KR20200020927A - 대장암을 검출하기 위한 바이오마커 - Google Patents
대장암을 검출하기 위한 바이오마커 Download PDFInfo
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Abstract
대장암을 조기에 검출하기 위한 바이오마커의 제공. 하기 1∼22의 22개의 단백질 중 적어도 1개의 단백질, 또는 1∼22의 단백질의 부분 펩티드 중 적어도 1개의 펩티드로 이루어지는 대장암 검출을 위한 대장암 바이오마커:
1. 아넥신 A11;
2. 아넥신 A3;
3. 아넥신 A4;
4. 테나신-N;
5. 트랜스페린 수용체 단백질 1;
6. 글루코오스 트랜스포터 1;
7. 보체 성분 C9;
8. CD88 항원;
9. 78kDa 글루코오스 제어 단백질;
10. α-1-산성 글리코프로테인;
11. 매트릭스메탈로프로테아제 9;
12. 앙기오포이에틴-1;
13. CD67 항원;
14. 뮤신 -5B;
15. 어댑터 단백질 GRB2;
16. 아넥신 A5;
17. 올팍토메딘-4;
18. 중성 아미노산 트랜스포터 B(0);
19. 트리펩티딜펩티다제 1;
20. 열쇼크 관련 70kDa 단백질 2;
21. 프로테아좀 서브유닛 α타입-5; 또는
22. 호중구 젤라티나아제 관련 리포칼린.
1. 아넥신 A11;
2. 아넥신 A3;
3. 아넥신 A4;
4. 테나신-N;
5. 트랜스페린 수용체 단백질 1;
6. 글루코오스 트랜스포터 1;
7. 보체 성분 C9;
8. CD88 항원;
9. 78kDa 글루코오스 제어 단백질;
10. α-1-산성 글리코프로테인;
11. 매트릭스메탈로프로테아제 9;
12. 앙기오포이에틴-1;
13. CD67 항원;
14. 뮤신 -5B;
15. 어댑터 단백질 GRB2;
16. 아넥신 A5;
17. 올팍토메딘-4;
18. 중성 아미노산 트랜스포터 B(0);
19. 트리펩티딜펩티다제 1;
20. 열쇼크 관련 70kDa 단백질 2;
21. 프로테아좀 서브유닛 α타입-5; 또는
22. 호중구 젤라티나아제 관련 리포칼린.
Description
본 발명은, 대장암의 검출에 사용할 수 있는 신규한 단백질 또는 펩티드 바이오마커에 관한 것이다.
대장암(CRC)은, 세계에서 가장 빈도가 높은 암의 하나이며, CRC를 위한 효과적 바이오마커의 개발은, 인간의 생존율 향상에 불가결하다. 그러나, 현재 사용되는 대장암의 진단법은 변잠혈이나 CEA 등 대단히 정밀도가 낮은 것뿐이며, 대장암을 조기에 고정밀도로 진단할 수 있는 새로운 바이오마커는 발견되고 있지 않으며, 혈중 바이오마커가 절실하게 요구되고 있다.
지금까지 대규모 오믹스 연구에 의해, 다수의 암 관련 인자 및 암의 바이오마커 후보가 발견되어 왔음에도 불구하고, 임상응용에 이른 혈중 바이오마커는 아직 존재하지 않고 있다. 이것을 뒷받침하는 증거로서, 최근의, 주식은 미국 식품 의약국(FDA)에 의해 승인된 바이오마커는, 매년 2건 이하로 극히 적다. 이러한 정체의 원인의 하나는, 바이오마커 개발의 전략에 심각한 문제가 있는 것으로 여겨지고 있다.
종래, 많은 임상검사에 있어서, 단백질 바이오마커의 검출은 항체 베이스의 정량화 분석법(주로 효소결합 항체면역측정법(ELISA)을 사용함)에 의해 행해져 왔다. 이 방법은 항체의 품질에 크게 의존하고 있으므로, 정밀도, 특히 특이도에 문제가 있으며, 또한 다항목의 마커 후보를 동시에 평가하는 것은 곤란하다.
질량분석계(MS)의 최근의 진보에 의해, 임상검사법이 크게 바뀔 가능성이 있다. 그 이유로서, 타깃 프로테오믹스를 대표하는 방법인 선택반응 모니터링/다중반응 모니터링법(SRM/MRM)은, 고정밀도이며 바이오마커 단백질의 정량을 행할 수 있을 뿐만 아니라, 다항목의 마커를 동시에 정량할 수 있기 때문이다. 이전의 보고에서, Whiteaker 등은, SRM/MRM법을 사용하여 환자 혈장 중의 다항목의 유방암 바이오마커 후보 단백질의 정량을 실시하였다(비특허문헌 1을 참조). 이 외에도, SRM/MRM법을 사용하여 다양한 암의 바이오마커 후보 단백질을 검증한 예는 본 발명자들 그룹의 보고도 포함하여 몇 개 보고되어 있다(비특허문헌 2∼4를 참조).
이와 같이, SRM/MRM법을 사용한 타깃 프로테오믹스는, 바이오마커 발견을 위한 강력한 툴이 된다.
Whiteaker, J. et al., Nat. BIotechnol.29, 625-634(2011)
Kume, H. et al., Mol. Cell. Proteomics 13, 1471-1484(2014)
Muraoka, S. et al., J. Proteome Res.11, 4201-4210(2012)
Narumi, R. et al., J. Proteome Res.11, 5311-5322(2012)
본 발명은, 대장암을 조기에 검출하기 위한 바이오마커의 제공을 목적으로 한다.
본 발명자들은, 먼저 PubMed의 문헌검색으로부터 CRC 바이오마커 후보 단백질을 검색했다. 이들 바이오마커 후보 단백질을 혈중에서 검출하기 위하여, 혈중의 세포외소포(EV)에 착안했다. 왜냐하면, EV는 세포간 커뮤니케이션의 중개자로서 기능하는 것이 최근 주목받고 있을 뿐만 아니라, 다양한 질병의 발증이나 진전(進展)에 관계하는 것으로 알려져 있어, 바이오마커 후보를 많이 포함하고 있는 것으로 고려되고 있기 때문이다. 또한, 질량분석계를 사용하여 혈중의 미량의 단백질을 검출하고자 할 때, 알부민 등의 혈중에 다량으로 존재하는 협잡단백질에 의해, 미량의 마커 후보 단백질의 검출이 저해되는 경우가 있다. 그러나, 혈중의 EV를 정제할 때, 다량의 협잡 단백질이 제거되므로, EV 중의 미량의 바이오마커 후보 단백질의 검출이 가능하게 된다. 따라서, EV 함유 단백질은 유망한 바이오마커 후보로 여겨졌다.
본 발명자들은 문헌검색으로 발견한 바이오마커 후보 단백질 중에서, 혈중 EV에 존재할 가능성이 있는 단백질에 후보를 좁히고, SRM/MRM법을 사용하여 이들 단백질의 정량을 행하였다. 그 결과, CRC의 조기진단을 위한 몇 개의 바이오마커 후보를 특정하고, 본 발명을 완성시키기에 이르렀다.
즉, 본 발명의 태양은 하기와 같다.
[1] 하기 1∼22의 22개의 단백질 중 적어도 1개의 단백질, 또는 1∼22의 단백질의 부분 펩티드 중 적어도 1개의 펩티드로 이루어지는 대장암 검출을 위한 대장암 바이오마커:
1. 아넥신 A11(Annexin A11)(ANXA 11)(서열번호 1);
2. 아넥신 A3(Annexin A3)(ANXA 3)(서열번호 2);
3. 아넥신 A4(Annexin A4)(ANXA 4)(서열번호 3);
4. 테나신-N(Tanascin-N)(TNN)(서열번호 4);
5. 트랜스페린 수용체 단백질 1(Transferrin receptor protein 1)(TFRC)(서열번호 5);
6. 글루코오스 트랜스포터 1(GLUT-1)(SLC2A1)(서열번호 6);
7. 보체 성분 C9(Complement component C9)(C9)(서열번호 7);
8. CD88 항원(CD88 antigen)(C5AR1)(서열번호 8);
9.78kDa 글루코오스 제어 단백질(78kDa glucose-regulated protein)(HSPA5)(서열번호 9);
10. α-1-산성 글리코프로테인(α-1-acid glycoprotein)(ORM1)(서열번호 10);
11. 매트릭스메탈로프로테아제 9(Matrix metalloproteinase-9)(MMP9)(서열번호 11);
12. 앙기오포이에틴-1(Angiopoietin-1)(ANGPT1)(서열번호 12);
13. CD67 항원(CD67 antigen)(CEACAM8)(서열번호 13);
14. 뮤신-5B(Mucin-5B)(MUC5B)(서열번호 14);
15. 어댑터 단백질 GRB2(Adapter protein GRB2)(GRB2)(서열번호 15);
16. 아넥신 A5(Annexin A5)(ANXA 5)(서열번호 16);
17. 올팍토메딘-4(Olfactomedin-4)(OLFM4)(서열번호 17);
18. 중성 아미노산 트랜스포터 B(0)(Neutral amino acid transporter B(0))(SLC1A5)(서열번호 18);
19. 트리펩티딜펩티다제 1(Tripeptidyl-peptidase 1)(TPP1)(서열번호 19);
20. 열쇼크 관련 70kDa 단백질 2(Heat shock-related 70kDa protein 2)(HSPA2)(서열번호 20);
21. 프로테아좀 서브유닛 α 타입-5(Proteasome subunit alpha type-5)(PSMA5)(서열번호 21); 또는
22. 호중구(好中球) 젤라티나아제 관련 리포칼린(Neutrophil gelatinase-associated lipocalin)(LCN2)(서열번호 22).
[2] [1]의 1∼22의 22개의 단백질 중 2개 이상의 단백질, 또는 1∼22의 단백질의 부분 펩티드 중 2개 이상의 펩티드를 조합하여 이루어지는, [1]의 대장암 검출을 위한 대장암 바이오마커.
[3] [1]의 1∼22의 단백질의 부분 펩티드가 서열번호 23∼59로 표시되는 아미노산서열로 이루어지는 펩티드인, [1] 또는 [2]의 대장암 검출을 위한 대장암 바이오마커.
[4] 하기 12개의 단백질 중 적어도 1개의 단백질, 또는 상기 12개의 단백질의 부분 펩티드 중 적어도 1개의 펩티드로 이루어지는, [1]의 대장암 검출을 위한 대장암 바이오마커:
1. 아넥신 A11(서열번호 1);
2. 아넥신 A3(서열번호 2);
3. 아넥신 A4(서열번호 3);
4. 테나신-N (서열번호 4);
5. 트랜스페린 수용체 단백질 1(서열번호 5);
6. 글루코오스 트랜스포터 1(서열번호 6);
8. CD88 항원(서열번호 8);
11. 매트릭스메탈로프로테아제 9(서열번호 11);
16. 아넥신 A5(서열번호 16);
17. 올팍토메딘-4(서열번호 17);
19. 트리펩티딜펩티다제 1(서열번호 19); 또는
22. 호중구 젤라티나아제 관련 리포칼린(서열번호 22).
[5] [4]의 12개의 단백질 중 2개 이상의 단백질, 또는 상기 12개의 단백질의 부분 펩티드 중 2개 이상의 펩티드를 조합하여 이루어지는, [4]의 대장암 검출을 위한 대장암 바이오마커.
[6] [4]의 12개의 단백질의 부분 펩티드가 서열번호 23∼34, 37, 38, 43, 44, 53, 54, 56 및 59로 표시되는 아미노산서열로 이루어지는 펩티드인, [4] 또는 [5]의 대장암 검출을 위한 대장암 바이오마커.
[7] 아넥신 A4 혹은 아넥신 A11, 또는 이들의 부분 펩티드로 이루어지는, [1]의 대장암 검출을 위한 대장암 바이오마커.
[8] 아넥신 A4와 아넥신 A11, 또는 아넥신 A4의 부분 펩티드와 아넥신 A11의 부분 펩티드를 조합하여 이루어지는, [7]의 대장암 검출을 위한 대장암 바이오마커.
[9] 아넥신 A4 및 아넥신 A11의 부분 펩티드가 서열번호 23, 24, 27 및 28로 표시되는 아미노산서열로 이루어지는 펩티드인, [7] 또는 [8]에 기재된 대장암 검출을 위한 대장암 바이오마커.
[10] [1]∼[9] 중 어느 쪽인가의 대장암 바이오마커와 CEA를 조합하여 이루어지는, 대장암 검출을 위한 대장암 바이오마커.
[11] 생체시료 중의 [1]∼[10] 중 어느 하나의 대장암 바이오마커를 측정하는 것을 포함하는 대장암 검출 방법.
[12] 생체시료 중의 [1]∼[10] 중 어느 하나의 대장암 바이오마커를 측정하고, 상기 바이오마커가 정상인과 비교하여 고농도로 존재하는 경우에, 대장암에 이환(罹患)되어 있는 것으로 판단하는, 대장암 검출 방법.
[13] 생체시료가 혈액 중의 세포외소포(EV)인, [11] 또는 [12]의 대장암 검출 방법.
[14] 검출이 면역학적 측정법 또는 질량분석법에 의해 행해지는, [11]∼[13] 중 어느 하나의 대장암 검출 방법.
[15] 생체시료 중의 [1]∼[10] 중 어느 하나의 대장암 바이오마커에 대한 항체를 포함하는 대장암 검출 키트.
본 명세서는 본원의 우선권 기초가 되는 일본특허출원 번호 2017-129941호의 개시 내용을 포함한다.
본 발명의 바이오마커에 의해 대장암을 고감도로 또한 고특이적으로 검출할 수 있고, 특히 조기의 대장암을 검출할 수 있다. 또한, 바이오마커를 조합함으로써, 더욱 고감도로 또한 고특이적인 검출할 수 있다.
도 1은 세포외소포(EV) 중의 대장암 마커의 탐색을 위한 전략을 나타낸 도면이다. 도면 중에는, 각각의 공정에서 선발된 후보 단백질의 수를 나타낸다.
도 2는 EV에서의, CRC 바이오마커 후보 단백질을 위한 샷건·프로테오믹스 분석의 방법을 나타낸 도면이다. 도 2의 a는 EV의 조제 및 MS 분석의 공정을 나타내고, 도 2의 b는 샷건프로테옴 해석에 의해 동정된 바이오마커 후보 단백질 및 EV단백질의 벤다이어그램 해석의 결과를 나타낸다. 혈청 또는 세포배양상청액으로부터 동정된 EV 단백질 중, 356개의 대장암 바이오마커 후보 단백질이 EV 단백질로서 동정되었다.
도 3은 SRM 표적 단백질(46) 및 펩티드(71)를 나타낸 도면이다.
도 4는 고도의 정확도(AUC>0.7)로 검증된 단백질의 리스트를 나타낸 도면이다.
도 5a는 SR M분석에 의한 3군(N, C 및 Cm) 사이의 혈청중 펩티드의 상대 적정량의 결과를 나타낸 도면이다. N은 비암(非癌) 대조 환자를 나타내고, C는 전이가 없는 암 환자를 나타내고, Cm은 전이가 있는 암 환자를 나타낸다. 도트플롯그래프는, SI 펩티드에 대한 내재적 펩티드의 피크 면적비를 나타낸다(*; p<0.05, **; p<0.01, N. S; 유의차없음). 세로축은 Area Ratio(면적비)를 나타낸다.
도 5b는 SRM 분석에 의한 3군(N, C 및 Cm) 사이의 펩티드의 상대적 정량의 결과를 나타낸 도면이다(도 5a의 계속).
도 5c는 SRM 분석에 의한 3군(N, C 및 Cm) 사이의 펩티드의 상대 적정량의 결과를 나타낸 도면이다(도 5b의 계속).
도 5d는 SRM 분석에 의한 3군(N, C 및 Cm) 사이의 펩티드의 상대 적정량의 결과를 나타낸 도면이다(도 5c의 계속).
도 5e는 SRM 분석에 의한 3군(N, C 및 Cm) 사이의 펩티드의 상대 적정량의 결과를 나타낸 도면이다(도 5d의 계속).
도 5f는 SRM 분석에 의한 3군(N, C 및 Cm) 사이의 펩티드의 상대 적정량의 결과를 나타낸 도면이다(도 5e의 계속).
도 6a는 표적 펩티드의 통계적 해석의 결과를 나타낸 도면이다(part 1). 도 6a의 a는 SRM 분석에 의한 3군(N, C 및 Cm) 사이의 펩티드의 상대 적정량의 결과를 나타낸다. N은 비암 대조를 나타내고, C는 전이가 없는 암을 나타내고, Cm은 전이가 있는 암을 나타낸다. 도트플롯 그래프는, SI 펩티드에 대한 내재적 펩티드의 피크 면적비를 나타낸다(*; p<0.05, **; p<0.01, N. S; 유의차없음). 세로축은 Area Ratio(면적비)를 나타낸다. 도 6a의 b는 N과 C를 식별하기 위한 ROC 곡선 분석의 결과(1) 및 C와 Cm을 식별하기 위한 ROC 곡선 분석의 결과(2)를 나타낸다. 식별을 위한 곡선 아래의 면적(AUC)을 각각의 그래프에 나타낸다. 세로축은 sensitivity(감도)를 나타내고, 가로축은 1-specificity(특이성)를 나타낸다.
도 6b는 표적 펩티드의 통계적 해석의 결과를 나타낸 도면이다(part 2). 도 6b의 c는 SRM 분석에 의한 3군(N, C 및 Cm) 사이의 펩티드의 상대 적정량의 결과를 나타낸다. N은 비암 대조를 나타내고, C는 전이가 없는 암을 나타내고, Cm은 전이가 있는 암을 나타낸다. 도트플롯 그래프는, SI 펩티드에 대한 내재적 펩티드의 피크 면적비를 나타낸다(*; p<0.05, **; p<0.01, N. S; 유의차없음). 세로축은 Area Ratio(면적비)를 나타낸다. 도 6b의 d는 N과 C를 식별하기 위한 ROC 곡선 분석의 결과(1) 및 C와 Cm을 식별하기 위한 ROC 곡선 분석의 결과(2)를 나타낸다. 식별을 위한 곡선 아래의 면적(AUC)을 각각의 그래프에 나타낸다. 세로축은sensitivity(감도)를 나타내고, 가로축은 1-specificity(특이성)를 나타낸다.
도 7a는 N과 C를 식별하기 위한 ROC 곡선(1) 및 C와 Cm을 식별하기 위한 ROC 곡선(2)을 나타낸 도면이다(part 1). 식별을 위한 곡선 아래의 면적(AUC)을 각각의 그래프에 나타낸다. 세로축은 sensitivity(감도)를 나타내고, 가로축은 1-specificity(특이도)를 나타낸다.
도 7b는 N과 C를 식별하기 위한 ROC 곡선(1) 및 C와 Cm을 식별하기 위한 ROC 곡선(2)을 나타낸 도면이다(도 7a의 계속).
도 7c는 N과 C를 식별하기 위한 ROC 곡선(1) 및 C와 Cm을 식별하기 위한 ROC 곡선(2)을 나타낸 도면이다(도 7b의 계속).
도 7d는 N과 C를 식별하기 위한 ROC 곡선(1) 및 C와 Cm을 식별하기 위한 ROC 곡선(2)을 나타낸 도면이다(도 7c의 계속).
도 7e는 N과 C를 식별하기 위한 ROC 곡선(1) 및 C와 Cm을 식별하기 위한 ROC 곡선(2)을 나타낸 도면이다(도 7d의 계속).
도 7f는 N과 C를 식별하기 위한 ROC 곡선(1) 및 C와 Cm을 식별하기 위한 ROC 곡선(2)을 나타낸 도면이다(도 7e의 계속).
도 8a는 표적 펩티드 조합의 ROC 곡선 분석의 결과를 나타낸 도면이다(part 1). 펩티드를 조합했을 때의 진단 감도를 N과 C의 사이에서 평가했다. 곡선 아래의 면적(AUC), 감도(sensitivity) 및 특이도(specificity)를 각각의 그래프에 나타내었다.
도 8b는 표적 펩티드 조합의 ROC 곡선 분석의 결과를 나타낸 도면이다(part 2). 펩티드를 조합했을 때의 진단 감도를 N과 C의 사이에서 평가했다. 곡선 아래의 면적(AUC), 감도(sensitivity) 및 특이성(specificity)을 각각의 그래프에 나타내었다.
도 9는 표적 펩티드 조합의 ROC 곡선 분석의 결과를 나타낸 도면이다. 펩티드가 조합했을 때의 진단 감도를 N과 C의 사이에서 평가했다. 곡선 아래의 면적(AUC), 감도(sensitivity) 및 특이도(specificity)를 각각의 그래프에 나타내었다. 도 9는, 높은 정확성(AUC>0.9)의 조합을 나타낸다. 다른 조합은 도 8a 및 도 8b에 나타내었다.
