 : 1921 acatcgtcaatcctgtcaatgacacagttgttctttcagaaaatattccactcaacacca 1980 llillllllllllllll111lll1ll1l111ll1111l1lll1ll1l1lll11l1ll1l1l1 V.5 1921 acatcgtcaatcctgtcaatgacacagttgttctttcagaaaatattccactcaacacca 1980 V.1 1981 aaattgctctcataactgtgacggataaggatgcggaccataatggcagggtgacatgct 2040 III 11111 li I1111111|1|1111|1|| | | | | | | | | | |11 ||||||||||||||||i V.5 1981 aaattgctctcataactgtgacggataaggatgcggaccataatggcagggtgacatgct 2040 V.1 2041 tcacagatcatgaaatccctttcagattaaggccagtattcagtaatcagttcctcctgg 2100 111i I11111111I I i ii 1111 I l IIIIIii i I IiII 1111111 1 I 1I11111I111| II V.5 2041 tcacagatcatgaaatccctttcagattaaggccagtattcagtaatcagttcctcctgg 2100 V.1 2101 agactgcagcatatcttgactatgagtccacaaaagaatatgccattaaattactggctg 2160 V.5 2101 agactgcagcatatcttgactatgagtccacaaaagaatatgccattaaattactggctg 2160 V.1 2161 cagatgctggcaaacctcctttgaatcagtcagcaatgctcttcatcaaagtgaaagatg 2220 Il1 li il l i lllllllllllllllllllllll111 l1l11 lll11 l11 l11 l1 ll11 li V.5 2161 cagatgctggcaaacctcctttgaatcagtcagcaatgctcttcatcaaagtgaaagatg 2220 V.1 2221 aaaatgacaatgctccagttttcacccagtctttcgtaactgtttctattcctgagaata 2280 V.5 2221 aaaatgacaatgctccagttttcacccagtctttcgtaactgtttctattcctgagaata 2280 V.1 2281 actctcctggcatccagttgacgaaagtaagtgcaatggatgcagacagtgggcctaatg 2340 I ill111 Il 11|||I 1ll 11i 1 11I1I||11ll 1lllilll 11il 1I li l lilli lllllll V.5 2281 actctcctggcatccagttgacgaaagtaagtgcaatggatgcagacagtgggcctaatg 2340 V.1 2341 ctaagatcaattacctgctaggccctgatgctccacctgaattcagcctggattgtcgta 2400 |111Il li i l Iil l il I l ||||||I II I ll li l I 1 ll 1111 illi V.5 2341 ctaagatcaattacctgctaggccctgatgctccacctgaattcagcctggattgtcgta 2400 V.1 : 2401 caggcatgctgactgtagtgaagaaactagatagagaaaaagaggataaatatttattca 2460 11l li111111111111111 11|Itt illi I Il ililil1111|||1 111 2460 V.5 :2401 caggcatgctgactgtagtgaagaaactagatagagaaaaagaggataaatatttattca 2460 271 V.1 : 2461 caattctggcaaaagataacggggtaccacccttaaccagcaatgtcacagtctttgtaa 2520 |||||||il l ilil llil 1|||||1||||1||||l||i||||||1|1|||||||11ll V.5 : 2461 caattctggcaaaagataacggggtaccacccttaaccagcaatgtcacagtctttgtaa 2520 V.1 : 2521 gcattattgatcagaatgacaatagcccagttttcactcacaatgaatacaacttctatg 2580 l|i|i ill 11||111|11ll1|||||||| |i||||111||||1||1||1|||1|||||lil V.5 : 2521 gcattattgatcagaatgacaatagcccagttttcactcacaatgaatacaacttctatg 2580 V.1 : 2581 tcccagaaaaccttccaaggcatggtacagtaggactaatcactgtaactgatcctgatt 2640 V.5 : 2581 tcccagaaaaccttccaaggcatggtacagtaggactaatcactgtaactgatcctgatt 2640 V.1 : 2641 atggagacaattctgcagttacgctctccattttagatgagaatgatgacttcaccattg 2700 I1 I IIi |l l l il I I lilil | 1 il lii i l| 111 111|| 11||||||||| V.5 : 2641 atggagacaattctgcagttacgctctccattttagatgagaatgatgacttcaccattg 2700 V.1 : 2701 attcacaaactggtgtcatccgaccaaatatttcatttgatagagaaaaacaagaatctt 2760 I1 II 1 II l I|| | i I l IliilI11 i ||I l i l|1 |||||111 ||||1|1|||1 ||| V.5 : 2701 attcacaaactggtgtcatccgaccaaatatttcatttgatagagaaaaacaagaatctt 2760 V.1 : 2761 acactttctatgtaaaggctgaggatggtggtagagtatcacgttcttcaagtgccaaag 2820 V.5 : 2761 acactttctatgtaaaggctgaggatggtggtagagtatcacgttcttcaagtgccaaag 2820 V.1 : 2821 taaccataaatgtggttgatgtcaatgacaacaaaccagttttcattgtccctccttcca 2880 lI11II1ll Il i1 I llllllllill lillil I1111111||lIi i i| ||||| V.5 2821 taaccataaatgtggttgatgtcaatgacaacaaaccagttttcattgtccetccttcca 2880 V.1 2881 actgttcttatgaattggttctaccgtccactaatccaggcacagtggtctttcaggtaa 2940 iIl lillI iii||||1|Il1I lillil lli1l|||1|111 li1 |||11 l ll1 llilli I1 V.5 2881 actgttcttatgaattggttctaccgtccactaatccaggcacagtggtctttcaggtaa 2940 V.1 2941 ttgctgttgacaatgacactggcatgaatgcagaggttcgttacagcattgtaggaggaa 3000 i|I1II l iIl1lill I ll il i 111 I I I| 11 11|111|| il 1li l lili ll11I V.5 2941 ttgctgttgacaatgacactggcatgaatgcagaggttcgttacagcattgtaggaggaa 3000 V.1 3001 acacaagagatctgtttgcaatcgaccaagaaacaggcaacataacattgatggagaaat 3060 V.5 3001 acacaagagatctgtttgcaatcgaccaagaaacaggcaacataacattgatggagaaat 3060 V.1 3061 gtgatgttacagaccttggtttacacagagtgttggtcaaagctaatgacttaggacagc 3120 i||I IIl I iIIl~j~II 11111111|||il111 Il|111|||1||| 111ll 111il V.5 3061 gtgatgttacagaccttggtttacacagagtgttggtcaaagctaatgacttaggacagc 3120 V.1 3121 ctgattctctcttcagtgttgtaattgtcaatctgttcgtgaatgagtcggtgaccaatg 3180 1il1111illi 1||1|1|||||||||||il ||||||11 ||||1|11 |11 ||||1 ||1 1 | 11 V.5 3121 ctgattctctcttcagtgttgtaattgtcaatctgttcgtgaatgagtcggtgaccaatg 3180 V.1 : 3181 ctacactgattaatgaactggtgcgcaaaagcactgaagcaccagtgaccccaaatactg 3240 V.5 : 3181 ctacactgattaatgaactggtgcgcaaaagcactgaagcaccagtgaccccaaatactg 3240 V.1 : 3241 agatagctgatgtatcctcaccaactagtgactatgtcaagatcctggttgcagctgttg 3300 V li: 241 i I |II I |||I 1111 11 1111| I ll1 l|1 ||||||||11 ll1 1 li 3l V.5 :3241 agatagctgatgtatcctcaccaactagtgactatgtcaagatcctggttgcagctgttg 3300 272 V.1 : 3301 ctggcaccataactgtcgttgtagttattttcatcactgctgtagtaagatgtcgccagg 3360 jlllillllllllllllll 1llll Illlllilllll1111111111|||111111 V.5 : 3301 ctggcaccataactgtcgttgtagttattttcatcactgctgtagtaagatgtcgccagg 3360 V.1 : 3361 caccacaccttaaggctgctcagaaaaacaagcagaattctgaatgggctaccccaaacc 3420 l ilii l I1 1 ll iiIli l 1 Ill11 i l i|1 II i l il Illi 111 l lI111 |||1 l i V.5 3361 caccacaccttaaggctgctcagaaaaacaagcagaattctgaatgggctaccccaaacc 3420 V.1 3421 cagaaaacaggcagatgataatgatgaagaaaaagaaaaagaagaagaagcattccccta 3480 i 1 |||1 11 11 1 11 11|1||1 || 1|| || 111II|| |1 11 1 | 1 ||||||i1 ||111 I I V.5 3421 cagaaaacaggcagatgataatgatgaagaaaaagaaaaagaagaagaagcattccccta 3480 V.1 3481 agaacttgctgcttaattttgtcactattgaagaaactaaggcagatgatgttgacagtg 3540 lill Il1111I 1 1l| 1I 11ll1lill1 1111ll1 1l111ll111I i l l l l l l 111 l I I||1 V.5 3481 agaacttgctgcttaattttgtcactattgaagaaactaaggcagatgatgttgacagtg 3540 V.1 3541 atggaaacagagtcacactagaccttcctattgatctagaagagcaaacaatgggaaagt 3600 1li ii 1 ll ll li I illl lIl~l ll l ill11li lll1l1 ilill1 ll1 il 1 ||| V.5 3541 atggaaacagagtcacactagaccttcctattgatctagaagagcaaacaatgggaaagt 3600 V.1 3601 acaattgggtaactacacctactactttcaagcccgacagccctgatttggcccgacact 3660 1I11lll11l1l11ll1llliiilll1ll11l1111ll111lllll1l1llllillll1lll V.5 3601 acaattgggtaactacacctactactttcaagcccgacagccctgatttggcccgacact 3660 V.1 3661 acaaatctgcctctccacagcctgccttccaaattcagcctgaaactcccctgaattcga 3720 V.5 3661 acaaatctgcctctccacagcctgccttccaaattcagcctgaaactcccctgaattcga 3720 V.1 3721 agcaccacatcatccaagaactgcctctcgataacacctttgtggcctgtgactctatct 3780 V.5 3721 agcaccacatcatccaagaactgcctctcgataacacctttgtggcctgtgactctatct 3780 V.1 3781 ccaagtgttcctcaagcagttcagatccctacagcgtttctgactgtggctatccagtga 3840 V.5 3781 ccaagtgttcctcaagcagttcagatccctacagcgtttctgactgtggctatccagtga 3840 V.1 3841 cgaccttcgaggtacctgtgtccgtacacaccagaccg 3878 V.5 3841 cgaccttcgaggtacctgtgtccgtacacaccagaccg 3878 Table UV(d). Peptide sequences of protein coded by 109PiD4 v.5 (SEQ ID NO: 258) MDLLSGTYIF AVLLACVVFH SGAQEKNYTI REEMPENVLI GDLLKDLNLS LIPNKSLTTA 60 MQFKLVYKTG DVPLIRIEED TGEIFTTGAR IDREKLCAGI PRDEHCFYEV EVAILPDEIF 120 RLVKIRFLIE DINDNAPLFP ATVINISIPE NSAINSKYTL PAAVDPDVGI NGVQNYELIK 180 SQNIFGLDVI ETPEGDKMPQ LIVQKELDRE EKDTYVMKVK VEDGGFPQRS STAILQVSVT 240 DTNDNHPVFK ETEIEVSIPE NAPVGTSVTQ LHATDADIGE NAKIHFSFSN LVSNIARRLF 300 HLNATTGLIT IKEPLDREET PNHKLLVLAS DGGLMPARAM VLVNVTDVND NVPSIDIRYI 360 VNPVNDTVVL SENIPLNTKI ALITVTDKDA DHNGRVTCFT DHEIPFRLRP VFSNQFLLET 420 AAYLDYESTK EYAIKLLAAD AGKPPLNQSA MLFIKVKDEN DNAPVFTQSF VTVSIPENNS 480 PGIQLTKVSA MDADSGPNAK INYLLGPDAP PEFSLDCRTG MLTVVKKLDR EKEDKYLFTI 540 LAKDNGVPPL TSNVTVFVSI IDQNDNSPVF THNEYNFYVP ENLPRHGTVG LITVTDPDYG 600 DNSAVTLSIL DENDDFTIDS QTGVIRPNIS FDREKQESYT FYVKAEDGGR VSRSSSAKVT 660 INVVDVNDNK PVFIVPPSNC SYELVLPSTN PGTVVFQVIA VDNDTGMNAE VRYSIVGGNT 720 RDLFAIDQET GNITLMEKCD VTDLGLHRVL VKANDLGQPD SLFSVVIVNL FVNESVTNAT 780 LINELVRKST EAPVTPNTEI ADVSSPTSDY VKILVAAVAG TITVVVVIFI TAVVRCRQAP 840 273 HLKAAQKNKQ NSEWATPNPE NRQMIMMKKK KKKKKHSPKN LLLNFVTIEE TKADDVDSDG 900 NRVTLDLPID LEEQTMGKYN WVTTPTTFKP DSPDLARHYK SASPQPAFQI QPETPLNSKH 960 HIIQELPLDN TFVACDSISK CSSSSSDPYS VSDCGYPVTT FEVPVSVHTR PSQRRVTFHL 1020 PEGSQESSSD GGLGDHDAGS LTSTSHGLPL GYPQEEYFDR ATPSNRTEGD GNSDPESTFI 1080 PGLKKAAEIT VQPTVEEASD NCTQECLIYG HSDACWMPAS LDHSSSSQAQ ASALCHSPPL 1140 SQASTQHHSP RVTQTIALCH SPPVTQTIAL CHSPPPIQVS ALHHSPPLVQ ATALHHSPPS 1200 AQASALCYSP PLAQAAAISH SSPLPQVIAL HRSQAQSSVS LQQGWVQGAD GLCSVDQGVQ 1260 GSATSQFYTM SERLHPSDDS IKVIPLTTFT PRQQARPSRG DSPIMEEHPL 1310 Table LV(d). Amino acid sequence alignment of 109P1D4 v.1 (SEQ ID NO: 259) and 109P1D4 v.5 (SEQ ID NO: 260) Score = 2005 bits (5195), Expect = 0.0ldentities = 1011/1011 (100%), Posifives = 1011/1011 (100%) V.1 1 MDLLSGTYIFAVLLACVVFHSGAQEKNYTIREEMPENVLIGDLLKDLNLSLIPNKSLTTA 60 MDLLSGTYIFAVLLACVVFHSGAQEKNYTIREEMPENVLIGDLLKDLNLSLIPNKSLTTA V.5 1 MDLLSGTYIFAVLLACVVFHSGAQEKNYTIREEMPENVLIGDLLKDLNLSLIPNKSLTTA 60 V.1 61 MQFKLVYKTGDVPLIRIEEDTGEIFTTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIF 120 MQFKLVYKTGDVPLIRIEEDTGEIETTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIF V.5 61 MQFKLVYKTGDVPLIRIEEDTGEIFTTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIF 120 V.1 121 RLVKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIK 180 RLVKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIK V.5 121 RLVKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIK 180 V.1 181 SQNIFGLDVIETPEGDKMPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVT 240 SQNIFGLDVIETPEGDKMPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVT V.5 : 181 SQNIFGLDVIETPEGDKMPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVT 240 V.1 241 DTNDNHPVFKETEIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSFSNLVSNIARRLF 300 DTNDNHPVFKETEIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSFSNLVSNIARRLF V.5 241 DTNDNHPVFKETEIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSFSNLVSNIARRLF 300 V.1 301 HLNATTGLITIKEPLDREETPNHKLLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYI 360 HLNATTGLITIKEPLDREETPNHKLLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYI V.5 301 HLNATTGLITIKEPLDREETPNHKLLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYI 360 V.1 361 VNPVNDTVVLSENIPLNTKIALITVTDKDADHNGRVTCFTDHEIPFRLRPVFSNQFLLET 420 VNPVNDTVVLSENIPLNTKIALITVTDKDADHNGRVTCBTDHEIPFRLRPVFSNQFLLET V.5 361 VNPVNDTVVLSENIPLNTKIALITVTDKDADHNGRVTCFTDHEIPFRLRPVFSNQFLLET 420 V.1 421 AAYLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDENDNAPVFTQSFVTVSIPENNS 480 AAYLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDENDNAPVFTQSFVTVSIPENNS V.5 : 421 AAYLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDENDNAPVFTQSFVTVSIPENNS 480 V.1 : 481 PGIQLTKVSAMDADSGPNAKINYLLGPDAPPEFSLDCRTGMLTVVKKLDREKEDKYLFTI 540 PGIQLTKVSAMDADSGPNAKINYLLGPDAPPEFSLDCRTGMLTVVKKLDREKEDKYLFTI V.5 : 481 PGIQLTKVSAMDADSGPNAKINYLLGPDAPPEFSLDCRTGMLTVVKKLDREKEDKYLFTI 540 V.1 : 541 LAKDNGVPPLTSNVTVFVSIIDQNDNSPVFTHNEYNFYVPENLPRHGTVGLITVTDPDYG 600 LAKDNGVPPLTSNVTVFVSIIDQNDNSPVFTHNEYNFYVPENLPRHGTVGLITVTDPDYG V.5 : 541 LAKDNGVPPLTSNVTVFVSIIDQNDNSPVETHNEYNFYVPENLPRHGTVGLITVTDPDYG 600 V.1 : 601 DNSAVTLSILDENDDFTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVT 660 DNSAVTLSILDENDDETIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVT V.5 : 601 DNSAVTLSILDENDDFTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVT 660 V.1 : 661 INVVDVNDNKPVFIVPPSNCSYELVLPSTNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNT 720 INVVDVNDNKPVFIVPPSNCSYELVLPSTNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNT V.5 : 661 INVVDVNDNKPVFIVPPSNCSYELVLPSTNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNT 720 V.1 : 721 RDLFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPDSLFSVVIVNLFVNESVTNAT 780 RDLFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPDSLFSVVIVNLFVNESVTNAT V.5 : 721 RDLFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPDSLFSVVIVNLFVNESVTNAT 780 V.1 : 781 LINELVRKSTEAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVRCRQAP 840 LINELVRKSTEAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVRCRQAP V.5 : 781 LINELVRKSTEAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVRCRQAP 840 274 V.1 841 HLKAAQKNKQNSEWATPNPENRQMIMMKICKKKKKKKHSPKNLLLNFVTIEETKADDVDSDG 900 HLKAAQKNKQNSEWATPNPENRQMIMMKKKKKKKKHSPKNLLLNEVTIEETKADDVDSDG V.5 841 HLKAAQKNKQNSEWATPNPENRQMIMKKKKKKKKHSPKNLLLNFVTIEETKADDVDSDG 900 V.1 901 NRVTLDLPIDLEEQTMGKYNWVTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLNSKH 960 NRVTLDLPIDLEEQTMGKYNWVTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLNSKH V.5 901 NRVTLDLPIDLEEQTMGKYNWVTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLNSKH 960 V.1 961 HIIQELPLDNTFVACDSISKCSSSSSDPYSVSDCGYPVTTFEVPVSVHTRP 1011 HIIQELPLDNTFVACDSISKCSSSSSDPYSVSDCGYPVTTFEVPVSVHTRP V.5 961 HIIQELPLDNTFVACDSISKCSSSSSDPYSVSDCGYPVTTFEVPVSVHTRP 1011 Table Ul(e). Nucleotide sequence of transcript variant 109PI D4 v.6 (SEQ ID NO: 261) ggcagtcggc gaactgtctg ggcgggagga gccgtgagca gtagctgcac tcagctgccc 60 gcgcggcaaa gaggaaggca agccaaacag agtgcgcaga gtggcagtgc cagcggcgac 120 acaggcagca caggcagccc gggctgcctg aatagcctca gaaacaacct cagcgactcc 180 ggctgctctg cggactgcga gctgtggcgg tagagcccgc tacagcagtc gcagtctccg 240 tggagcgggc ggaagccttt tttctccctt tcgtttacct cttcattcta ctctaaaggc 300 atcgttatta gagggtgctt aaaaagtaca gatcaactgg atggatgaat ggatggaaga 360 ggatggaata tcttaacaaa acacattttc cttaagtaaa ttcatgcata ctccaaataa 420 aatacagaat gtgaagtatc tctgaactgt gctgttgaat atggtagcta ctagctacat 480 gaaaatcctg ttgtgaataa gaaggattcc acagatcaca taccagagcg gttttgcctc 540 agctgctctc aactttgtaa tcttgtgaag aagctgacaa gcttggctga ttgcagtgca 600 ctatgaggac tgaatgacag tgggttttaa ttcagatatt tcaagtgttg tgcgggttaa 660 tacaacaaac tgtcacaagt gtttgttgtc cgggacgtac attttcgcgg tcctgctagt 720 atgcgtggtg ttccactctg gcgcccagga gaaaaactac accatccgag aagaaattcc 780 agaaaacgtc ctgataggca acttgttgaa agaccttaac ttgtcgctga ttccaaacaa 840 gtccttgaca actactatgc agttcaagct agtgtacaag accggagatg tgccactgat 900 tcgaattgaa gaggatactg gtgagatctt cactaccggc gctcgcattg atcgtgagaa 960 attatgtgct ggtatcccaa gggatgagca ttgcttttat gaagtggagg ttgccatttt 1020 gccggatgaa atatttagac tggttaagat acgttttctg atagaagata taaatgataa 1080 tgcaccattg ttcccagcaa cagttatcaa catatcaatt ccagagaact cggctataaa 1140 ctctaaatat actctcccag cggctgttga tcctgacgta ggcataaacg gagttcaaaa 1200 ctacgaacta attaagagtc aaaacatttt tggcctcgat gtcattgaaa caccagaagg 1260 agacaagatg ccacaactga ttgttcaaaa ggagttagat agggaagaga aggataccta 1320 tgtgatgaaa gtaaaggttg aagatggtgg ctttcctcaa agatccagta ctgctatttt 1380 gcaagtaagt gttactgata caaatgacaa ccacccagtc tttaaggaga cagagattga 1440 agtcagtata ccagaaaatg ctcctgtagg cacttcagtg acacagctcc atgccacaga 1500 tgctgacata ggtgaaaatg ccaagatcca cttctctttc agcaatctag tctccaacat 1560 tgccaggaga ttatttcacc tcaatgccac cactggactt atcacaatca aagaaccact 1620 ggatagggaa gaaacaccaa accacaagtt actggttttg gcaagtgatg gtggattgat 1680 gccagcaaga gcaatggtgc tggtaaatgt tacagatgtc aatgataatg tcccatccat 1740 tgacataaga tacatcgtca atcctgtcaa tgacacagtt gttctttcag aaaatattcc 1800 actcaacacc aaaattgctc tcataactgt gacggataag gatgcggacc ataatggcag 1860 ggtgacatgc ttcacagatc atgaaattcc tttcagatta aggccagtat tcagtaatca 1920 gttcctcctg gagaatgcag catatcttga ctatgagtcc acaaaagaat atgccattaa 1980 attactggct gcagatgctg gcaaacctcc tttgaatcag tcagcaatgc tcttcatcaa 2040 agtgaaagat gaaaatgaca atgctccagt tttcacccag tctttcgtaa ctgtttctat 2100 tcctgagaat aactctcctg gcatccagtt gatgaaagta agtgcaacgg atgcagacag 2160 tgggcctaat gctgagatca attacctgct aggccctgat gctccacctg aattcagcct 2220 ggatcgtcgt acaggcatgc tgactgtagt gaagaaacta gatagagaaa aagaggataa 2280 atatttattc acaattctgg caaaagataa tggggtacca cccttaacca gcaatgtcac 2340 agtctttgta agcattattg atcagaatga caatagccca gttttcactc acaatgaata 2400 caaattctat gtcccagaaa accttccaag gcatggtaca gtaggactaa tcactgtaac 2460 tgatcctgat tatggagaca attctgcagt tacgctctcc attttagatg agaatgatga 2520 cttcaccatt gattcacaaa ctggtgtcat ccgaccaaat atttcatttg atagagaaaa 2580 acaagaatct tacactttct atgtaaaggc tgaggatggt ggtagagtat cacgttcttc 2640 aagtgccaaa gtaaccataa atgtggttga tgtcaatgac aacaaaccag ttttcattgt 2700 ccctccttac aactattctt atgaattggt tctaccgtcc actaatccag gcacagtggt 2760 ctttcaggta attgctgttg acaatgacac tggcatgaat gcagaggttc gttacagcat 2820 tgtaggagga aacacaagag atctgtttgc aatcgaccaa gaaacaggca acataacatt 2880 gatggagaaa tgtgatgtta cagaccttgg tttacacaga gtgttggtca aagctaatga 2940 275 cttaggacag cctgattctc tcttcagtgt tgtaattgtc aatctgttcg tgaatgagtc 3000 agtgaccaat gctacactga ttaatgaact ggtgcgcaaa agcattgaag caccagtgac 3060 cccaaatact gagatagctg atgtatcctc accaactagt gactatgtca agatcctggt 3120 tgcagctgtt gctggcacca taactgtcgt tgtagttatt ttcatcactg ctgtagtaag 3180 atgtcgccag gcaccacacc ttaaggctgc tcagaaaaac atgcagaatt ctgaatgggc 3240 taccccaaac ccagaaaaca ggcagatgat aatgatgaag aaaaagaaaa agaagaagaa 3300 gcattcccct aagaacctgc tgcttaattt tgtcactatt gaagaaacta aggcagatga 3360 tgttgacagt gatggaaaca gagtcacact agaccttcct attgatctag aagagcaaac 3420 aatgggaaag tacaattggg taactacacc tactactttc aagcctgaca gccctgattt 3480 ggcccgacac tacaaatctg cctctccaca gcctgccttc caaattcagc ctgaaactcc 3540 cctgaatttg aagcaccaca tcatccaaga actgcctctc gataacacct ttgtggcctg 3600 tgactctatc tccaagtgtt cctcaagcag ttcagatccc tacagcgttt ctgactgtgg 3660 ctatccagtg acaaccttcg aggtacctgt gtccgtacac accagaccga ctgattccag 3720 gacatgaact attgaaatct gcagtgagat gtaactttct aggaacaaca aaattccatt 3780 ccccttccaa aaaatttcaa tggattgtga tttcaaaatt aggctaagat cattaatttt 3840 gtaatctaga tttcccatta taaaagcaag caaaaatcat cttaaaaatg atgtcctagt 3900 gaaccttgtg ctttctttag ctgtaatctg gcaatggaaa tttaaaattt atggaagaga 3960 cagtgcagca caataacaga gtactctcat gctgtttctc tgtttgctct gaatcaacag 4020 ccatgatgta atataaggct gtcttggtgt atacacttat ggttaatata tcagtcatga 4080 aacatgcaat tacttgccct gtctgattgt tgaataatta aaacattatc ttccaggagt 4140 ttggaagtga gctgaactag ccaaactact ctctgaaagg tatccagggc aagagacatt 4200 tttaagaccc caaacaaaca aaaaacaaaa ccaaaacact ctggttcagt gttttgaaaa 4260 tattcactaa cataatattg ctgagaaaat catttttatt acccaccact ctgcttaaaa 4320 gttgagtggg ccgggcgcgg tggctcacgc ctgtaatccc agcactttgg gaggccgagg 4380 cgggtggatc acgaggtcag gagattgaga ccatcctggc taacacggtg aaaccccatc 4440 tccactaaaa atacaaaaaa ttagcctggc gtggtggcgg gcgcctgtag tcccagctac 4500 tcgggaggct gaggcaggag aatagcgtga acccgggagg cggagcttgc agtgagccga 4560 gatggcgcca ctctgcactc cagcctgggt gacagagcaa gactctgtct caaaaagaaa 4620 aaaatgttca atgatagaaa ataattttac taggttttta tgttgattgt actcatggtg 4680 ttccactcct tttaattatt aaaaagttat ttttggggtg ggtgtggtgg ctcacaccgt 4740 aatcccagca ctttgggagg ccgaggtggg tggatcacct gaggtcagga gttcaagacc 4800 agtntggcca acatggcgaa accccgtttt 4830 Table Ull(e). Nucleotide sequence alignment of 109PiD4 v.1 (SEQ ID NO: 262) and 109P1D4 v.6 (SEQ ID NO: 263) Score = 5676 bits (2952), Expect = 0.0ldentites = 3002/3027 (99%) Strand = Plus / Plus V.1 852 ttgttgtccgggacgtacattttcgcggtcctgctagcatgcgtggtgttccactctggc 911 1|111 l 1||111 l 1111I Il 111111111 11| 1Il lI 111 l|11 I 1111 llil V.6 683 ttgttgtccgggacgtacattttcgcggtcctgctagtatgcgtggtgttccactctggc 742 V.1 912 gcccaggagaaaaactacaccatccgagaagaaatgccagaaaacgtcctgataggcgac 971 111111111111111111l11l1111Il IllII1llil li I I l l1111 1 111I | V.6 743 gcccaggagaaaaactacaccatccgagaagaaattccagaaaacgtcctgataggcaac 802 V.1 972 ttgttgaaagaccttaacttgtcgctgattccaaacaagtccttgacaactgctatgcag 1031 lllllIllllllIlIll11lllllllll111|||||I|| 1i111lli V.6 803 ttgttgaaagaccttaacttgtcgctgattccaaacaagtccttgacaactactatgcag 862 V.1 1032 ttcaagctagtgtacaagaccggagatgtgccactgattcgaattgaagaggatactggt 1091 I lil il llll|||I111 Ill l iiI I I 11| lil lili 11I I 1llll 11ll 1ll1 I1ll V.6 863 ttcaagctagtgtacaagaccggagatgtgccactgattcgaattgaagaggatactggt 922 V.1 1092 gagatcttcactactggcgctcgcattgatcgtgagaaattatgtgctggtatcccaagg 1151 11ill1111ill11 1111 il11111 ll1I1ll11111111l|1 lillil 11||1111Ili V.6 923 gagatcttcactaccggcgctcgcattgatcgtgagaaattatgtgctggtatcccaagg 982 V.1 1152 gatgagcattgcttttatgaagtggaggttgccattttgccggatgaaatatttagactg 1211 V.llilll l illllll 1I1 IIlIII illllll I lllllll l1ItlIl lll 1 4 V. 6 :983 gatgagcattgcttttatgaagtggaggttgccattttgccggatgaaatatttagactg 1042 276 V.1 : 1212 gttaagatacgttttctgatagaagatataaatgataatgcaccattgttcccagcaaca 1271 ||I1Il|11l ill Il111 il Ii l I 1 11 1 11 1 11111111111|| l| II lI l i lll V.6 : 1043 gttaagatacgttttctgatagaagatataaatgataatgcaccattgttcccagcaaca 1102 V.1 : 1272 gttatcaacatatcaattccagagaactcggctataaactctaaatatactctcccagcg 1331 It lilt il I l ill Ill l il11tIll 1 il llll ltI ll| I | lil Ilil lilll I V.6 : 1103 gttatcaacatatcaattccagagaactcggctataaactctaaatatactctcccagcg 1162 V.1 : 1332 gctgttgatcctgacgtaggaataaacggagttcaaaactacgaactaattaagagtcaa 1391 lilll111l11111l11l11 lill11lllll1l1lilllllll1lllllilllllll11i V.6 : 1163 gctgttgatcctgacgtaggcataaacggagttcaaaactacgaactaattaagagtcaa 1222 V.1 : 1392 aacatttttggcctcgatgtcattgaaacaccagaaggagacaagatgccacaactgatt 1451 lit lilliII| Itil 1 1111|lil l lll11lillll 1 I II IIlil illi Illli V.6 : 1223 aacatttttggcctcgatgtcattgaaacaccagaaggagacaagatgccacaactgatt 1282 V.1 : 1452 gttcaaaaggagttagatagggaagagaaggatacctacgtgatgaaagtaaaggttgaa 1511 t illllllllllllIttl iIlllll l il l lllt 11 111lllllll11llll1 lll i V.6 : 1283 gttcaaaaggagttagatagggaagagaaggatacctatgtgatgaaagtaaaggttgaa 1342 V.1 : 1512 gatggtggctttcctcaaagatccagtactgctattttgcaagtgagtgttactgataca 1571 lilllllllllllllllllllllllllllllllllllI lll111 i liilllll li ii V.6 : 1343 gatggtggctttcctcaaagatccagtactgctattttgcaagtaagtgttactgataca 1402 V.1 : 1572 aatgacaaccacccagtctttaaggagacagagattgaagtcagtataccagaaaatgct 1631 V.6 : 1403 aatgacaaccacccagtctttaaggagacagagattgaagtcagtataccagaaaatgct 1462 V.1 1632 cctgtaggcacttcagtgacacagctccatgccacagatgctgacataggtgaaaatgcc 1691 V.6 1463 cctgtaggcacttcagtgacacagctccatgccacagatgctgacataggtgaaaatgcc 1522 V.1 1692 aagatccacttctctttcagcaatctagtctccaacattgccaggagattatttcacctc 1751 V.6 1523 aagatccacttctctttcagcaatctagtctccaacattgccaggagattatttcacctc 1582 V.1 1752 aatgccaccactggacttatcacaatcaaagaaccactggatagggaagaaacaccaaac 1811 11111111111111111|| lllllilllllllllll Illll1l1ll1illl1lll1ll11 V.6 : 1583 aatgccaccactggacttatcacaatcaaagaaccactggatagggaagaaacaccaaac 1642 V.1 : 1812 cacaagttactggttttggcaagtgatggtggattgatgccagcaagagcaatggtgctg 1871 V.6 : 1643 cacaagttactggttttggcaagtgatggtggattgatgccagcaagagcaatggtgctg 1702 V.1 1872 gtaaatgttacagatgtcaatgataatgtcccatccattgacataagatacatcgtcaat 1931 11l1i111ll11l11l1l11l11l11l11l11ll ltllllllllllll111lll1l1l V.6 1703 gtaaatgttacagatgtcaatgataatgtcccatccattgacataagatacatcgtcaat 1762 V.1 1932 cctgtcaatgacacagttgttctttcagaaaatattccactcaacaccaaaattgctctc 1991 tillllllll11ll1lllll1ll1lll11l11lllll1ll1l11ll11111111111|11|11 V.6 1763 cctgtcaatgacacagttgttctttcagaaaatattccactcaacaccaaaattgctctc 1822 V.1 1992 ataactgtgacggataaggatgcggaccataatggcagggtgacatgcttcacagatcat 2051 11111111111llll111 1lll 11lll 11ll li li llllilllii 277 V.6 1823 ataactgtgacggataaggatgcggaccataatggcagggtgacatgcttcacagatcat 1882 V.1 2052 gaaatccctttcagattaaggccagtattcagtaatcagttcctcctggagactgcagca 2111 V.6 1883 gaaattcctttcagattaaggccagtattcagtaatcagttcctcctggagaatgcagca 1942 V.1 2112 tatcttgactatgagtccacaaaagaatatgccattaaattactggtgcagatgctggc 2171 liiill lll l lll lll l l ill iillll 1llll llllill1 lillll lllll V.6 1943 tatcttgactatgagtccacaaaagaatatgccattaaattactggtgcagatgctggc 2002 V.1 2172 aaacctcctttgaatcagtcagcaatgctcttcatcaaagtgaaagatgaaaatgacaat 2231 1111lilli1i 111 Ili I lill|||||li11Il11 I I11||1|||i illilllI1illi V.6 2003 aaacctcctttgaatcagtcagcaatgctcttcatcaaagtgaaagatgaaaatgacaat 2062 V.1 2232 gctccagttttcacccagtctttcgtaactgtttctattcctgagaataactctcctggc 2291 I lll I l l i ll II l li 11 1 1i 1 1 1 1 l il i l illllil I1I||I l lilil 1illi V.6 2063 gctccagttttcacccagtctttcgtaactgtttctattcctgagaataactctcctggc 2122 V.1 2292 atccagttgacgaaagtaagtgcaatggatgcagacagtgggcctaatgctaagatcaat 2351 I lilli I I il li II III I i 11 li l i l li1|I li I l I I Ili l lil11 l i V.6 2123 atccagttgatgaaagtaagtgcaacggatgcagacagtgggcctaatgctgagatcaat 2182 V.1 2352 tacctgctaggccctgatgctccacctgaattcagcctggattgtcgtacaggcatgctg 2411 1ill1l11111111I1l I I 111111 11|||Ill1111 llil I lI I lli ll1111 lilll1 V.6 2183 tacctgctaggccctgatgctccacctgaattcagcctggatcgtcgtacaggcatgctg 2242 V.1 2412 actgtagtgaagaaactagatagagaaaaagaggataaatatttattcacaattctggca 2471 II I|I I I || 1 I ||II 11I I I I lI I I I I 11||I I1Ill1lillll|||| V.6 2243 actgtagtgaagaaactagatagagaaaaagaggataaatatttattcacaattctggca 2302 V.1 2472 aaagataacggggtaccaccttaaccagcaatgtcacagtctttgtaagcattattgat 2531 111111! l 111I 1l111111111l1ll1ll11lil11lil1111i I 1il I 11ill 11ilil V.6 2303 aaagataatggggtaccacccttaaccagcaatgtcacagtctttgtaagcattattgat 2362 V.1 2532 cagaatgacaatagcccagttttcactcacaatgaatacaacttctatgtcccagaaaac 2591 liillll lil lill lll11l11l1l1llllilllll1 IllllllIIIllilllli V.6 2363 cagaatgacaatagcccagttttcactcacaatgaatacaaattctatgtcccagaaaac 2422 V.1 2592 cttccaaggcatggtacagtaggactaatcactgtaactgatcctgattatggagacaat 2651 V.6 : 2423 cttccaaggcatggtacagtaggactaatcactgtaactgatcctgattatggagacaat 2482 V.1 : 2652 tctgcagttacgctctccattttagatgagaatgatgacttcaccattgattcacaaact 2711 |I1lI||1 I11 I I1I i | l l l l lIlI l I1l I llII I lill111ll1l ll11il lill V.6 : 2483 tctgcagttacgctctccattttagatgagaatgatgacttcaccattgattcacaaact 2542 V.1 : 2712 ggtgtcatccgaccaaatatttcatttgatagagaaaaacaagaatcttacactttctat 2771 lilllll liliilll1111111l111111l1l11l11ll1lll1111ll1lll111l1 V.6 : 2543 ggtgtcatccgaccaaatatttcatttgatagagaaaaacaagaatcttacactttctat 2602 V.1 : 2772 gtaaaggctgaggatggtggtagagtatcacgttcttcaagtgccaaagtaaccataaat 2831 1I| 1Iil I I111111 I 1 ill l illllll 11i 1 li il 111111111ll1111ill1 V. : 2603 gtaaaggctgaggatggtggtagagtatcacgttcttcaagtgccaaagtaaccataaat 2662 V.1 : 2832 gtggttgatgtcaatgacaacaaaccagttttcattgtccctccttccaactgttcttat 2891 278 I I l 11 I II I I I I | 1 || | | | 1 II i I I I I I i I I11 l i l II 1 V..6 2663 gtggttgatgtcaatgacaacaaaccagttttcattgtccctccttacaactattcttat 2722 V.1 2892 gaattggttctaccgtccactaatccaggcacagtggtctttcaggtaattgctgttgac 2951 lllllilll1llllll1|11|111111|ill lllllllllllllli I V.6 2723 gaattggttctaccgtccactaatccaggcacagtggtctttcaggtaattgctgttgac 2782 V.1 2952 aatgacactggcatgaatgcagaggttcgttacagcattgtaggaggaaacacaagagat 3011 V.6 2783 aatgacactggcatgaatgcagaggttcgttacagcattgtaggaggaaacacaagagat 2842 V.1 3012 ctgtttgcaatcgaccaagaaacaggcaacataacattgatggagaaatgtgatgttaca 3071 lI 11i lillllllll il i llI 1l IIl lllll lll lll llll1ll V.6 2843 ctgtttgcaatcgaccaagaaacaggcaacataacattgatggagaaatgtgatgttaca 2902 V.1 3072 gaccttggtttacacagagtgttggtcaaagctaatgacttaggacagcctgattctctc 3131 lillIIli l i lii 1 111 11 l I|||1111II11il 1llil I1ill1 lil11 I1l1I|| V.6 2903 gaccttggtttacacagagtgttggtcaaagctaatgacttaggacagcctgattctctc 2962 V.1 3132 ttcagtgttgtaattgtcaatctgttcgtgaatgagtcggtgaccaatgctacactgatt 3191 V.6 2963 ttcagtgttgtaattgtcaatctgttcgtgaatgagtcagtgaccaatgctacactgatt 3022 V.1 3192 aatgaactggtgcgcaaaagcactgaagcaccagtgaccccaaatactgagatagctgat 3251 lillil llllll lll ll i Ill11 illllillllll1 llll I1llllllll 111111 V.6 3023 aatgaactggtgcgcaaaagcattgaagcaccagtgaccccaaatactgagatagctgat 3082 V.1 3252 gtatcctcaccaactagtgactatgtcaagatcctggttgcagctgttgctggcaccata 3311 lIllllllllil l lilll lillillilllllilli liiillll1111I1I 111111 V.6 3083 gtatcctcaccaactagtgactatgtcaagatcctggttgcagctgttgctggcaccata 3142 V.1 3312 actgtcgttgtagttattttcatcactgctgtagtaagatgtcgccaggcaccacacctt 3371 V.6 3143 actgtcgttgtagttattttcatcactgctgtagtaagatgtcgccaggcaccacacctt 3202 V.1 3372 aaggctgctcagaaaaacaagcagaattctgaatgggctaccccaaacccagaaaacagg 3431 Illlllll11 l l1111 |i 1l1 11i lill li ll lllllll111 ll111 l ll V.6 3203 aaggctgctcagaaaaacatgcagaattctgaatgggctaccccaaacccagaaaacagg 3262 V.1 3432 cagatgataatgatgaagaaaaagaaaaagaagaagaagcattcccctaagaacttgctg 3491 lill! I l lll Il IIIIIIIIIIIII li ll ll l l l ll l ll l l l ll l 1ill V.6 3263 cagatgataatgatgaagaaaaagaaaaagaagaagaagcattcccctaagaacctgctg 3322 V.1 3492 cttaattttgtcactattgaagaaactaaggcagatgatgttgacagtgatggaaacaga 3551 11||11111liii I11|11111 Illii llillillll illl lllll llll11Ill1l V.6 3323 cttaattttgtcactattgaagaaactaaggcagatgatgttgacagtgatggaaacaga 3382 V.1 3552 gtcacactagaccttcctattgatctagaagagcaaacaatgggaaagtacaattgggta 3611 lIIIIIlll llII l l llll1111111 l l111 1111 l11 il|||||| V.6 : 3383 gtcacactagaccttcctattgatctagaagagcaaacaatgggaaagtacaattgggta 3442 V.1 : 3612 actacacctactactttcaagcccgacagccctgatttggcccgacactacaaatctgcc 3671 V.6 : 3443 actacacctactactttcaagcctgacagccctgatttggcccgacactacaaatctgcc 3502 279 V.1 : 3672 tctccacagcctgccttccaaattcagcctgaaactcccctgaattcgaagcaccacatc 3731 l ill l l l lll ll I 11 1 1 l i ll i l i ll i111 I l illl l1llll V.6 : 3503 tctccacagcctgccttccaaattcagcctgaaactcccctgaatttgaagcaccacatc 3562 V.1 : 3732 atccaagaactgcctctcgataacacctttgtggcctgtgactctatctccaagtgttcc 3791 Ill11111Ill 111illl1l11l1l1 1I111111 lI l lIl l l||i1Ililll 111 li | Il V.6 : 3563 atccaagaactgcctctcgataacacctttgtggcctgtgactctatctccaagtgttcc 3622 V.1 : 3792 tcaagcagttcagatccctacagcgtttctgactgtggctatccagtgacgaccttcgag 3851 V.6 : 3623 tcaagcagttcagatccctacagcgtttctgactgtggctatccagtgacaaccttcgag 3682 V.1 : 3852 gtacctgtgtccgtacacaccagaccg 3878 V.6 : 3683 gtacctgtgtccgtacacaccagaccg 3709 Table LIV(e). Peptide sequences of protein coded by 109P1D4 v.6 (SEQ ID NO: 264) MTVGFNSDIS SVVRVNTTNC HKCLLSGTYI FAVLLVCVVF HSGAQEKNYT IREEIPENVL 60 IGNLLKDLNL SLIPNKSLTT TMQFKLVYKT GDVPLIRIEE DTGEIFTTGA RIDREKLCAG 120 IPRDEHCFYE VEVAILPDEI FRLVKIRFLI EDINDNAPLF PATVINISIP ENSAINSKYT 180 LPAAVDPDVG INGVQNYELI KSQNIFGLDV IETPEGDKMP QLIVQKELDR EEKDTYVMKV 240 KVEDGGFPQR SSTAILQVSV TDTNDNHPVF KETEIEVSIP ENAPVGTSVT QLHATDADIG 300 ENAKIHFSFS NLVSNIARRL FHLNATTGLI TIKEPLDREE TPNHKLLVLA SDGGLMPARA 360 MVLVNVTDVN DNVPSIDIRY IVNPVNDTVV LSENIPLNTK IALITVTDKD ADHNGRVTCF 420 TDHEIPFRLR PVFSNQFLLE NAAYLDYEST KEYAIKLLAA DAGKPPLNQS AMLFIKVKDE 480 NDNAPVFTQS FVTVSIPENN SPGIQLMKVS ATDADSGPNA EINYLLGPDA PPEFSLDRRT 540 GMLTVVKKLD REKEDKYLFT ILAKDNGVPP LTSNVTVFVS IIDQNDNSPV FTHNEYKFYV 600 PENLPRHGTV GLITVTDPDY GDNSAVTLSI LDENDDFTID SQTGVIRPNI SFDREKQESY 660 TFYVKAEDGG RVSRSSSAKV TINVVDVNDN KPVFIVPPYN YSYELVLPST NPGTVVFQVI 720 AVDNDTGMNA EVRYSIVGGN TRDLFAIDQE TGNITLMEKC DVTDLGLHRV LVKANDLGQP 780 DSLFSVVIVN LFVNESVTNA TLINELVRKS IEAPVTPNTE IADVSSPTSD YVKILVAAVA 840 GTITVVVVIF ITAVVRCRQA PHLKAAQKNM QNSEWATPNP ENRQMIMMKK KKKKKKHSPK 900 NLLLNFVTIE ETKADDVDSD GNRVTLDLPI DLEEQTMGKY NWVTTPTTFK PDSPDLARHY 960 KSASPQPAFQ IQPETPLNLK HHIIQELPLD NTFVACDSIS KCSSSSSDPY SVSDCGYPVT 1020 TFEVPVSVHT RPTDSRT 1037 Table LV(e). Amino acid sequence alignment of 109P1D4 v.1 (SEQ ID NO: 265) and 109P1D4 v.6 (SEQ ID NO: 266) Score = 1966 bits (5093), Expect = 0.01dentities = 994/1009 (98%), Positives = 997/1009 (98%) V.1 3 LLSGTYIFAVLLACVVFHSGAQEKNYTIREEMPENVLIGDLLKDLNLSLIPNKSLTTAMQ 62 LLSGTYIFAVLL CVVFHSGAQEKNYTIREE+PENVLIG+LLKDLNLSLIPNKSLTT MQ V.6 24 LLSGTYIFAVLLVCVVFHSGAQEKNYTIREEIPENVLIGNLLKDLNLSLIPNKSLTTTMQ 83 V.1 63 FKLVYKTGDVPLIRIEEDTGEIFTTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIFRL 122 FKLVYKTGDVPLIRIEEDTGEIFTTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIFRL V.6 84 FKLVYKTGDVPLIRIEEDTGEIFTTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIFRL 143 V.1 123 VKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIKSQ 182 VKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIKSQ V.6 : 144 VKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIKSQ 203 V.1 183 NIFGLDVIETPEGDKMPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVTDT 242 NIFGLDVIETPEGDKMPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVTDT V.6 204 NIFGLDVIETPEGDKMPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVTDT 263 V.1 243 NDNHPVEKETEIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSFSNLVSNIARRLFHL 302 NDNHPVFKETEIEVSIPENAPVGTSVTOLHATDADIGENAKIHFSFSNLVSNIARRLFHL V.6 264 NDNHPVFKETEIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSFSNLVSNIARRLFHL 323 V.1 : 303 NATTGLITIKEPLDREETPNHKLLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYIVN 362 NATTGLITIKEPLDREETPNHKLLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYIVN V.6 324 NATTGLITIKEPLDREETPNHKLLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYIVN 383 280 V.1 363 PVNDTVVLSENIPLNTKIALITVTDKDADHINGRVTCFTDHEIPFRLRPVFSNQFLLETAA 422 PVNDTVVLSENIPLNTKIALITVTDKDADHNGRVTCFTDHEIPFRLRPVFSNQFLLE AA V.6 384 PVNDTVVLSENIPLNTKIALITVTDKDADHNGRVTCFTDHEIPFRLRPVFSNQFLLENAA 443 V.1 423 YLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDENDNAPVFTQSFVTVSIPENNSPG 482 YLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDENDNAPVFTQSFVTVSIPENNSPG V.6 444 YLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDENDNAPVFTQSFVTVSIPENNSPG 503 V.1 483 IQLTKVSAMDADSGPNAKINYLLGPDAPPEFSLDCRTGMLTVVKKLDREKEDKYLETILA 542 IQL KVSA DADSGPNA+INYLLGPDAPPEFSLD RTGMLTVVKKLDREKEDKYLFTILA V.6 504 IQLMKVSATDADSGPNAEINYLLGPDAPPEFSLDRRTGMLTVVKKLDREKEDKYLFTILA 563 V.1 543 KDNGVPPLTSNVTVFVSIIDQNDNSPVETHNEYNFYVPENLPRHGTVGLITVTDPDYGDN 602 KDNGVPPLTSNVTVFVSIIDQNDNSPVFTHNEY FYVPENLPRHGTVGLITVTDPDYGDN V.6 564 KDNGVPPLTSNVTVFVSIIDQNDNSPVETHNEYKFYVPENLPRHGTVGLITVTDPDYGDN 623 V.1 603 SAVTLSILDENDDFTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVTIN 662 SAVTLSILDENDDFTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVTIN V.6 624 SAVTLSILDENDDFrIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVTIN 683 V.1 663 VVDVNDNKPVFIVPPSNCSYELVLPSTNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNTRD 722 VVDVNDNKPVFIVPP N SYELVLPSTNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNTRD V.6 684 VVDVNDNKPVFIVPPYNYSYELVLPSTNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNTRD 743 V.1 723 LFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPDSLFSVVIVNLFVNESVTNATLI 782 LFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPDSLFSVVIVNLFVNESVTNATLI V.6 744 LFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPDSLFSVVIVNLFVNESVTNATLI 803 V.1 783 NELVRKSTEAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVRCRQAPHL 842 NELVRKS EAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVRCRQAPHL V.6 804 NELVRKSIEAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVRCRQAPHL 863 V.1 843 KAAQKNKQNSEWATPNPENRQMIMMKKKKKKKKHSPKNLLLNFVTIEETKADDVDSDGNR 902 KAAQKN QNSEWATPNPENRQMIMMKKKKKKKKHSPKNLLLNFVTIEETKADDVDSDGNR V.6 : 864 KAAQKNMQNSEWATPNPENRQMIMMKKKKKKKKHSPKNLLLNFVTIEETKADDVDSDGNR 923 V.1 : 903 VTLDLPIDLEEQTMGKYNWVTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLNSKHI 962 VTLDLPIDLEEQTMGKYNWVTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLN KHHI V.6 : 924 VTLDLPIDLEEQTMGKYNWVTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLNLKHHI 983 V.1 : 963 IQELPLDNTFVACDSISKCSSSSSDPYSVSDCGYPVTTFEVPVSVHTRP 1011 IQELPLDNTFVACDSISKCSSSSSDPYSVSDCGYPVTTFEVPVSVHTRP V.6 : 984 IQELPLDNTFVACDSISKCSSSSSDPYSVSDCGYPVTTFEVPVSVHTRP 1032 Table 111(f). Nucleotide sequence of transcript variant 109PiD4 v.7 (SEQ ID NO: 267) ggtggtccag tacctccaaa gatatggaat acactcctga aatatcctga aacctttttt 60 ttttcagaat cctttaataa gcagttatgt caatctgaaa gttgcttact tgtactttat 120 attaatagct attcttgttt ttcttatcca aagaaaaatc ctctaatccc cttttcacat 180 gatagttgtt accatgttta ggcgttagtc acatcaaccc ctctcctctc ccaaacttct 240 cttcttcaaa tcaaacttta ttagtccctc ctttataatg attccttgcc tccttttatc 300 cagatcaatt ttttttcact ttgatgccca gagctgaaga aatggactat tgtataaatt 360 attcattgcc aagagaataa ttgcatttta aacccatgtt ataacaaaga ataatgatta 420 tattttgtga tttgtaacaa atacccttta ttttccctta actattgaat taaatatttt 480 aattatttgt attctcttta actatcttgg tatattaaag tattatcttt tatatattta 540 tcaatggtgg acacttttat aggtactctg tgtcattttt gatactgtag gtatcttatt 600 tcatttatct ttattcttaa tgtacgaatt cataatattt gattcagaac agatttatca 660 ctaattaaca gagtgtcaat tatgctaaca tctcatttac tgattttaat ttaaaacagt 720 ttttgttaac atgcatgttt agggttggct tcttaataat ttcttcttcc tcttctctct 780 ctcctcttct tttggtcagt gttgtgcggg ttaatacaac aaactgtcac aagtgtttgt 840 tgtccgggac gtacattttc gcggtcctgc tagtatgcgt ggtgttccac tctggcgccc 900 aggagaaaaa ctacaccatc cgagaagaaa ttccagaaaa cgtcctgata ggcaacttgt 960 tgaaagacct taacttgtcg ctgattccaa acaagtcctt gacaactact atgcagttca 1020 agctagtgta caagaccgga gatgtgccac tgattcgaat tgaagaggat actggtgaga 1080 tcttcactac -cggcgctcgc attgatcgtg agaaattatg tgctggtatc ccaagggatg 1140 agcattgctt ttatgaagtg gaggttgcca ttttgccgga tgaaatattt agactggtta 1200 agatacgttt tctgatagaa gatataaatg ataatgcacc attgttccca gcaacagtta 1260 281 tcaacatatc aattccagag aactcggcta taaactctaa atatactctc ccagcggctg 1320 ttgatcctga cgtaggcata aacggagttc aaaactacga actaattaag agtcaaaaca 1380 tttttggcct cgatgtcatt gaaacaccag aaggagacaa gatgccacaa ctgattgttc 1440 aaaaggagtt agatagggaa gagaaggata cctatgtgat gaaagtaaag gttgaagatg 1500 gtggctttcc toaaagatcc agtactgcta ttttgcaagt aagtgttact gatacaaatg 1560 acaaccaccc agtctttaag gagacagaga ttgaagtcag tataccagaa aatgctcctg 1620 taggcacttc agtgacacag ctccatgcca cagatgctga cataggtgaa aatgccaaga 1680 tccacttctc tttcagcaat ctagtctcca acattgccag gagattattt cacctcaatg 1740 ccaccactgg acttatcaca atcaaagaac cactggatag ggaagaaaca ccaaaccaca 1800 agttactggt tttggcaagt gatggtggat tgatgccagc aagagcaatg gtgctggtaa 1860 atgttacaga tgtcaatgat aatgtcccat ccattgacat aagatacatc gtcaatcctg 1920 tcaatgacac agttgttctt tcagaaaata ttccactcaa caccaaaatt gctctcataa 1980 ctgtgacgga taaggatgcg gaccataatg gcagggtgac atgcttcaca gatcatgaaa 2040 ttcctttcag attaaggcca gtattcagta atcagttcct cctggagaat gcagcatatc 2100 ttgactatga gtccacaaaa gaatatgcca ttaaattact ggctgcagat gctggcaaac 2160 ctcctttgaa tcagtcagca atgctcttca tcaaagtgaa agatgaaaat gacaatgctc 2220 cagttttcac ccagtctttc gtaactgttt ctattcctga gaataactct cctggcatcc 2280 agttgatgaa agtaagtgca acggatgcag acagtgggcc taatgctgag atcaattacc 2340 tgctaggccc tgatgctcca cctgaattca gcctggatcg tcgtacaggc atgctgactg 2400 tagtgaagaa actagataga gaaaaagagg ataaatattt attcacaatt ctggcaaaag 2460 ataatggggt accaccctta accagcaatg tcacagtctt tgtaagcatt attgatcaga 2520 atgacaatag cccagttttc actcacaatg aatacaaatt ctatgtccca gaaaaccttc 2580 caaggcatgg tacagtagga ctaatcactg taactgatcc tgattatgga gacaattctg 2640 cagttacgct ctccatttta gatgagaatg atgacttcac cattgattca caaactggtg 2700 tcatccgacc aaatatttca tttgatagag aaaaacaaga atcttacact ttctatgtaa 2760 aggctgagga tggtggtaga gtatcacgtt cttcaagtgc caaagtaacc ataaatgtgg 2820 ttgatgtcaa tgacaacaaa ccagttttca ttgtccctcc ttacaactat tcttatgaat 2880 tggttctacc gtccactaat ccaggcacag tggtctttca ggtaattgct gttgacaatg 2940 acactggcat gaatgcagag gttcgttaca gcattgtagg aggaaacaca agagatctgt 3000 ttgcaatcga ccaagaaaca ggcaacataa cattgatgga gaaatgtgat gttacagacc 3060 ttggtttaca cagagtgttg gtcaaagcta atgacttagg acagcctgat tctctcttca 3120 gtgttgtaat tgtcaatctg ttcgtgaatg agtcagtgac caatgctaca ctgattaatg 3180 aactggtgcg caaaagcatt gaagcaccag tgaccccaaa tactgagata gctgatgtat 3240 cctcaccaac tagtgactat gtcaagatcc tggttgcagc tgttgctggc accataactg 3300 tcgttgtagt tattttcatc actgctgtag taagatgtcg ccaggcacca caccttaagg 3360 ctgctcagaa aaacatgcag aattctgaat gggctacccc aaacccagaa aacaggcaga 3420 tgataatgat gaagaaaaag aaaaagaaga agaagcattc ccctaagaac ctgctgctta 3480 atgttgtcac tattgaagaa actaaggcag atgatgttga cagtgatgga aacagagtca 3540 cactagacct tcctattgat ctagaagagc aaacaatggg aaagtacaat tgggtaacta 3600 cacctactac tttcaagcct gacagccctg atttggcccg acactacaaa tctgcctctc 3660 cacagcctgc cttccaaatt cagcctgaaa ctcccctgaa tttgaagcac cacatcatcc 3720 aagaactgcc tctcgataac acctttgtgg cctgtgactc tatctccaat tgttcctcaa 3780 gcagttcaga tccctacagc gtttctgact gtggctatcc agtgacaacc ttcgaggtac 3840 ctgtgtccgt acacaccaga ccgactgatt ccaggacatg aactattgaa atctgcagtg 3900 agatgtaact ttctaggaac aacaaaattc cattcccctt ccaaaaaatt tcaatgattg 3960 tgatttcaaa attaggctaa gatcattaat tttgtaatct agatttccca ttataaaagc 4020 aagcaaaaat catcttaaaa atgatgtcct agtgaacctt gtgctttctt tagctgtaat 4080 ctggcaatgg aaatttaaaa tttatggaag agacagtgca gcgcaataac agagtactct 4140 catgctgttt ctctgtttgc tctgaatcaa cagccatgat gtaatataag gctgtcttgg 4200 tgtatacact tatggttaat atatcagtca tgaaacatgc aattacttgc cctgtctgat 4260 tgttgaataa ttaaaacatt atctccagga gtttggaagt gagctgaact agccaaacta 4320 ctctctgaaa ggtatccagg gcaagagaca tttttaagac cccaaacaaa caaaaaacaa 4380 aaccaaaaca ctctggttca gtgttttgaa aatattgact aacataatat tgctgagaaa 4440 atcattttta ttacccacca ctctgcttaa aagttgagtg ggccgggcgc ggtggctcac 4500 gcctgtaatt ccagcacttt gggaggccga ggcgggtgga tcacgaggtc aggatattga 4560 *gaccatcctg gctaacatgg tgaaacccca tctccactaa aaatacaaaa aattagctgg 4620 gcgtggtggc gggcgcctgt agtcccagct actcgggagg ctgaggcagg agaatggcgt 4680 gaacccggga ggcggagctt gcagtgagcc gagatggcgc cactgcactc cagcctgggt 4740 gacagagcaa gactctgtct caaaaagaaa aaaatgttca gtgatagaaa ataattttac 4800 taggttttta tgttgattgt actcatgctg ttccactcct tttaattatt aaaaagttat 4860 ttttggctgg gtgtggtggc tcatacctgt aatcccagca ctttgggagg ccgaggcggg 4920 tggatcacct gaggtcagga gttcaagacc agtctggcca acat 4964 282 Table Lll1(f). Nucleotide sequence alignment of 109P1 D4 v.1 (SEQ ID NO: 268) and 109P1 D4 v.7 (SEQ ID NO: 269) Score = 5664 bits (2946), Expect = 0.01dentities = 3000/3027 (99%) Strand = Plus / Plus V.1 852 ttgttgtccgggacgtacattttcgcggtcctgctagcatgcgtggtgttccactctggc 911 V.7 837 ttgttgtccgggacgtacattttcgcggtcctgctagtatgcgtggtgttccactctggc 896 V.1 912 gcccaggagaaaaactacaccatccgagaagaaatgccagaaaacgtcctgataggcgac 971 l l i lll llllll1l111lll li llll11 ||| 11 11 11 |l l l l l li1 111l i | V.7 897 gcccaggagaaaaactacaccatccgagaagaaattccagaaaacgtcctgataggcaac 956 V.1 972 ttgttgaaagaccttaacttgtcgctgattccaaacaagtccttgacaactgctatgcag 1031 V.7 957 ttgttgaaagaccttaacttgtcgctgattccaaacaagtccttgacaactactatgcag 1016 V.1 1032 ttcaagctagtgtacaagaccggagatgtgccactgattcgaattgaagaggatactggt 1091 lil1l111l111ll1l1111111l11111ll111 ill I lillilllllllll11i lli V.7 1017 ttcaagctagtgtacaagaccggagatgtgccactgattcgaattgaagaggatactggt 1076 V.1 1092 gagatcttcactactggcgctcgcattgatcgtgagaaattatgtgctggtatcccaagg 1151 lil l lli 11 1 lillllllll 11l l illl ll lllllll1111 |1111 11 V.7 1077 gagatcttcactaccggcgctcgcattgatcgtgagaaattatgtgctggtatcccaagg 1136 V.1 1152 gatgagcattgcttttatgaagtggaggttgccattttgccggatgaaatatttagactg 1211 lil lll ll Il ll1 l I l Il lillll llll1 lllll 11ll ll 1111l1l11 V.7 1137 gatgagcattgcttttatgaagtggaggttgccattttgccggatgaaatat tagactg 1196 V.1 1212 gttaagatacgttttctgatagaagatataaatgataatgcaccattgttcccagcaaca 1271 lil li lll ll ll lll ll ll I l illlll1ill 11lIll illlllilll| Illll V.7 : 1197 gttaagatacgttttctgatagaagatataaatgataatgcaccattgttcccagcaaca 1256 V.1 : 1272 gttatcaacatatcaattccagagaactcggctataaactctaaatatactctcccagcg 1331 lilll111lllll111ll11l11llllllll1llllilllllllilllllllllll111 V.7 : 1257 gttatcaacatatcaattccagagaactcggctataaactctaaatatactctcccagcg 1316 V.1 : 1332 gctgttgatcctgacgtaggaataaacggagttcaaaactacgaactaattaagagtcaa 1391 lillllllli1 Illl lillillll11l1illllilllllllllll11111|||1 V.7 : 1317 gctgttgatcctgacgtaggcataaacggagttcaaaactacgaactaattaagagtcaa 1376 V.1 : 1392 aacatttttggcctcgatgtcattgaaacaccagaaggagacaagatgccacaactgatt 1451 lill lll ll l lllllllllllll ll lllll lll 1 1 1llll1l1ll1lll V.7 : 1377 aacatttttggcctcgatgtcattgaaacaccagaaggagacaagatgccacaactgatt 1436 V.1 : 1452 gttcaaaaggagttagatagggaagagaaggatacctacgtgatgaaagtaaaggttgaa 1511 lllllllll1111111l111l11ll111lllili111111 lillllllilllill1l| V.7 : 1437 gttcaaaaggagttagatagggaagagaaggatacctatgtgatgaaagtaaaggttgaa 1496 V.1 : 1512 gatggtggctttcctcaaagatccagtactgctattttgcaagtgagtgttactgataca 1571 lillllllllllilllilllilillllllilllllillllllli 1|111111|11 V.7 1497 gatggtggctttcctcaaagatccagtactgctattttgcaagtaagtgttactgataca 1556 V.1 1572 aatgacaaccacccagtctttaaggagacagagattgaagtcagtataccagaaaatgct 1631 V.7 1557 aatgacaaccacccagtctttaaggagacagagattgaagtcagtataccagaaaatgct 1616 283 V.1 1632 cctgtaggcacttcagtgacacagctccatgccacagatgctgacataggtgaaaatgcc 1691 lill i II ll|I 111||111||1111111|| li ||l11I111111111il lili V.7 1617 cctgtaggcacttcagtgacacagctccatgccacagatgctgacataggtgaaaatgcc 1676 V.1 1692 aagatccacttctctttcagcaatctagtctccaacattgccaggagattatttcacctc 1751 11l1I1ll 111ilil 11l1l11111111l1111i1|11 I 1il| |Ill1ll li il ll Ill illl V.7 1677 aagatccacttctctttcagcaatctagtctccaacattgccaggagattatttcacctc 1736 v.1 1752 aatgccaccactggacttatcacaatcaaagaaccactggatagggaagaaacaccaaac 1811 lill i li lli11l lil1I1|1111 |I1l1i1 illl I||lillii11 illll1I111 llli V.7 1737 aatgccaccactggacttatcacaatcaaagaaccactggatagggaagaaacaccaaac 1796 v.1 1812 cacaagttactggttttggcaagtgatggtggattgatgccagcaagagcaatggtgctg 1871 I llilI lllilil|lil l li li l lili11 I1 lillil1 I l1 ill lillllll111 I1I1ll V.7 1797 cacaagttactggttttggcaagtgatggtggattgatgccagcaagagcaatggtgctg 1856 V.1 1872 gtaaatgttacagatgtcaatgataatgtcccatccattgacataagatacatcgtcaat 1931 V.7 1857 gtaaatgttacagatgtcaatgataatgtcccatccattgacataagatacatcgtcaat 1916 V.1 1932 cctgtcaatgacacagttgttctttcagaaaatattccactcaacaccaaaattgctctc 1991 IlIllllllil~lIlllllil 1llllllllllllllllllllli V.7 1917 cctgtcaatgacacagttgttctttcagaaaatattccactcaacaccaaaattgctctc 1976 V.1 1992 ataactgtgacggataaggatgcggaccataatggcagggtgacatgcttcacagatcat 2051 V.7 1977 ataactgtgacggataaggatgcggaccataatggcagggtgacatgcttcacagatcat 2036 V.1 2052 gaaatccctttcagattaaggccagtattcagtaatcagttcctcctggagactgcagca 2111 11111 llil Il I ii 111 || || I l 11 1|| | 11 1111 V.7 2037 gaaattcctttcagattaaggccagtattcagtaatcagttcctcctggagaatgcagca 2096 V.1 2112 tatcttgactatgagtccacaaaagaatatgccattaaattactggctgcagatgctggc 2171 liiill liiil lilllll 1 llll lllllllljlll liIlllllllllli V.7 2097 tatcttgactatgagtccacaaaagaatatgccattaaattactggctgcagatgctggc 2156 V.1 2172 aaacctcctttgaatcagtcagcaatgctcttcatcaaagtgaaagatgaaaatgacaat 2231 lilil111Ill11il11i1111 liliill11111111111I 111I1l1I|1|1|I1l111I1lli V.7 2157 aaacctcctttgaatcagtcagcaatgctcttcatcaaagtgaaagatgaaaatgacaat 2216 V.1 2232 gctccagttttcacccagtctttcgtaactgtttctattcctgagaataactctcctggc 2291 lilillllli111l11llilllll1l1l1l1l11l11l11ll1ll1l1lllllll1lll1 V.7 2217 gctccagttttcacccagtctttcgtaactgtttctattcctgagaataactctcctggc 2276 V.1 2292 atccagttgacgaaagtaagtgcaatggatgcagacagtgggcctaatgctaagatcaat 2351 I ll11lill 1I111111111 11 Illllil111 lilli lilllllllllllllllil V.7 2277 atccagttgatgaaagtaagtgcaacggatgcagacagtgggcctaatgctgagatcaat 2336 V.1 2352 tacctgctaggccctgatgctccacctgaattcagcctggattgtcgtacaggcatgctg 2411 l1l 11IIll l I I Il li1l l 1 ll lll1 11 i llllll111 ll11 V.7 2337 tacctgctaggccctgatgctccacctgaattcagcctggatcgtcgtacaggcatgctg 2396 V.1 2412 actgtagtgaagaaactagatagagaaaaagaggataaatatttattcacaattctggca 2471 V.7 2397 actgtagtgaagaaactagatagagaaaaagaggataaatatttattcacaattctggca 2456 284 V.1 2472 aaagataacggggtaccacccttaaccagcaatgtcacagtctttgtaagcattattgat 2531 V.7 2457 aaagataatggggtaccaccttaaccagcaatgtcacagtctttgtaagcattattgat 2516 V.1 2532 cagaatgacaatagcccagttttcactcacaatgaatacaacttctatgtcccagaaaac 2591 11111|1111111111111111111ilIIIi iII lII II 1111111il I iii I 11111I| V.7 2517 cagaatgacaatagcccagttttcactcacaatgaatacaaattctatgtcccagaaaac 2576 V.1 2592 cttccaaggcatggtacagtaggactaatcactgtaactgatcctgattatggagacaat 2651 liIIII1iil11111 Iii I|111111 jill! 1 iii 111111Ill 1I11 I1 Ii V.7 2577 cttccaaggcatggtacagtaggactaatcactgtaactgatcctgattatggagacaat 2636 V.1 2652 tctgcagttacgctctccattttagatgagaatgatgacttcaccattgattcacaaact 2711 V.7 : 2637 tctgcagttacgctctccattttagatgagaatgatgacttcaccattgattcacaaact 2696 V.1 : 2712 ggtgtcatccgaccaaatatttcatttgatagagaaaaacaagaatcttacactttctat 2771 Ili1I I I I i| I I I II I li lii I I||1|| I | | I I Il II til I 1illi V.7 : 2697 ggtgtcatccgaccaaatatttcatttgatagagaaaaacaagaatcttacactttctat 2756 V.1 : 2772 gtaaaggctgaggatggtggtagagtatcacgttcttcaagtgccaaagtaaccataaat 2831 ||11I1 Il 111111111111111111! i IIIII|1 iIII lII 1111111| I |I i I||| V.7 : 2757 gtaaaggctgaggatggtggtagagtatcacgttcttcaagtgccaaagtaaccataaat 2816 V.1 : 2832 gtggttgatgtcaatgacaacaaaccagttttcattgtccctccttccaactgttcttat 2891 1111l 11 iiII I I I I I I ii I II IIIIII I |I I I11 I I| || ||| V.7 : 2817 gtggttgatgtcaatgacaacaaaccagttttcattgtccctccttacaactattcttat 2876 V.1 : 2892 gaattggttctaccgtccactaatccaggcacagtggtctttcaggtaattgctgttgac 2951 11|111|| 111 lI i ii 11|| 1 liil 11111 I lI 111 I 1111 il 1 V.7 : 2877 gaattggttctaccgtccactaatccaggcacagtggtctttcaggtaattgctgttgac 2936 V.1 : 2952 aatgacactggcatgaatgcagaggttcgttacagcattgtaggaggaaacacaagagat 3011 V.7 2937 aatgacactggcatgaatgcagaggttcgttacagcattgtaggaggaaacacaagagat 2996 V.1 3012 ctgtttgcaatcgaccaagaaacaggcaacataacattgatggagaaatgtgatgttaca 3071 V.7 2997 ctgtttgcaatcgaccaagaaacaggcaacataacattgatggagaaatgtgatgttaca 3056 V.1 3072 gaccttggtttacacagagtgttggtcaaagctaatgacttaggacagcctgattctctc 3131 V.7 3057 gaccttggtttacacagagtgttggtcaaagctaatgacttaggacagcctgattctctc 3116 V.1 3132 ttcagtgttgtaattgtcaatctgttcgtgaatgagtcggtgaccaatgctacactgatt 3191 111111111111111 I I I I|||II 111111!