도 10a는 표적 펩티드와 CEA의 감도(sensitivity)의 비교 결과를 나타낸 도면이다. 컷오프값을 N의 최대 피크 면적에 설정한 경우의 감도는, 샘플의 비율로서 산출된다(점선은, 특이도가 100%인 것을 나타낸다). 세로축은 Area Ratio(면적비)를 나타낸다.
도 10b는 표적 펩티드와 CEA의 감도(sensitivity)의 비교 결과를 나타낸 도면이다(도 10a의 계속).
도 10c는 표적 펩티드와 CEA의 감도(sensitivity)의 비교 결과를 나타낸 도면이다(도 10b의 계속).
도 11은 표적 펩티드와 CEA의 감도의 비교 결과를 나타낸 도면이다. 컷오프값(Cutoff)을 N의 최대 피크 면적에 설정한 경우의 감도(sensitivity)는, 샘플의 비율로서 산출된다(점선은, 특이성이 100%인 것을 나타낸다). 도 11에 있어서는, N과 C의 식별에서의 감도가 탑 3개의 펩티드를 나타낸다. 3개의 펩티드에 관한 그래프의 세로축은 Area Ratio(면적비)를 나타낸다. CEA 보다 감도가 높은 다른 펩티드는 도 10a∼10c에 나타내었다.
도 2는 EV에서의, CRC 바이오마커 후보 단백질을 위한 샷건·프로테오믹스 분석의 방법을 나타낸 도면이다. 도 2의 a는 EV의 조제 및 MS 분석의 공정을 나타내고, 도 2의 b는 샷건프로테옴 해석에 의해 동정된 바이오마커 후보 단백질 및 EV단백질의 벤다이어그램 해석의 결과를 나타낸다. 혈청 또는 세포배양상청액으로부터 동정된 EV 단백질 중, 356개의 대장암 바이오마커 후보 단백질이 EV 단백질로서 동정되었다.
도 3은 SRM 표적 단백질(46) 및 펩티드(71)를 나타낸 도면이다.
도 4는 고도의 정확도(AUC>0.7)로 검증된 단백질의 리스트를 나타낸 도면이다.
도 5a는 SR M분석에 의한 3군(N, C 및 Cm) 사이의 혈청중 펩티드의 상대 적정량의 결과를 나타낸 도면이다. N은 비암(非癌) 대조 환자를 나타내고, C는 전이가 없는 암 환자를 나타내고, Cm은 전이가 있는 암 환자를 나타낸다. 도트플롯그래프는, SI 펩티드에 대한 내재적 펩티드의 피크 면적비를 나타낸다(*; p<0.05, **; p<0.01, N. S; 유의차없음). 세로축은 Area Ratio(면적비)를 나타낸다.
도 5b는 SRM 분석에 의한 3군(N, C 및 Cm) 사이의 펩티드의 상대적 정량의 결과를 나타낸 도면이다(도 5a의 계속).
도 5c는 SRM 분석에 의한 3군(N, C 및 Cm) 사이의 펩티드의 상대 적정량의 결과를 나타낸 도면이다(도 5b의 계속).
도 5d는 SRM 분석에 의한 3군(N, C 및 Cm) 사이의 펩티드의 상대 적정량의 결과를 나타낸 도면이다(도 5c의 계속).
도 5e는 SRM 분석에 의한 3군(N, C 및 Cm) 사이의 펩티드의 상대 적정량의 결과를 나타낸 도면이다(도 5d의 계속).
도 5f는 SRM 분석에 의한 3군(N, C 및 Cm) 사이의 펩티드의 상대 적정량의 결과를 나타낸 도면이다(도 5e의 계속).
도 6a는 표적 펩티드의 통계적 해석의 결과를 나타낸 도면이다(part 1). 도 6a의 a는 SRM 분석에 의한 3군(N, C 및 Cm) 사이의 펩티드의 상대 적정량의 결과를 나타낸다. N은 비암 대조를 나타내고, C는 전이가 없는 암을 나타내고, Cm은 전이가 있는 암을 나타낸다. 도트플롯 그래프는, SI 펩티드에 대한 내재적 펩티드의 피크 면적비를 나타낸다(*; p<0.05, **; p<0.01, N. S; 유의차없음). 세로축은 Area Ratio(면적비)를 나타낸다. 도 6a의 b는 N과 C를 식별하기 위한 ROC 곡선 분석의 결과(1) 및 C와 Cm을 식별하기 위한 ROC 곡선 분석의 결과(2)를 나타낸다. 식별을 위한 곡선 아래의 면적(AUC)을 각각의 그래프에 나타낸다. 세로축은 sensitivity(감도)를 나타내고, 가로축은 1-specificity(특이성)를 나타낸다.
도 6b는 표적 펩티드의 통계적 해석의 결과를 나타낸 도면이다(part 2). 도 6b의 c는 SRM 분석에 의한 3군(N, C 및 Cm) 사이의 펩티드의 상대 적정량의 결과를 나타낸다. N은 비암 대조를 나타내고, C는 전이가 없는 암을 나타내고, Cm은 전이가 있는 암을 나타낸다. 도트플롯 그래프는, SI 펩티드에 대한 내재적 펩티드의 피크 면적비를 나타낸다(*; p<0.05, **; p<0.01, N. S; 유의차없음). 세로축은 Area Ratio(면적비)를 나타낸다. 도 6b의 d는 N과 C를 식별하기 위한 ROC 곡선 분석의 결과(1) 및 C와 Cm을 식별하기 위한 ROC 곡선 분석의 결과(2)를 나타낸다. 식별을 위한 곡선 아래의 면적(AUC)을 각각의 그래프에 나타낸다. 세로축은sensitivity(감도)를 나타내고, 가로축은 1-specificity(특이성)를 나타낸다.
도 7a는 N과 C를 식별하기 위한 ROC 곡선(1) 및 C와 Cm을 식별하기 위한 ROC 곡선(2)을 나타낸 도면이다(part 1). 식별을 위한 곡선 아래의 면적(AUC)을 각각의 그래프에 나타낸다. 세로축은 sensitivity(감도)를 나타내고, 가로축은 1-specificity(특이도)를 나타낸다.
도 7b는 N과 C를 식별하기 위한 ROC 곡선(1) 및 C와 Cm을 식별하기 위한 ROC 곡선(2)을 나타낸 도면이다(도 7a의 계속).
도 7c는 N과 C를 식별하기 위한 ROC 곡선(1) 및 C와 Cm을 식별하기 위한 ROC 곡선(2)을 나타낸 도면이다(도 7b의 계속).
도 7d는 N과 C를 식별하기 위한 ROC 곡선(1) 및 C와 Cm을 식별하기 위한 ROC 곡선(2)을 나타낸 도면이다(도 7c의 계속).
도 7e는 N과 C를 식별하기 위한 ROC 곡선(1) 및 C와 Cm을 식별하기 위한 ROC 곡선(2)을 나타낸 도면이다(도 7d의 계속).
도 7f는 N과 C를 식별하기 위한 ROC 곡선(1) 및 C와 Cm을 식별하기 위한 ROC 곡선(2)을 나타낸 도면이다(도 7e의 계속).
도 8a는 표적 펩티드 조합의 ROC 곡선 분석의 결과를 나타낸 도면이다(part 1). 펩티드를 조합했을 때의 진단 감도를 N과 C의 사이에서 평가했다. 곡선 아래의 면적(AUC), 감도(sensitivity) 및 특이도(specificity)를 각각의 그래프에 나타내었다.
도 8b는 표적 펩티드 조합의 ROC 곡선 분석의 결과를 나타낸 도면이다(part 2). 펩티드를 조합했을 때의 진단 감도를 N과 C의 사이에서 평가했다. 곡선 아래의 면적(AUC), 감도(sensitivity) 및 특이성(specificity)을 각각의 그래프에 나타내었다.
도 9는 표적 펩티드 조합의 ROC 곡선 분석의 결과를 나타낸 도면이다. 펩티드가 조합했을 때의 진단 감도를 N과 C의 사이에서 평가했다. 곡선 아래의 면적(AUC), 감도(sensitivity) 및 특이도(specificity)를 각각의 그래프에 나타내었다. 도 9는, 높은 정확성(AUC>0.9)의 조합을 나타낸다. 다른 조합은 도 8a 및 도 8b에 나타내었다.
도 10a는 표적 펩티드와 CEA의 감도(sensitivity)의 비교 결과를 나타낸 도면이다. 컷오프값을 N의 최대 피크 면적에 설정한 경우의 감도는, 샘플의 비율로서 산출된다(점선은, 특이도가 100%인 것을 나타낸다). 세로축은 Area Ratio(면적비)를 나타낸다.
도 10b는 표적 펩티드와 CEA의 감도(sensitivity)의 비교 결과를 나타낸 도면이다(도 10a의 계속).
도 10c는 표적 펩티드와 CEA의 감도(sensitivity)의 비교 결과를 나타낸 도면이다(도 10b의 계속).
도 11은 표적 펩티드와 CEA의 감도의 비교 결과를 나타낸 도면이다. 컷오프값(Cutoff)을 N의 최대 피크 면적에 설정한 경우의 감도(sensitivity)는, 샘플의 비율로서 산출된다(점선은, 특이성이 100%인 것을 나타낸다). 도 11에 있어서는, N과 C의 식별에서의 감도가 탑 3개의 펩티드를 나타낸다. 3개의 펩티드에 관한 그래프의 세로축은 Area Ratio(면적비)를 나타낸다. CEA 보다 감도가 높은 다른 펩티드는 도 10a∼10c에 나타내었다.
이하, 본 발명을 상세하게 설명한다.
본 발명은, 대장암(CRC: colorectal cancer)을 검출하기 위한 바이오마커로서의 단백질 또는 그 부분 펩티드이다. 또한 본 발명은, 상기 바이오마커를 사용하여 대장암을 검출하는 방법이다. 또한 본 발명은, 상기 바이오마커를 사용하여 대장암을 진단하기 위한 보조적 데이터를 취득하는 방법이다. 본 발명의 바이오마커를 사용함으로써, 대장암을 조기에 검출하는 것이 가능하다.
본 발명에서 사용하는 바이오마커는, 예를 들면, 프로테옴 해석 기술에 의해 탐색할 수 있다. 예를 들면, 이하의 공정으로 탐색할 수 있다.
처음에, 대장암 환자의 조직을 사용하여 정량 샷건·프로테오믹스에 의해 바이오마커의 후보가 되는 단백질을 탐색한다. 이 때, 겐(健) 정상인의 대장조직 또는 대장양성종양조직과 전이가 없는 대장암 증례의 조직과 전이가 있는 대장암 증례의 조직 사이에 비교 정량을 행하고, 조직간에서 변동이 인정되는 단백질을 후보 단백질로서 좁힐 수 있다. 또한, 바이오마커 후보 단백질의 탐색은, 선행 연구에 있어서, 대장암의 발증이나 진전에 관련되는 것으로 알려진진 단백질을 사용함으로써도 실시할 수 있다. 이들 바이오마커 후보에 대하여, 특정 질량의 친이온을 선택적으로 파괴하고, 생성한 딸이온(daughter ion) 중 특정 이온을 검출함으로써 복잡한 샘플 내에서 표적으로 하는 단백질유래의 펩티드를 고감도로 검출할 수 있는SRM/MRM(Selected reaction monitoring(선택 반응 모니터링)/Multiple reaction monitoring(다중반응 모니터링))법(Gillette MA et al., Nat Methods.2013; 10: 28-34)을 사용한 타깃 프로테오믹스법에 의해 조직간에서의 발현량의 변동의 검증을 행할 수 있다. 이 검증에 의해, 대장암 바이오마커의 최종후보를 선발할 수 있다. 다음으로, 이 바이오마커 후보가 혈액 등의 생체시료 중에서 검출, 정량할 수 있는지를 확인한다. 이 때, 바람직하게는 혈중의 세포외소포(EV) 획분 중에 의해 검출, 정량을 행한다.
본 발명의 방법에 있어서, 이하의 단백질을 대장암 검출을 위한 바이오마커로서 예로 들 수 있다.
1. 아넥신 A11(Annexin A11)(ANXA 11)(서열번호 1)
2. 아넥신 A3(Annexin A3)(ANXA 3)(서열번호 2)
3. 아넥신 A4(Annexin A4)(ANXA 4)(서열번호 3)
4. 테나신-N(Tanascin-N)(TNN)(서열번호 4)
5. 트랜스페린 수용체 단백질 1(Transferrin receptor protein 1)(TFRC)(서열번호 5)
6. 글루코오스 트랜스포터 1(GLUT-1)(SLC2A1)(서열번호 6)
7. 보체성분 C9(Complement component C9)(C9)(서열번호 7)
8. CD88 항원(CD88 antigen)(C5AR1)(서열번호 8)
9. 78kDa 글루코오스 제어 단백질(78kDa glucose-regulated protein)(HSPA5)(서열번호 9)
10. α-1-산성 글리코프로테인(α-1-acid glycoprotein)(ORM1)(서열번호 10)
11. 매트릭스메탈로프로테아제 9(Matrix metalloproteinase-9)(MMP9)(서열번호 11)
12. 앙기오포이에틴-1(Angiopoietin-1)(ANGPT1)(서열번호 12)
13. CD67 항원(CD67 antigen)(CEACAM8)(서열번호 13)
14. 뮤신-5B(Mucin-5B)(MUC5B)(서열번호 14)
15. 어댑터 단백질 GRB2(Adapter protein GRB2)(GRB2)(서열번호 15)
16. 아넥신 A5(Annexin A5)(ANXA 5)(서열번호 16)
17. 올팍토메딘-4(Olfactomedin-4)(OLFM4)(서열번호 17)
18. 중성 아미노산 트랜스포터 B(0)(Neutral amino acid transporter B(0))(SLC1A5)(서열번호 18)
19. 트리펩티딜펩티다제 1(Tripeptidyl-peptidase 1)(TPP1)(서열번호 19)
20. 열쇼크 관련 70kDa 단백질 2(Heat shock-related 70kDa protein 2)(HSPA2)(서열번호 20)
21. 프로테아좀 서브유닛 α 타입-5(Proteasome subunit alpha type-5)(PSMA5)(서열번호 21)
22. 호중구 젤라티나아제 관련 리포칼린(Neutrophil gelatinase-associated lipocalin)(LCN2)(서열번호 22)
또한, 대장암 검출을 위한 바이오마커로서 사용할 수 있는 상기 단백질의 부분 펩티드로서,
서열번호 23 또는 24로 표시되는 아미노산서열로 이루어지는 펩티드(아넥신 A11의 부분 펩티드),
서열번호 25 또는 26으로 표시되는 아미노산서열로 이루어지는 펩티드(아넥신 A3의 부분 펩티드),
서열번호 27 또는 28로 표시되는 아미노산서열로 이루어지는 펩티드(아넥신 A4의 부분 펩티드),
서열번호 29 또는 30으로 표시되는 아미노산서열로 이루어지는 펩티드(테나신-N의 부분 펩티드),
서열번호 31 또는 32로 표시되는 아미노산서열로 이루어지는 펩티드(트랜스페린 수용체 단백질 1의 부분 펩티드),
서열번호 33 또는 34로 표시되는 아미노산서열로 이루어지는 펩티드(글루코오스 트랜스포터 1의 부분 펩티드),
서열번호 35 또는 36으로 표시되는 아미노산서열로 이루어지는 펩티드(보체성분 C9의 부분 펩티드),
서열번호 37 또는 38로 표시되는 아미노산서열로 이루어지는 펩티드(CD88 항원의 부분 펩티드),
서열번호 39 또는 40으로 표시되는 아미노산서열로 이루어지는 펩티드 (78kDa 글루코오스 제어 단백질의 부분 펩티드),
서열번호 41 또는 42로 표시되는 아미노산서열로 이루어지는 펩티드(α-1-산성 글리코프로테인의 부분 펩티드),
서열번호 43 또는 44로 표시되는 아미노산서열로 이루어지는 펩티드(매트릭스메탈로프로테아제 9의 부분 펩티드),
서열번호 45 또는 46으로 표시되는 아미노산서열로 이루어지는 펩티드(앙기오포이에틴-1의 부분 펩티드),
서열번호 47 또는 48로 표시되는 아미노산서열로 이루어지는 펩티드(CD67 항원의 부분 펩티드),
서열번호 49 또는 50으로 표시되는 아미노산서열로 이루어지는 펩티드(뮤신-5B의 부분 펩티드),
서열번호 51 또는 52로 표시되는 아미노산서열로 이루어지는 펩티드(어댑터 단백질 GRB2의 부분 펩티드),
서열번호 53으로 표시되는 아미노산서열로 이루어지는 펩티드(아넥신 A5의 부분 펩티드),
서열번호 54로 표시되는 아미노산서열로 이루어지는 펩티드(올팍토메딘-4의 부분 펩티드),
서열번호 55로 표시되는 아미노산서열로 이루어지는 펩티드(중성 아미노산 트랜스포터 B(0)의 부분 펩티드),
서열번호 56으로 표시되는 아미노산서열로 이루어지는 펩티드(트리펩티딜펩티다제 1의 부분 펩티드),
서열번호 57로 표시되는 아미노산서열로 이루어지는 펩티드(열쇼크 관련 70kDa 단백질 2의 부분 펩티드),
서열번호 58로 표시되는 아미노산서열로 이루어지는 펩티드(프로테아좀 서브유닛 α 타입-5의 부분 펩티드),
서열번호 59로 표시되는 아미노산서열로 이루어지는 펩티드(호중구 젤라티나아제 관련 리포칼린의 부분 펩티드) 등을 예로 들 수 있다.
본 발명에 있어서는, 상기한 단백질 혹은 그 단백질의 부분 펩티드를 바이오마커로서 사용하지만, 서열번호 1∼59로 표시되는 아미노산서열에 있어서, 1개 또는 수개의 아미노산이 결실, 치환, 부가한 아미노산서열로 이루어지는 단백질 또는 펩티드도 포함하며, 이들 단백질 또는 펩티드도 본 발명의 방법에 있어서 바이오마커로서 사용할 수 있다. 여기서, 「1개 또는 수개」란 「1개 또는 3개」, 「1개 또는 2개」 또는 「1개」를 일컫는다.
펩티드는, 일반적으로는 분자량 1만 이하의 아미노산이 펩티드 결합에 의해 연결한 것을 일컬으며, 아미노산잔기의 개수로서는 수개로부터 50개 이하 정도를 일컫는다. 본 명세서에 있어서는, 단백질 또는 그 부분 펩티드를 바이오마커로서 사용할 수 있고, 부분 펩티드라고 하는 경우, 단백질이 가지는 아미노산서열의 일부의 부분적 아미노산서열을 가지는 펩티드이며 분자량은 한정되지 않지만, 바람직하게는 1만 이하인 것을 일컫는다. 부분 펩티드는, 전사·번역에 의한 발현 합성 과정에서 생성하는 경우도 있으며, 또한 단백질로서 합성된 후에, 생체 내에서 소화 분해되어 소화분해산물 펩티드로서 생성하는 경우도 있다.
이들 단백질 및 펩티드 중에서도 ROC 해석 결과, 양호한 검출감도 및 특이도로 대장암을 검출할 수 있는 것이 판명된, 글루코오스 트랜스포터 1, 트랜스페린 수용체 단백질 1, 아넥신 A5, 매트릭스메탈로프로테아제 9, 아넥신 A4, 아넥신 A11, 테나신-N, 아넥신 A3, 올팍토메딘-4, CD88 항원, 호중구 젤라티나아제 관련 리포칼린 또는 트리펩티딜펩티다제 1, 또는 이들의 부분 펩티드를 대장암 검출을 위한 바이오마커로서 사용하는 것이 바람직하다. 또한, 아넥신 A4 또는 아넥신 A11, 또는 이들의 부분 펩티드를 대장암 검출을 위한 바이오마커로서 사용하는 것이 바람직하다.
본 발명에 있어서, 바이오마커로서 상기한 22개의 단백질 및 부분 펩티드 중에서 적어도 하나의 단백질 및/또는 부분 펩티드를 사용할 수 있지만, 바람직하게는 2종류 이상, 더욱 바람직하게는 3종류 이상, 4종류 이상, 5종류 이상, 6종류 이상, 7종류 이상, 8종류 이상, 9종류 이상, 10종류 이상, 11종류 이상, 12종류 이상, 13종류 이상, 14종류 이상, 15종류 이상, 16종류 이상, 17종류 이상, 18종류 이상, 19종류 이상, 20종류 이상, 21종류 이상, 또는 22종류의 단백질 또는 부분 펩티드을 사용하면 보다 고정밀도로 대장암을 검출할 수 있다. 이 경우에, 다른 단백질의 조합이라도 되고, 어떤 단백질과 그 단백질 이외의 단백질의 부분 펩티드 혹은 부분 펩티드의 조합이라도 된다. 또한, 복수의 인택트한 단백질만을 바이오마커로 해도 된다. 이와 같이, 복수의 단백질 또는 부분 펩티드를 바이오마커로서 사용함으로써, 대장암을 보다 정확하게 검출할 수 있고, 또한 대장암의 진행 상태를 정확하게 판단할 수 있다.
예를 들면, 글루코오스 트랜스포터 1과 트랜스페린 수용체 단백질 1의 조합, 글루코오스 트랜스포터 1과 앙기오포이에틴-1의 조합, 매트릭스메탈로프로테아제 9와 트랜스페린 수용체 단백질 1의 조합, 트랜스페린 수용체 단백질 1과 호중구 젤라티나아제 관련 리포칼린의 조합, 트랜스페린 수용체 단백질 1과 앙기오포이에틴-1의 조합, 트랜스페린 수용체 단백질 1과 어댑터 단백질의 조합, 78kDa 글루코오스 제어 단백질과 트리펩티딜펩티다제 1의 조합, 테나신-N과 호중구 젤라티나아제 관련 리포칼린의 조합, 트랜스페린 수용체 단백질 1과 호중구 젤라티나아제 관련 리포칼린과 앙기오포이에틴-1의 조합, 트랜스페린 수용체 단백질 1과 올팍토메딘-4의 조합, 테나신-N과 앙기오포이에틴-1의 조합, 올팍토메딘-4와 앙기오포이에틴-1의 조합, 테나신-N과 올팍토메딘-4의 조합, 올팍토메딘-4와 트리펩티딜펩티다제 1의 조합 등이 있다. 각각의 단백질의 부분 펩티드의 조합이라도 된다.
또한, 상기한 단백질 또는 부분 펩티드를, 종래부터 대장암의 바이오마커로서 알려져 있는 CEA(암태아성 항원)와 조합하여 대장암 검출을 위한 바이오마커로서 사용함으로써, 단독으로 사용하는 것보다 고감도로 또한 고특이도로 검출할 수 있다.
대장암 환자에 있어서, 상기 단백질 또는 부분 펩티드의 발현이 상승한다. 따라서, 혈액 중의 이들 단백질 또는 부분 펩티드를 정량하면 된다. 여기서, 혈액은, 혈청 및 혈장을 포함한다. 또한, 상기 단백질은 세포외소포(EV) 중에 존재한다. 따라서, 혈중에 존재하는 EV를 단리하고, 필요하다면 농축 후, EV 중의 단백질 또는 부분 펩티드를 검출해도 된다. EV는, 예를 들면, 초원심분리에 의해 EV 획분으로서 분리할 수 있다. 또한, EV에 특이적인 마커에 의해 단리할 수 있다. EV의 마커로서, CD9, CD63, CD81 등을 예로 들 수 있고, 이들 마커에 대한 항체를 결합시킨 자기(磁氣) 비즈 등을 이용하여 분리할 수 있다. 또한, 다른 EV의 마커로서 포스파티딜세린(PS)을 예로 들 수 있고, 포스파티딜세린에 대하여 친화성을 가지는포스파티딜세린 결합 단백질을 결합시킨 자기 비즈 등을 이용하여 분리할 수 있다. 포스파티딜세린 결합 단백질로서는, 예를 들면, T세포 면역 글로불린·뮤신 도메인 함유 분자 4(Tim4), 아넥신 A5(Annexin A5), 아넥신 V(Annexin V), 유지방구(乳脂肪球)-EGF 인자 단백질 8(MFG-E8) 등이 있다.
본 발명의 방법에 있어서, 생체 시료 중의 단백질/부분 펩티드 프로파일을 조사하지만, 사용하는 생체시료는 한정되지 않는다. 예를 들면, 생체로부터 채취할 수 있는 액체시료, 예를 들면, 전혈, 혈청, 혈장, 오줌, 타액 등의 체액이 있다. 그리고, 생체시료의 보존 상태에 따라서는, 생체시료 중의 단백질, 부분 단백질 및 부분 펩티드가 더욱 분해되는 경우도 있으므로, 생체시료는 동결 융해를 반복하지 않고 사용하는 것이 바람직하다. 또한, 생체시료 중에 프로테아제 인히비터 등을 첨가해도 된다. 혹은, FACS 또는 플로우 사이토미터를 사용하여, 상기 마커를 지표로 엑소솜을 분리할 수도 있다.
단리한 엑소솜으로부터 단백질이나 펩티드를 추출하고, 상기 단백질 또는 펩티드를 측정하면 된다.
단백질 또는 부분 펩티드는 다양한 방법으로 검출할 수 있다. 이하에 예시하지만, 이들로는 한정되지 않는다.
예를 들면, 검출하고자 하는 각각의 단백질 또는 부분 펩티드에 대한 항체를 사용한 면역학적 측정법에 의해 측정할 수 있다. 면역학적 측정법으로서는, 예를 들면, 고상(固相)면역측정법(RIA, EIA, FIA, CLIA 등), 도트·블로팅법, 라텍스 응집법(LA: Latex Agglutination-Turbidimetric Immunoassay), 이뮤노크로마토법 등이 있다. 항체는 기판 상에 고정화하여 사용할 수 있다.
이 중에서도, 정량성의 관점에서 EIA(Enzyme Immunoassay)법의 일종인 ELISA(Enzyme-Linked ImmunoSorbent Assay)법이 바람직하다. ELISA법에서는, 항체를 고상화한 마이크로타이터 플레이트의 웰에 검체를 첨가하고, 항원·항체 반응을 행하게 하고, 또한 효소 표지한 항체를 첨가하고, 항원·항체 반응을 시키고, 세정 후, 효소기질과 반응·발색시켜, 흡광도를 측정하여 샘플 중의 마커 단백질 또는 부분 펩티드를 검출하고, 또한 그 측정값으로부터 검체 중의 단백질 또는 부분 펩티드 농도를 산출할 수 있다. 또한, 형광 표지한 항체를 사용하여, 항원·항체 반응을 시킨 후에 형광을 측정해도 된다. 항원 항체 반응은 4℃∼45℃, 보다 바람직하게는 20℃∼40℃, 더욱 바람직하게는 25℃∼38℃에서 행할 수 있고, 또한, 반응 시간은, 10분∼18시간, 보다 바람직하게는 10분∼1시간, 더욱 바람직하게는 30분∼1시간 정도이다.
면역학적 방법에 있어서 사용되는 마커 단백질 또는 부분 펩티드에 대한 항체는, 모노클로널 항체라도 되고, 폴리클로널 항체라도 되고, 모노클로널 항체의 Fab, F(ab'), F(ab')2 등의 결합 활성 단편을 사용할 수도 있다.
본 발명은 상기한 22종의 단백질 혹은 그의 부분 펩티드 중 1개 또는 복수에 대한 항체를 포함하는, 대장암 검출용 검사 시약 또는 키트도 포함한다.
대장암 검출을 위한 바이오마커 단백질 또는 그의 부분 펩티드를 질량분석계를 사용한 질량분석법에 의해 해석할 수도 있다. 질량분석법은, 특히 부분 펩티드의 검출에 적합하다.
또한, 질량분석계를 사용하여 검출할 수도 있다. 특히, 바이오마커 단백질의 부분 펩티드의 검출에는 질량분석계의 사용이 적합하다. 질량분석계는, 시료도입부, 이온화실, 분석부, 검출부, 기록부 등을 포함한다. 이온화법으로서는 전자충격이온화(EI)법, 화학이온화(CI)법, 전계탈리(FD; field desorption)법, 2차 이온화(SIMS)법, 고속원자충돌(FAB)법, matrix-assisted laser desorption ionization(MALDI)법, 일렉트로 스프레이 이온화(ESI)법 등을 사용하면 된다. 또한, 분석부는, 2중수렴 질량분석계, 4중 극형 질량분석계, 비행시간형 질량분석계, 푸리에 변환 질량분석계, 이온 사이클로트론 질량분석계 등이 사용된다. 정밀한 분석을 위하여 질량분석계를 2대 결합한, 텐덤 질량분석계(MS/MS)를 사용할 수도 있다.
질량분석계는 단독으로, 사용되어도 되고, 액체 크로마토그래피 등의 분리기기나 측정기기 등과 접속해도 되고, 고속액체 크로마토그래피와 조합한 액체 크로마토그래프 질량분석(LC/MS, LC/MS/MS)으로 분석할 수 있다. 질량분석은 펩티드의 정량적 검출을 위하여 당 분야에 있어서 널리 사용되고 있는 LC/MS(LC/MS/MS) 시스템의, 트리플 4중 극형 질량분석계에 의한 선택 반응 모니터링(SRM: Selected reaction monitoring, SRM) 또는 다중 반응 모니터링(MRM: Multiple reaction monitoring))에 의해 행할 수 있다. SRM/MRM에 의해, 다인자를 동시에 측정할 수 있고, 1회의 측정으로 몇백 종류의 단백질이나 펩티드를 동시에 측정할 수 있다.
피험체로부터 채취한 샘플 중에 상기 바이오마커 단백질 또는 부분 펩티드가 많이 존재하고 있는 경우, 즉 양성인 경우, 상기 피험체는 대장암에 이환되어 있는 것으로 판단할 수 있다.
본 발명에 있어서는, 정상인으로부터 채취한 샘플을 음성 대상으로 하여 동시에 측정해도 된다. 이 경우에, 피험체가 대장암에 이환되어 있는 경우, 피험체의 검체 중의 바이오마커 단백질 또는 부분 펩티드 농도가 정상인에 비해 상승하므로, 피험체에서의 바이오마커 단백질 또는 부분 펩티드 농도가 정상인보다 많은 경우, 바이오마커 단백질 또는 부분 펩티드는 양성으로 판단되고, 피험체가 대장암에 이환되어 있는 것으로 판단할 수 있다. 샘플 중의 바이오마커 단백질 또는 부분 펩티드가 양성인지의 여부는, 미리 SRM/MRM법에 의해 검출된 바이오마커 펩티드의 피크의 면적값과 내부 표준인 안정 동위체 표지 펩티드의 피크 면적값의 비 또는 항체 측정값에 대하여 컷오프값을 정해 두고, 상기 컷오프값을 기준으로 하여 컷오프값을 초과한 경우에, 양성인 것으로 판단할 수 있다.
컷오프값은, 예를 들면, ROC(receiver operating characteristic curve: 수신자 동작 특성 곡선) 해석에 의해 정할 수 있다. 또한, ROC 해석에 의해 본 발명의 방법에 의한 진단 정밀도(감도 및 특이성)를 결정할 수 있다. ROC 해석은, 시료로서 대장암 환자로부터 채취한 시료와 정상인으로부터 채취한 시료에 대하여 바이오마커 단백질 또는 부분 펩티드를 측정하고, 각 컷오프값에서의 감도 및 위양성율(1-특이성)을 산출하고, 가로축을 1-특이성으로 하고, 세로축을 감도로 한 좌표위로 플롯한다.
본 발명의 방법의 측정 결과에 대하여 ROC 해석에 의해 진단 정밀도를 해석 한 경우의, 곡선 하 면적(AUC: area under the curve)은 0.9 이상으로 높고, 감도는 70% 이상, 바람직하게는 80% 이상, 보다 바람직하게는 85% 이상, 더욱 바람직하게는 90% 이상이며, 특이성은 70% 이상, 바람직하게는 75% 이상, 더욱 바람직하게는 80% 이상이다. 본 발명의 방법에 의해, 매우 높은 정밀도로 초기의 대장암을 검출할 수 있다.
[실시예]
본 발명을 이하의 실시예에 의해 구체적으로 설명하지만, 본 발명은 이들 실시예에 의해 한정되는 것은 아니다.
방법
대장암 환자 및 정상인 혈청 및 대장암 배양 세포
대장암 환자 51명, 및 정상인 26명의 혈청(지바(千葉)대 의학부에서 채취)을 채취했다. 각 검체 혈청 샘플은, 해석할 때까지 -80℃로 보존해 두었다.
4개의 대장암 세포주 HCT116(ATCC; CCL-247), DLD-1(ATCC; CCL-221), SW480(ATCC; CCL-228) and SW620(ATCC; CCL-227)은 10% 소혈청(FBS) 및 항생 물질 함유 RPMI-1640 배지(Gibco Laboratories)로 배양했다.
세포가 서브컨플루언트까지 증식할 때까지, 각 세포는 5% CO2의 인큐베이터에서 37℃로 유지하여 배양하고, 서브컨플루언트까지 증식시켰다. 그 후, 이 배양 세포는, FBS 비함유 배지로 세정하고, 신선한 FBS 비함유 배지를 첨가했다. 또한 인큐베이터에서 48시간 배양한 후에, 순화 상청 배지를 모으고, EV(extracellular vesicle)를 단리용의 샘플로 했다.
EV(extracellular vesicle: 세포외소포)의 단리
EV의 단리는, 초원심법에 의해 행하였다. 원심관의 바닥에 자당 완충제를 까는 것에 의해, EV 회수 시에 저밀도의 협잡물을 효율적으로 분리할 수 있다. 초원심 전의 처리로서, 혈청 100μl를 300g으로 10분간, 원심분리하여, 큰 협잡물을 제거했다. 그 후, 회수한 상청액을, 0.22㎛ 스핀 필터(Agilent Technologies, Santa Clara, CA)로 통과시키고, 100,000g으로 90분간, 30%의 자당/D2O 완충제로 원심분리를 행하였다. 완충제를 회수하고, 또한 100,000g으로 70분간 초원심분리기로 2회 원심분리한 후, 원심관에 침전한 EV 획분을 회수했다.
EV로부터의 단백질 추출 및 소화
단백질 추출 및 단백질 소화는, 상간 이동 용해제(PTS: Phase transfer surfactant) 프로토콜(Masuda T et al. J. Proteome Res.7, 731-740(2008))에 의해 행하였다. EV 획분 단백질은 MPEX PTS 시약 키트(GL Science, 일본)로 용해한 후, 디티오트레이톨을 최종농도 5mM로 가하여 실온에서 30분간 환원 반응을 행하고, 또한 요오드아세트아미드를 최종농도 20mM로 가하여 알킬화 반응을 행하였다.
그 후, 샘플에 1%(w/w) 트립신(proteomics grade; Roche Mannheim, Germany)을 첨가하여, 37℃ 오버나이트로 소화했다. 소화 후, 액량과 등량의 아세트산 에틸과 최종농도 1%의 3플루오로아세트산을 가하고 보텍스(vortex)하여, 액중의 계면활성제를 유기층으로 분리했다. 원심분리 후, 펩티드를 포함하고 있는 수상(水相)을 회수하고, Stage Tips(Rappsilber J. et al., Nat. Protoc.2, 1896-1906(2007))에 의한 탈염을 행하였다.
액체 크로마토그래피(LC)-질량분석계(MS/MS) 및 프로테옴의 데이터 분석
소화된 펩티드는, C18-SCX StageTip 크로마토그래피 컬럼에 의해 7분획했다. 그 후, LC(UltiMate3000 Nanoflow HPLC system(Dionex, 서니베일, CA))을 연결한 질량분석계(Q-Exactive(Thermo Scientific, 브레멘, 독일))로 분석했다. 샘플의 질량분석기로의 도입은, 내경(內徑) 75㎛ 길이 300mm의 니들에 1.9㎛의 C18-AQ 수지를 봉입(封入)한 자체 제작한 분석 컬럼을 사용하여 행하였다. LC의 이동상은, 완충액 A(0.1% 포름산 및 2% 아세토니트릴) 및 B(0.1% 포름산 및 90% 아세토니트릴)로 구성된다. 소화된 펩티드를 완충액 A에 용해하고, 트랩 컬럼 0.075×20 mm, Acclaim PepMap RSLC Nano-Trap Column; Thermo Scientific)에 로드했다. 나노 LC는 280nL/분으로 송액(送液)되고, 이동상은 120분으로 5∼35 % B의 구배로 전개되었다. 질량분석은 Full MS 스캔(350∼1800 m/z, 이온 적산 3×106 분해능 70,000) 및MS/MS 스캔(Top10 프리커서 이온(precursor ion), 인젝션 타임 120ms, 분해능 35,000, MS/MS 이온 선택 임계값 5×104 카운트, 분리 폭 3.0Da)으로 측정했다. 데이터 파일의 해석은, MaxQuant 소프트웨어(Ver 1.5.1.2)에 의해 행하였다. 검색 엔진에는 Andromeda, UniProt 인간 단백질 데이터베이스에 대하여, 피크 리스트의 검색을 행하였다. 프리커서 질량 오차 범위는 7ppm, 단편 이온 질량 오차 범위는 0.01Da로 설정했다. 확인 단백질 및 펩티드는, 리버스 데이터베이스에 대한 1% 미만의 위양성율(FDR 1%>)로 판정했다.
LC-SRM/MRM 해석
LC-SRM/MRM 해석은 이전에 보고된 방법에 의해 행하였다(Kume, H. et al., Mol. Cell. Proteomics 13, 1471-1484 (2014): Muraoka, S. et al., J. Proteome Res.11, 4201-4210 (2012): Narumi, R. et al., J. Proteome Res.11, 5311-5322(2012)). 소화 펩티드는 0.1%의 트리플루오로아세트산(TFA)을 포함하는 2%의 아세토니트릴 용액에 용해되고, 그 후, 나노 플로우 LC Paradigm MS2(Michrom BioResources, Auburn, CA)를 연결한 트리플 4중극 질량분석계 TSQ-Vantage(Thermo Fisher Scientific, Bremen, Germany)를 사용하여 분석했다. 샘플의 질량 분석기로의 도입은, 내경 75㎛ 길이 100mm의 니들에 1.9㎛의 C18-AQ 수지를 봉입한 자체 제작한 분석 컬럼을 사용하여 행하였다. LC의 이동상은, 완충액 A(0.1% 포름산 및 2% 아세토니트릴) 및 B(0.1% 포름산 및 90% 아세토니트릴)로 구성된다. 소화된 펩티드를 완충액 A에 용해하고, 트랩 컬럼 0.075×20 mm, Acclaim PepMap RSLC Nano-Trap Column; Thermo Scientific)에 로드했다. 나노 LC는 280nL/분으로 송액되고, 이동상은 60분으로 5∼35 % B의 구배로 전개되었다. SRM 모드에서의 해석은 이하의 조건에서 행하였다(Q1 Peak Width 0.7 FWHM, Cycle time: 1 sec, Collision Gass Pressure 1.8 mTorr). 충돌 에너지는 SRM 트랜지션마다 최적화되어, 각 트랜지션의 강도는 피크 시간 폭 5분의 스케쥴 모드로 측정했다.
SI-펩티드를 사용한 표적 펩티드의 정량
SRM에 의한 표적 펩티드의 정량은, 내부 표준으로서 표적 펩티드와 동일한 서열의 Stable isotope-labeled peptide(SI-펩티드)를 각 검체 혈청으로부터 조제한 EV에 혼합하고, SRM 해석에 의해 검출된 내재성 펩티드/SI-펩티드의 피크 영역비(Peak Area Ratio)에 의해 산출했다. 표적 펩티드와 동일한 서열의 SI-펩티드의 스파이크량은 사전 분석을 실행함으로써 내재성 펩티드에 근접하도록 조정했다.
SRM 해석에 의한 피크 영역 비율의 통계 분석
SRM 해석에 의해 산출된 각 검체의 Peak Area Ratio로부터, 표적 펩티드의 대장 바이오마커로서의 평가를 행하기 위해, SRM 데이터의 통계 분석을 행하였다. 통계 분석에는, SPSS 소프트웨어(버전23)(SPSS Inc., Chicago, IL)를 사용했다. 먼저, 각각의 표적 펩티드 단독에서의 바이오마커로서의 평가를, ROC 해석(ROC: Receiver Operating Characteristic)에 의한 AUC(AUC: Area under the Curve)의 값을 산출하여 행하였다. 또한, 복수의 표적 펩티드를 조합한, 멀티 마커로서의 평가도 진행되었다. 표적 펩티드의 조합에는 SPSS 소프트웨어를 사용하여 로지스틱 회귀 모델을 작성하고, 평가했다. 모델이 유효한 펩티드의 조합에 대하여, 동일하게 ROC 해석에 의해 산출한 AUC의 값에 의해 평가했다.
결과
CRC 관련 바이오마커 후보 단백질의 탐색
도 1에, 본건의 바이오마커 후보 탐색의 전략을 나타낸다. CRC 바이오마커 후보 단백질의 리스트를, 의학과 생물학 문헌의 PubMed Database로부터 얻었다. 검색식으로서, 「cancer」 AND 「colorectal」 AND 「expression」을 사용하여, 2003년부터 2014년의 데이터베이스 상의 문헌 검색을 행하여, 대장암 관련의 687 단백질에 대하여 CRC 바이오마커 후보로서 리스트화했다. 후보 단백질의 선택은 하기 (1)∼(4)의 기준에 의해 행하였다.
(1) 인간 CRC 조직 또는 혈액에서의 단백질 발현을, 웨스턴 블롯, ELISA 또는 면역 조직 화학에 의해 확인하였다.