|I III ii i||! 1 |11111 V.7 3117 ttcagtgttgtaattgtcaatctgttcgtgaatgagtcagtgaccaatgctacactgatt 3176 V.1 3192 aatgaactggtgcgcaaaagcactgaagcaccagtgaccccaaatactgagatagctgat 3251 11111111111 111111111I11ll1111l11111I111i11 IIIl II II I|1| V.7 3177 aatgaactggtgcgcaaaagcattgaagcaccagtgaccccaaatactgagatagctgat 3236 V.1 3252 gtatcctcaccaactagtgactatgtcaagatcctggttgcagctgttgctggcaccata 3311 111V. 32 111111llil I I I|111111 I 111I Ili1I||11111I|Illil 11111 32 V.7 :3237 gtatcctcaccaactagtgactatgtcaagatcctggttgcagctgttgctggcaccata 3296 285 V.1 : 3312 actgtcgttgtagttattttcatcactgctgtagtaagatgtcgccaggcaccacacctt 3371 V.7 : 3297 actgtcgttgtagttattttcatcactgctgtagtaagatgtcgccaggcaccacacctt 3356 V.1 : 3372 aaggctgctcagaaaaacaagcagaattctgaatgggctaccccaaacccagaaaacagg 3431 |||||i1111 i Ill||1| |||||1|Illlil I111111||||||1||||||1111I| V.7 : 3357 aaggctgctcagaaaaacatgcagaattctgaatgggctaccccaaacccagaaaacagg 3416 V.1 : 3432 cagatgataatgatgaagaaaaagaaaaagaagaagaagcattcccctaagaacttgctg 3491 i i l i I 11I1II 1ll 1ill lil l1I1l1I ill liil| 1 11| 1 1111111 ll 11111 II| V.7 : 3417 cagatgataatgatgaagaaaaagaaaaagaagaagaagcattcccctaagaacctgctg 3476 V.1 : 3492 cttaattttgtcactattgaagaaactaaggcagatgatgttgacagtgatggaaacaga 3551 IM l I 1l 11l iii I lilli Il11 lllilil i I 1111lll I 11lill V.7 : 3477 cttaatgttgtcactattgaagaaactaaggcagatgatgttgacagtgatggaaacaga 3536 V.1 : 3552 gtcacactagaccttcctattgatctagaagagcaaacaatgggaaagtacaattgggta 3611 11111111I lii lllllll1llll111l1lllll11illllliltlill1lll1l1llll1l V.7 : 3537 gtcacactagaccttcctattgatctagaagagcaaacaatgggaaagtacaattgggta 3596 V.1 : 3612 actacacctactactttcaagcccgacagccctgatttggcccgacactacaaatctgcc 3671 lillllll111ll11ll11lllll111 lill 111llllll1lllllll1ll1ill1l V.7 : 3597 actacacctactactttcaagcctgacagccctgatttggcccgacactacaaatctgcc 3656 V.1 3672 tctccacagcctgccttccaaattcagcctgaaactcccctgaattcgaagcaccacatc 3731 lil1 lll lli ll ll l ll llllll 111 11 1 1 11 |111 111|1 ||II lilll11l lil il V.7 3657 tctccacagcctgccttccaaattcagcctgaaactcccctgaatttgaagcaccacatc 3716 V.1 3732 atccaagaactgcctctcgataacacctttgtggcctgtgactctatctccaagtgttcc 3791 lilll1ll ll l ll lllll ll l| I iH1 1 |M111111 1 |1 | 1llill V.7 3717 atccaagaactgcctctcgataacacctttgtggcctgtgactctatctccaattgttcc 3776 V.1 3792 tcaagcagttcagatccctacagcgtttctgactgtggctatccagtgacgaccttcgag 3851 1 I i I l il 11 1 1 1 llllll illllllllllllllll lill1ll1 l V.7 3777 tcaagcagttcagatccctacagcgtttctgactgtggctatccagtgacaaccttcgag 3836 V.1 3852 gtacctgtgtccgtacacaccagaccg 3878 V.7 : 3837 gtacctgtgtccgtacacaccagaccg 3863 Score = 1567 bits (815), Expect - 0.OIdentities = 829/836 (99%) Strand - Plus / Plus V.1 : 3 ggtggtccagtacctccaaagatatggaatacactcctgaaatatcctgaaaactttttt 62 V.7 : 1 ggtggtccagtacctccaaagatatggaatacactcctgaaatatcctgaaacctttttt 60 V.1 : 63 ttttcagaatcctttaataagcagttatgtcaatctgaaagttgcttacttgtactttat 122 I lI II 1 l Illlli 111 1 I llilil II||| 1111 lil I 1lil11ll1l ll111 V.7 : 61 ttttcagaatcctttaataagcagttatgtcaatctgaaagttgcttacttgtactttat 120 V.1 : 123 attaatagctattcttgtttttcttatccaaagaaaaatcctctaatccccttttcacat 182 Ill Ill lll llllll1111 111111 l111111 lll11111 lll1 V.7 :121 attaatagctattcttgtttttcttatccaaagaaaaatcctctaatccccttttcacat 180 286 V.1 : 183 gatagttgttaccatgtttaggcattagtcacatcaacccctctcctctcccaaacttct 242 V.7 : 181 gatagttgttaccatgtttaggcgttagtcacatcaacccctctcctctcccaaacttct 240 V.1 : 243 cttcttcaaatcaaactttattagtccctcctttataatgattccttgcctcgttttatc 302 I l 1llI|| I1 I l li i ll il1Ill li1IIl liiilil1I11 1111I11I11111 1111li1 V.7 : 241 cttcttcaaatcaaactttattagtccctcctttataatgattccttgcctccttttatc 300 V.1 : 303 cagatcaattttttttcactttgatgcccagagctgaagaaatggactactgtataaatt 362 I I l I lI||1||1|1lillili li ill li l 1illl I1III1I lii l i i| 11 l 111 V.7 : 301 cagatcaattttttttcactttgatgcccagagctgaagaaatggactattgtataaatt 360 V.1 : 363 attcattgccaagagaataattgcattttaaacccatattataacaaagaataatgatta 422 lillil IIIIII l I I111111 l||11 ||||||1 |1lil 11111ll|1 li1 lil1 11 l1ii V.7 : 361 attcattgccaagagaataattgcattttaaacccatgttataacaaagaataatgatta 420 V.1 : 423 tattttgtgatttgtaacaaataccctttattttcccttaactattgaattaaatatttt 482 l 11Il il I1 I1I1 Ilill Ililll illI 11ll I il ll i 11l11l111il Ill11 IIll V.7 : 421 tattttgtgatttgtaacaaataccctttattttcccttaactattgaattaaatatttt 480 V.1 483 aattatttgtattctctttaactatcttggtatattaaagtattatcttttatatattta 542 111|11I11l111||11 il1lillll11lli I 111 111 I jll ili 1 ||I j ill l lil|1 V.7 481 aattatttgtattctctttaactatcttggtatattaaagtattatcttttatatattta 540 V.1 543 tcaatggtggacacttttataggtactctgtgtcatttttgatactgtaggtatcttatt 602 V.7 : 541 tcaatggtggacacttttataggtactctgtgtcatttttgatactgtaggtatcttatt 600 V.1 : 603 tcatttatctttattcttaatgtacgaattcataatatttgattcagaacaaatttatca 662 V.7 : 601 tcatttatctttattcttaatgtacgaattcataatatttgattcagaacagatttatca 660 V.1 : 663 ctaattaacagagtgtcaattatgctaacatctcatttactgattttaatttaaaacagt 722 1 1 |1 1 1 1 1 11 l l l l 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1*1 1 1 1 1 1 1 1 1 1 |1 1 11 1 1 1 1 1 1 11 1 1 11 V.7 : 661 ctaattaacagagtgtcaattatgctaacatctcatttactgattttaatttaaaacagt 720 V.1 : 723 ttttgttaacatgcatgtttagggttggcttcttaataatttcttcttcctcttctctct 782 Illlilllll l llllllllli lllilllllll111 llll ll lillllllllllllil V.7 : 721 ttttgttaacatgcatgtttagggttggcttcttaataatttcttcttcctcttctctct 780 V.1 : 783 ctcctcttcttttggtcagtgttgtgcgggttaatacaacaaactgtaacaagtgt 838 I llllllil lillllll11111111111111111||| j11111||1 illl Illi V.7 : 781 ctcctcttcttttggtcagtgttgtgcgggttaatacaacaaactgtcacaagtgt 836 Table UV(f). Peptide sequences of protein coded by 109P1D4 v.7 (SEQ ID NO: 270) MFRVGFLIIS SSSSLSPLLL VSVVRVNTTN CHKCLLSGTY IFAVLLVCVV FHSGAQEKNY 60 TIREEIPENV LIGNLLKDLN LSLIPNKSLT TTMQFKLVYK TGDVPLIRIE EDTGEIFTTG 120 ARIDREKLCA GIPRDEHCFY EVEVAILPDE IFRLVKIRFL IEDINDNAPL FPATVINISI 180 PENSAINSKY TLPAAVDPDV GINGVQNYEL IKSQNIFGLD VIETPEGDKM PQLIVQKELD 240 REEKDTYVMK VKVEDGGFPQ RSSTAILQVS VTDTNDNHPV FKETEIEVSI PENAPVGTSV 300 TQLHATDADI GENAKIHFSF SNLVSNIARR LFHLNATTGL ITIKEPLDRE ETPNHKLLVL 360 ASDGGLMPAR AMVLVNVTDV NDNVPSIDIR YIVNPVNDTV VLSENIPLNT KIALITVTDK 420 DADHNGRVTC FTDHEIPFRL RPVFSNQFLL ENAAYLDYES TKEYAIKLLA ADAGKPPLNQ 480 SAMLFIKVKD ENDNAPVFTQ SFVTVSIPEN NSPGIQLMKV SATDADSGPN AEINYLLGPD 540 APPEFSLDRR TGMLTVVKKL DREKEDKYLF TILAKDNGVP PLTSNVTVFV SIIDQNDNSP 600 VFTHNEYKFY VPENLPRHGT VGLITVTDPD YGDNSAVTLS ILDENDDFTI DSQTGVIRPN 660 287 ISFDREKQES YTFYVKAEDG GRVSRSSSAK VTINVVDVND NKPVFIVPPY NYSYELVLPS 720 TNPGTVVFQV IAVDNDTGMN AEVRYSIVGG NTRDLFAIDQ ETGNITLMEK CDVTDLGLHR 780 VLVKANDLGQ PDSLFSVVIV NLFVNESVTN ATLINELVRK SIEAPVTPNT EIADVSSPTS 840 DYVKILVAAV AGTITVVVVI FITAVVRCRQ APHLKAAQKN MQNSEWATPN PENRQMIMMK 900 KKKKKKKHSP KNLLLNVVTI EETKADDVDS DGNRVTLDLP IDLEEQTMGK YNWVTTPTTF 960 KPDSPDLARH YKSASPQPAF QIQPETPLNL KHHIIQELPL DNTFVACDSI SNCSSSSSDP 1020 YSVSDCGYPV TTFEVPVSVH TRPTDSRT 1048 Table LV(f). Amino acid sequence alignment of 109PID4 v.1 (SEQ ID NO: 271) and 109PID4 v.7 (SEQ ID NO: 272) Score = 1961 bits (5081), Expect = 0.01dentities = 992/1009 (98%), Positives = 995/1009 (98%) V.1 3 LLSGTYIFAVLLACVVFHSGAQEKNYTIREEMPENVLIGDLLKDLNLSLIPNKSLTTAMQ 62 LLSGTYIFAVLL CVVFHSGAQEKNYTIREE+PENVLIG+LLKDLNLSLIPNKSLTT MQ V.7 35 LLSGTYIFAVLLVCVVFHSGAQEKNYTIREEIPENVLIGNLLKDLNLSLIPNKSLTTTMQ 94 V.1 63 FKLVYKTGDVPLIRIEEDTGEIFTTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIFRL 122 FKLVYKTGDVPLIRIEEDTGEIETTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIFRL V.7 95 FKLVYKTGDVPLIRIEEDTGEIFTTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIFRL 154 V.1 123 VKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIKSQ 182 VKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIKSQ V.7 155 VKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIKSQ 214 V.1 183 NIFGLDVIETPEGDKMPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVTDT 242 NIFGLDVIETPEGDKMPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVTDT V.7 215 NIFGLDVIETPEGDKMPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILOVSVTDT 274 V.1 243 NDNHPVFKETEIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSFSNLVSNIARRLFHL 302 NDNHPVFKETEIEVSIPENAPVGTSVTOLHATDADIGENAKIHFSFSNLVSNIARRLFHL V.7 275 NDNHPVFKETEIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSFSNLVSNIARRLFHL 334 V.1 303 NATTGLITIKEPLDREETPNHKLLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYIVN 362 NATTGLITIKEPLDREETPNHKLLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYIVN V.7 335 NATTGLITIKEPLDREETPNHKLLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYIVN 394 V.1 363 PVNDTVVLSENIPLNTKIALITVTDKDADHNGRVTCFTDHEIPFRLRPVFSNQFLLETAA 422 PVNDTVVLSENIPLNTKIALITVTDKDADHNGRVTCFTDHEIPFRLRPVFSNQFLLE AA V.7 395 PVNDTVVLSENIPLNTKIALITVTDKDADHNGRVTCFTDHEIPFRLRPVFSNQFLLENAA 454 V.1 423 YLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDENDNAPVFrQSFVTVSIPENNSPG 482 YLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDENDNAPVFQSFVTVSIPENNSPG V.7 455 YLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDENDNAPV~rQSFVTVSIPENNSPG 514 V.1 483 IQLTKVSAMDADSGPNAKINYLLGPDAPPEFSLDCRTGMLTVVKKLDREKEDKYLFTILA 542 IQL KVSA DADSGPNA+INYLLGPDAPPEFSLD RTGMLTVVKKLDREKEDKYLFTILA V.7 515 IQLMKVSATDADSGPNAEINYLLGPDAPPEFSLDRRTGMLTVVKKLDREKEDKYLFTILA 574 V.1 543 KDNGVPPLTSNVTVFVSIIDQNDNSPVFTHNEYNFYVPENLPRHGTVGLITVTDPDYGDN 602 KDNGVPPLTSNVTVFVSIIDQNDNSPVFTHNEY FYVPENLPRHGTVGLITVTDPDYGDN V.7 575 KDNGVPPLTSNVTVFVSIIDQNDNSPVFTHNEYKFYVPENLPRHGTVGLITVTDPDYGDN 634 V.1 603 SAVTLSILDENDDFTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVTIN 662 SAVTLSILDENDDFTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVTIN V.7 635 SAVTLSILDENDDFTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVTIN 694 V.1 663 VVDVNDNKPVFIVPPSNCSYELVLPSTNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNTRD 722 VVDVNDNKPVFIVPP N SYELVLPSTNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNTRD V.7 695 VVDVNDNKPVFIVPPYNYSYELVLPSTNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNTRD 754 V.1 723 LFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPDSLFSVVIVNLFVNESVTNATLI 782 LFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGOPDSLFSVVIVNLFVNESVTNATLI V.7 755 LFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPDSLFSVVIVNLFVNESVTNATLI 814 V.1 783 NELVRKSTEAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVRCRQAPHL 842 NELVRKS EAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVRCRQAPHL V.7 815 NELVRKSIEAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVRCRQAPHL 874 V.1 843 KAAQKNKQNSEWATPNPENRQMIMMKKKKKKKKHSPKNLLLNFVTIEETKADDVDSDGNR 902 288 KAAQKN QNSEWATPNPENRQMIMMKKKKKKKKHSPKNLLLN VTIEETKADDVDSDGNR V.7 875 KAAQKNMQNSEWATPNPENRQMIMMKKKKKKKKHSPKNLLLNVVTIEETKADDVDSDGNR 934 V.1 903 VTLDLPIDLEEQTMGKYNWVTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLNSKHHI 962 VTLDLPIDLEEQTMGKYNWVTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLN KHHI V.7 935 VTLDLPIDLEEQTMGKYNWVTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLNLKHHI 994 V.1 963 IQELPLDNTFVACDSISKCSSSSSDPYSVSDCGYPVTTFEVPVSVHTRP 1011 IQELPLDNTFVACDSIS CSSSSSDPYSVSDCGYPVTTFEVPVSVHTRP V.7 995 IQELPLDNTFVACDSISNCSSSSSDPYSVSDCGYPVTTFEVPVSVHTRP 1043 Table Ul(g). Nucleotide sequence of transcript variant 109PiD4v.8 (SEQ ID NO: 273) ggtggtccag tacctccaaa gatatggaat acactcctga aatatcctga aacctttttt 60 ttttcagaat cctttaataa gcagttatgt caatctgaaa gttgcttact tgtactttat 120 attaatagct attcttgttt ttcttatcca aagaaaaatc ctctaatccc cttttcacat 180 gatagttgtt accatgttta ggcgttagtc acatcaaccc ctctcctctc ccaaacttct 240 cttcttcaaa tcaaacttta ttagtccctc ctttataatg attccttgcc tccttttatc 300 cagatcaatt ttttttcact ttgatgccca gagctgaaga aatggactat tgtataaatt 360 attcattgcc aagagaataa ttgcatttta aacccatgtt ataacaaaga ataatgatta 420 tattttgtga tttgtaacaa atacccttta ttttccctta actattgaat taaatatttt 480 aattatttgt attctcttta actatcttgg tatattaaag tattatcttt tatatattta 540 tcaatggtgg acacttttat aggtactctg tgtcattttt gatactgtag gtatcttatt 600 tcatttatct ttattcttaa tgtacgaatt cataatattt gattcagaac agatttatca 660 ctaattaaca gagtgtcaat tatgctaaca tctcatttac tgattttaat ttaaaacagt 720 ttttgttaac atgcatgttt agggttggct tcttaataat ttcttcttcc tcttctctct 780 ctcctcttct tttggtcagt gttgtgcggg ttaatacaac aaactgtcac aagtgtttgt 840 tgtccgggac gtacattttc gcggtcctgc tagtatgcgt ggtgttccac tctggcgccc 900 aggagaaaaa ctacaccatc cgagaagaaa ttccagaaaa cgtcctgata ggcaacttgt 960 tgaaagacct taacttgtcg ctgattccaa acaagtcctt gacaactact atgcagttca 1020 agctagtgta caagaccgga gatgtgccac tgattcgaat tgaagaggat actggtgaga 1080 tcttcactac cggcgctcgc attgatcgtg agaaattatg tgctggtatc ccaagggatg 1140 agcattgctt ttatgaagtg gaggttgcca ttttgccgga tgaaatattt agactggtta 1200 agatacgttt tctgatagaa gatataaatg ataatgcacc attgttccca gcaacagtta 1260 tcaacatatc aattccagag aactcggcta taaactctaa atatactctc ccagcggctg 1320 ttgatcctga cgtaggcata aacggagttc aaaactacga actaattaag agtcaaaaca 1380 tttttggcct cgatgtcatt gaaacaccag aaggagacaa gatgccacaa ctgattgttc 1440 aaaaggagtt agatagggaa gagaaggata cctatgtgat gaaagtaaag gttgaagatg 1500 gtggctttcc tcaaagatcc agtactgcta ttttgcaagt aagtgttact gatacaaatg 1560 acaaccaccc agtctttaag gagacagaga ttgaagtcag tataccagaa aatgctcctg 1620 taggcacttc agtgacacag ctccatgcca cagatgctga cataggtgaa aatgccaaga 1680 tccacttctc tttcagcaat ctagtctcca acattgccag gagattattt cacctcaatg 1740 ccaccactgg acttatcaca atcaaagaac cactggatag ggaagaaaca ccaaaccaca 1800 agttactggt tttggcaagt gatggtggat tgatgccagc aagagcaatg gtgctggtaa 1860 atgttacaga tgtcaatgat aatgtcccat ccattgacat aagatacatc gtcaatcctg 1920 tcaatgacac agttgttctt tcagaaaata ttccactcaa caccaaaatt gctctcataa 1980 ctgtgacgga taaggatgcg gaccataatg gcagggtgac atgcttcaca gatcatgaaa 2040 ttcctttcag attaaggcca gtattcagta atcagttcct cctggagaat gcagcatatc 2100 ttgactatga gtccacaaaa gaatatgcca ttaaattact ggctgcagat gctggcaaac 2160 ctcctttgaa tcagtcagca atgctcttca tcaaagtgaa agatgaaaat gacaatgctc 2220 cagttttcac ccagtctttc gtaactgttt ctattcctga gaataactct cctggcatcc 2280 agttgatgaa agtaagtgca acggatgcag acagtgggcc taatgctgag atcaattacc 2340 tgctaggccc tgatgctcca cctgaattca gcctggatcg tcgtacaggc atgctgactg 2400 tagtgaagaa actagataga gaaaaagagg ataaatattt attcacaatt ctggcaaaag 2460 ataatggggt accaccctta accagcaatg tcacagtctt tgtaagcatt attgatcaga 2520 atgacaatag cccagttttc actcacaatg aatacaaatt ctatgtccca gaaaaccttc 2580 caaggcatgg tacagtagga ctaatcactg taactgatcc tgattatgga gacaattctg 2640 cagttacgct ctccatttta gatgagaatg atgacttcac cattgattca caaactggtg 2700 tcatccgacc aaatatttca tttgatagag aaaaacaaga atcttacact ttctatgtaa 2760 aggctgagga tggtggtaga gtatcacgtt cttcaagtgc caaagtaacc ataaatgtgg 2820 ttgatgtcaa tgacaacaaa ccagttttca ttgtccctcc ttacaactat tcttatgaat 2880 tggttctacc gtccactaat ccaggcacag tggtctttca ggtaattgct gttgacaatg 2940 acactggcat gaatgcagag gttcgttaca gcattgtagg aggaaacaca agagatctgt 3000 289 ttgcaatcga ccaagaaaca ggcaacataa cattgatgga gaaatgtgat gttacagacc 3060 ttggtttaca cagagtgttg gtcaaagcta atgacttagg acagcctgat tctctcttca 3120 gtgttgtaat tgtcaatctg ttcgtgaatg agtcagtgac caatgctaca ctgattaatg 3180 aactggtgcg caaaagcatt gaagcaccag tgaccccaaa tactgagata gctgatgtat 3240 cctcaccaac tagtgactat gtcaagatcc tggttgcagc tgttgctggc accataactg 3300 tcgttgtagt tattttcatc actgctgtag taagatgtcg ccaggcacca