(2) 표적 단백질이 암에 있어서 발현 상승하고 있는 것이 확인되고 있다(발현이 상승하는 단백질은 발현이 감소하는 단백질보다 검출이 용이하므로, 바이오마커에 적합하다).
(3) 암의 발현 및 진행과 관련된 표적 단백질의 분자 기능이, RNAi 또는 분자의 과잉 발현에 의해 실험적으로 확인되고 있다.
(4) 대규모 분석(예를 들면, omics 분석)에서만 특정된 단백질은, 제외했다.
또한, 본 발명자들은, 이전 임상 검체의 표적 프로테오믹스에 의해, 44의 CRC 바이오마커 후보 단백질을 특별히 정하고 있었다(Kume, H. et al., Mol. Cell. Proteomics 13, 1471-1484(2014)). 이들 44의 단백질은 상기한 바이오마커 후보와 합쳐서, 중복되는 단백질을 제외한, 합계 725의 단백질을, CRC 바이오마커 후보로서 선택했다.
샷건·프로테오믹스해석에 의한 EV 함유 바이오마커 후보의 선택
선택된 바이오마커 후보 단백질 중에서, EV에 존재하는 단백질을 선택하기 위하여, 혈청 및 배양 세포 상청액으로부터 조제한 EV를 사용하고, 샷건·프로테오믹스 해석에 의해 EV 단백질의 정성 해석을 행하였다. 샷건·프로테오믹스의 워크 플로우를 도 2a에 나타낸다.
혈청과 세포 상청액으로부터의 EV의 조제는 초원심법에 들렸다 행하였다. 혈청 EV는, 정상인, 전이가 없는 암환자, 전이가 있는 암환자 각각 8명으로부터 채취했다. 배양 세포 상청액은, 4개의 CRC 세포(HCT116, DLD-1, SW480, SW620)로부터 채취했다. 추출한 단백질은 상관이동용해제(PTS)법을 사용함으로써 소화한 후, C-18 Stage SCX Tip 컬럼에 의해 분획했다(Masuda, T et al., J. Proteome Res.7, 731-740 (2008); Adachi, J. et al. Anal. Chem.88, 7899-7903(2016)). 분획 샘플을 LC-MS/MS로 분석하고, 마스코트· 데이터베이스 검색에 의해, 각각 702(혈청 EV) 및 4749의 (세포 상청액 EV) 단백질을 확인했다. 이들 EV 동정 단백질과 바이오마커 후보 단백질의 비교에 의해, 356의 단백질이, EV 단백질 함유의 바이오마커 후보인 것으로 동정되었다(도 2b).
EV 중에 동정된 바이오마커 후보 단백질로부터의 SRM 타깃 펩티드의 선택
후보 단백질이 바이오마커로서 유효인지 검증하기 위하여, CRC 환자 혈청으로부터 채취한 EV 분획의 SRM 해석을 행하였다. SRM 후보 펩티드는, 샷건·프로테오믹스로 특정된 펩티드로부터 선택했다. 후보 펩티드 선택의 기준으로서, 하기 (1)∼(3)을 사용했다.
(1) 동정된 단백질은 단백질에 고유한 펩티드 서열이며, 복수 있는 경우에는 샷건 해석에 있어서 강도가 높은 표적을 선택했다.
(2) 트립신에 의한 절단 미스나, SRM 해석에 적합하지 않은 아미노산 수식(예를 들면, 산화된 메티오닌 등)을 가지는 펩티드는 제외했다.
(3) 지나치게 긴 펩티드(>20 아미노산)는, 안정 동위체 표지 펩티드(SI-펩티드)를 합성하는 것이 곤란하므로, 표적 펩티드로부터 제외했다.
이러한 기준을 만족시키는 펩티드는, 모든 동정된 펩티드 중에서 3316 펩티드(346의 단백질) 존재했다.
다음으로, 이들 후보로부터 SRM 표적 펩티드를 선택하기 위하여, 비암 컨트롤의 정상인(N) 풀혈청(n=26), 전이가 없는 암환자(C)의 풀혈청(n=26), 전이가 있는 암환자(Cm)의 풀혈청(n=25)으로부터 조제한 EV 분획을 사용하여 SRM 분석을 행하였다. 샷건 해석의 결과로부터, 펩티드 당 3개 또는 4개의 트랜지션(프리커서 이온(precursor ion)과 프로덕트 이온(product ion)의 쌍)을 선택했다. SRM 해석은 각각의 풀마다 3회 반복하여 측정하고, 펩티드 피크 면적은 Skyline소프트웨어를 사용하여 정량화했다. 피크 면적이 풀 샘플(N 대 C 또는 C 대 Cm)의 사이에 2배 이상 유의하게(p<0.01) 증가한 표적 펩티드를 마커 후보 펩티드로서 선택했다. 2개 이상의 후보 펩티드가 검출된 단백질에 대해서는, SRM 해석에서의 피크 강도가 높은 2개의 펩티드를 선택했다. 이러한 기준을 고려하여, 71의 펩티드(46의 단백질)를, 바이오마커 후보의 표적 펩티드로서 선택하였다(도 3).
혈청 EV 획분에서의 표적 펩티드의 SRM에 의한 정량
각각의 환자의 혈청으로부터 조제한 EV 획분 중의 37 바이오마커 후보 펩티드에 대하여, SRM에 의한 정량 해석을 행하였다. 각각의 EV 획분은, 3개 군의 환자혈청(정상인(N); n=26, 전이없음 암환자(C); n=26, 전이있는 암환자(Cm); n=25)의 그룹으로부터 조제했다. 각 검체에는 동일량의 SI-peptide를 내부 표준으로서 가하고, 내재성의 표적 펩티드에 대한 피크 면적비를 Skyline소프트웨어를 사용하여 산출했다. 각각의 표적 펩티드에 대하여, N, C, 및 Cm의 그룹 사이에서의 정량값의 비교를 t검정에 의해 행한 바, N과 C 또는 C와 Cm 사이에 유의한 정량값의 증가가 관찰되었다(p<0.05)(도 4 및 도 5a, 5b, 5c, 5d, 5e 및 5f).
표적 펩티드의 통계 분석에 의한 바이오마커로서의 평가
바이오마커의 후보 펩티드의 평가를 하기 위하여, 37 펩티드에 대하여 ROC(Receiver Operating Characteristic, 수신자동작특성) 분석을 행하였다. 각 후보 펩티드에 대하여, N과 C 사이 및 C와 Cm 사이의 구별을 평가했다. 4개의 펩티드(3개의 단백질)는 매우 감도가 높은 단백질(AUC>0.9, 도 6a의 a, b)이었다. 그리고, 22의 펩티드는 N과 C를 식별하기 위해 충분히 감도가 높았다(0.7-0.9 AUC, 도 7a, 7b, 7c, 7d, 7e 및 7f). 한편, 11의 펩티드는 C와 Cm(도 6b의 c, d)을 식별하기 위해 충분히 감도가 높았다.
다음으로, 후보 펩티드를 조합하여 멀티마커로서 보다 높은 감도가 얻어지는지의 여부를, 로지스틱 회귀분석에 의해 조사했다. 펩티드의 유의한 조합에 대해서는, SPSS소프트웨어를 사용하여 평가했다. 2개 이상의 펩티드에 의한 로지스틱 분석의 결과는, 멀티마커의 ROC 곡선의 AUC에 의해 평가했다. 후보 펩티드의 14 조합에 대해서는 AUC는 마커 단독의 값보다 증가하고(도 8a 및 8b), 특히 8개의 조합에 대해서는 AUC가 0.9<였다(도 9). 가장 높은 AUC(0.97)은, 3개의 펩티드(트랜스페린 수용체 단백질 1, 호중구 젤라티나아제 관련 리포칼린 및 앙기오포이에틴-1)의 조합에 의해 얻어졌다. 이러한 결과는, 복수의 마커의 조합이 대장암의 진단 정밀도를 개선하는 데 유효한 것을 시사하고 있다.
널리 사용되고 있는 종양 마커(암태아성 항원 CEA)와 표적 펩티드의 감도의 비교
CEA는 오늘날, 가장 널리 사용되고 있는 대장암의 혈중 마커의 하나이다. 그러나, CEA의 감도는, 조기 스테이지 환자를 찾는 데 충분하지 않으며, 스테이지 2의 환자에게 대한 감도는 30% 정도인 것으로 보고되어 있다. 이에, 새로이 확립한 37의 바이오마커 후보와 CEA 비교의 비교를 행하였다. 각 표적 펩티드의 SRM 정량값의 컷오프점은, CEA 특이성이 거의 100%이므로, 100%의 특이성으로 설정했다. 검증에 사용한 검체 그룹 C에 대한 CEA의 감도는, 38.8%였다. 한편, 37의 표적 펩티드 중 17의 펩티드(12의 단백질; Annexin A3, Annexin A4, Annexin A5, Annexin A11, Tenascin-N, Transferrin 수용체 단백질 1, GLUT-1, 매트릭스·메탈로프로테아제-9, Olfactomedin-4, CD88 항원, Tripeptidyl-펩티다제 1, Neutrophil 젤라티나아제 관련의 lipocalin)의 감도는 CEA를 크게 상회하고 있었다(도 10a, 10b 및 10c). 특히, Annexin A4 및 A11의 3개의 펩티드의 감도는, 80%<였다(도 11).
[산업상 이용가능성]
본 발명의 방법에 의해 대장암을 조기에 검출할 수 있다.
본 명세서에서 인용한 모든 간행물, 특허 및 특허출원은 그대로 인용에 의해 본 명세서에 원용하는 것으로 한다.
SEQUENCE LISTING
<110> National Institutes of Biomedical Innovation, Health and
Nutrition
DENKA SEIKEN Co., Ltd.
<120> A biomarker for detecting colorectal cancer
<130> PH-7502-PCT
<150> JP 2017-129941
<151> 2017-06-30
<160> 59
<170> PatentIn version 3.5
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Ala Pro Gly Gly Gly Pro Trp Gly Gly Ala Ala Tyr Pro Pro Pro Pro
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Ser Met Pro Pro Ile Gly Leu Asp Asn Val Ala Thr Tyr Ala Gly Gln
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Phe Asn Gln Asp Tyr Leu Ser Gly Met Ala Ala Asn Met Ser Gly Thr
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Gln Gln Pro Val Pro Pro Tyr Gly Met Tyr Pro Pro Pro Gly Gly Asn
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Pro Pro Ser Arg Met Pro Ser Tyr Pro Pro Tyr Pro Gly Ala Pro Val
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Pro Gly Gln Pro Met Pro Pro Pro Gly Gln Gln Pro Pro Gly Ala Tyr
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Pro Gly Gln Pro Pro Val Thr Tyr Pro Gly Gln Pro Pro Val Pro Leu
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Pro Gly Gln Gln Gln Pro Val Pro Ser Tyr Pro Gly Tyr Pro Gly Ser
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Gly Thr Val Thr Pro Ala Val Pro Pro Thr Gln Phe Gly Ser Arg Gly
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Thr Ile Thr Asp Ala Pro Gly Phe Asp Pro Leu Arg Asp Ala Glu Val
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Leu Arg Lys Ala Met Lys Gly Phe Gly Thr Asp Glu Gln Ala Ile Ile
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Asp Cys Leu Gly Ser Arg Ser Asn Lys Gln Arg Gln Gln Ile Leu Leu
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Ser Phe Lys Thr Ala Tyr Gly Lys Asp Leu Ile Lys Asp Leu Lys Ser
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Glu Leu Ser Gly Asn Phe Glu Lys Thr Ile Leu Ala Leu Met Lys Thr
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Pro Val Leu Phe Asp Ile Tyr Glu Ile Lys Glu Ala Ile Lys Gly Val
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Gly Thr Asp Glu Ala Cys Leu Ile Glu Ile Leu Ala Ser Arg Ser Asn
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Glu His Ile Arg Glu Leu Asn Arg Ala Tyr Lys Ala Glu Phe Lys Lys
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Thr Leu Glu Glu Ala Ile Arg Ser Asp Thr Ser Gly His Phe Gln Arg
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Leu Leu Ile Ser Leu Ser Gln Gly Asn Arg Asp Glu Ser Thr Asn Val
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Asp Met Ser Leu Ala Gln Arg Asp Ala Gln Glu Leu Tyr Ala Ala Gly
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Glu Asn Arg Leu Gly Thr Asp Glu Ser Lys Phe Asn Ala Val Leu Cys
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Ser Arg Ser Arg Ala His Leu Val Ala Val Phe Asn Glu Tyr Gln Arg
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Gly Ile Gly Thr Asp Glu Lys Met Leu Ile Ser Ile Leu Thr Glu Arg
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Ser Asn Ala Gln Arg Gln Leu Ile Val Lys Glu Tyr Gln Ala Ala Tyr
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Gly Lys Glu Leu Lys Asp Asp Leu Lys Gly Asp Leu Ser Gly His Phe
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Glu His Leu Met Val Ala Leu Val Thr Pro Pro Ala Val Phe Asp Ala
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Lys Gln Leu Lys Lys Ser Met Lys Gly Ala Gly Thr Asn Glu Asp Ala
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Leu Ile Glu Ile Leu Thr Thr Arg Thr Ser Arg Gln Met Lys Asp Ile
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Ser Gln Ala Tyr Tyr Thr Val Tyr Lys Lys Ser Leu Gly Asp Asp Ile
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Ser Ser Glu Thr Ser Gly Asp Phe Arg Lys Ala Leu Leu Thr Leu Ala
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Asp Gly Arg Arg Asp Glu Ser Leu Lys Val Asp Glu His Leu Ala Lys
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Met Ala Thr Lys Gly Gly Thr Val Lys Ala Ala Ser Gly Phe Asn Ala
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Met Glu Asp Ala Gln Thr Leu Arg Lys Ala Met Lys Gly Leu Gly Thr
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Asp Glu Asp Ala Ile Ile Ser Val Leu Ala Tyr Arg Asn Thr Ala Gln
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Arg Gln Glu Ile Arg Thr Ala Tyr Lys Ser Thr Ile Gly Arg Asp Leu
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Ile Asp Asp Leu Lys Ser Glu Leu Ser Gly Asn Phe Glu Gln Val Ile
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Val Gly Met Met Thr Pro Thr Val Leu Tyr Asp Val Gln Glu Leu Arg
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Leu Ala Ser Arg Thr Pro Glu Glu Ile Arg Arg Ile Ser Gln Thr Tyr
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Asp Val Pro Lys Ser Ala Leu Val Gln Val Asp Ala Asp Pro Gln Pro
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Leu Leu Pro Gly Thr Lys Tyr Ile Val Thr Leu Arg Asn Val Lys Asn
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Glu Val Ser Ser Ser Pro Gln His Leu Leu Ala Thr Thr Asp Leu Ala
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Val Leu Gly Thr Ala Trp Val Thr Asp Glu Thr Glu Asn Ser Leu Asp
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Val Glu Trp Glu Asn Pro Ser Thr Glu Val Asp Tyr Tyr Lys Leu Arg
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Tyr Gly Pro Met Thr Gly Gln Glu Val Ala Glu Val Thr Val Pro Lys
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Ser Ser Asp Pro Lys Ser Arg Tyr Asp Ile Thr Gly Leu His Pro Gly
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Thr Glu Tyr Lys Ile Thr Val Val Pro Met Arg Gly Glu Leu Glu Gly
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Lys Pro Ile Leu Leu Asn Gly Arg Thr Glu Ile Asp Ser Pro Thr Asn
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Val Val Thr Asp Arg Val Thr Glu Asp Thr Ala Thr Val Ser Trp Asp
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Pro Val Gln Ala Val Ile Asp Lys Tyr Val Val Arg Tyr Thr Ser Ala
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Asp Gly Asp Thr Lys Glu Met Ala Val His Lys Asp Glu Ser Ser Thr
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Val Leu Thr Gly Leu Lys Pro Gly Glu Ala Tyr Lys Val Tyr Val Trp
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Ala Glu Arg Gly Asn Gln Gly Ser Lys Lys Ala Asp Thr Asn Ala Leu
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Thr Glu Ile Asp Ser Pro Ala Asn Leu Val Thr Asp Arg Val Thr Glu
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Asn Thr Ala Thr Ile Ser Trp Asp Pro Val Gln Ala Thr Ile Asp Lys
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Val Pro Val Gly Lys Glu Gln Ser Ser Thr Val Leu Thr Gly Leu Arg
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Glu Ser Lys Lys Ala Asp Thr Lys Ala Gln Thr Asp Ile Asp Ser Pro
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Gln Asn Leu Val Thr Asp Trp Val Thr Glu Asn Thr Ala Thr Val Ser
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Ser Ala Asn Gly Glu Thr Arg Glu Val Pro Val Gly Lys Glu Gln Ser
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Ser Thr Val Leu Thr Gly Leu Arg Pro Gly Met Glu Tyr Thr Val His
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Val Trp Ala Gln Lys Gly Asn Gln Glu Ser Lys Lys Ala Asp Thr Lys
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Ala Gln Thr Glu Ile Asp Gly Pro Lys Asn Leu Val Thr Asp Trp Val
885 890 895
Thr Glu Asn Met Ala Thr Val Ser Trp Asp Pro Val Gln Ala Thr Ile
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Asp Lys Tyr Met Val Arg Tyr Thr Ser Ala Asp Gly Glu Thr Arg Glu
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Val Pro Val Gly Lys Glu His Ser Ser Thr Val Leu Thr Gly Leu Arg
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Pro Gly Met Glu Tyr Met Val His Val Trp Ala Gln Lys Gly Ala Gln
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Glu Ser Lys Lys Ala Asp Thr Lys Ala Gln Thr Glu Leu Asp Pro Pro
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Arg Asn Leu Arg Pro Ser Ala Val Thr Gln Ser Gly Gly Ile Leu Thr
980 985 990
Trp Thr Pro Pro Ser Ala Gln Ile His Gly Tyr Ile Leu Thr Tyr Gln
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Gln Arg Phe Ala Leu Gln Gly Leu Glu Gln Gly Ala Thr Tyr Pro
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Val Ser Leu Val Ala Phe Lys Gly Gly Arg Arg Ser Arg Asn Val
1040 1045 1050
Ser Thr Thr Leu Ser Thr Val Gly Ala Arg Phe Pro His Pro Ser
1055 1060 1065
Asp Cys Ser Gln Val Gln Gln Asn Ser Asn Ala Ala Ser Gly Leu
1070 1075 1080
Tyr Thr Ile Tyr Leu His Gly Asp Ala Ser Arg Pro Leu Gln Val
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Tyr Cys Asp Met Glu Thr Asp Gly Gly Gly Trp Ile Val Phe Gln
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Arg Arg Asn Thr Gly Gln Leu Asp Phe Phe Lys Arg Trp Arg Ser
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Tyr Val Glu Gly Phe Gly Asp Pro Met Lys Glu Phe Trp Leu Gly
1130 1135 1140
Leu Asp Lys Leu His Asn Leu Thr Thr Gly Thr Pro Ala Arg Tyr
1145 1150 1155
Glu Val Arg Val Asp Leu Gln Thr Ala Asn Glu Ser Ala Tyr Ala
1160 1165 1170
Ile Tyr Asp Phe Phe Gln Val Ala Ser Ser Lys Glu Arg Tyr Lys
1175 1180 1185
Leu Thr Val Gly Lys Tyr Arg Gly Thr Ala Gly Asp Ala Leu Thr
1190 1195 1200
Tyr His Asn Gly Trp Lys Phe Thr Thr Phe Asp Arg Asp Asn Asp
1205 1210 1215
Ile Ala Leu Ser Asn Cys Ala Leu Thr His His Gly Gly Trp Trp
1220 1225 1230
Tyr Lys Asn Cys His Leu Ala Asn Pro Asn Gly Arg Tyr Gly Glu
1235 1240 1245
Thr Lys His Ser Glu Gly Val Asn Trp Glu Pro Trp Lys Gly His
1250 1255 1260
Glu Phe Ser Ile Pro Tyr Val Glu Leu Lys Ile Arg Pro His Gly
1265 1270 1275
Tyr Ser Arg Glu Pro Val Leu Gly Arg Lys Lys Arg Thr Leu Arg
1280 1285 1290
Gly Arg Leu Arg Thr Phe
1295
<210> 5
<211> 760
<212> PRT
<213> Homo sapiens
<400> 5
Met Met Asp Gln Ala Arg Ser Ala Phe Ser Asn Leu Phe Gly Gly Glu
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Pro Leu Ser Tyr Thr Arg Phe Ser Leu Ala Arg Gln Val Asp Gly Asp
20 25 30
Asn Ser His Val Glu Met Lys Leu Ala Val Asp Glu Glu Glu Asn Ala
35 40 45
Asp Asn Asn Thr Lys Ala Asn Val Thr Lys Pro Lys Arg Cys Ser Gly
50 55 60
Ser Ile Cys Tyr Gly Thr Ile Ala Val Ile Val Phe Phe Leu Ile Gly
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Phe Met Ile Gly Tyr Leu Gly Tyr Cys Lys Gly Val Glu Pro Lys Thr
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Gly Glu Asp Phe Pro Ala Ala Arg Arg Leu Tyr Trp Asp Asp Leu Lys
115 120 125
Arg Lys Leu Ser Glu Lys Leu Asp Ser Thr Asp Phe Thr Gly Thr Ile
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Lys Leu Leu Asn Glu Asn Ser Tyr Val Pro Arg Glu Ala Gly Ser Gln
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Lys Asp Glu Asn Leu Ala Leu Tyr Val Glu Asn Gln Phe Arg Glu Phe
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Lys Leu Ser Lys Val Trp Arg Asp Gln His Phe Val Lys Ile Gln Val
180 185 190
Lys Asp Ser Ala Gln Asn Ser Val Ile Ile Val Asp Lys Asn Gly Arg
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Leu Val Tyr Leu Val Glu Asn Pro Gly Gly Tyr Val Ala Tyr Ser Lys
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Ala Ala Thr Val Thr Gly Lys Leu Val His Ala Asn Phe Gly Thr Lys
225 230 235 240
Lys Asp Phe Glu Asp Leu Tyr Thr Pro Val Asn Gly Ser Ile Val Ile
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Val Arg Ala Gly Lys Ile Thr Phe Ala Glu Lys Val Ala Asn Ala Glu
260 265 270
Ser Leu Asn Ala Ile Gly Val Leu Ile Tyr Met Asp Gln Thr Lys Phe
275 280 285
Pro Ile Val Asn Ala Glu Leu Ser Phe Phe Gly His Ala His Leu Gly
290 295 300
Thr Gly Asp Pro Tyr Thr Pro Gly Phe Pro Ser Phe Asn His Thr Gln
305 310 315 320
Phe Pro Pro Ser Arg Ser Ser Gly Leu Pro Asn Ile Pro Val Gln Thr
325 330 335
Ile Ser Arg Ala Ala Ala Glu Lys Leu Phe Gly Asn Met Glu Gly Asp
340 345 350
Cys Pro Ser Asp Trp Lys Thr Asp Ser Thr Cys Arg Met Val Thr Ser
355 360 365
Glu Ser Lys Asn Val Lys Leu Thr Val Ser Asn Val Leu Lys Glu Ile
370 375 380
Lys Ile Leu Asn Ile Phe Gly Val Ile Lys Gly Phe Val Glu Pro Asp
385 390 395 400
His Tyr Val Val Val Gly Ala Gln Arg Asp Ala Trp Gly Pro Gly Ala
405 410 415
Ala Lys Ser Gly Val Gly Thr Ala Leu Leu Leu Lys Leu Ala Gln Met
420 425 430
Phe Ser Asp Met Val Leu Lys Asp Gly Phe Gln Pro Ser Arg Ser Ile
435 440 445
Ile Phe Ala Ser Trp Ser Ala Gly Asp Phe Gly Ser Val Gly Ala Thr
450 455 460
Glu Trp Leu Glu Gly Tyr Leu Ser Ser Leu His Leu Lys Ala Phe Thr
465 470 475 480
Tyr Ile Asn Leu Asp Lys Ala Val Leu Gly Thr Ser Asn Phe Lys Val
485 490 495
Ser Ala Ser Pro Leu Leu Tyr Thr Leu Ile Glu Lys Thr Met Gln Asn
500 505 510
Val Lys His Pro Val Thr Gly Gln Phe Leu Tyr Gln Asp Ser Asn Trp
515 520 525
Ala Ser Lys Val Glu Lys Leu Thr Leu Asp Asn Ala Ala Phe Pro Phe
530 535 540
Leu Ala Tyr Ser Gly Ile Pro Ala Val Ser Phe Cys Phe Cys Glu Asp
545 550 555 560
Thr Asp Tyr Pro Tyr Leu Gly Thr Thr Met Asp Thr Tyr Lys Glu Leu
565 570 575
Ile Glu Arg Ile Pro Glu Leu Asn Lys Val Ala Arg Ala Ala Ala Glu
580 585 590
Val Ala Gly Gln Phe Val Ile Lys Leu Thr His Asp Val Glu Leu Asn
595 600 605
Leu Asp Tyr Glu Arg Tyr Asn Ser Gln Leu Leu Ser Phe Val Arg Asp
610 615 620
Leu Asn Gln Tyr Arg Ala Asp Ile Lys Glu Met Gly Leu Ser Leu Gln
625 630 635 640
Trp Leu Tyr Ser Ala Arg Gly Asp Phe Phe Arg Ala Thr Ser Arg Leu
645 650 655
Thr Thr Asp Phe Gly Asn Ala Glu Lys Thr Asp Arg Phe Val Met Lys
660 665 670
Lys Leu Asn Asp Arg Val Met Arg Val Glu Tyr His Phe Leu Ser Pro
675 680 685
Tyr Val Ser Pro Lys Glu Ser Pro Phe Arg His Val Phe Trp Gly Ser
690 695 700
Gly Ser His Thr Leu Pro Ala Leu Leu Glu Asn Leu Lys Leu Arg Lys
705 710 715 720
Gln Asn Asn Gly Ala Phe Asn Glu Thr Leu Phe Arg Asn Gln Leu Ala
725 730 735
Leu Ala Thr Trp Thr Ile Gln Gly Ala Ala Asn Ala Leu Ser Gly Asp
740 745 750
Val Trp Asp Ile Asp Asn Glu Phe
755 760
<210> 6
<211> 492
<212> PRT
<213> Homo sapiens
<400> 6
Met Glu Pro Ser Ser Lys Lys Leu Thr Gly Arg Leu Met Leu Ala Val
1 5 10 15
Gly Gly Ala Val Leu Gly Ser Leu Gln Phe Gly Tyr Asn Thr Gly Val
20 25 30
Ile Asn Ala Pro Gln Lys Val Ile Glu Glu Phe Tyr Asn Gln Thr Trp
35 40 45
Val His Arg Tyr Gly Glu Ser Ile Leu Pro Thr Thr Leu Thr Thr Leu
50 55 60
Trp Ser Leu Ser Val Ala Ile Phe Ser Val Gly Gly Met Ile Gly Ser
65 70 75 80
Phe Ser Val Gly Leu Phe Val Asn Arg Phe Gly Arg Arg Asn Ser Met
85 90 95
Leu Met Met Asn Leu Leu Ala Phe Val Ser Ala Val Leu Met Gly Phe
100 105 110
Ser Lys Leu Gly Lys Ser Phe Glu Met Leu Ile Leu Gly Arg Phe Ile
115 120 125
Ile Gly Val Tyr Cys Gly Leu Thr Thr Gly Phe Val Pro Met Tyr Val
130 135 140
Gly Glu Val Ser Pro Thr Ala Leu Arg Gly Ala Leu Gly Thr Leu His
145 150 155 160
Gln Leu Gly Ile Val Val Gly Ile Leu Ile Ala Gln Val Phe Gly Leu
165 170 175
Asp Ser Ile Met Gly Asn Lys Asp Leu Trp Pro Leu Leu Leu Ser Ile
180 185 190
Ile Phe Ile Pro Ala Leu Leu Gln Cys Ile Val Leu Pro Phe Cys Pro
195 200 205
Glu Ser Pro Arg Phe Leu Leu Ile Asn Arg Asn Glu Glu Asn Arg Ala
210 215 220
Lys Ser Val Leu Lys Lys Leu Arg Gly Thr Ala Asp Val Thr His Asp
225 230 235 240
Leu Gln Glu Met Lys Glu Glu Ser Arg Gln Met Met Arg Glu Lys Lys
245 250 255
Val Thr Ile Leu Glu Leu Phe Arg Ser Pro Ala Tyr Arg Gln Pro Ile
260 265 270
Leu Ile Ala Val Val Leu Gln Leu Ser Gln Gln Leu Ser Gly Ile Asn
275 280 285
Ala Val Phe Tyr Tyr Ser Thr Ser Ile Phe Glu Lys Ala Gly Val Gln
290 295 300
Gln Pro Val Tyr Ala Thr Ile Gly Ser Gly Ile Val Asn Thr Ala Phe
305 310 315 320
Thr Val Val Ser Leu Phe Val Val Glu Arg Ala Gly Arg Arg Thr Leu
325 330 335
His Leu Ile Gly Leu Ala Gly Met Ala Gly Cys Ala Ile Leu Met Thr
340 345 350
Ile Ala Leu Ala Leu Leu Glu Gln Leu Pro Trp Met Ser Tyr Leu Ser
355 360 365
Ile Val Ala Ile Phe Gly Phe Val Ala Phe Phe Glu Val Gly Pro Gly
370 375 380
Pro Ile Pro Trp Phe Ile Val Ala Glu Leu Phe Ser Gln Gly Pro Arg
385 390 395 400
Pro Ala Ala Ile Ala Val Ala Gly Phe Ser Asn Trp Thr Ser Asn Phe
405 410 415
Ile Val Gly Met Cys Phe Gln Tyr Val Glu Gln Leu Cys Gly Pro Tyr
420 425 430
Val Phe Ile Ile Phe Thr Val Leu Leu Val Leu Phe Phe Ile Phe Thr
435 440 445
Tyr Phe Lys Val Pro Glu Thr Lys Gly Arg Thr Phe Asp Glu Ile Ala
450 455 460
Ser Gly Phe Arg Gln Gly Gly Ala Ser Gln Ser Asp Lys Thr Pro Glu
465 470 475 480
Glu Leu Phe His Pro Leu Gly Ala Asp Ser Gln Val
485 490
<210> 7
<211> 559
<212> PRT
<213> Homo sapiens
<400> 7
Met Ser Ala Cys Arg Ser Phe Ala Val Ala Ile Cys Ile Leu Glu Ile
1 5 10 15
Ser Ile Leu Thr Ala Gln Tyr Thr Thr Ser Tyr Asp Pro Glu Leu Thr
20 25 30
Glu Ser Ser Gly Ser Ala Ser His Ile Asp Cys Arg Met Ser Pro Trp
35 40 45
Ser Glu Trp Ser Gln Cys Asp Pro Cys Leu Arg Gln Met Phe Arg Ser
50 55 60
Arg Ser Ile Glu Val Phe Gly Gln Phe Asn Gly Lys Arg Cys Thr Asp
65 70 75 80
Ala Val Gly Asp Arg Arg Gln Cys Val Pro Thr Glu Pro Cys Glu Asp
85 90 95
Ala Glu Asp Asp Cys Gly Asn Asp Phe Gln Cys Ser Thr Gly Arg Cys
100 105 110
Ile Lys Met Arg Leu Arg Cys Asn Gly Asp Asn Asp Cys Gly Asp Phe
115 120 125
Ser Asp Glu Asp Asp Cys Glu Ser Glu Pro Arg Pro Pro Cys Arg Asp
130 135 140
Arg Val Val Glu Glu Ser Glu Leu Ala Arg Thr Ala Gly Tyr Gly Ile
145 150 155 160
Asn Ile Leu Gly Met Asp Pro Leu Ser Thr Pro Phe Asp Asn Glu Phe
165 170 175
Tyr Asn Gly Leu Cys Asn Arg Asp Arg Asp Gly Asn Thr Leu Thr Tyr
180 185 190
Tyr Arg Arg Pro Trp Asn Val Ala Ser Leu Ile Tyr Glu Thr Lys Gly
195 200 205
Glu Lys Asn Phe Arg Thr Glu His Tyr Glu Glu Gln Ile Glu Ala Phe
210 215 220
Lys Ser Ile Ile Gln Glu Lys Thr Ser Asn Phe Asn Ala Ala Ile Ser
225 230 235 240
Leu Lys Phe Thr Pro Thr Glu Thr Asn Lys Ala Glu Gln Cys Cys Glu
245 250 255
Glu Thr Ala Ser Ser Ile Ser Leu His Gly Lys Gly Ser Phe Arg Phe
260 265 270
Ser Tyr Ser Lys Asn Glu Thr Tyr Gln Leu Phe Leu Ser Tyr Ser Ser
275 280 285
Lys Lys Glu Lys Met Phe Leu His Val Lys Gly Glu Ile His Leu Gly
290 295 300
Arg Phe Val Met Arg Asn Arg Asp Val Val Leu Thr Thr Thr Phe Val
305 310 315 320
Asp Asp Ile Lys Ala Leu Pro Thr Thr Tyr Glu Lys Gly Glu Tyr Phe
325 330 335
Ala Phe Leu Glu Thr Tyr Gly Thr His Tyr Ser Ser Ser Gly Ser Leu
340 345 350
Gly Gly Leu Tyr Glu Leu Ile Tyr Val Leu Asp Lys Ala Ser Met Lys
355 360 365
Arg Lys Gly Val Glu Leu Lys Asp Ile Lys Arg Cys Leu Gly Tyr His
370 375 380
Leu Asp Val Ser Leu Ala Phe Ser Glu Ile Ser Val Gly Ala Glu Phe
385 390 395 400
Asn Lys Asp Asp Cys Val Lys Arg Gly Glu Gly Arg Ala Val Asn Ile
405 410 415
Thr Ser Glu Asn Leu Ile Asp Asp Val Val Ser Leu Ile Arg Gly Gly
420 425 430
Thr Arg Lys Tyr Ala Phe Glu Leu Lys Glu Lys Leu Leu Arg Gly Thr
435 440 445
Val Ile Asp Val Thr Asp Phe Val Asn Trp Ala Ser Ser Ile Asn Asp
450 455 460
Ala Pro Val Leu Ile Ser Gln Lys Leu Ser Pro Ile Tyr Asn Leu Val
465 470 475 480
Pro Val Lys Met Lys Asn Ala His Leu Lys Lys Gln Asn Leu Glu Arg
485 490 495
Ala Ile Glu Asp Tyr Ile Asn Glu Phe Ser Val Arg Lys Cys His Thr
500 505 510
Cys Gln Asn Gly Gly Thr Val Ile Leu Met Asp Gly Lys Cys Leu Cys
515 520 525
Ala Cys Pro Phe Lys Phe Glu Gly Ile Ala Cys Glu Ile Ser Lys Gln
530 535 540
Lys Ile Ser Glu Gly Leu Pro Ala Leu Glu Phe Pro Asn Glu Lys
545 550 555
<210> 8
<211> 350
<212> PRT
<213> Homo sapiens
<400> 8
Met Asp Ser Phe Asn Tyr Thr Thr Pro Asp Tyr Gly His Tyr Asp Asp
1 5 10 15
Lys Asp Thr Leu Asp Leu Asn Thr Pro Val Asp Lys Thr Ser Asn Thr
20 25 30
Leu Arg Val Pro Asp Ile Leu Ala Leu Val Ile Phe Ala Val Val Phe
35 40 45
Leu Val Gly Val Leu Gly Asn Ala Leu Val Val Trp Val Thr Ala Phe
50 55 60
Glu Ala Lys Arg Thr Ile Asn Ala Ile Trp Phe Leu Asn Leu Ala Val
65 70 75 80
Ala Asp Phe Leu Ser Cys Leu Ala Leu Pro Ile Leu Phe Thr Ser Ile
85 90 95
Val Gln His His His Trp Pro Phe Gly Gly Ala Ala Cys Ser Ile Leu
100 105 110
Pro Ser Leu Ile Leu Leu Asn Met Tyr Ala Ser Ile Leu Leu Leu Ala
115 120 125
Thr Ile Ser Ala Asp Arg Phe Leu Leu Val Phe Lys Pro Ile Trp Cys
130 135 140
Gln Asn Phe Arg Gly Ala Gly Leu Ala Trp Ile Ala Cys Ala Val Ala
145 150 155 160
Trp Gly Leu Ala Leu Leu Leu Thr Ile Pro Ser Phe Leu Tyr Arg Val
165 170 175
Val Arg Glu Glu Tyr Phe Pro Pro Lys Val Leu Cys Gly Val Asp Tyr
180 185 190
Ser His Asp Lys Arg Arg Glu Arg Ala Val Ala Ile Val Arg Leu Val
195 200 205
Leu Gly Phe Leu Trp Pro Leu Leu Thr Leu Thr Ile Cys Tyr Thr Phe
210 215 220
Ile Leu Leu Arg Thr Trp Ser Arg Arg Ala Thr Arg Ser Thr Lys Thr
225 230 235 240
Leu Lys Val Val Val Ala Val Val Ala Ser Phe Phe Ile Phe Trp Leu
245 250 255
Pro Tyr Gln Val Thr Gly Ile Met Met Ser Phe Leu Glu Pro Ser Ser
260 265 270
Pro Thr Phe Leu Leu Leu Lys Lys Leu Asp Ser Leu Cys Val Ser Phe
275 280 285
Ala Tyr Ile Asn Cys Cys Ile Asn Pro Ile Ile Tyr Val Val Ala Gly
290 295 300
Gln Gly Phe Gln Gly Arg Leu Arg Lys Ser Leu Pro Ser Leu Leu Arg
305 310 315 320
Asn Val Leu Thr Glu Glu Ser Val Val Arg Glu Ser Lys Ser Phe Thr
325 330 335
Arg Ser Thr Val Asp Thr Met Ala Gln Lys Thr Gln Ala Val
340 345 350
<210> 9
<211> 654
<212> PRT
<213> Homo sapiens
<400> 9
Met Lys Leu Ser Leu Val Ala Ala Met Leu Leu Leu Leu Ser Ala Ala
1 5 10 15
Arg Ala Glu Glu Glu Asp Lys Lys Glu Asp Val Gly Thr Val Val Gly
20 25 30
Ile Asp Leu Gly Thr Thr Tyr Ser Cys Val Gly Val Phe Lys Asn Gly
35 40 45
Arg Val Glu Ile Ile Ala Asn Asp Gln Gly Asn Arg Ile Thr Pro Ser
50 55 60
Tyr Val Ala Phe Thr Pro Glu Gly Glu Arg Leu Ile Gly Asp Ala Ala
65 70 75 80
Lys Asn Gln Leu Thr Ser Asn Pro Glu Asn Thr Val Phe Asp Ala Lys
85 90 95
Arg Leu Ile Gly Arg Thr Trp Asn Asp Pro Ser Val Gln Gln Asp Ile