caccttaagg 3360 ctgctcagaa aaacatgcag aattctgaat gggctacccc aaacccagaa aacaggcaga 3420 tgataatgat gaagaaaaag aaaaagaaga agaagcattc ccctaagaac ctgctgctta 3480 atgttgtcac tattgaagaa actaaggcag atgatgttga cagtgatgga aacagagtca 3540 cactagacct tcctattgat ctagaagagc aaacaatggg aaagtacaat tgggtaacta 3600 cacctactac tttcaagcct gacagccctg atttggcccg acactacaaa tctgcctctc 3660 cacagcctgc cttccaaatt cagcctgaaa ctcccctgaa tttgaagcac cacatcatcc 3720 aagaactgcc tctcgataac acctttgtgg cctgtgactc tatctccaat tgttectcaa 3780 gcagttcaga tccctacagc gtttctgact gtggctatcc agtgacaacc ttcgaggtac 3840 ctgtgtccgt acacaccaga ccgtcccagc ggcgtgtcac atttcacctg ccagaaggct 3900 ctcaggaaag cagcagtgat ggtggactgg gagaccatga tgcaggcagc cttaccagca 3960 catcccatgg cctgcccctt ggctatcctc aggaggagta ctttgatcgt gctacaccca 4020 gcaatcgcac tgaaggggat ggcaactccg atcctgaatc tactttcata cctggactaa 4080 agaaagaaat aactgttcaa ccaactgtgg aagaggcctc tgacaactgc actcaagaat 4140 gtctcatcta tggccattct gatgcctgct ggatgccggc atctctggat cattccagct 4200 cttcacaagc acaggcctct gctctatgcc acagcccacc actgtcacag gcctctactc 4260 agcaccacag cccaccagtg acacagacca ttgttctctg ccacagccct ccagtgacac 4320 agaccatcgc attgtgccac agcccaccac cgatacaggt gtctgctctc caccacagtc 4380 ctcctctagt gcagggtact gcacttcacc acagcccacc atcagcacag gcctcagccc 4440 tctgctacag ccctccttta gcacaggctg ctgcaatcag ccacagctct tctctgccac 4500 aggttattgc cctccatcgt agtcaggccc aatcatcagt cagtttgcag caaggttggg 4560 tgcaaggtgc taatggacta tgctctgttg atcagggagt gcaaggtagt gcaacatctc 4620 agttttacac catgtctgaa agacttcatc ccagtgatga ttcaattaaa gtcattcctt 4680 tgacaacctt cgctccacgc caacaggcca gaccgtccag aggtgattcc cccattatgg 4740 aaacacatcc cttgtaaagc taaaatagtt acttcaaatt ttcagaaaag atgtatatag 4800 tcaaaattta agatacaatt ccaatgagta ttctgattat cagatttgta aataactatg 4860 taaatagaaa cagataccag aataaatcta cagctagacc cttagtcaat agttaaccaa 4920 aaaattgcaa tttgtttaat tcagaatgtg tatttaaaaa gaaaaggaat ttaacaattt 4980 gcatcccctt gtacagtaag gcttatcatg acagagcgta ctatttctga tgtacagtat 5040 tttttgttgt ttttatcatc atgtgcaata ttactgattt gtttccatgc tgattgtgtg 5100 gaaccagtat gtagcaaatg gaaagcctag aaatatctta ttttctaagt ttacctttag 5160 tttacctaaa cttttgttca gataatgtta aaaggtatac gtactctagc cttttttggg 5220 gctttctttt tgatttttgt ttgtggtttt cagttttttt gttgttgtta gtgagtctcc 5280 cttcaaaata cacagtaggt agtgtaaata ctgcttgttt gtgtctctct gctgtcatgt 5340 tttctacctt attccaatac tatattgttg ataaaatttg tatatacatt ttcaataaag 5400 aatatgtata aactgtacag atctagatct acaacctatt tctctactct ttagtagagt 5460 tcgagacaca gaagtgcaat aactgcccta attaagcaac tatttgttaa aaagggcccc 5520 tttttacttt aatagtttag tgtaaagtac atcagaaata aaactgtatc tgacatttta 5580 agcctgtagt ccattattac ttgggtcttt acttctggga atttgtatgt aacagcctag 5640 aaaattaaaa ggaggtggat gcatccaaag cacgagtcac ttaaaatatc gacggtaaac 5700 tactattttg tagagaaact caggaagatt taaatgttga tttgacagct caataggctg 5760 ttaccaaagg gtgttcagta aaaataacaa atacatgtaa ctgtagataa aaccacatac 5820 taaatctata agactaaggg atttttgtta ttctagctca acttactgaa gaaaaccact 5880 aataacaaca agaatatcag gaaggaactt ttcaagaaat gtaattataa atctacatca 5940 aacagaattt taaggaaaaa tgcagaggga gaaataaggc acatgactgc ttcttgcagt 6000 caagaagaaa taccaataac acacacagaa caaaaaccat caaaatctca tatatgaaat 6060 aaaatatatt cttctaagca aagaaacagt actattcata gaaaacatta gttttctcct 6120 gttgtctgtt atttccttct tttatcctct taactggcca ttatcttgta tgtgcacatt 6180 ttataaatgt acagaaacat caccaacttg attttcttcc atagcaaaac tgagaaaata 6240 ccttgtttca gtataacact aaaccaagag acaattgatg tttaatgggg gcggttgggg 6300 ttggggggga gtcaatatct cctattgatt aacttagaca tagattttgt aatgtataac 6360 ttgatattta atttatgatt aaactgtaat tttgtaacat aaactgtggt aattgcataa 6420 tttcattggt gaggatttcc tttgaatatt gagaaagttt cttttcatgt gcccagcagg 6480 ttaagtagcg ttttcagaat atacattatt cccatccatt gtaaagttcc ttaagtcata 6540 tttgactggg cgtgcagaat aacttcttaa ctattaacta tcagagtttg attaataaaa 6600 ttaattaatt ttttttctcc ttcgtgttgt taatgttcca agggatttgg agcatactgg 6660 ttttccaggt gcatgtgaat cccgaaggac tgatgatatt tgaatgttta ttaaattatt 6720 290 atcacacaaa tgtgttgata ttgtggctat tgttgatgtt gaaaattgta aacttgggga 6780 agattaagaa aagaaccaat agtgacaaaa atcagtgctt ccagtagatt ttagaacatt 6840 ctttgcctca aaaaacctgc aaagatgatg tgagattttt tcttgtgttt taattatttt 6900 cacattttct ctctgcaaac ctttagtttt ctgatgatct acacacacac atacacacac 6960 acacacacac acgtgcacac acacacattt aaaggatata aaaagaagag gttgaaagat 7020 tattaaataa cttatcaggc atctcaatgg ttactatcta tgttagtgaa aatcaaatag 7080 gactcaaagt tggatatttg ggatttttct tctgacagta taatttattg agttactagg 7140 gaggttctta aatcctcata tctggaaact tgtgaagttt tgacaccttt cctatagata 7200 taggaatgaa ccaatacgct tttattaccc tttctaactc tgattttata atcagactta 7260 gattgtgttt agaatattaa atgactgggc accctcttct tggtttttac cagagaggct 7320 ttgaatggaa gcaggctgag agtagccaaa gaggcaaggg gtattagccc agttattctc 7380 ccctatgcct tctcttccta agcgtccact aggtctggcc ttggaaatct gttacttcta 7440 cggcttcaga tctgatgata tctttttcat cacattacaa gttatttctt tgactgaata 7500 gacagtggta taggttgaca cagcacacaa gtggctattg tgatgtatga tgtatgtagt 7560 cccacaactg caaaacgtct tactgaagca acaatcgaaa aatggttctg ttttaaaaag 7620 gattttgttt gatttgaaat taaaacttca aactgaatga cttatatgag aataatatgt 7680 tcaatcaaag tagttattct attttgtgtc catattccat tagattgtga ttattaattt 7740 tctagctatg gtattactat atcacacttg tgagtatgta ttcaaatact aagtatctta 7800 tatgctacgt gcatacacat tcttttctta aactttacct gtgttttaac taatattgtg 7860 tcagtgtatt aaaaattagc ttttacatat gatatctaca atgtaataaa tttagagagt 7920 aattttgtgt attcttattt acttaacatt ttacttttaa ttatgtaaat ttggttagaa 7980 aataataata aatggttagt gctattgtgt aatggtagca gttacaaaga gcctctgcct 8040 tcccaaacta atatttatca cacatggtca ttaaatggga aaaaaataga ctaaacaaat 8100 cacaaattgt tcagttctta aaatgtaatt atgtcacaca cacaaaaaaa tccttttcaa 8160 tcctgagaaa attaaaggtg ttttactcac atggatattt caacattagt tttttttgtt 8220 tgtttctttt tcatggtatt actgaaggtg tgtatactcc ctaatacaca tttatgaaaa 8280 tctacttgtt tagactttta tttatactct tctgatttat attttttatt ataattatta 8340 tttcttatct tcttttatat tttttggaaa ccaaatttat agttagttta ggtaaacttt 8400 ttattatgac cattagaaac tattttgaat gtttccaact ggctcaattg gctgggaaaa 8460 catgggaaca agagaagctg aaatatattt ctgcaagaac ctttctatat tatgtgccaa 8520 ttaccacacc agatcaattt tatgcagagg ccttaaaata ttctttcaca gtagctttct 8580 tacactaacc gtcatgtgct tttagtaaat atgattttta aaagcagttc aagttgacaa 8640 cagcagaaac agtaacaaaa aaatctgctc agaaaaatgt atgtgcacaa ataaaaaaaa 8700 ttaatggcaa ttgtttagtg actgtaagtg atacttttta aagagtaaac tgtgtgaaat 8760 ttatactatc cctgcttaaa atattaagat ttttatgaaa tatgtattta tgtttgtatt 8820 gtgggaagat tcctcctctg tgatatcata cagcatctga aagtgaacag tatcccaaag 8880 cagttccaag catgctttgg aagtaagaag gttgactatt gtatggccaa ggatggcagt 8940 atgtaatcca gaagcaaact tgtattaatt gttctatttc aggttctgta ttgcatgttt 9000 tcttattaat atatattaat aaaagttatg agaaat 9036 Table LIl(g). Nucleotide sequence alignment of 109P1D4v.1 (SEQ ID NO: 274)and 109PID4v.8 (SEQ ID NO: 275) Score 5664 bits (2946), Expect = 0.0ldentities = 3000/3027 (99%) Strand = Plus / Plus V.1 852 ttgttgtccgggacgtacattttcgcggtcctgctagcatgcgtggtgttccactctggc 911 V.8 837 ttgttgtccgggacgtacattttcgcggtcctgctagtatgcgtggtgttccactctggc 896 V.1 912 gcccaggagaaaaactacaccatccgagaagaaatgccagaaaacgtcctgataggcgac 971 lill11111lillllilll11lllllllIllllI III11111111I11111 11|1111 Il V.8 897 gcccaggagaaaaactacaccatccgagaagaaattccagaaaacgtcctgataggcaac 956 V.1 972 ttgttgaaagaccttaacttgtcgctgattccaaacaagtccttgacaactgctatgcag 1031 l 1i l 11 l lll lll ll llIll1111||1I|1||I111ill111 V.8 957 ttgttgaaagaccttaacttgtcgctgattccaaacaagtccttgacaactactatgcag 1016 V.1 1032 ttcaagctagtgtacaagaccggagatgtgccactgattcgaattgaagaggatactggt 1091 Il11lil 1ll llill l l l l l llll lii1 1 1 11 I 1lI llll l l lllli llI ll li V.8 1017 ttcaagctagtgtacaagaccggagatgtgccactgattcgaattgaagaggatactggt 1076 V.1 1092 gagatcttcactactggcgctcgcattgatcgtgagaaattatgtgctggtatcccaagg 1151 Ill|1111l11lllI lililllllllllil111il1ll11l11l1ll1llll1llillli 291 V.8 : 1077 gagatcttcactaccggcgctcgcattgatcgtgagaaattatgtgctggtatcccaagg 1136 V.1 : 1152 gatgagcattgcttttatgaagtggaggttgccattttgccggatgaaatatttagactg 1211 l I ll l illlll11I llil iillll I lllIlI llIlli I ||il I11 lill I ll V.8 : 1137 gatgagcattgcttttatgaagtggaggttgccattttgccggatgaaatatttagactg 1196 V.1 : 1212 gttaagatacgttttctgatagaagatataaatgataatgcaccattgttcccagcaaca 1271 V.8 : 1197 gttaagatacgttttctgatagaagatataaatgataatgcaccattgttcccagcaaca 1256 V.1 : 1272 gttatcaacatatcaattccagagaactcggctataaactctaaatatactctcccagcg 1331 11ll liil I11111111iliiillill Ill I1il1l11 lil111 li 11||11111li| V.8 : 1257 gttatcaacatatcaattccagagaactcggctataaactctaaatatactctcccagcg 1316 V.1 : 1332 gctgttgatcctgacgtaggaataaacggagttcaaaactacgaactaattaagagtcaa 1391 * 11 I|1I lii l I11 1 1111 li l i||11 I lli 11I lil ll 1 II Illi I| V.8 : 1317 gctgttgatcctgacgtaggcataaacggagttcaaaactacgaactaattaagagtcaa 1376 V.1 : 1392 aacatttttggcctcgatgtcattgaaacaccagaaggagacaagatgccacaactgatt 1451 I111ll1lllil lilli111111111111111111 111! l li |ll 11I lilI1li1li V.8 : 1377 aacatttttggcctcgatgtcattgaaacaccagaaggagacaagatgccacaactgatt 1436 V.1 : 1452 gttcaaaaggagttagatagggaagagaaggatacctacgtgatgaaagtaaaggttgaa 1511 V.8 1437 gttcaaaaggagttagatagggaagagaaggatacctatgtgatgaaagtaaaggttgaa 1496 V.1 1512 gatggtggctttcctcaaagatccagtactgctattttgcaagtgagtgttactgataca 1571 I lllll I11111llll llllllllllllllll1l11 lill lillllll1l1lli V.8 1497 gatggtggctttcctcaaagatccagtactgctattttgcaagtaagtgttactgataca 1556 V.1 1572 aatgacaaccacccagtctttaaggagacagagattgaagtcagtataccagaaaatgct 1631 ti1lIl I llilIl1l||I lIllllll~ill lil IIl 11111I l 1I 1lil 1|| 1l| V.8 1557 aatgacaaccacccagtctttaaggagacagagattgaagtcagtataccagaaaatgct 1616 V.1 : 1632 cctgtaggcacttcagtgacacagctccatgccacagatgctgacataggtgaaaatgcc 1691 Il I ll1Il11I l11Il1I I llllil lll lililll1lI lll1 ill i i V.8 : 1617 cctgtaggcacttcagtgacacagctccatgccacagatgctgacataggtgaaaatgcc 1676 V.1 : 1692 aagatccacttctctttcagcaatctagtctccaacattgccaggagattatttcacctc 1751 11 1 1 1 1 1 11 1 111 lI | Il l i lil i llli I I I1 ll lil1I ll 1I I 1li i| V.8 : 1677 aagatccacttctctttcagcaatctagtctccaacattgccaggagattatttcacctc 1736 V.1 : 1752 aatgccaccactggacttatcacaatcaaagaaccactggatagggaagaaacaccaaac 1811 t li lll 11I11I111I lll111Illl 111| 111111 l |I111lill11111l V.8 : 1737 aatgccaccactggacttatcacaatcaaagaaccactggatagggaagaaacaccaaac 1796 V.1 : 1812 cacaagttactggttttggcaagtgatggtggattgatgccagcaagagcaatggtgctg 1871 V.8 : 1797 cacaagttactggttttggcaagtgatggtggattgatgccagcaagagcaatggtgctg 1856 V.1 : 1872 gtaaatgttacagatgtcaatgataatgtcccatccattgacataagatacatcgtcaat 1931 V.8 : 1857 gtaaatgttacagatgtcaatgataatgtcccatccattgacataagatacatcgtcaat 1916 V.1 : 1932 cctgtcaatgacacagttgttctttcagaaaatattccactcaacaccaaaattgctctc 1991 292 ||||||||||||||||||||||I |I |lil ll lilll 1 l 1llll 11 111|| 1|Ili l i li V.8 : 1917 cctgtcaatgacacagttgttctttcagaaaatattccactcaacaccaaaattgctctc 1976 V.1 : 1992 ataactgtgacggataaggatgcggaccataatggcagggtgacatgcttcacagatcat 2051 lill lI lll111 11 1 11 I lill 1111 11 11 llllllil li lilli V.8 : 1977 ataactgtgacggataaggatgcggaccataatggcagggtgacatgcttcacagatcat 2036 V.1 : 2052 gaaatccctttcagattaaggccagtattcagtaatcagttcctcctggagactgcagca 2111 I111 l |||I 1llllil 11 I I 1I11 1 l l l l|1 Ill I ii 1 1 l II I Ii V.8 : 2037 gaaattcctttcagattaaggccagtattcagtaatcagttcctcctggagaatgcagca 2096 V.1 : 2112 tatcttgactatgagtccacaaaagaatatgccattaaattactggctgcagatgctggc 2171 V.8 : 2097 tatcttgactatgagtccacaaaagaatatgccattaaattactggctgcagatgctggc 2156 V.1 : 2172 aaacctcctttgaatcagtcagcaatgctcttcatcaaagtgaaagatgaaaatgacaat 2231 lill ll l lllillll11 1 11 1lilllllllllllllllllllIllll ll 11 11ii V.8 : 2157 aaacctcctttgaatcagtcagcaatgctcttcatcaaagtgaaagatgaaaatgacaat 2216 V.1 : 2232 gctccagttttcacccagtctttcgtaactgtttctattcctgagaataactctcctggc 2291 V.8 : 2217 gctccagttttcacccagtctttcgtaactgtttctattcctgagaataactctcctggc 2276 V.1 2292 atccagttgacgaaagtaagtgcaatggatgcagacagtgggcctaatgctaagatcaat 2351 li I iI |11111 1||||||| li| |||||||| 1||||||||||| 1 | 1|||||||| V.8 2277 atccagttgatgaaagtaagtgcaacggatgcagacagtgggcctaatgctgagatcaat 2336 V.1 2352 tacctgctaggccctgatgctccacctgaattcagcctggattgtcgtacaggcatgctg 2411 V.8 : 2337 tacctgctaggccctgatgctccacctgaattcagcctggatcgtcgtacaggcatgctg 2396 V.1 : 2412 actgtagtgaagaaactagatagagaaaaagaggataaatatttattcacaattctggca 2471 I11ll11 I I lllllil 1 1111 I ll lill I ll 'Il||1 |||1 i I 1 1 Il 1111111 I I V.8 : 2397 actgtagtgaagaaactagatagagaaaaagaggataaatatttattcacaattctggca 2456 V.1 : 2472 aaagataacggggtaccacccttaaccagcaatgtcacagtctttgtaagcattattgat 2531 V.8 : 2457 aaagataatggggtaccacccttaaccagcaatgtcacagtctttgtaagcattattgat 2516 V.1 : 2532 cagaatgacaatagcccagttttcactcacaatgaatacaacttctatgtcccagaaaac 2591 ||| 1i lil il lll I I l I I 1 IlI I1 1 l I l ll1111111 I ill1I1 lil11 |1 Il1lil V.8 : 2517 cagaatgacaatagcccagttttcactcacaatgaatacaaattctatgtcccagaaaac 2576 V.1 : 2592 cttccaaggcatggtacagtaggactaatcactgtaactgatcctgattatggagacaat 2651 ||1I II II III I I i II| 1 I III I|11II1 I I I 11I11 I 1I i I IIIi I 11111I1II1I1111i V.8 : 2577 cttccaaggcatggtacagtaggactaatcactgtaactgatcctgattatggagacaat 2636 V.1 : 2652 tctgcagttacgctctccattttagatgagaatgatgacttcaccattgattcacaaact 2711 li1 I111111 1 1 i i IIII I III 11111111lil1l1lllllllll llllllllll llll il V.8 2637 tctgcagttacgctctccattttagatgagaatgatgacttcaccattgattcacaaact 2696 V.1 2712 ggtgtcatccgaccaaatatttcatttgatagagaaaaacaagaatcttacactttctat 2771 V.8 2697 ggtgtcatccgaccaaatatttcatttgatagagaaaaacaagaatcttacactttctat 2756 293 v.1 2772 gtaaaggctgaggatggtggtagagtatcacgttcttcaagtgccaaagtaaccataaat 2831 ilillI Ill 11il li Ii ll I 11111 Il I 1 III|illllIlil IIi I I i V.8 2757 gtaaaggctgaggatggtggtagagtatcacgttcttcaagtgccaaagtaaccataaat 2816 V.1 2832 gtggttgatgtcaatgacaacaaaccagttttcattgtccctccttccaactgttcttat 2891 11illililllilll l il I lli lill~l IlIIll Ill 11|| l lil l 111111 V.8 2817 gtggttgatgtcaatgacaacaaaccagttttcattgtccctccttacaactattcttat 2876 V.1 2892 gaattggttctaccgtccactaatccaggcacagtggtctttcaggtaattgctgttgac 2951 I lill1 Illli1 l ll1 I 1 I1I1 illl1 11 I llillilil I|llilli 11 ||lil1 I1I1li V.8 2877 gaattggttctaccgtccactaatccaggcacagtggtctttcaggtaattgctgttgac 2936 V.1 2952 aatgacactggcatgaatgcagaggttcgttacagcattgtaggaggaaacacaagagat 3011 V.8 2937 aatgacactggcatgaatgcagaggttcgttacagcattgtaggaggaaacacaagagat 2996 V.1 3012 ctgtttgcaatcgaccaagaaacaggcaacataacattgatggagaaatgtgatgttaca 3071 V.8 2997 ctgtttgcaatcgaccaagaaacaggcaacataacattgatggagaaatgtgatgttaca 3056 V.1 3072 gaccttggtttacacagagtgttggtcaaagctaatgacttaggacagcctgattctctc 3131 1|1 111 || t ll I ||li111 1 l1l1ll||lil1 l Ill lil I I 1ill lil li lill l V.8 : 3057 gaccttggtttacacagagtgttggtcaaagctaatgacttaggacagcctgattctctc 3116 V.1 : 3132 ttcagtgttgtaattgtcaatctgttcgtgaatgagtcggtgaccaatgctacactgatt 3191 V.8 : 3117 ttcagtgttgtaattgtcaatctgttcgtgaatgagtcagtgaccaatgctacactgatt 3176 V.1 : 3192 aatgaactggtgcgcaaaagcactgaagcaccagtgaccccaaatactgagatagctgat 3251 llllllllll illll illlll i11111111 llllllllilllllllllllllll i V.8 : 3177 aatgaactggtgcgcaaaagcattgaagcaccagtgaccccaaatactgagatagctgat 3236 V.1 : 3252 gtatcctcaccaactagtgactatgtcaagatcctggttgcagctgttgtggcaccata 3311 V.8 : 3237 gtatcctcaccaactagtgactatgtcaagatcctggttgcagctgttgctggcaccata 3296 V.1 : 3312 actgtcgttgtagttattttcatcactgctgtagtaagatgtcgccaggcaccacacctt 3371 l1illllllllllllllllllllilllllllllllllllllllllll1lllll1l11llll1i V.8 : 3297 actgtcgttgtagttattttcatcactgctgtagtaagatgtcgccaggcaccacacctt 3356 V.1 : 3372 aaggctgctcagaaaaacaagcagaattctgaatgggctaccccaaacccagaaaacagg 3431 l ill ll lll l ll li I li ll lllli lilllll ll Iti llll Itl lillIil lill V.8 : 3357 aaggctgctcagaaaaacatgcagaattctgaatgggctaccccaaacccagaaaacagg 3416 V.1 : 3432 cagatgataatgatgaagaaaaagaaaaagaagaagaagcattcccctaagaacttgctg 3491 Itliltl 111l 11lll Itlil lil illlllltlll 1 lll tlllllllllllllli lil lilli V.8 : 3417 cagatgataatgatgaagaaaaagaaaaagaagaagaagcattcccctaagaacctgctg 3476 V.1 : 3492 cttaattttgtcactattgaagaaactaaggcagatgatgttgacagtgatggaaacaga 3551 Ii I li I ill Iili I Ii ll I i|Ilill11ililil Il I ill 1lil I lillll I V.8 3477 cttaatgttgtcactattgaagaaactaaggcagatgatgttgacagtgatggaaacaga 3536 V.1 3552 gtcacactagaccttcctattgatctagaagagcaaacaatgggaaagtacaattgggta 3611 lil l l l lill llll li llllI il ll I ill lll li I ii li i li iii 11 1 3 V.8: 3537 gtcacactagaccttcctattgatctagaagagcaaacaatgggaaagtacaattgggta 3596 294 V.1 : 3612 actacacctactactttcaagcccgacagccctgatttggcccgacactacaaatctgcc 3671 1I 111l 1|| 11|| 11I l 11111|| Il Ili 1 1 11 1||||||1|I lli II l 1 I||I 1 | V.8 : 3597 actacacctactactttcaagcctgacagccctgatttggcccgacactacaaatctgcc 3656 V.1 : 3672 tctccacagcctgccttccaaattcagcctgaaactcccctgaattcgaagcaccacatc 3731 I1 1 111I I 11 I lil Illl li llili111 |11lii I l 111I I i ! 