100 105 110
Lys Phe Leu Pro Phe Lys Val Val Glu Lys Lys Thr Lys Pro Tyr Ile
115 120 125
Gln Val Asp Ile Gly Gly Gly Gln Thr Lys Thr Phe Ala Pro Glu Glu
130 135 140
Ile Ser Ala Met Val Leu Thr Lys Met Lys Glu Thr Ala Glu Ala Tyr
145 150 155 160
Leu Gly Lys Lys Val Thr His Ala Val Val Thr Val Pro Ala Tyr Phe
165 170 175
Asn Asp Ala Gln Arg Gln Ala Thr Lys Asp Ala Gly Thr Ile Ala Gly
180 185 190
Leu Asn Val Met Arg Ile Ile Asn Glu Pro Thr Ala Ala Ala Ile Ala
195 200 205
Tyr Gly Leu Asp Lys Arg Glu Gly Glu Lys Asn Ile Leu Val Phe Asp
210 215 220
Leu Gly Gly Gly Thr Phe Asp Val Ser Leu Leu Thr Ile Asp Asn Gly
225 230 235 240
Val Phe Glu Val Val Ala Thr Asn Gly Asp Thr His Leu Gly Gly Glu
245 250 255
Asp Phe Asp Gln Arg Val Met Glu His Phe Ile Lys Leu Tyr Lys Lys
260 265 270
Lys Thr Gly Lys Asp Val Arg Lys Asp Asn Arg Ala Val Gln Lys Leu
275 280 285
Arg Arg Glu Val Glu Lys Ala Lys Arg Ala Leu Ser Ser Gln His Gln
290 295 300
Ala Arg Ile Glu Ile Glu Ser Phe Tyr Glu Gly Glu Asp Phe Ser Glu
305 310 315 320
Thr Leu Thr Arg Ala Lys Phe Glu Glu Leu Asn Met Asp Leu Phe Arg
325 330 335
Ser Thr Met Lys Pro Val Gln Lys Val Leu Glu Asp Ser Asp Leu Lys
340 345 350
Lys Ser Asp Ile Asp Glu Ile Val Leu Val Gly Gly Ser Thr Arg Ile
355 360 365
Pro Lys Ile Gln Gln Leu Val Lys Glu Phe Phe Asn Gly Lys Glu Pro
370 375 380
Ser Arg Gly Ile Asn Pro Asp Glu Ala Val Ala Tyr Gly Ala Ala Val
385 390 395 400
Gln Ala Gly Val Leu Ser Gly Asp Gln Asp Thr Gly Asp Leu Val Leu
405 410 415
Leu Asp Val Cys Pro Leu Thr Leu Gly Ile Glu Thr Val Gly Gly Val
420 425 430
Met Thr Lys Leu Ile Pro Arg Asn Thr Val Val Pro Thr Lys Lys Ser
435 440 445
Gln Ile Phe Ser Thr Ala Ser Asp Asn Gln Pro Thr Val Thr Ile Lys
450 455 460
Val Tyr Glu Gly Glu Arg Pro Leu Thr Lys Asp Asn His Leu Leu Gly
465 470 475 480
Thr Phe Asp Leu Thr Gly Ile Pro Pro Ala Pro Arg Gly Val Pro Gln
485 490 495
Ile Glu Val Thr Phe Glu Ile Asp Val Asn Gly Ile Leu Arg Val Thr
500 505 510
Ala Glu Asp Lys Gly Thr Gly Asn Lys Asn Lys Ile Thr Ile Thr Asn
515 520 525
Asp Gln Asn Arg Leu Thr Pro Glu Glu Ile Glu Arg Met Val Asn Asp
530 535 540
Ala Glu Lys Phe Ala Glu Glu Asp Lys Lys Leu Lys Glu Arg Ile Asp
545 550 555 560
Thr Arg Asn Glu Leu Glu Ser Tyr Ala Tyr Ser Leu Lys Asn Gln Ile
565 570 575
Gly Asp Lys Glu Lys Leu Gly Gly Lys Leu Ser Ser Glu Asp Lys Glu
580 585 590
Thr Met Glu Lys Ala Val Glu Glu Lys Ile Glu Trp Leu Glu Ser His
595 600 605
Gln Asp Ala Asp Ile Glu Asp Phe Lys Ala Lys Lys Lys Glu Leu Glu
610 615 620
Glu Ile Val Gln Pro Ile Ile Ser Lys Leu Tyr Gly Ser Ala Gly Pro
625 630 635 640
Pro Pro Thr Gly Glu Glu Asp Thr Ala Glu Lys Asp Glu Leu
645 650
<210> 10
<211> 201
<212> PRT
<213> Homo sapiens
<400> 10
Met Ala Leu Ser Trp Val Leu Thr Val Leu Ser Leu Leu Pro Leu Leu
1 5 10 15
Glu Ala Gln Ile Pro Leu Cys Ala Asn Leu Val Pro Val Pro Ile Thr
20 25 30
Asn Ala Thr Leu Asp Gln Ile Thr Gly Lys Trp Phe Tyr Ile Ala Ser
35 40 45
Ala Phe Arg Asn Glu Glu Tyr Asn Lys Ser Val Gln Glu Ile Gln Ala
50 55 60
Thr Phe Phe Tyr Phe Thr Pro Asn Lys Thr Glu Asp Thr Ile Phe Leu
65 70 75 80
Arg Glu Tyr Gln Thr Arg Gln Asp Gln Cys Ile Tyr Asn Thr Thr Tyr
85 90 95
Leu Asn Val Gln Arg Glu Asn Gly Thr Ile Ser Arg Tyr Val Gly Gly
100 105 110
Gln Glu His Phe Ala His Leu Leu Ile Leu Arg Asp Thr Lys Thr Tyr
115 120 125
Met Leu Ala Phe Asp Val Asn Asp Glu Lys Asn Trp Gly Leu Ser Val
130 135 140
Tyr Ala Asp Lys Pro Glu Thr Thr Lys Glu Gln Leu Gly Glu Phe Tyr
145 150 155 160
Glu Ala Leu Asp Cys Leu Arg Ile Pro Lys Ser Asp Val Val Tyr Thr
165 170 175
Asp Trp Lys Lys Asp Lys Cys Glu Pro Leu Glu Lys Gln His Glu Lys
180 185 190
Glu Arg Lys Gln Glu Glu Gly Glu Ser
195 200
<210> 11
<211> 707
<212> PRT
<213> Homo sapiens
<400> 11
Met Ser Leu Trp Gln Pro Leu Val Leu Val Leu Leu Val Leu Gly Cys
1 5 10 15
Cys Phe Ala Ala Pro Arg Gln Arg Gln Ser Thr Leu Val Leu Phe Pro
20 25 30
Gly Asp Leu Arg Thr Asn Leu Thr Asp Arg Gln Leu Ala Glu Glu Tyr
35 40 45
Leu Tyr Arg Tyr Gly Tyr Thr Arg Val Ala Glu Met Arg Gly Glu Ser
50 55 60
Lys Ser Leu Gly Pro Ala Leu Leu Leu Leu Gln Lys Gln Leu Ser Leu
65 70 75 80
Pro Glu Thr Gly Glu Leu Asp Ser Ala Thr Leu Lys Ala Met Arg Thr
85 90 95
Pro Arg Cys Gly Val Pro Asp Leu Gly Arg Phe Gln Thr Phe Glu Gly
100 105 110
Asp Leu Lys Trp His His His Asn Ile Thr Tyr Trp Ile Gln Asn Tyr
115 120 125
Ser Glu Asp Leu Pro Arg Ala Val Ile Asp Asp Ala Phe Ala Arg Ala
130 135 140
Phe Ala Leu Trp Ser Ala Val Thr Pro Leu Thr Phe Thr Arg Val Tyr
145 150 155 160
Ser Arg Asp Ala Asp Ile Val Ile Gln Phe Gly Val Ala Glu His Gly
165 170 175
Asp Gly Tyr Pro Phe Asp Gly Lys Asp Gly Leu Leu Ala His Ala Phe
180 185 190
Pro Pro Gly Pro Gly Ile Gln Gly Asp Ala His Phe Asp Asp Asp Glu
195 200 205
Leu Trp Ser Leu Gly Lys Gly Val Val Val Pro Thr Arg Phe Gly Asn
210 215 220
Ala Asp Gly Ala Ala Cys His Phe Pro Phe Ile Phe Glu Gly Arg Ser
225 230 235 240
Tyr Ser Ala Cys Thr Thr Asp Gly Arg Ser Asp Gly Leu Pro Trp Cys
245 250 255
Ser Thr Thr Ala Asn Tyr Asp Thr Asp Asp Arg Phe Gly Phe Cys Pro
260 265 270
Ser Glu Arg Leu Tyr Thr Gln Asp Gly Asn Ala Asp Gly Lys Pro Cys
275 280 285
Gln Phe Pro Phe Ile Phe Gln Gly Gln Ser Tyr Ser Ala Cys Thr Thr
290 295 300
Asp Gly Arg Ser Asp Gly Tyr Arg Trp Cys Ala Thr Thr Ala Asn Tyr
305 310 315 320
Asp Arg Asp Lys Leu Phe Gly Phe Cys Pro Thr Arg Ala Asp Ser Thr
325 330 335
Val Met Gly Gly Asn Ser Ala Gly Glu Leu Cys Val Phe Pro Phe Thr
340 345 350
Phe Leu Gly Lys Glu Tyr Ser Thr Cys Thr Ser Glu Gly Arg Gly Asp
355 360 365
Gly Arg Leu Trp Cys Ala Thr Thr Ser Asn Phe Asp Ser Asp Lys Lys
370 375 380
Trp Gly Phe Cys Pro Asp Gln Gly Tyr Ser Leu Phe Leu Val Ala Ala
385 390 395 400
His Glu Phe Gly His Ala Leu Gly Leu Asp His Ser Ser Val Pro Glu
405 410 415
Ala Leu Met Tyr Pro Met Tyr Arg Phe Thr Glu Gly Pro Pro Leu His
420 425 430
Lys Asp Asp Val Asn Gly Ile Arg His Leu Tyr Gly Pro Arg Pro Glu
435 440 445
Pro Glu Pro Arg Pro Pro Thr Thr Thr Thr Pro Gln Pro Thr Ala Pro
450 455 460
Pro Thr Val Cys Pro Thr Gly Pro Pro Thr Val His Pro Ser Glu Arg
465 470 475 480
Pro Thr Ala Gly Pro Thr Gly Pro Pro Ser Ala Gly Pro Thr Gly Pro
485 490 495
Pro Thr Ala Gly Pro Ser Thr Ala Thr Thr Val Pro Leu Ser Pro Val
500 505 510
Asp Asp Ala Cys Asn Val Asn Ile Phe Asp Ala Ile Ala Glu Ile Gly
515 520 525
Asn Gln Leu Tyr Leu Phe Lys Asp Gly Lys Tyr Trp Arg Phe Ser Glu
530 535 540
Gly Arg Gly Ser Arg Pro Gln Gly Pro Phe Leu Ile Ala Asp Lys Trp
545 550 555 560
Pro Ala Leu Pro Arg Lys Leu Asp Ser Val Phe Glu Glu Arg Leu Ser
565 570 575
Lys Lys Leu Phe Phe Phe Ser Gly Arg Gln Val Trp Val Tyr Thr Gly
580 585 590
Ala Ser Val Leu Gly Pro Arg Arg Leu Asp Lys Leu Gly Leu Gly Ala
595 600 605
Asp Val Ala Gln Val Thr Gly Ala Leu Arg Ser Gly Arg Gly Lys Met
610 615 620
Leu Leu Phe Ser Gly Arg Arg Leu Trp Arg Phe Asp Val Lys Ala Gln
625 630 635 640
Met Val Asp Pro Arg Ser Ala Ser Glu Val Asp Arg Met Phe Pro Gly
645 650 655
Val Pro Leu Asp Thr His Asp Val Phe Gln Tyr Arg Glu Lys Ala Tyr
660 665 670
Phe Cys Gln Asp Arg Phe Tyr Trp Arg Val Ser Ser Arg Ser Glu Leu
675 680 685
Asn Gln Val Asp Gln Val Gly Tyr Val Thr Tyr Asp Ile Leu Gln Cys
690 695 700
Pro Glu Asp
705
<210> 12
<211> 498
<212> PRT
<213> Homo sapiens
<400> 12
Met Thr Val Phe Leu Ser Phe Ala Phe Leu Ala Ala Ile Leu Thr His
1 5 10 15
Ile Gly Cys Ser Asn Gln Arg Arg Ser Pro Glu Asn Ser Gly Arg Arg
20 25 30
Tyr Asn Arg Ile Gln His Gly Gln Cys Ala Tyr Thr Phe Ile Leu Pro
35 40 45
Glu His Asp Gly Asn Cys Arg Glu Ser Thr Thr Asp Gln Tyr Asn Thr
50 55 60
Asn Ala Leu Gln Arg Asp Ala Pro His Val Glu Pro Asp Phe Ser Ser
65 70 75 80
Gln Lys Leu Gln His Leu Glu His Val Met Glu Asn Tyr Thr Gln Trp
85 90 95
Leu Gln Lys Leu Glu Asn Tyr Ile Val Glu Asn Met Lys Ser Glu Met
100 105 110
Ala Gln Ile Gln Gln Asn Ala Val Gln Asn His Thr Ala Thr Met Leu
115 120 125
Glu Ile Gly Thr Ser Leu Leu Ser Gln Thr Ala Glu Gln Thr Arg Lys
130 135 140
Leu Thr Asp Val Glu Thr Gln Val Leu Asn Gln Thr Ser Arg Leu Glu
145 150 155 160
Ile Gln Leu Leu Glu Asn Ser Leu Ser Thr Tyr Lys Leu Glu Lys Gln
165 170 175
Leu Leu Gln Gln Thr Asn Glu Ile Leu Lys Ile His Glu Lys Asn Ser
180 185 190
Leu Leu Glu His Lys Ile Leu Glu Met Glu Gly Lys His Lys Glu Glu
195 200 205
Leu Asp Thr Leu Lys Glu Glu Lys Glu Asn Leu Gln Gly Leu Val Thr
210 215 220
Arg Gln Thr Tyr Ile Ile Gln Glu Leu Glu Lys Gln Leu Asn Arg Ala
225 230 235 240
Thr Thr Asn Asn Ser Val Leu Gln Lys Gln Gln Leu Glu Leu Met Asp
245 250 255
Thr Val His Asn Leu Val Asn Leu Cys Thr Lys Glu Gly Val Leu Leu
260 265 270
Lys Gly Gly Lys Arg Glu Glu Glu Lys Pro Phe Arg Asp Cys Ala Asp
275 280 285
Val Tyr Gln Ala Gly Phe Asn Lys Ser Gly Ile Tyr Thr Ile Tyr Ile
290 295 300
Asn Asn Met Pro Glu Pro Lys Lys Val Phe Cys Asn Met Asp Val Asn
305 310 315 320
Gly Gly Gly Trp Thr Val Ile Gln His Arg Glu Asp Gly Ser Leu Asp
325 330 335
Phe Gln Arg Gly Trp Lys Glu Tyr Lys Met Gly Phe Gly Asn Pro Ser
340 345 350
Gly Glu Tyr Trp Leu Gly Asn Glu Phe Ile Phe Ala Ile Thr Ser Gln
355 360 365
Arg Gln Tyr Met Leu Arg Ile Glu Leu Met Asp Trp Glu Gly Asn Arg
370 375 380
Ala Tyr Ser Gln Tyr Asp Arg Phe His Ile Gly Asn Glu Lys Gln Asn
385 390 395 400
Tyr Arg Leu Tyr Leu Lys Gly His Thr Gly Thr Ala Gly Lys Gln Ser
405 410 415
Ser Leu Ile Leu His Gly Ala Asp Phe Ser Thr Lys Asp Ala Asp Asn
420 425 430
Asp Asn Cys Met Cys Lys Cys Ala Leu Met Leu Thr Gly Gly Trp Trp
435 440 445
Phe Asp Ala Cys Gly Pro Ser Asn Leu Asn Gly Met Phe Tyr Thr Ala
450 455 460
Gly Gln Asn His Gly Lys Leu Asn Gly Ile Lys Trp His Tyr Phe Lys
465 470 475 480
Gly Pro Ser Tyr Ser Leu Arg Ser Thr Thr Met Met Ile Arg Pro Leu
485 490 495
Asp Phe
<210> 13
<211> 349
<212> PRT
<213> Homo sapiens
<400> 13
Met Gly Pro Ile Ser Ala Pro Ser Cys Arg Trp Arg Ile Pro Trp Gln
1 5 10 15
Gly Leu Leu Leu Thr Ala Ser Leu Phe Thr Phe Trp Asn Pro Pro Thr
20 25 30
Thr Ala Gln Leu Thr Ile Glu Ala Val Pro Ser Asn Ala Ala Glu Gly
35 40 45
Lys Glu Val Leu Leu Leu Val His Asn Leu Pro Gln Asp Pro Arg Gly
50 55 60
Tyr Asn Trp Tyr Lys Gly Glu Thr Val Asp Ala Asn Arg Arg Ile Ile
65 70 75 80
Gly Tyr Val Ile Ser Asn Gln Gln Ile Thr Pro Gly Pro Ala Tyr Ser
85 90 95
Asn Arg Glu Thr Ile Tyr Pro Asn Ala Ser Leu Leu Met Arg Asn Val
100 105 110
Thr Arg Asn Asp Thr Gly Ser Tyr Thr Leu Gln Val Ile Lys Leu Asn
115 120 125
Leu Met Ser Glu Glu Val Thr Gly Gln Phe Ser Val His Pro Glu Thr
130 135 140
Pro Lys Pro Ser Ile Ser Ser Asn Asn Ser Asn Pro Val Glu Asp Lys
145 150 155 160
Asp Ala Val Ala Phe Thr Cys Glu Pro Glu Thr Gln Asn Thr Thr Tyr
165 170 175
Leu Trp Trp Val Asn Gly Gln Ser Leu Pro Val Ser Pro Arg Leu Gln
180 185 190
Leu Ser Asn Gly Asn Arg Thr Leu Thr Leu Leu Ser Val Thr Arg Asn
195 200 205
Asp Val Gly Pro Tyr Glu Cys Glu Ile Gln Asn Pro Ala Ser Ala Asn
210 215 220
Phe Ser Asp Pro Val Thr Leu Asn Val Leu Tyr Gly Pro Asp Ala Pro
225 230 235 240
Thr Ile Ser Pro Ser Asp Thr Tyr Tyr His Ala Gly Val Asn Leu Asn
245 250 255
Leu Ser Cys His Ala Ala Ser Asn Pro Pro Ser Gln Tyr Ser Trp Ser
260 265 270
Val Asn Gly Thr Phe Gln Gln Tyr Thr Gln Lys Leu Phe Ile Pro Asn
275 280 285
Ile Thr Thr Lys Asn Ser Gly Ser Tyr Ala Cys His Thr Thr Asn Ser
290 295 300
Ala Thr Gly Arg Asn Arg Thr Thr Val Arg Met Ile Thr Val Ser Asp
305 310 315 320
Ala Leu Val Gln Gly Ser Ser Pro Gly Leu Ser Ala Arg Ala Thr Val
325 330 335
Ser Ile Met Ile Gly Val Leu Ala Arg Val Ala Leu Ile
340 345
<210> 14
<211> 5762
<212> PRT
<213> Homo sapiens
<400> 14
Met Gly Ala Pro Ser Ala Cys Arg Thr Leu Val Leu Ala Leu Ala Ala
1 5 10 15
Met Leu Val Val Pro Gln Ala Glu Thr Gln Gly Pro Val Glu Pro Ser
20 25 30
Trp Glu Asn Ala Gly His Thr Met Asp Gly Gly Ala Pro Thr Ser Ser
35 40 45
Pro Thr Arg Arg Val Ser Phe Val Pro Pro Val Thr Val Phe Pro Ser
50 55 60
Leu Ser Pro Leu Asn Pro Ala His Asn Gly Arg Val Cys Ser Thr Trp
65 70 75 80
Gly Asp Phe His Tyr Lys Thr Phe Asp Gly Asp Val Phe Arg Phe Pro
85 90 95
Gly Leu Cys Asn Tyr Val Phe Ser Glu His Cys Arg Ala Ala Tyr Glu
100 105 110
Asp Phe Asn Val Gln Leu Arg Arg Gly Leu Val Gly Ser Arg Pro Val
115 120 125
Val Thr Arg Val Val Ile Lys Ala Gln Gly Leu Val Leu Glu Ala Ser
130 135 140
Asn Gly Ser Val Leu Ile Asn Gly Gln Arg Glu Glu Leu Pro Tyr Ser
145 150 155 160
Arg Thr Gly Leu Leu Val Glu Gln Ser Gly Asp Tyr Ile Lys Val Ser
165 170 175
Ile Arg Leu Val Leu Thr Phe Leu Trp Asn Gly Glu Asp Ser Ala Leu
180 185 190
Leu Glu Leu Asp Pro Lys Tyr Ala Asn Gln Thr Cys Gly Leu Cys Gly
195 200 205
Asp Phe Asn Gly Leu Pro Ala Phe Asn Glu Phe Tyr Ala His Asn Ala
210 215 220
Arg Leu Thr Pro Leu Gln Phe Gly Asn Leu Gln Lys Leu Asp Gly Pro
225 230 235 240
Thr Glu Gln Cys Pro Asp Pro Leu Pro Leu Pro Ala Gly Asn Cys Thr
245 250 255
Asp Glu Glu Gly Ile Cys His Arg Thr Leu Leu Gly Pro Ala Phe Ala
260 265 270
Glu Cys His Ala Leu Val Asp Ser Thr Ala Tyr Leu Ala Ala Cys Ala
275 280 285
Gln Asp Leu Cys Arg Cys Pro Thr Cys Pro Cys Ala Thr Phe Val Glu
290 295 300
Tyr Ser Arg Gln Cys Ala His Ala Gly Gly Gln Pro Arg Asn Trp Arg
305 310 315 320
Cys Pro Glu Leu Cys Pro Arg Thr Cys Pro Leu Asn Met Gln His Gln
325 330 335
Glu Cys Gly Ser Pro Cys Thr Asp Thr Cys Ser Asn Pro Gln Arg Ala
340 345 350
Gln Leu Cys Glu Asp His Cys Val Asp Gly Cys Phe Cys Pro Pro Gly
355 360 365
Thr Val Leu Asp Asp Ile Thr His Ser Gly Cys Leu Pro Leu Gly Gln
370 375 380
Cys Pro Cys Thr His Gly Gly Arg Thr Tyr Ser Pro Gly Thr Ser Phe
385 390 395 400
Asn Thr Thr Cys Ser Ser Cys Thr Cys Ser Gly Gly Leu Trp Gln Cys
405 410 415
Gln Asp Leu Pro Cys Pro Gly Thr Cys Ser Val Gln Gly Gly Ala His
420 425 430
Ile Ser Thr Tyr Asp Glu Lys Leu Tyr Asp Leu His Gly Asp Cys Ser
435 440 445
Tyr Val Leu Ser Lys Lys Cys Ala Asp Ser Ser Phe Thr Val Leu Ala
450 455 460
Glu Leu Arg Lys Cys Gly Leu Thr Asp Asn Glu Asn Cys Leu Lys Ala
465 470 475 480
Val Thr Leu Ser Leu Asp Gly Gly Asp Thr Ala Ile Arg Val Gln Ala
485 490 495
Asp Gly Gly Val Phe Leu Asn Ser Ile Tyr Thr Gln Leu Pro Leu Ser
500 505 510
Ala Ala Asn Ile Thr Leu Phe Thr Pro Ser Ser Phe Phe Ile Val Val
515 520 525
Gln Thr Gly Leu Gly Leu Gln Leu Leu Val Gln Leu Val Pro Leu Met
530 535 540
Gln Val Phe Val Arg Leu Asp Pro Ala His Gln Gly Gln Met Cys Gly
545 550 555 560
Leu Cys Gly Asn Phe Asn Gln Asn Gln Ala Asp Asp Phe Thr Ala Leu
565 570 575
Ser Gly Val Val Glu Ala Thr Gly Ala Ala Phe Ala Asn Thr Trp Lys
580 585 590
Ala Gln Ala Ala Cys Ala Asn Ala Arg Asn Ser Phe Glu Asp Pro Cys
595 600 605
Ser Leu Ser Val Glu Asn Glu Asn Tyr Ala Arg His Trp Cys Ser Arg
610 615 620
Leu Thr Asp Pro Asn Ser Ala Phe Ser Arg Cys His Ser Ile Ile Asn
625 630 635 640
Pro Lys Pro Phe His Ser Asn Cys Met Phe Asp Thr Cys Asn Cys Glu
645 650 655
Arg Ser Glu Asp Cys Leu Cys Ala Ala Leu Ser Ser Tyr Val His Ala
660 665 670
Cys Ala Ala Lys Gly Val Gln Leu Ser Asp Trp Arg Asp Gly Val Cys
675 680 685
Thr Lys Tyr Met Gln Asn Cys Pro Lys Ser Gln Arg Tyr Ala Tyr Val
690 695 700
Val Asp Ala Cys Gln Pro Thr Cys Arg Gly Leu Ser Glu Ala Asp Val
705 710 715 720
Thr Cys Ser Val Ser Phe Val Pro Val Asp Gly Cys Thr Cys Pro Ala
725 730 735
Gly Thr Phe Leu Asn Asp Ala Gly Ala Cys Val Pro Ala Gln Glu Cys
740 745 750
Pro Cys Tyr Ala His Gly Thr Val Leu Ala Pro Gly Glu Val Val His
755 760 765
Asp Glu Gly Ala Val Cys Ser Cys Thr Gly Gly Lys Leu Ser Cys Leu
770 775 780
Gly Ala Ser Leu Gln Lys Ser Thr Gly Cys Ala Ala Pro Met Val Tyr
785 790 795 800
Leu Asp Cys Ser Asn Ser Ser Ala Gly Thr Pro Gly Ala Glu Cys Leu
805 810 815
Arg Ser Cys His Thr Leu Asp Val Gly Cys Phe Ser Thr His Cys Val
820 825 830
Ser Gly Cys Val Cys Pro Pro Gly Leu Val Ser Asp Gly Ser Gly Gly
835 840 845
Cys Ile Ala Glu Glu Asp Cys Pro Cys Val His Asn Glu Ala Thr Tyr
850 855 860
Lys Pro Gly Glu Thr Ile Arg Val Asp Cys Asn Thr Cys Thr Cys Arg
865 870 875 880
Asn Arg Arg Trp Glu Cys Ser His Arg Leu Cys Leu Gly Thr Cys Val
885 890 895
Ala Tyr Gly Asp Gly His Phe Ile Thr Phe Asp Gly Asp Arg Tyr Ser
900 905 910
Phe Glu Gly Ser Cys Glu Tyr Ile Leu Ala Gln Asp Tyr Cys Gly Asp
915 920 925
Asn Thr Thr His Gly Thr Phe Arg Ile Val Thr Glu Asn Ile Pro Cys
930 935 940
Gly Thr Thr Gly Thr Thr Cys Ser Lys Ala Ile Lys Leu Phe Val Glu
945 950 955 960
Ser Tyr Glu Leu Ile Leu Gln Glu Gly Thr Phe Lys Ala Val Ala Arg
965 970 975
Gly Pro Gly Gly Asp Pro Pro Tyr Lys Ile Arg Tyr Met Gly Ile Phe
980 985 990
Leu Val Ile Glu Thr His Gly Met Ala Val Ser Trp Asp Arg Lys Thr
995 1000 1005
Ser Val Phe Ile Arg Leu His Gln Asp Tyr Lys Gly Arg Val Cys
1010 1015 1020
Gly Leu Cys Gly Asn Phe Asp Asp Asn Ala Ile Asn Asp Phe Ala
1025 1030 1035
Thr Arg Ser Arg Ser Val Val Gly Asp Ala Leu Glu Phe Gly Asn
1040 1045 1050
Ser Trp Lys Leu Ser Pro Ser Cys Pro Asp Ala Leu Ala Pro Lys
1055 1060 1065
Asp Pro Cys Thr Ala Asn Pro Phe Arg Lys Ser Trp Ala Gln Lys
1070 1075 1080
Gln Cys Ser Ile Leu His Gly Pro Thr Phe Ala Ala Cys Arg Ser
1085 1090 1095
Gln Val Asp Ser Thr Lys Tyr Tyr Glu Ala Cys Val Asn Asp Ala
1100 1105 1110
Cys Ala Cys Asp Ser Gly Gly Asp Cys Glu Cys Phe Cys Thr Ala
1115 1120 1125
Val Ala Ala Tyr Ala Gln Ala Cys His Asp Ala Gly Leu Cys Val
1130 1135 1140
Ser Trp Arg Thr Pro Asp Thr Cys Pro Leu Phe Cys Asp Phe Tyr
1145 1150 1155
Asn Pro His Gly Gly Cys Glu Trp His Tyr Gln Pro Cys Gly Ala
1160 1165 1170
Pro Cys Leu Lys Thr Cys Arg Asn Pro Ser Gly His Cys Leu Val
1175 1180 1185
Asp Leu Pro Gly Leu Glu Gly Cys Tyr Pro Lys Cys Pro Pro Ser
1190 1195 1200
Gln Pro Phe Phe Asn Glu Asp Gln Met Lys Cys Val Ala Gln Cys
1205 1210 1215
Gly Cys Tyr Asp Lys Asp Gly Asn Tyr Tyr Asp Val Gly Ala Arg
1220 1225 1230
Val Pro Thr Ala Glu Asn Cys Gln Ser Cys Asn Cys Thr Pro Ser
1235 1240 1245
Gly Ile Gln Cys Ala His Ser Leu Glu Ala Cys Thr Cys Thr Tyr
1250 1255 1260
Glu Asp Arg Thr Tyr Ser Tyr Gln Asp Val Ile Tyr Asn Thr Thr
1265 1270 1275
Asp Gly Leu Gly Ala Cys Leu Ile Ala Ile Cys Gly Ser Asn Gly
1280 1285 1290
Thr Ile Ile Arg Lys Ala Val Ala Cys Pro Gly Thr Pro Ala Thr
1295 1300 1305
Thr Pro Phe Thr Phe Thr Thr Ala Trp Val Pro His Ser Thr Thr
1310 1315 1320
Ser Pro Ala Leu Pro Val Ser Thr Val Cys Val Arg Glu Val Cys
1325 1330 1335
Arg Trp Ser Ser Trp Tyr Asn Gly His Arg Pro Glu Pro Gly Leu
1340 1345 1350
Gly Gly Gly Asp Phe Glu Thr Phe Glu Asn Leu Arg Gln Arg Gly
1355 1360 1365
Tyr Gln Val Cys Pro Val Leu Ala Asp Ile Glu Cys Arg Ala Ala
1370 1375 1380
Gln Leu Pro Asp Met Pro Leu Glu Glu Leu Gly Gln Gln Val Asp
1385 1390 1395
Cys Asp Arg Met Arg Gly Leu Met Cys Ala Asn Ser Gln Gln Ser
1400 1405 1410
Pro Pro Leu Cys His Asp Tyr Glu Leu Arg Val Leu Cys Cys Glu
1415 1420 1425
Tyr Val Pro Cys Gly Pro Ser Pro Ala Pro Gly Thr Ser Pro Gln
1430 1435 1440
Pro Ser Leu Ser Ala Ser Thr Glu Pro Ala Val Pro Thr Pro Thr
1445 1450 1455
Gln Thr Thr Ala Thr Glu Lys Thr Thr Leu Trp Val Thr Pro Ser
1460 1465 1470
Ile Arg Ser Thr Ala Ala Leu Thr Ser Gln Thr Gly Ser Ser Ser
1475 1480 1485
Gly Pro Val Thr Val Thr Pro Ser Ala Pro Gly Thr Thr Thr Cys
1490 1495 1500
Gln Pro Arg Cys Gln Trp Thr Glu Trp Phe Asp Glu Asp Tyr Pro
1505 1510 1515
Lys Ser Glu Gln Leu Gly Gly Asp Val Glu Ser Tyr Asp Lys Ile
1520 1525 1530
Arg Ala Ala Gly Gly His Leu Cys Gln Gln Pro Lys Asp Ile Glu
1535 1540 1545
Cys Gln Ala Glu Ser Phe Pro Asn Trp Thr Leu Ala Gln Val Gly
1550 1555 1560
Gln Lys Val His Cys Asp Val His Phe Gly Leu Val Cys Arg Asn
1565 1570 1575
Trp Glu Gln Glu Gly Val Phe Lys Met Cys Tyr Asn Tyr Arg Ile
1580 1585 1590
Arg Val Leu Cys Cys Ser Asp Asp His Cys Arg Gly Arg Ala Thr
1595 1600 1605
Thr Pro Pro Pro Thr Thr Glu Leu Glu Thr Ala Thr Thr Thr Thr
1610 1615 1620
Thr Gln Ala Leu Phe Ser Thr Pro Gln Pro Thr Ser Ser Pro Gly
1625 1630 1635
Leu Thr Arg Ala Pro Pro Ala Ser Thr Thr Ala Val Pro Thr Leu
1640 1645 1650
Ser Glu Gly Leu Thr Ser Pro Arg Tyr Thr Ser Thr Leu Gly Thr
1655 1660 1665
Ala Thr Thr Gly Gly Pro Thr Thr Pro Ala Gly Ser Thr Glu Pro
1670 1675 1680
Thr Val Pro Gly Val Ala Thr Ser Thr Leu Pro Thr Arg Ser Ala
1685 1690 1695
Leu Pro Gly Thr Thr Gly Ser Leu Gly Thr Trp Arg Pro Ser Gln
1700 1705 1710
Pro Pro Thr Leu Ala Pro Thr Thr Met Ala Thr Ser Arg Ala Arg
1715 1720 1725
Pro Thr Gly Thr Ala Ser Thr Ala Ser Lys Glu Pro Leu Thr Thr
1730 1735 1740
Ser Leu Ala Pro Thr Leu Thr Ser Glu Leu Ser Thr Ser Gln Ala
1745 1750 1755
Glu Thr Ser Thr Pro Arg Thr Glu Thr Thr Met Ser Pro Leu Thr
1760 1765 1770
Asn Thr Thr Thr Ser Gln Gly Thr Thr Arg Cys Gln Pro Lys Cys
1775 1780 1785
Glu Trp Thr Glu Trp Phe Asp Val Asp Phe Pro Thr Ser Gly Val
1790 1795 1800
Ala Gly Gly Asp Met Glu Thr Phe Glu Asn Ile Arg Ala Ala Gly
1805 1810 1815
Gly Lys Met Cys Trp Ala Pro Lys Ser Ile Glu Cys Arg Ala Glu
1820 1825 1830
Asn Tyr Pro Glu Val Ser Ile Asp Gln Val Gly Gln Val Leu Thr
1835 1840 1845
Cys Ser Leu Glu Thr Gly Leu Thr Cys Lys Asn Glu Asp Gln Thr
1850 1855 1860
Gly Arg Phe Asn Met Cys Phe Asn Tyr Asn Val Arg Val Leu Cys
1865 1870 1875
Cys Asp Asp Tyr Ser His Cys Pro Ser Thr Pro Ala Thr Ser Ser
1880 1885 1890
Thr Ala Thr Pro Ser Ser Thr Pro Gly Thr Thr Trp Ile Leu Thr
1895 1900 1905
Lys Pro Thr Thr Thr Ala Thr Thr Thr Ala Ser Thr Gly Ser Thr
1910 1915 1920
Ala Thr Pro Thr Ser Thr Leu Arg Thr Ala Pro Pro Pro Lys Val
1925 1930 1935
Leu Thr Thr Thr Ala Thr Thr Pro Thr Val Thr Ser Ser Lys Ala
1940 1945 1950
Thr Pro Ser Ser Ser Pro Gly Thr Ala Thr Ala Leu Pro Ala Leu
1955 1960 1965
Arg Ser Thr Ala Thr Thr Pro Thr Ala Thr Ser Val Thr Pro Ile
1970 1975 1980
Pro Ser Ser Ser Leu Gly Thr Thr Trp Thr Arg Leu Ser Gln Thr
1985 1990 1995
Thr Thr Pro Thr Ala Thr Met Ser Thr Ala Thr Pro Ser Ser Thr
2000 2005 2010
Pro Glu Thr Ala His Thr Ser Thr Val Leu Thr Ala Thr Ala Thr
2015 2020 2025
Thr Thr Gly Ala Thr Gly Ser Val Ala Thr Pro Ser Ser Thr Pro
2030 2035 2040
Gly Thr Ala His Thr Thr Lys Val Pro Thr Thr Thr Thr Thr Gly
2045 2050 2055
Phe Thr Ala Thr Pro Ser Ser Ser Pro Gly Thr Ala Leu Thr Pro
2060 2065 2070
Pro Val Trp Ile Ser Thr Thr Thr Thr Pro Thr Thr Arg Gly Ser
2075 2080 2085
Thr Val Thr Pro Ser Ser Ile Pro Gly Thr Thr His Thr Ala Thr
2090 2095 2100
Val Leu Thr Thr Thr Thr Thr Thr Val Ala Thr Gly Ser Met Ala
2105 2110 2115
Thr Pro Ser Ser Ser Thr Gln Thr Ser Gly Thr Pro Pro Ser Leu
2120 2125 2130
Thr Thr Thr Ala Thr Thr Ile Thr Ala Thr Gly Ser Thr Thr Asn
2135 2140 2145
Pro Ser Ser Thr Pro Gly Thr Thr Pro Ile Pro Pro Val Leu Thr
2150 2155 2160
Thr Thr Ala Thr Thr Pro Ala Ala Thr Ser Asn Thr Val Thr Pro
2165 2170 2175
Ser Ser Ala Leu Gly Thr Thr His Thr Pro Pro Val Pro Asn Thr
2180 2185 2190
Met Ala Thr Thr His Gly Arg Ser Leu Pro Pro Ser Ser Pro His
2195 2200 2205
Thr Val Arg Thr Ala Trp Thr Ser Ala Thr Ser Gly Ile Leu Gly
2210 2215 2220
Thr Thr His Ile Thr Glu Pro Ser Thr Val Thr Ser His Thr Leu
2225 2230 2235
Ala Ala Thr Thr Gly Thr Thr Gln His Ser Thr Pro Ala Leu Ser
2240 2245 2250
Ser Pro His Pro Ser Ser Arg Thr Thr Glu Ser Pro Pro Ser Pro
2255 2260 2265
Gly Thr Thr Thr Pro Gly His Thr Thr Ala Thr Ser Arg Thr Thr
2270 2275 2280
Ala Thr Ala Thr Pro Ser Lys Thr Arg Thr Ser Thr Leu Leu Pro
2285 2290 2295
Ser Ser Pro Thr Ser Ala Pro Ile Thr Thr Val Val Thr Met Gly
2300 2305 2310
Cys Glu Pro Gln Cys Ala Trp Ser Glu Trp Leu Asp Tyr Ser Tyr
2315 2320 2325
Pro Met Pro Gly Pro Ser Gly Gly Asp Phe Asp Thr Tyr Ser Asn
2330 2335 2340
Ile Arg Ala Ala Gly Gly Ala Val Cys Glu Gln Pro Leu Gly Leu
2345 2350 2355
Glu Cys Arg Ala Gln Ala Gln Pro Gly Val Pro Leu Arg Glu Leu
2360 2365 2370
Gly Gln Val Val Glu Cys Ser Leu Asp Phe Gly Leu Val Cys Arg
2375 2380 2385
Asn Arg Glu Gln Val Gly Lys Phe Lys Met Cys Phe Asn Tyr Glu
2390 2395 2400
Ile Arg Val Phe Cys Cys Asn Tyr Gly His Cys Pro Ser Thr Pro
2405 2410 2415
Ala Thr Ser Ser Thr Ala Met Pro Ser Ser Thr Pro Gly Thr Thr
2420 2425 2430
Trp Ile Leu Thr Glu Leu Thr Thr Thr Ala Thr Thr Thr Glu Ser
2435 2440 2445
Thr Gly Ser Thr Ala Thr Pro Ser Ser Thr Pro Gly Thr Thr Trp
2450 2455 2460
Ile Leu Thr Glu Pro Ser Thr Thr Ala Thr Val Thr Val Pro Thr
2465 2470 2475
Gly Ser Thr Ala Thr Ala Ser Ser Thr Gln Ala Thr Ala Gly Thr
2480 2485 2490
Pro His Val Ser Thr Thr Ala Thr Thr Pro Thr Val Thr Ser Ser
2495 2500 2505
Lys Ala Thr Pro Phe Ser Ser Pro Gly Thr Ala Thr Ala Leu Pro
2510 2515 2520
Ala Leu Arg Ser Thr Ala Thr Thr Pro Thr Ala Thr Ser Phe Thr
2525 2530 2535
Ala Ile Pro Ser Ser Ser Leu Gly Thr Thr Trp Thr Arg Leu Ser
2540 2545 2550
Gln Thr Thr Thr Pro Thr Ala Thr Met Ser Thr Ala Thr Pro Ser
2555 2560 2565
Ser Thr Pro Glu Thr Val His Thr Ser Thr Val Leu Thr Thr Thr
2570 2575 2580
Ala Thr Thr Thr Gly Ala Thr Gly Ser Val Ala Thr Pro Ser Ser
2585 2590 2595
Thr Pro Gly Thr Ala His Thr Thr Lys Val Leu Thr Thr Thr Thr
2600 2605 2610
Thr Gly Phe Thr Ala Thr Pro Ser Ser Ser Pro Gly Thr Ala Arg
2615 2620 2625
Thr Leu Pro Val Trp Ile Ser Thr Thr Thr Thr Pro Thr Thr Arg
2630 2635 2640
Gly Ser Thr Val Thr Pro Ser Ser Ile Pro Gly Thr Thr His Thr
2645 2650 2655
Pro Thr Val Leu Thr Thr Thr Thr Thr Thr Val Ala Thr Gly Ser
2660 2665 2670
Met Ala Thr Pro Ser Ser Ser Thr Gln Thr Ser Gly Thr Pro Pro
2675 2680 2685
Ser Leu Thr Thr Thr Ala Thr Thr Ile Thr Ala Thr Gly Ser Thr
2690 2695 2700
Thr Asn Pro Ser Ser Thr Pro Gly Thr Thr Pro Ile Pro Pro Val
2705 2710 2715
Leu Thr Thr Thr Ala Thr Thr Pro Ala Ala Thr Ser Ser Thr Val
2720 2725 2730
Thr Pro Ser Ser Ala Leu Gly Thr Thr His Thr Pro Pro Val Pro
2735 2740 2745
Asn Thr Thr Ala Thr Thr His Gly Arg Ser Leu Ser Pro Ser Ser
2750 2755 2760
Pro His Thr Val Arg Thr Ala Trp Thr Ser Ala Thr Ser Gly Thr
2765 2770 2775
Leu Gly Thr Thr His Ile Thr Glu Pro Ser Thr Gly Thr Ser His
2780 2785 2790
Thr Pro Ala Ala Thr Thr Gly Thr Thr Gln His Ser Thr Pro Ala
2795 2800 2805
Leu Ser Ser Pro His Pro Ser Ser Arg Thr Thr Glu Ser Pro Pro