1111li1 I V.8 3657 tctccacagcctgccttccaaattcagcctgaaactcccctgaatttgaagcaccacatc 3716 V.1 3732 atccaagaactgcctctcgataacacctttgtggcctgtgactctatctccaagtgttcc 3791 l i l l l I l i l li l 1 1 l l l lll l lll ll l l l l l l ll l l l i l l 1l l l l 1 I l l il i V.8 3717 atccaagaactgcctctcgataacacctttgtggcctgtgactctatctccaattgttcc 3776 V.1 3792 tcaagcagttcagatccctacagcgtttctgactgtggctatccagtgacgaccttcgag 3851 lilll l ll 1 lllllllili lIIll11 11 illl lll ll I1II1| 111 1111 V.8 : 3777 tcaagcagttcagatccctacagcgtttctgactgtggctatccagtgacaaccttcgag 3836 V.1 : 3852 gtacctgtgtccgtacacaccagaccg 3878 11l11|1 lii 11I| 1 11 l I ll I li i V.8 : 3837 gtacctgtgtccgtacacaccagaccg 3863 Score 1567 bits (815), Expect - 0.0Identities = 829/836 (99%) Strand = Plus / Plus V.1 : 3 ggtggtccagtacctccaaagatatggaatacactcctgaaatatcctgaaaactttttt 62 I I1|||I1l1I1II 1I I I ll 11 1 11 11111111Ill l l 1 11l I l11il 11 1 1 l |||I V.8 1 ggtggtccagtacctccaaagatatggaatacactcctgaaatatcctgaaacctttttt 60 V.1 63 ttttcagaatcctttaataagcagttatgtcaatctgaaagttgcttacttgtactttat 122 V.8 61 ttttcagaatcctttaataagcagttatgtcaatctgaaagttgcttacttgtactttat 120 V.1 123 attaatagctattcttgtttttcttatccaaagaaaaatcctctaatccccttttcacat 182 I111l111 IlII IIIIlIIIIIII ii i111illI|111I lli 111111||||| lli V.8 121 attaatagctattcttgtttttcttatccaaagaaaaatcctctaatccccttttcacat 180 V.1 183 gatagttgttaccatgtttaggcattagtcacatcaacccctctcctctcccaaacttct 242 V.8 181 gatagttgttaccatgtttaggcgttagtcacatcaacccctctcctctcccaaacttct 240 V.1 243 cttcttcaaatcaaactttattagtccctcctttataatgattccttgcctcgttttatc 302 1Ill1 1lill 11111|111111111111lli111111ll111111Ill 1 1|||| V.8 241 cttcttcaaatcaaactttattagtccctcctttataatgattccttgcctccttttatc 300 V.1 303 cagatcaattttttttcactttgatgcccagagctgaagaaatggactactgtataaatt 362 1 11111|||li l illl ll1I i llI lll1 lll lli | 111111 ||||||1111I V.8 301 cagatcaattttttttcactttgatgcccagagctgaagaaatggactattgtataaatt 360 V.1 363 attcattgccaagagaataattgcattttaaacccatattataacaaagaataatgatta 422 I1l11ll1lll11li1ll1l1llll111ll1l111111 11111111||11 ||II||11 V.8 : 361 attcattgccaagagaataattgcattttaaacccatgttataacaaagaataatgatta 420 V.1 : 423 tattttgtgatttgtaacaaataccctttattttcccttaactattgaattaaatatttt 482 lill: 1ll11 ll l l li ll l l l l l li l 11111 lill l1llllllll1 ll1 4 V.8 :421 tattttgtgatttgtaacaaataccctttattttcccttaactattgaattaaatatttt 480 295 V.1 483 aattatttgtattctctttaactatcttggtatattaaagtattatcttttatatattta 542 111 1 1 1 1 1 11 1 | || 1 111 l i l 1l l li l ll l ll l l ll l l l I l ll11 I I li V.8 481 aattatttgtattctctttaactatcttggtatattaaagtattatcttttatatattta 540 V.1 543 tcaatggtggacacttttataggtactctgtgtcatttttgatactgtaggtatcttatt 602 111 111l1illi1 11 111 11 lIl l i l 1 |11 lil 1 lil111Illi1||| ll I11 V.8 541 tcaatggtggacacttttataggtactctgtgtcatttttgatactgtaggtatcttatt 600 V.1 603 tcatttatctttattcttaatgtacgaattcataatatttgattcagaacaaatttatca 662 ||i111111111I1111ill111l1l1111 I1II1111ll1 lill IIllil I I I 1|I 11111I V.8 601 tcatttatctttattcttaatgtacgaattcataatatttgattcagaacagatttatca 660 V.1 663 ctaattaacagagtgtcaattatgctaacatctcatttactgattttaatttaaaacagt 722 li l111111111I111 1||11 11il |1Il1 lilllI11 illil11 I I11 I1 l l I l1I|| V.8 661 ctaattaacagagtgtcaattatgctaacatctcatttactgattttaatttaaaacagt 720 V.1 : 723 ttttgttaacatgcatgtttagggttggcttcttaataatttcttcttcctcttctctct 782 I l illII lIII lI11lIIl IIII IlIl I l l 11 11 illi|11 11 V.8 : 721 ttttgttaacatgcatgtttagggttggcttcttaataatttcttcttcctcttctctct 780 V.1 : 783 ctcctcttcttttggtcagtgttgtgcgggttaatacaacaaactgtaacaagtgt 838 1111il l lIi111 ll llllilli lllIlll lili l lillll illlillIl V.8 : 781 ctcctcttcttttggtcagtgttgtgcgggttaatacaacaaactgtcacaagtgt 836 Table LIV(g). Peptide sequences of protein coded by 109P1D4 v.8 (SEQ ID NO: 276) MFRVGFLIIS SSSSLSPLLL VSVVRVNTTN CHKCLLSGTY IFAVLLVCVV FHSGAQEKNY 60 TIREEIPENV LIGNLLKDLN LSLIPNKSLT TTMQFKLVYK TGDVPLIRIE EDTGEIFTTG 120 ARIDREKLCA GIPRDEHCFY EVEVAILPDE IFRLVKIRFL IEDINDNAPL FPATVINISI 180 PENSAINSKY TLPAAVDPDV GINGVQNYEL IKSQNIFGLD VIETPEGDKM PQLIVQKELD 240 REEKDTYVMK VKVEDGGFPQ RSSTAILQVS VTDTNDNHPV FKETEIEVSI PENAPVGTSV 300 TQLHATDADI GENAKIHFSF SNLVSNIARR LFHLNATTGL ITIKEPLDRE ETPNHKLLVL 360 ASDGGLMPAR AMVLVNVTDV NDNVPSIDIR YIVNPVNDTV VLSENIPLNT KIALITVTDK 420 DADHNGRVTC FTDHEIPFRL RPVFSNQFLL ENAAYLDYES TKEYAIKLLA ADAGKPPLNQ 480 SAMLFIKVKD ENDNAPVFTQ SFVTVSIPEN NSPGIQLMKV SATDADSGPN AEINYLLGPD 540 APPEFSLDRR TGMLTVVKKL DREKEDKYLF TILAKDNGVP PLTSNVTVFV SIIDQNDNSP 600 VFTHNEYKFY VPENLPRHGT VGLITVTDPD YGDNSAVTLS ILDENDDFTI DSQTGVIRPN 660 ISFDREKQES YTFYVKAEDG GRVSRSSSAK VTINVVDVND NKPVFIVPPY NYSYELVLPS 720 TNPGTVVFQV IAVDNDTGMN AEVRYSIVGG NTRDLFAIDQ ETGNITLMEK CDVTDLGLHR 780 VLVKANDLGQ PDSLFSVVIV NLFVNESVTN ATLINELVRK SIEAPVTPNT EIADVSSPTS 840 DYVKILVAAV AGTITVVVVI FITAVVRCRQ APHLKAAQKN MQNSEWATPN PENRQMIMMK 900 KKKKKKKHSP KNLLLNVVTI EETKADDVDS DGNRVTLDLP IDLEEQTMGK YNWVTTPTTF 960 KPDSPDLARH YKSASPQPAF QIQPETPLNL KHHIIQELPL DNTFVACDSI SNCSSSSSDP 1020 YSVSDCGYPV TTFEVPVSVH TRPSQRRVTF HLPEGSQESS SDGGLGDHDA GSLTSTSHGL 1080 PLGYPQEEYF DRATPSNRTE GDGNSDPEST FIPGLKKEIT VQPTVEEASD NCTQECLIYG 1140 HSDACWMPAS LDHSSSSQAQ ASALCHSPPL SQASTQHHSP PVTQTIVLCH SPPVTQTIAL 1200 CHSPPPIQVS ALHHSPPLVQ GTALHHSPPS AQASALCYSP PLAQAAAISH SSSLPQVIAL 1260 HRSQAQSSVS LQQGWVQGAN GLCSVDQGVQ GSATSQFYTM SERLHPSDDS IKVIPLTTFA 1320 PRQQARPSRG DSPIMETHPL 1340 Table LV(g). Amino acid sequence alignment of 109P1D4 v.1 (SEQ ID NO: 277) and 109P1D4 v.8 (SEQ ID NO: 278) Score 1961 bits (5081), Expect = 0.0ldentitles = 99211009 (98%), PosItives = 99511009 (98%) V.1 3 LLSGTYIFAVLLACVVFHSGAQEKNYTIREEMPENVLIGDLLKDLNLSLIPNKSLTTAMQ 62 LLSGTYIFAVLL CVVFHSGAQEKNYTIREE+PENVLIG+LLKDLNLSLIPNKSLTT MQ V.8 35 LLSGTYIFAVLLVCVVFHSGAQEKNYTIREEIPENVLIGNLLKDLNLSLIPNKSLTTTMQ 94 V.1 63 FKLVYKTGDVPLIRIEEDTGEIETTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIFRL 122 FKLVYKTGDVPLIRIEEDTGEIFTTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIFRL V.8 95 FKLVYKTGDVPLIRIEEDTGEIFTTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIFRL 154 296 V.1 123 VKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIKSQ 182 VKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIKSQ V.8 155 VKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIKSQ 214 V.1 183 NIFGLDVIETPEGDKMPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVTDT 242 NIFGLDVIETPEGDKMPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVTDT v.8 215 NIFGLDVIETPEGDKMPQLIVQKELDREEKDTYVMIKVKVEDGGFPQRSSTAILQVSVTDT 274 V.1 243 NDNHPVFKETEIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSFSNLVSNIARRLFHL 302 NDNHPVFKETEIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSFSNLVSNIARRLFHL V.8 : 275 NDNHPVFKETEIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSFSNLVSNIARRLFHL 334 V.1 : 303 NATTGLITIKEPLDREETPNHKLLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYIVN 362 NATTGLITIKEPLDREETPNHKLLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYIVN V.8 : 335 NATTGLITIKEPLDREETPNHKLLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYIVN 394 V.1 : 363 PVNDTVVLSENIPLNTKIALITVTDKDADHNGRVTCFrDHEIPFRLRPVFSNQFLLETAA 422 PVNDTVVLSENIPLNTKIALITVTDKDADHNGRVTCFrDHEIPFRLRPVFSNQFLLE AA V.8 : 395 PVNDTVVLSENIPLNTKIALITVTDKDADHNGRVTCFTIDHEIPFRLRPVFSNQFLLENAA 454 V.1 : 423 YLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDENDNAPVflQSFVTVSIPENNSPG 482 YLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDENDNAPVFTQSFVTVSIPENNSPG V.8 : 455 YLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDENDNAPVrQSFVTVSIPENNSPG 514 V.1 : 483 IQLTKVSAMDADSGPNAKINYLLGPDAPPEFSLDCRTGMLTVVKKLDREKEDKYLFTILA 542 IQL KVSA DADSGPNA+INYLLGPDAPPEFSLD RTGMLTVVKKLDREKEDKYLE7ILA V.8 : 515 IQLMKVSATDADSGPNAEINYLLGPDAPPEFSLDRRTGMLTVVKKLDREKEDKYLFTILA 574 V.1 : 543 KDNGVPPLTSNVTVFVSIIDQNDNSPVFTHNEYNFYVPENLPRHGTVGLITVTDPDYGDN 602 KDNGVPPLTSNVTVFVSIIDQNDNSPVFTHNEY FYVPENLPRHGTVGLITVTDPDYGDN V.8 : 575 KDNGVPPLTSNVTVFVSIIDQNDNSPVFTHNEYKFYVPENLPRHGTVGLITVTDPDYGDN 634 V.1 : 603 SAVTLSILDENDDFTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVTIN 662 SAVTLSILDENDDFTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVTIN V.8 : 635 SAVTLSILDENDDFTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVTIN 694 V.1 : 663 VVDVNDNKPVFIVPPSNCSYELVLPSTNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNTRD 722 VVDVNDNKPVFIVPP N S.YELVLPSTNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNTRD V.8 : 695 VVDVNDNKPVFIVPPYNYSYELVLPSTNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNTRD 754 V.1 723 LFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPDSLFSVVIVNLFVNESVTNATLI 782 LFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPDSLFSVVIVNLFVNESVTNATLI V.8 755 LFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPDSLFSVVIVNLFVNESVTNATLI 814 V.1 783 NELVRKSTEAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVRCRQAPHL 842 NELVRKS EAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVRCRQAPHL V.8 : 815 NELVRKSIEAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVRCRQAPHL 874 V.1 : 843 KAAQKNKQNSEWATPNPENRQMIMMKKKKKKKKHSPKNLLLNFVTIEETKADDVDSDGNR 902 KAAQKN QNSEWATPNPENRQMIMMKKKKKKKKHSPKNLLLN VTIEETKADDVDSDGNR V.8 : 875 KAAQKNMQNSEWATPNPENRQMIMMKKKKKKKKHSPKNLLLNVVTIEETKADDVDSDGNR 934 V.1 : 903 VTLDLPIDLEEQTMGKYNWVTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLNSKHHI 962 VTLDLPIDLEEQTMGKYNWVTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLN KHHI V.8 : 935 VTLDLPIDLEEQTMGKYNWVTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLNLKHHI 994 V.1 : 963 IQELPLDNTFVACDSISKCSSSSSDPYSVSDCGYPVTTFEVPVSVHTRP 1011 IQELPLDNTFVACDSIS CSSSSSDPYSVSDCGYPVTTFEVPVSVHTRP V.8 : 995 IQELPLDNTFVACDSISNCSSSSSDPYSVSDCGYPVTTFEVPVSVLTRP 1043 Table Ul(h). Nucleotide sequence of transcript variant 109PI D4 v.9 (SEQ ID NO: 279) cccctttctc cccctctgtt aagtccctcc ccctcgccat tcaaaagggc tggctcggca 60 ctggctcctt gcagtcggcg aactgtctgg gcgggaggag ccgtgagcag tagctgcact 120 cagctgcccg cgcggcaaag aggaaggcaa gccaaacaga gtgcgcagag tggcagtgcc 180 agcggcgaca caggcagcac aggcagcccg ggctgcctga atagcctcag aaacaacctc 240 agcgactccg gctgctctgc ggactgcgag ctgtggcggt agagcccgct acagcagtcg 300 cagtctccgt ggagcgggcg gaagcctttt ttctcccttt cgtttacctc ttcattctac 360 297 tctaaaggca tcgttattag gaaaatcctg ttgtgaataa gaaggattcc acagatcaca 420 taccagagcg gttttgcctc agctgctctc aactttgtaa tcttgtgaag aagctgacaa 480 gcttggctga ttgcagtgca ctatgaggac tgaatgacag tgggttttaa ttcagatatt 540 tcaagtgttg tgcgggttaa tacaacaaac tgtcacaagt gtttgttgtc cgggacgtac 600 attttcgcgg tcctgctagt atgcgtggtg ttccactctg gcgcccagga gaaaaactac 660 accatccgag aagaaattcc agaaaacgtc ctgataggca acttgttgaa agaccttaac 720 ttgtcgctga ttccaaacaa gtccttgaca actactatgc agttcaagct agtgtacaag 780 accggagatg tgccactgat tcgaattgaa gaggatactg gtgagatctt cactaccggc 840 gctcgcattg atcgtgagaa attatgtgct ggtatcccaa gggatgagca ttgcttttat 900 gaagtggagg ttgccatttt gccggatgaa atatttagac tggttaagat acgttttctg 960 atagaagata taaatgataa tgcaccattg ttcccagcaa cagttatcaa catatcaatt 1020 ccagagaact cggctataaa ctctaaatat actctcccag cggctgttga tcctgacgta 1080 ggcataaacg gagttcaaaa ctacgaacta attaagagtc aaaacatttt tggcctcgat 1140 gtcattgaaa caccagaagg agacaagatg ccacaactga ttgttcaaaa ggagttagat 1200 agggaagaga aggataccta tgtgatgaaa gtaaaggttg aagatggtgg ctttcctcaa 1260 agatccagta ctgctatttt gcaagtaagt gttactgata caaatgacaa ccacccagtc 1320 tttaaggaga cagagattga agtcagtata ccagaaaatg ctcctgtagg cacttcagtg 1380 acacagctcc atgccacaga tgctgacata ggtgaaaatg ccaagatcca cttctctttc 1440 agcaatctag tctccaacat tgccaggaga ttatttcacc tcaatgccac cactggactt 1500 atcacaatca aagaaccact ggatagggaa gaaacaccaa accacaagtt actggttttg 1560 gcaagtgatg gtggattgat gccagcaaga gcaatggtgc tggtaaatgt tacagatgtc 1620 aatgataatg tcccatccat tgacataaga tacatcgtca atcctgtcaa tgacacagtt 1680 gttctttcag aaaatattcc actcaacacc aaaattgctc tcataactgt gacggataag 1740 gatgcggacc ataatggcag ggtgacatgc ttcacagatc atgaaattcc tttcagatta 1800 aggccagtat tcagtaatca gttcctcctg gagaatgcag catatcttga ctatgagtcc 1860 acaaaagaat atgccattaa attactggct gcagatgctg gcaaacctcc tttgaatcag 1920 tcagcaatgc tcttcatcaa agtgaaagat gaaaatgaca atgctccagt tttcacccag 1980 tctttcgtaa ctgtttctat tcctgagaat aactctcctg gcatccagtt gatgaaagta 2040 agtgcaacgg atgcagacag tgggcctaat gctgagatca attacctgct aggccctgat 2100 gctccacctg aattcagcct ggatcgtcgt acaggcatgc tgactgtagt gaagaaacta 2160 gatagagaaa aagaggataa atatttattc acaattctgg caaaagataa tggggtacca 2220 cccttaacca gcaatgtcac agtctttgta agcattattg atcagaatga caatagccca 2280 gttttcactc acaatgaata caaattctat gtcccagaaa accttccaag gcatggtaca 2340 gtaggactaa tcactgtaac tgatcctgat tatggagaca attctgcagt tacgctctcc 2400 attttagatg agaatgatga cttcaccatt gattcacaaa ctggtgtcat ccgaccaaat 2460 atttcatttg atagagaaaa acaagaatct tacactttct atgtaaaggc tgaggatggt 2520 ggtagagtat cacgttcttc aagtgccaaa gtaaccataa atgtggttga tgtcaatgac 2580 aacaaaccag ttttcattgt ccctccttac aactattctt atgaattggt tctaccgtcc 2640 actaatccag gcacagtggt ctttcaggta attgctgttg acaatgacac tggcatgaat 2700 gcagaggttc gttacagcat tgtaggagga aacacaagag atctgtttgc aatcgaccaa 2760 gaaacaggca acataacatt gatggagaaa tgtgatgtta cagaccttgg tttacacaga 2820 gtgttggtca aagctaatga cttaggacag cctgattctc tcttcagtgt tgtaattgtc 2880 aatctgttcg tgaatgagtc agtgaccaat gctacactga ttaatgaact ggtgcgcaaa 2940 agcattgaag caccagtgac cccaaatact gagatagctg atgtatcctc accaactagt 3000 gactatgtca agatcctggt tgcagctgtt gctggcacca taactgtcgt tgtagttatt 3060 ttcatcactg ctgtagtaag atgtcgccag gcaccacacc ttaaggctgc tcagaaaaac 3120 atgcagaatt ctgaatgggc taccccaaac ccagaaaaca ggcagatgat aatgatgaag 3180 aaaaagaaaa agaagaagaa gcattcccct aagaacctgc tgcttaatgt tgtcactatt 3240 gaagaaacta aggcagatga tgttgacagt gatggaaaca gagtcacact agaccttcct 3300 attgatctag aagagcaaac aatgggaaag tacaattggg taactacacc tactactttc 3360 aagcctgaca gccctgattt ggcccgacac tacaaatctg cctctccaca gcctgccttc 3420 caaattcagc ctgaaactcc cctgaatttg aagcaccaca tcatccaaga actgcctctc 3480 gataacacct ttgtggcctg tgactctatc tccaattgtt cctcaagcag ttcagatccc 3540 tacagcgttt ctgactgtgg ctatccagtg acaaccttcg aggtacctgt gtccgtacac 3600 accagaccga ctgattccag gacatgaact attgaaatct gcagtgagat gtaactttct 3660 aggaacaaca aaattccatt ccccttccaa aaaatttcaa tgattgtgat ttcaaaatta 3720 ggctaagatc attaattttg taatctagat ttcccattat aaaagcaagc aaaaatcatc 3780 ttaaaaatga tgtcctagtg aaccttgtgc tttctttagc tgtaatctgg caatggaaat 3840 ttaaaattta tggaagagac agtgcagcgc aataacagag tactctcatg ctgtttctct 3900 gtttgctctg aatcaacagc catgatgtaa tataaggctg tcttggtgta tacacttatg 3960 gttaatatat cagtcatgaa acatgcaatt acttgccctg tctgattgtt gaataattaa 4020 aacattatct ccaggagttt ggaagtgagc tgaactagcc aaactactct ctgaaaggta 4080 298 tccagggcaa gagacatttt taagacccca aacaaacaaa aaacaaaacc aaaacactct 4140 ggttcagtgt tttgaaaata ttgactaaca taatattgct gagaaaatca tttttattac 4200 ccaccactct gcttaaaagt tgagtgggcc gggcgcggtg gctcacgcct gtaattccag 4260 cactttggga ggccgaggcg ggtggatcac gaggtcagga tattgagacc atcctggcta 4320 acatggtgaa accccatctc cactaaaaat acaaaaaatt agctgggcgt ggtggcgggc 4380 gcctgtagtc ccagctactc gggaggctga ggcaggagaa tggcgtgaac ccgggaggcg 4440 gagcttgcag tgagccgaga tggcgccact gcactccagc ctgggtgaca gagcaagact 4500 ctgtctcaaa aagaaaaaaa tgttcagtga tagaaaataa ttttactagg tttttatgtt 4560 gattgtactc atgctgttcc actcctttta attattaaaa agttattttt ggctgggtgt 4620 ggtggctcat acctgtaatc ccagcacttt gggaggccga ggcgggtgga tcacctgagg 4680 tcaggagttc aagaccagtc tggccaacat 4710 Table Ull(h). Nucleotide sequence alignment of 109P1D4 v.1 (SEQ ID NO: 280) and 109P1D4 v.9 (SEQ ID NO: 281) Score = 5664 bits (2946), Expect = 0.01dentities = 3000/3027 (99%) Strand = Plus / Plus V.1: 852 ttgttgtccgggacgtacattttcgcggtcctgctagcatgcgtggtgttccactctggc 911 lilllllllll11 1 llll 1 1llll 1ll 1l lil 1l1ll lil111l 1llllll lilllllli V.9 583 ttgttgtccgggacgtacattttcgcggtcctgctagtatgcgtggtgttccactctggc 642 V.1 912 gcccaggagaaaaactacaccatccgagaagaaatgccagaaaacgtcctgataggcgac 971 ||| 11 1| |11 11 il lll ll lill ll 11 1 1 1 l ll iilllll 1llll 1lli il V.9 643 gcccaggagaaaaactacaccatccgagaagaaattccagaaaacgtcctgataggcaac 702 V.1 972 ttgttgaaagaccttaacttgtcgctgattccaaacaagtccttgacaactgctatgcag 1031 ||||||1I l II liiill-i llllillllllllllllllll lilllll I i ll li V.9 703 ttgttgaaagaccttaacttgtcgctgattccaaacaagtccttgacaactactatgcag 762 V.1 1032 ttcaagctagtgtacaagaccggagatgtgccactgattcgaattgaagaggatactggt 1091 lil1lll il l llllllllllllllil illlllll ill lillll1 l Ili ili V.9 763 ttcaagctagtgtacaagaccggagatgtgccactgattcgaattgaagaggatactggt 822 V.1 1092 gagatcttcactactggcgctcgcattgatcgtgagaaattatgtgctggtatcccaagg 1151 V.9 823 gagatcttcactaccggcgctcgcattgatcgtgagaaattatgtgctggtatcccaagg 882 V.1 : 1152 gatgagcattgcttttatgaagtggaggttgccattttgccggatgaaatatttagactg 1211 V.9 : 883 gatgagcattgcttttatgaagtggaggttgccattttgccggatgaaatatttagactg 942 V.1 : 1212 gttaagatacgttttctgatagaagatataaatgataatgcaccattgttcccagcaaca 1271 l111l 11l li l li llllillllllllllllllllllllllllllll III 11 ll llli V.9 : 943 gttaagatacgttttctgatagaagatataaatgataatgcaccattgttcccagcaaca 1002 V.1 : 1272 gttatcaacatatcaattccagagaactcggctataaactctaaatatactctcccagcg 1331 lil11l 1ll1l i lll 11i l lilllllllll il lll 11 11 illlI1lllill V.9 : 1003 gttatcaacatatcaattccagagaactcggctataaactctaaatatactctcccagcg 1062 V.1 : 1332 gctgttgatcctgacgtaggaataaacggagttcaaaactacgaactaattaagagtcaa 1391 li lllll llll ll li llllllllll11lll1111 Illlllll11li ill 1lllllill V.9 : 1063 gctgttgatcctgacgtaggcataaacggagttcaaaactacgaactaattaagagtcaa 1122 V.1 : 1392 aacatttttggcctcgatgtcattgaaacaccagaaggagacaagatgccacaactgatt 1451 1111|lilli lll llll1111 i11111111111111 lllll V.9 : 1123 aacatttttggcctcgatgtcattgaaacaccagaaggagacaagatgccacaactgatt 1182 V.1 : 1452 gttcaaaaggagttagatagggaagagaaggatacctacgtgatgaaagtaaaggttgaa 1511 lillllll11111|1111111111||11ill ill11l1lillllllillill1 299 V.9 1183 gttcaaaaggagttagatagggaagagaaggatacctatgtgatgaaagtaaaggttgaa 1242 V.1 1512 gatggtggctttcctcaaagatccagtactgctattttgcaagtgagtgttactgataca 1571 Illll111 11 l l ll li ll l l llllil111 1 1 11 1 1 lili i lillill V.9 1243 gatggtggctttcctcaaagatccagtactgctattttgcaagtaagtgttactgataca 1302 V.1 1572 aatgacaaccacccagtctttaaggagacagagattgaagtcagtataccagaaaatgct 1631 11lll11lill l1ll1l1l 1l111l1l1111lil111ill1ll1ll1ll11l1lilli1l V.9 1303 aatgacaaccacccagtctttaaggagacagagattgaagtcagtataccagaaaatgct 1362 V.1 1632 cctgtaggcacttcagtgacacagctccatgccacagatgctgacataggtgaaaatgcc 1691 11llllll 1l1li11lll 1l 1l1l1l1llIl i lllll111 IlI llllll1 il1ll1i li li V.9 1363 cctgtaggcacttcagtgacacagctccatgccacagatgctgacataggtgaaaatgcc 1422 V.1 1692 aagatccacttctctttcagcaatctagtctccaacattgccaggagattatttcacctc 1751 lillllillll1111l11111111ll111111llI llill1il1il1i1 V.9 1423 aagatccacttctctttcagcaatctagtctccaacattgccaggagattatttcacctc 1482 V.1 : 1752 aatgccaccactggacttatcacaatcaaagaaccactggatagggaagaaacaccaaac 1811 l 11 II l Il llI llll Ilillll Illili llllll1 Ili ii!lllillil1il111 V.9 : 1483 aatgccaccactggacttatcacaatcaaagaaccactggatagggaagaaacaccaaac 1542 V.1 : 1812 cacaagttactggttttggcaagtgatggtggattgatgccagcaagagcaatggtgctg 1871 V.9 1543 cacaagttactggttttggcaagtgatggtggattgatgccagcaagagcaatggtgctg 1602 V.1 1872 gtaaatgttacagatgtcaatgataatgtcccatccattgacataagatacatcgtcaat 1931 11111! 1 1111111l i II|| 1111111| || IiI 1 il l lil llIlill IlI V.9 1603 gtaaatgttacagatgtcaatgataatgtcccatccattgacataagatacatcgtcaat 1662 V.1 1932 cctgtcaatgacacagttgttctttcagaaaatattccactcaacaccaaaattgctctc 1991 V.9 : 1663 cctgtcaatgacacagttgttctttcagaaaatattccactcaacaccaaaattgctctc 1722 V.1 : 1992 ataactgtgacggataaggatgcggaccataatggcagggtgacatgcttcacagatcat 2051 V.9 : 1723 ataactgtgacggataaggatgcggaccataatggcagggtgacatgcttcacagatcat 1782 V.1 : 2052 gaaatccctttcagattaaggccagtattcagtaatcagttcctcctggagactgcagca 2111 H11ll 11111l11lllIIllIIl ll lll lll ll illilli1 1111111 V.9 : 1783 gaaattcctttcagattaaggccagtattcagtaatcagttcctcctggagaatgcagca 1842 V.1 : 2112 tatcttgactatgagtccacaaaagaatatgccattaaattactggctgcagatgctggc 2171 V.9 : 1843 tatcttgactatgagtccacaaaagaatatgccattaaattactggctgcagatgctggc 1902 V.1 : 2172 aaacctcctttgaatcagtcagcaatgctcttcatcaaagtgaaagatgaaaatgacaat 2231 1111111 i I 11111111 111i 1 I|I II I I iIIIIIIIII1111111 I V.9 : 1903 aaacctcctttgaatcagtcagcaatgctcttcatcaaagtgaaagatgaaaatgacaat 1962 V.1 2232 gctccagttttcacccagtctttcgtaactgtttctattcctgagaataactctcctggc 2291 1I I I I 1111 I I I I i iiIIii I I I IIII iiii ii I11111 l ii I i iii I I i V.9 1963 gctccagttttcacccagtctttcgtaactgtttctattcctgagaataactctcctggc 2022 V.1 2292 atccagttgacgaaagtaagtgcaatggatgcagacagtgggcctaatgctaagatcaat 2351 300 lI i ll Ill l1 illl l iiillll i lllllllllll llllll i l il l Illi v.9 2023 atccagttgatgaaagtaagtgcaacggatgcagacagtgggcctaatgctgagatcaat 2082 V.1 2352 tacctgctaggccctgatgctccacctgaattcagcctggattgtcgtacaggcatgctg 2411 V.9 2083 tacctgctaggccctgatgctccacctgaattcagcctggatcgtcgtacaggcatgctg 2142 V.1 2412 actgtagtgaagaaactagatagagaaaaagaggataaatatttattcacaattctggca 2471 l ill 1lll11l11ll1l111 lllllllill lillllll illllil 11111il111 ij II V.9 2143 actgtagtgaagaaactagatagagaaaaagaggataaatatttattcacaattctggca 2202 V.1 2472 aaagataacggggtaccacccttaaccagcaatgtcacagtctttgtaagcattattgat 2531 |1111111 l ill ill1ll 1llillll lllllllll illl1l illl illillill IillI V.9 2203 aaagataatggggtaccacccttaaccagcaatgtcacagtctttgtaagcattattgat 2262 V.1 2532 cagaatgacaatagcccagttttcactcacaatgaatacaacttctatgtcccagaaaac 2591 V.9 2263 cagaatgacaatagcccagttttcactcacaatgaatacaaattctatgtcccagaaaac 2322 V.1 2592 cttccaaggcatggtacagtaggactaatcactgtaactgatcctgattatggagacaat 2651 V.9 2323 cttccaaggcatggtacagtaggactaatcactgtaactgatcctgattatggagacaat 2382 V.1 2652 tctgcagttacgctctccattttagatgagaatgatgacttcaccattgattcacaaact 2711 V.9 2383 tctgcagttacgctctccattttagatgagaatgatgacttcaccattgattcacaaact 2442 V.1 2712 ggtgtcatccgaccaaatatttcatttgatagagaaaaacaagaatcttacactttctat 2771 Il il lllll l ll 1111 111i 1llll lll l l1ll1ll111111 lill V.9 2443 ggtgtcatccgaccaaatatttcatttgatagagaaaaacaagaatcttacactttctat 2502 V.1 2772 gtaaaggctgaggatggtggtagagtatcacgttcttcaagtgccaaagtaaccataaat 2831 V.9 2503 gtaaaggctgaggatggtggtagagtatcacgttcttcaagtgccaaagtaaccataaat 2562 V.1 2832 gtggttgatgtcaatgacaacaaaccagttttcattgtccctccttccaactgttcttat 2891 I ll lll lIIIl l lllIl lIIlIIlIlIlIlIlllliI 11l11 l111111 V.9 2563 gtggttgatgtcaatgacaacaaaccagttttcattgtccctccttacaactattcttat 2622 V.1 2892 gaattggttctaccgtccactaatccaggcacagtggtctttcaggtaattgctgttgac 2951 V.9 2623 gaattggttctaccgtccactaatccaggcacagtggttttcaggtaattgctgttgac 2682 V.1 2952 aatgacactggcatgaatgcagaggttcgttacagcattgtaggaggaaacacaagagat 3011 IlIII l IIl Ill lll I I ill IllI lll i l ill1ill1111111111 V.9 2683 aatgacactggcatgaatgcagaggttcgttacagcattgtaggaggaaacacaagagat 2742 V.1 3012 ctgtttgcaatcgaccaagaaacaggcaacataacattgatggagaaatgtgatgttaca 3071 V.9 2743 ctgtttgcaatcgaccaagaaacaggcaacataacattgatggagaaatgtgatgttaca 2802 V.1 3072 gaccttggtttacacagagtgttggtcaaagctaatgacttaggacagcctgattctctc 3131 V.9 2803 gaccttggtttacacagagtgttggtcaaagctaatgacttaggacagcctgattctctc 2862 301 V.1 3132 ttcagtgttgtaattgtcaatctgttcgtgaatgagtcggtgaccaatgctacactgatt 3191 llll l ll llllll 1111111111lill llll li1 lill I 11111 I V.9 2863 ttcagtgttgtaattgtcaatctgttcgtgaatgagtcagtgaccaatgctacactgatt 2922 V.1 3192 aatgaactggtgcgcaaaagcactgaagcaccagtgaccccaaatactgagatagctgat 3251 1111111l11ll 1111lll ili lillllllillliillIIIl ill1111111111 Ii V.9 2923 aatgaactggtgcgcaaaagcattgaagcaccagtgaccccaaatactgagatagctgat 2982 V.1 3252 gtatcctcaccaactagtgactatgtcaagatcctggttgcagctgttgctggcaccata 3311 V.9 2983 gtatcctcaccaactagtgactatgtcaagatcctggttgcagctgttgctggcaccata 3042 V.1 3312 actgtcgttgtagttattttcatcactgctgtagtaagatgtcgccaggcaccacacctt 3371 V.9 3043 actgtcgttgtagttattttcatcactgctgtagtaagatgtcgccaggcaccacacctt 3102 V.1 3372 aaggctgctcagaaaaacaagcagaattctgaatgggctaccccaaacccagaaaacagg 3431 111 iii 1111llilli 1ill11|111il1illi1li1ililli11li111ill11l V.9 3103 aaggctgctcagaaaaacatgcagaattctgaatgggctaccccaaacccagaaaacagg 3162 V.1 3432 cagatgataatgatgaagaaaaagaaaaagaagaagaagcattcccctaagaacttgctg 3491 lilllilllllljjilllllllllllllillllllllIllliljlllIll 11111 V.9 3163 cagatgataatgatgaagaaaaagaaaaagaagaagaagcattcccctaagaacctgctg 3222 V.1 3492 cttaattttgtcactattgaagaaactaaggcagatgatgttgacagtgatggaaacaga 3551 1111 11llllllllllllllllllllllllll ill 1ill ill 111i l 1i I I i V. : 3223 cttaatgttgtcactattgaagaaactaaggcagatgatgttgacagtgatggaaacaga 3282 V.1 : 3552 gtcacactagaccttcctattgatctagaagagcaaacaatgggaaagtacaattgggta 3611 j l ii i l l l li l l l l l l lill Illillll11 11lll1 i1lll ill11 111 111 111 V.9 : 3283 gtcacactagaccttcctattgatctagaagagcaaacaatgggaaagtacaattgggta 3342 V.1 : 3612 actacacctactactttcaagcccgacagccctgatttggcccgacactacaaatctgcc 3671 l l l l l li lllil1 llll1 1lil 111l 11l1ll1ll111lilli!l1lil11l111 V.9 : 3343 actacacctactactttcaagcctgacagccctgatttggcccgacactacaaatctgcc 3402 V.1 : 3672 tctccacagcctgccttccaaattcagcctgaaactcccctgaattcgaagcaccacatc 3731 V.9 : 3403 tctccacagcctgccttccaaattcagcctgaaactcccctgaatttgaagcaccacatc 3462 V.1 : 3732 atccaagaactgcctctcgataacacctttgtggcctgtgactctatctccaagtgttcc 3791 V.9 : 3463 atccaagaactgcctctcgataacacctttgtggcctgtgactctatctccaattgttcc 3522 V.1 : 3792 tcaagcagttcagatccctacagcgtttctgactgtggctatccagtgacgaccttcgag 3851 1111 1111 1lllll 1l i lllll 111l1l lllll11ll11lll ill11il 1 i1l111i1 V.9 3523 tcaagcagttcagatccctacagcgtttctgactgtggctatccagtgacaaccttcgag 3582 V.1 3852 gtacctgtgtccgtacacaccagaccg 3878 111i1ll111111l illllllllllli V.9 3583 gtacctgtgtccgtacacaccagaccg 3609 Table LIV(h). Peptide sequences of protein coded by 109P1D4 v.9 (SEQ ID NO: 282) MTVGFNSDIS SVVRVNTTNC HKCLLSGTYI FAVLLVCVVF HSGAQEKNYT IREEIPENVL 60 IGNLLKDLNL SLIPNKSLTT TMQFKLVYKT GDVPLIRIEE DTGEIFTTGA RIDREKLCAG 120 IPRDEHCFYE VEVAILPDEI FRLVKIRFLI EDINDNAPLF PATVINISIP ENSAINSKYT 180 302 LPAAVDPDVG INGVQNYELI KSQNIFGLDV IETPEGDKMP QLIVQKELDR EEKDTYVMKV 240 KVEDGGFPQR SSTAILQVSV TDTNDNHPVF KETEIEVSIP ENAPVGTSVT QLHATDADIG 300 ENAKIHFSFS NLVSNIARRL FHLNATTGLI TIKEPLDREE TPNHKLLVLA SDGGLMPARA 360 MVLVNVTDVN DNVPSIDIRY IVNPVNDTVV LSENIPLNTK IALITVTDKD ADHNGRVTCF 420 TDHEIPFRLR PVFSNQFLLE NAAYLDYEST KEYAIKLLAA DAGKPPLNQS AMLFIKVKDE 480 NDNAPVFTQS FVTVSIPENN SPGIQLMKVS ATDADSGPNA EINYLLGPDA PPEFSLDRRT 540 GMLTVVKKLD REKEDKYLFT ILAKDNGVPP LTSNVTVFVS IIDQNDNSPV FTHNEYKFYV 600 PENLPRHGTV GLITVTDPDY GDNSAVTLSI LDENDDFTID SQTGVIRPNI SFDREKQESY 660 TFYVKAEDGG RVSRSSSAKV TINVVDVNDN KPVFIVPPYN YSYELVLPST NPGTVVFQVI 720 AVDNDTGMNA EVRYSIVGGN TRDLFAIDQE TGNITLMEKC DVTDLGLHRV LVKANDLGQP 780 DSLFSVVIVN LFVNESVTNA TLINELVRKS IEAPVTPNTE IADVSSPTSD YVKILVAAVA 840 GTITVVVVIF ITAVVRCRQA PHLKAAQKNM QNSEWATPNP ENRQMIMMKK KKKKKKHSPK 900 NLLLNVVTIE ETKADDVDSD GNRVTLDLPI DLEEQTMGKY NWVTTPTTFK PDSPDLARHY 960 KSASPQPAFQ IQPETPLNLK HHIIQELPLD NTFVACDSIS NCSSSSSDPY SVSDCGYPVT 1020 TFEVPVSVHT RPTDSRT 1037 Table LV(h). Amino acid sequence alignment of 109P1D4 v.1 (SEQ ID NO: 283) and 109P1D4 v.9 (SEQ ID NO: 284) Score = 1961 bits (5081), Expect = 0.0ldentitles = 99211009 (98%), Posifives = 995/1009 (98%) V.1 3 LLSGTYIFAVLLACVVFHSGAQEKNYTIREEMPENVLIGDLLKDLNLSLIPNKSLTTAMQ 62 LLSGTYIFAVLL CVVFHSGAQEKNYTIREE+PENVLIG+LLKDLNLSLIPNKSLTT MQ V.9 24 LLSGTYIFAVLLVCVVFHSGAQEKNYTIREEIPENVLIGNLLKDLNLSLIPNKSLTTTMQ 83 V.1 63 FKLVYKTGDVPLIRIEEDTGEIETTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIFRL 122 FKLVYKTGDVPLIRIEEDTGEIFTTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIFRL V.9 84 FKLVYKTGDVPLIRIEEDTGEIFTTGARIDREKLCAGIPRDEHCFYEVEVAILPDEIFRL 143 V.1 123 VKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIKSQ 182 VKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIKSQ V.9 144 VKIRFLIEDINDNAPLFPATVINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIKSQ 203 V.1 183 NIFGLDVIETPEGDKMPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVTDT 242 NIFGLDVIETPEGDKMPQLIVOKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVTDT V.9 204 NIFGLDVIETPEGDKMPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVTDT 263 V.1 : 243 NDNHPVFKETEIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSFSNLVSNIARRLFHL 302 NDNHPVFKETEIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSFSNLVSNIARRLFHL V.9 264 NDNHPVFETEIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSFSNLVSNIARRLFHL 323 V.1 303 NATTGLITIKEPLDREETPNHKLLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYIVN 362 NATTGLITIKEPLDREETPNHKLLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYIVN V.9 : 324 NATTGLITIKEPLDREETPNHKLLVLASDGGLMPARAMVLVNVTDVNDNVPSIDIRYIVN 383 V.1 : 363 PVNDTVVLSENIPLNTKIALITVTDKDADHNGRVTCFTDHEIPFRLRPVFSNQFLLETAA 422 PVNDTVVLSENIPLNTKIALITVTDKDADHNGRVTCFTDHEIPFRLRPVFSNQFLLE AA V.9 : 384 PVNDTVVLSENIPLNTKIALITVTDKDADHNGRVTCFTDHEIPFRLRPVFSNQFLLENAA 443 V.1 : 423 YLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDENDNAPVEQSFVTVSIPENNSPG 482 YLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDENDNAPVETQSFVTVSIPENNSPG V.9 : 444 YLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDENDNAPVfTQSFVTVSIPENNSPG 503 V.1 : 483 IQLTKVSAMDADSGPNAKINYLLGPDAPPEFSLDCRTGMLTVVKKLDREKEDKYLFTILA 542 IQL KVSA DADSGPNA+INYLLGPDAPPEFSLD RTGMLTVVKKLDREKEDKYLFTILA V.9 : 504 IQLMKVSATDADSGPNAEINYLLGPDAPPEFSLDRRTGMLTVVKKLDREKEDKYLFTILA 563 V.1 : 543 KDNGVPPLTSNVTVFVSIIDQNDNSPVFTHNEYNFYVPENLPRHGTVGLITVTDPDYGDN 602 KDNGVPPLTSNVTVFVSIIDQNDNSPVETHNEY FYVPENLPRHGTVGLITVTDPDYGDN V.9 : 564 KDNGVPPLTSNVTVFVSIIDQNDNSPVFTHNEYKFYVPENLPRHGTVGLITVTDPDYGDN 623 V.1 : 603 SAVTLSILDENDDFTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVTIN 662 SAVTLSILDENDDFTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVTIN V.9 : 624 SAVTLSILDENDDFTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVTIN 683 V.1 : 663 VVDVNDNKPVFIVPPSNCSYELVLPSTNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNTRD 722 VVDVNDNKPVFIVPP N SYELVLPSTNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNTRD V.9 : 684 WDVNDNKPVFIVPPYNYSYELVLPSTNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNTRD 743 303 V.1 723 LFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPDSLFSVVIVNLFVNESVTNATLI 782 LFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPDSLFSVVIVNLFVNESVTNATLI v.9 744 LFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPDSLFSVVIVNLFVNESVTNATLI 803 V.1 783 NELVRKSTEAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVRCROAPHL 842 NELVRKS EAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVRCRQAPHL V.9 : 804 NELVRKSIEAPVTPNTEIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVRCRQAPHL 863 V.1 : 843 KAAQKNKQNSEWATPNPENRQMIMM KKKKKKHSPKNLLLNFVTIEETKADDVDSDGNR 902 KAAQKN QNSEWATPNPENRQMIMMKKKKKKKKHSPKNLLLN VTIEETKADDVDSDGNR V.9 : 864 KAAQKNMQNSEWATPNPENRQMIMMKKKKKKKKHSPKNLLLNVVTIEETKADDVDSDGNR 923 V.1 : 903 VTLDLPIDLEEQTMGKYNWVTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLNSKHI 962 VTLDLPIDLEEQTMGKYNWVTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLN KHHI V.9 : 924 VTLDLPIDLEEQTMGKYNWVTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLNLKfHI 983 V.1 : 963 IQELPLDNTFVACDSISKCSSSSSDPYSVSDCGYPVTTFEVPVSVHTRP 1011 IQELPLDNTFVACDSIS CSSSSSDPYSVSDCGYPVTTFEVPVSVHTRP V.9 : 984 IQELPLDNTFVACDSISNCSSSSSDPYSVSDCGYPVTTFEVPVSVHTRP 1032

Claims (28)

1. An isolated polynucleotide that encodes a protein, wherein said polynucleotide comprises a sequence selected from the group consisting of: (a) the sequence set forth in SEQ ID NO: 4 from nucleotide residues 503 to 3667; (b) the sequence set forth in SEQ ID NO: 10 from nucleotide residues 846 to 4778; and (c) the sequence set forth in SEQ ID NO: 10.

2. The isolated polynucleotide according to claim 1 wherein the isolated polynucleotide consists of the sequence set forth in SEQ ID NO: 4 from nucleotide residues 503 to 3667 or the sequence set forth in SEQ ID NO: 10 from nucleotide residues 846 to 4778.

3. A recombinant expression vector comprising the isolated polynucleotide according to claim 1 or 2.

4. A host cell comprising the recombinant expression vector according to claim 3.

5. A process for producing a protein, said process comprising culturing the host cell according to claim 4 under conditions sufficient to produce a protein encoded by the recombinant expression vector, wherein said protein comprises the amino acid sequence set forth in SEQ ID NO: 5 or SEQ ID NO: 11.

6. The process according to claim 5, wherein said process further comprises recovering the protein so produced.

7. An isolated protein comprising an amino acid sequence set forth in SEQ ID NO: 5 or SEQ ID NO: 11.

8. A composition comprising the isolated protein according to claim 7 and a pharmaceutically acceptable carrier.

9. An isolated antibody or fragment thereof that specifically binds to an epitope of a protein comprising an amino acid sequence set forth in SEQ ID NO: 5 or SEQ ID NO: 11.

10. The isolated antibody or fragment thereof according to claim 9, wherein said antibody is a monoclonal antibody.

11. The isolated antibody or fragment thereof according to claim 9 or 10, wherein said antibody is a recombinant protein.

12. The isolated antibody or fragment thereof according to any one of claims 9 to 11, wherein said antibody or fragment is a Fab, F(ab')2, Fv or Sfv fragment.

13. The isolated antibody or fragment thereof according to claim 9 or 10, wherein said antibody is a human antibody or human antibody or a humanized antibody or antibody fragment.

14. The isolated antibody or fragment thereof according to any one of claims 9 to 13 when labeled with a cytotoxic agent. 305

15. The isolated antibody or fragment thereof according to claim 14, wherein the cytotoxic agent is selected from the group consisting of a radioactive isotope, a chemotherapeutic agent and a toxin.

16. The isolated antibody or fragment thereof according to claim 14 or 15, wherein the cytotoxic agent is a radioactive isotope selected from the group consisting of 2 1 At, 1311, 1251 S9Y, 8 6 Re, 15 3 Sm, 212Bi, 32P, and 177 LU or other radioactive isotope of Lu.

17. The isolated antibody or fragment thereof according to claim 14 or 15, wherein the cytotoxic agent is a chemotherapeutic agent selected from the group consisting of taxol, actinomycin, mitomycin, etoposide. tenoposide, vincristine, vinblastine, colchicine, gelonin and calicheamicin.

18. The isolated antibody or fragment thereof according to claim 14 or 15, wherein the cytotoxic agent is a toxin selected from the group consisting of diptheria toxin, enomycin, phenomycin, Pseudomonas exotoxin (PE) A, PE40, abrin, abrin A chain, mitogellin, modeccin A chain, and alpha sarcin.

19. A composition comprising the isolated antibody or fragment thereof according to any one of claims 9 to 18 and a pharmaceutically acceptable carrier.

20. A hybridoma that produces the antibody according to claim 10.

21. A recombinant vector comprising a polynucleotide that encodes the antibody or fragment thereof according to any one of claims 9 to 13.

22. A method of detecting the presence or absence of a protein in a test sample, said method comprising contacting the sample with the isolated antibody or fragment thereof according to any one of claims 9 to 13 and detecting binding of the antibody or fragment to a protein in the test sample.

23. The method according to claim 22, wherein the test sample is from a patient with a cancer.

24. The method according to claim 23, wherein the cancer is a lymphoma.

25. A method of delivering a cytotoxic agent to a cell that expresses a protein of SEQ ID NO: 5 or SEQ ID NO: 11, said method comprising providing to the cell an effective amount of the antibody or fragment thereof according to any one of claims 9 to 18 or the composition according to claim 19.

26. The method according to claim 25, wherein the cell is a cancer cell.

27. The method according to claim 26, wherein the cancer cell is a lymphoma cell, 306

28. The isolated polynucleotide according to claim 1 or 2 or the recombinant expression vector of claim 3 or the host cell of claim 4 or the process of claim 5 or 6 or the composition of claim 8 or 19 or the isolated protein of claim 7 or the isolated antibody or fragment thereof according to any one of claims 9 to 18 or the hybridoma of claim 20 or the recombinant vector of claim 21 or the method according to any on of claims 22 to 27 substantially as hereinbefore described with reference to the accompanying figures and/or examples. DATED this SEVENTEENTH day of APRIL, 2012 Agensis, Inc. by the Patent Attorneys for the Applicant: FB Rice