2810 2815 2820
Ser Pro Gly Thr Thr Thr Pro Gly His Thr Arg Ala Thr Ser Arg
2825 2830 2835
Thr Thr Ala Thr Ala Thr Pro Ser Lys Thr Arg Thr Ser Thr Leu
2840 2845 2850
Leu Pro Ser Ser Pro Thr Ser Ala Pro Ile Thr Thr Val Val Thr
2855 2860 2865
Met Gly Cys Glu Pro Gln Cys Ala Trp Ser Glu Trp Leu Asp Tyr
2870 2875 2880
Ser Tyr Pro Met Pro Gly Pro Ser Gly Gly Asp Phe Asp Thr Tyr
2885 2890 2895
Ser Asn Ile Arg Ala Ala Gly Gly Ala Val Cys Glu Gln Pro Leu
2900 2905 2910
Gly Leu Glu Cys Arg Ala Gln Ala Gln Pro Gly Val Pro Leu Arg
2915 2920 2925
Glu Leu Gly Gln Val Val Glu Cys Ser Leu Asp Phe Gly Leu Val
2930 2935 2940
Cys Arg Asn Arg Glu Gln Val Gly Lys Phe Lys Met Cys Phe Asn
2945 2950 2955
Tyr Glu Ile Arg Val Phe Cys Cys Asn Tyr Gly His Cys Pro Ser
2960 2965 2970
Thr Pro Ala Thr Ser Ser Thr Ala Thr Pro Ser Ser Thr Pro Gly
2975 2980 2985
Thr Thr Trp Ile Leu Thr Glu Gln Thr Thr Ala Ala Thr Thr Thr
2990 2995 3000
Ala Thr Thr Gly Ser Thr Ala Ile Pro Ser Ser Thr Pro Gly Thr
3005 3010 3015
Ala Pro Pro Pro Lys Val Leu Thr Ser Thr Ala Thr Thr Pro Thr
3020 3025 3030
Ala Thr Ser Ser Lys Ala Thr Ser Ser Ser Ser Pro Arg Thr Ala
3035 3040 3045
Thr Thr Leu Pro Val Leu Thr Ser Thr Ala Thr Lys Ser Thr Ala
3050 3055 3060
Thr Ser Phe Thr Pro Ile Pro Ser Phe Thr Leu Gly Thr Thr Gly
3065 3070 3075
Thr Leu Pro Glu Gln Thr Thr Thr Pro Met Ala Thr Met Ser Thr
3080 3085 3090
Ile His Pro Ser Ser Thr Pro Glu Thr Thr His Thr Ser Thr Val
3095 3100 3105
Leu Thr Thr Lys Ala Thr Thr Thr Arg Ala Thr Ser Ser Met Ser
3110 3115 3120
Thr Pro Ser Ser Thr Pro Gly Thr Thr Trp Ile Leu Thr Glu Leu
3125 3130 3135
Thr Thr Ala Ala Thr Thr Thr Ala Ala Thr Gly Pro Thr Ala Thr
3140 3145 3150
Pro Ser Ser Thr Pro Gly Thr Thr Trp Ile Leu Thr Glu Pro Ser
3155 3160 3165
Thr Thr Ala Thr Val Thr Val Pro Thr Gly Ser Thr Ala Thr Ala
3170 3175 3180
Ser Ser Thr Arg Ala Thr Ala Gly Thr Leu Lys Val Leu Thr Ser
3185 3190 3195
Thr Ala Thr Thr Pro Thr Val Ile Ser Ser Arg Ala Thr Pro Ser
3200 3205 3210
Ser Ser Pro Gly Thr Ala Thr Ala Leu Pro Ala Leu Arg Ser Thr
3215 3220 3225
Ala Thr Thr Pro Thr Ala Thr Ser Val Thr Ala Ile Pro Ser Ser
3230 3235 3240
Ser Leu Gly Thr Ala Trp Thr Arg Leu Ser Gln Thr Thr Thr Pro
3245 3250 3255
Thr Ala Thr Met Ser Thr Ala Thr Pro Ser Ser Thr Pro Glu Thr
3260 3265 3270
Val His Thr Ser Thr Val Leu Thr Thr Thr Thr Thr Thr Thr Arg
3275 3280 3285
Ala Thr Gly Ser Val Ala Thr Pro Ser Ser Thr Pro Gly Thr Ala
3290 3295 3300
His Thr Thr Lys Val Pro Thr Thr Thr Thr Thr Gly Phe Thr Ala
3305 3310 3315
Thr Pro Ser Ser Ser Pro Gly Thr Ala Leu Thr Pro Pro Val Trp
3320 3325 3330
Ile Ser Thr Thr Thr Thr Pro Thr Thr Arg Gly Ser Thr Val Thr
3335 3340 3345
Pro Ser Ser Ile Pro Gly Thr Thr His Thr Ala Thr Val Leu Thr
3350 3355 3360
Thr Thr Thr Thr Thr Val Ala Thr Gly Ser Met Ala Thr Pro Ser
3365 3370 3375
Ser Ser Thr Gln Thr Ser Gly Thr Pro Pro Ser Leu Thr Thr Thr
3380 3385 3390
Ala Thr Thr Ile Thr Ala Thr Gly Ser Thr Thr Asn Pro Ser Ser
3395 3400 3405
Thr Pro Gly Thr Thr Pro Ile Pro Pro Val Leu Thr Thr Thr Ala
3410 3415 3420
Thr Thr Pro Ala Ala Thr Ser Ser Thr Val Thr Pro Ser Ser Ala
3425 3430 3435
Leu Gly Thr Thr His Thr Pro Pro Val Pro Asn Thr Thr Ala Thr
3440 3445 3450
Thr His Gly Arg Ser Leu Pro Pro Ser Ser Pro His Thr Val Arg
3455 3460 3465
Thr Ala Trp Thr Ser Ala Thr Ser Gly Ile Leu Gly Thr Thr His
3470 3475 3480
Ile Thr Glu Pro Ser Thr Val Thr Ser His Thr Pro Ala Ala Thr
3485 3490 3495
Thr Ser Thr Thr Gln His Ser Thr Pro Ala Leu Ser Ser Pro His
3500 3505 3510
Pro Ser Ser Arg Thr Thr Glu Ser Pro Pro Ser Pro Gly Thr Thr
3515 3520 3525
Thr Pro Gly His Thr Arg Gly Thr Ser Arg Thr Thr Ala Thr Ala
3530 3535 3540
Thr Pro Ser Lys Thr Arg Thr Ser Thr Leu Leu Pro Ser Ser Pro
3545 3550 3555
Thr Ser Ala Pro Ile Thr Thr Val Val Thr Thr Gly Cys Glu Pro
3560 3565 3570
Gln Cys Ala Trp Ser Glu Trp Leu Asp Tyr Ser Tyr Pro Met Pro
3575 3580 3585
Gly Pro Ser Gly Gly Asp Phe Asp Thr Tyr Ser Asn Ile Arg Ala
3590 3595 3600
Ala Gly Gly Ala Val Cys Glu Gln Pro Leu Gly Leu Glu Cys Arg
3605 3610 3615
Ala Gln Ala Gln Pro Gly Val Pro Leu Arg Glu Leu Gly Gln Val
3620 3625 3630
Val Glu Cys Ser Leu Asp Phe Gly Leu Val Cys Arg Asn Arg Glu
3635 3640 3645
Gln Val Gly Lys Phe Lys Met Cys Phe Asn Tyr Glu Ile Arg Val
3650 3655 3660
Phe Cys Cys Asn Tyr Gly His Cys Pro Ser Thr Pro Ala Thr Ser
3665 3670 3675
Ser Thr Ala Thr Pro Ser Ser Thr Pro Gly Thr Thr Trp Ile Leu
3680 3685 3690
Thr Lys Leu Thr Thr Thr Ala Thr Thr Thr Glu Ser Thr Gly Ser
3695 3700 3705
Thr Ala Thr Pro Ser Ser Thr Pro Gly Thr Thr Trp Ile Leu Thr
3710 3715 3720
Glu Pro Ser Thr Thr Ala Thr Val Thr Val Pro Thr Gly Ser Thr
3725 3730 3735
Ala Thr Ala Ser Ser Thr Gln Ala Thr Ala Gly Thr Pro His Val
3740 3745 3750
Ser Thr Thr Ala Thr Thr Pro Thr Val Thr Ser Ser Lys Ala Thr
3755 3760 3765
Pro Phe Ser Ser Pro Gly Thr Ala Thr Ala Leu Pro Ala Leu Arg
3770 3775 3780
Ser Thr Ala Thr Thr Pro Thr Ala Thr Ser Phe Thr Ala Ile Pro
3785 3790 3795
Ser Ser Ser Leu Gly Thr Thr Trp Thr Arg Leu Ser Gln Thr Thr
3800 3805 3810
Thr Pro Thr Ala Thr Met Ser Thr Ala Thr Pro Ser Ser Thr Pro
3815 3820 3825
Glu Thr Ala His Thr Ser Thr Val Leu Thr Thr Thr Ala Thr Thr
3830 3835 3840
Thr Arg Ala Thr Gly Ser Val Ala Thr Pro Ser Ser Thr Pro Gly
3845 3850 3855
Thr Ala His Thr Thr Lys Val Pro Thr Thr Thr Thr Thr Gly Phe
3860 3865 3870
Thr Val Thr Pro Ser Ser Ser Pro Gly Thr Ala Arg Thr Pro Pro
3875 3880 3885
Val Trp Ile Ser Thr Thr Thr Thr Pro Thr Thr Ser Gly Ser Thr
3890 3895 3900
Val Thr Pro Ser Ser Val Pro Gly Thr Thr His Thr Pro Thr Val
3905 3910 3915
Leu Thr Thr Thr Thr Thr Thr Val Ala Thr Gly Ser Met Ala Thr
3920 3925 3930
Pro Ser Ser Ser Thr Gln Thr Ser Gly Thr Pro Pro Ser Leu Ile
3935 3940 3945
Thr Thr Ala Thr Thr Ile Thr Ala Thr Gly Ser Thr Thr Asn Pro
3950 3955 3960
Ser Ser Thr Pro Gly Thr Thr Pro Ile Pro Pro Val Leu Thr Thr
3965 3970 3975
Thr Ala Thr Thr Pro Ala Ala Thr Ser Ser Thr Val Thr Pro Ser
3980 3985 3990
Ser Ala Leu Gly Thr Thr His Thr Pro Pro Val Pro Asn Thr Thr
3995 4000 4005
Ala Thr Thr His Gly Arg Ser Leu Ser Pro Ser Ser Pro His Thr
4010 4015 4020
Val Arg Thr Ala Trp Thr Ser Ala Thr Ser Gly Thr Leu Gly Thr
4025 4030 4035
Thr His Ile Thr Glu Pro Ser Thr Gly Thr Ser His Thr Pro Ala
4040 4045 4050
Ala Thr Thr Gly Thr Thr Gln His Ser Thr Pro Ala Leu Ser Ser
4055 4060 4065
Pro His Pro Ser Ser Arg Thr Thr Glu Ser Pro Pro Ser Pro Gly
4070 4075 4080
Thr Thr Thr Pro Gly His Thr Thr Ala Thr Ser Arg Thr Thr Ala
4085 4090 4095
Thr Ala Thr Pro Ser Lys Thr Arg Thr Ser Thr Leu Leu Pro Ser
4100 4105 4110
Ser Pro Thr Ser Ala Pro Ile Thr Thr Val Val Thr Thr Gly Cys
4115 4120 4125
Glu Pro Gln Cys Ala Trp Ser Glu Trp Leu Asp Tyr Ser Tyr Pro
4130 4135 4140
Met Pro Gly Pro Ser Gly Gly Asp Phe Asp Thr Tyr Ser Asn Ile
4145 4150 4155
Arg Ala Ala Gly Gly Ala Val Cys Glu Gln Pro Leu Gly Leu Glu
4160 4165 4170
Cys Arg Ala Gln Ala Gln Pro Gly Val Pro Leu Gly Glu Leu Gly
4175 4180 4185
Gln Val Val Glu Cys Ser Leu Asp Phe Gly Leu Val Cys Arg Asn
4190 4195 4200
Arg Glu Gln Val Gly Lys Phe Lys Met Cys Phe Asn Tyr Glu Ile
4205 4210 4215
Arg Val Phe Cys Cys Asn Tyr Gly His Cys Pro Ser Thr Pro Ala
4220 4225 4230
Thr Ser Ser Thr Ala Met Pro Ser Ser Thr Pro Gly Thr Thr Trp
4235 4240 4245
Ile Leu Thr Glu Leu Thr Thr Thr Ala Thr Thr Thr Ala Ser Thr
4250 4255 4260
Gly Ser Thr Ala Thr Pro Ser Ser Thr Pro Gly Thr Ala Pro Pro
4265 4270 4275
Pro Lys Val Leu Thr Ser Pro Ala Thr Thr Pro Thr Ala Thr Ser
4280 4285 4290
Ser Lys Ala Thr Ser Ser Ser Ser Pro Arg Thr Ala Thr Thr Leu
4295 4300 4305
Pro Val Leu Thr Ser Thr Ala Thr Lys Ser Thr Ala Thr Ser Val
4310 4315 4320
Thr Pro Ile Pro Ser Ser Thr Leu Gly Thr Thr Gly Thr Leu Pro
4325 4330 4335
Glu Gln Thr Thr Thr Pro Val Ala Thr Met Ser Thr Ile His Pro
4340 4345 4350
Ser Ser Thr Pro Glu Thr Thr His Thr Ser Thr Val Leu Thr Thr
4355 4360 4365
Lys Ala Thr Thr Thr Arg Ala Thr Ser Ser Thr Ser Thr Pro Ser
4370 4375 4380
Ser Thr Pro Gly Thr Thr Trp Ile Leu Thr Glu Leu Thr Thr Ala
4385 4390 4395
Ala Thr Thr Thr Ala Ala Thr Gly Pro Thr Ala Thr Pro Ser Ser
4400 4405 4410
Thr Pro Gly Thr Thr Trp Ile Leu Thr Glu Leu Thr Thr Thr Ala
4415 4420 4425
Thr Thr Thr Ala Ser Thr Gly Ser Thr Ala Thr Pro Ser Ser Thr
4430 4435 4440
Pro Gly Thr Thr Trp Ile Leu Thr Glu Pro Ser Thr Thr Ala Thr
4445 4450 4455
Val Thr Val Pro Thr Gly Ser Thr Ala Thr Ala Ser Ser Thr Gln
4460 4465 4470
Ala Thr Ala Gly Thr Pro His Val Ser Thr Thr Ala Thr Thr Pro
4475 4480 4485
Thr Val Thr Ser Ser Lys Ala Thr Pro Ser Ser Ser Pro Gly Thr
4490 4495 4500
Ala Thr Ala Leu Pro Ala Leu Arg Ser Thr Ala Thr Thr Pro Thr
4505 4510 4515
Ala Thr Ser Phe Thr Ala Ile Pro Ser Ser Ser Leu Gly Thr Thr
4520 4525 4530
Trp Thr Arg Leu Ser Gln Thr Thr Thr Pro Thr Ala Thr Met Ser
4535 4540 4545
Thr Ala Thr Pro Ser Ser Thr Pro Glu Thr Val His Thr Ser Thr
4550 4555 4560
Val Leu Thr Ala Thr Ala Thr Thr Thr Gly Ala Thr Gly Ser Val
4565 4570 4575
Ala Thr Pro Ser Ser Thr Pro Gly Thr Ala His Thr Thr Lys Val
4580 4585 4590
Pro Thr Thr Thr Thr Thr Gly Phe Thr Ala Thr Pro Ser Ser Ser
4595 4600 4605
Pro Gly Thr Ala Leu Thr Pro Pro Val Trp Ile Ser Thr Thr Thr
4610 4615 4620
Thr Pro Thr Thr Thr Thr Pro Thr Thr Ser Gly Ser Thr Val Thr
4625 4630 4635
Pro Ser Ser Ile Pro Gly Thr Thr His Thr Ala Arg Val Leu Thr
4640 4645 4650
Thr Thr Thr Thr Thr Val Ala Thr Gly Ser Met Ala Thr Pro Ser
4655 4660 4665
Ser Ser Thr Gln Thr Ser Gly Thr Pro Pro Ser Leu Thr Thr Thr
4670 4675 4680
Ala Thr Thr Ile Thr Ala Thr Gly Ser Thr Thr Asn Pro Ser Ser
4685 4690 4695
Thr Pro Gly Thr Thr Pro Ile Thr Pro Val Leu Thr Ser Thr Ala
4700 4705 4710
Thr Thr Pro Ala Ala Thr Ser Ser Lys Ala Thr Ser Ser Ser Ser
4715 4720 4725
Pro Arg Thr Ala Thr Thr Leu Pro Val Leu Thr Ser Thr Ala Thr
4730 4735 4740
Lys Ser Thr Ala Thr Ser Phe Thr Pro Ile Pro Ser Ser Thr Leu
4745 4750 4755
Trp Thr Thr Trp Thr Val Pro Ala Gln Thr Thr Thr Pro Met Ser
4760 4765 4770
Thr Met Ser Thr Ile His Thr Ser Ser Thr Pro Glu Thr Thr His
4775 4780 4785
Thr Ser Thr Val Leu Thr Thr Thr Ala Thr Met Thr Arg Ala Thr
4790 4795 4800
Asn Ser Thr Ala Thr Pro Ser Ser Thr Leu Gly Thr Thr Arg Ile
4805 4810 4815
Leu Thr Glu Leu Thr Thr Thr Ala Thr Thr Thr Ala Ala Thr Gly
4820 4825 4830
Ser Thr Ala Thr Leu Ser Ser Thr Pro Gly Thr Thr Trp Ile Leu
4835 4840 4845
Thr Glu Pro Ser Thr Ile Ala Thr Val Met Val Pro Thr Gly Ser
4850 4855 4860
Thr Ala Thr Ala Ser Ser Thr Leu Gly Thr Ala His Thr Pro Lys
4865 4870 4875
Val Val Thr Thr Met Ala Thr Met Pro Thr Ala Thr Ala Ser Thr
4880 4885 4890
Val Pro Ser Ser Ser Thr Val Gly Thr Thr Arg Thr Pro Ala Val
4895 4900 4905
Leu Pro Ser Ser Leu Pro Thr Phe Ser Val Ser Thr Val Ser Ser
4910 4915 4920
Ser Val Leu Thr Thr Leu Arg Pro Thr Gly Phe Pro Ser Ser His
4925 4930 4935
Phe Ser Thr Pro Cys Phe Cys Arg Ala Phe Gly Gln Phe Phe Ser
4940 4945 4950
Pro Gly Glu Val Ile Tyr Asn Lys Thr Asp Arg Ala Gly Cys His
4955 4960 4965
Phe Tyr Ala Val Cys Asn Gln His Cys Asp Ile Asp Arg Phe Gln
4970 4975 4980
Gly Ala Cys Pro Thr Ser Pro Pro Pro Val Ser Ser Ala Pro Leu
4985 4990 4995
Ser Ser Pro Ser Pro Ala Pro Gly Cys Asp Asn Ala Ile Pro Leu
5000 5005 5010
Arg Gln Val Asn Glu Thr Trp Thr Leu Glu Asn Cys Thr Val Ala
5015 5020 5025
Arg Cys Val Gly Asp Asn Arg Val Val Leu Leu Asp Pro Lys Pro
5030 5035 5040
Val Ala Asn Val Thr Cys Val Asn Lys His Leu Pro Ile Lys Val
5045 5050 5055
Ser Asp Pro Ser Gln Pro Cys Asp Phe His Tyr Glu Cys Glu Cys
5060 5065 5070
Ile Cys Ser Met Trp Gly Gly Ser His Tyr Ser Thr Phe Asp Gly
5075 5080 5085
Thr Ser Tyr Thr Phe Arg Gly Asn Cys Thr Tyr Val Leu Met Arg
5090 5095 5100
Glu Ile His Ala Arg Phe Gly Asn Leu Ser Leu Tyr Leu Asp Asn
5105 5110 5115
His Tyr Cys Thr Ala Ser Ala Thr Ala Ala Ala Ala Arg Cys Pro
5120 5125 5130
Arg Ala Leu Ser Ile His Tyr Lys Ser Met Asp Ile Val Leu Thr
5135 5140 5145
Val Thr Met Val His Gly Lys Glu Glu Gly Leu Ile Leu Phe Asp
5150 5155 5160
Gln Ile Pro Val Ser Ser Gly Phe Ser Lys Asn Gly Val Leu Val
5165 5170 5175
Ser Val Leu Gly Thr Thr Thr Met Arg Val Asp Ile Pro Ala Leu
5180 5185 5190
Gly Val Ser Val Thr Phe Asn Gly Gln Val Phe Gln Ala Arg Leu
5195 5200 5205
Pro Tyr Ser Leu Phe His Asn Asn Thr Glu Gly Gln Cys Gly Thr
5210 5215 5220
Cys Thr Asn Asn Gln Arg Asp Asp Cys Leu Gln Arg Asp Gly Thr
5225 5230 5235
Thr Ala Ala Ser Cys Lys Asp Met Ala Lys Thr Trp Leu Val Pro
5240 5245 5250
Asp Ser Arg Lys Asp Gly Cys Trp Ala Pro Thr Gly Thr Pro Pro
5255 5260 5265
Thr Ala Ser Pro Ala Ala Pro Val Ser Ser Thr Pro Thr Pro Thr
5270 5275 5280
Pro Cys Pro Pro Gln Pro Leu Cys Asp Leu Met Leu Ser Gln Val
5285 5290 5295
Phe Ala Glu Cys His Asn Leu Val Pro Pro Gly Pro Phe Phe Asn
5300 5305 5310
Ala Cys Ile Ser Asp His Cys Arg Gly Arg Leu Glu Val Pro Cys
5315 5320 5325
Gln Ser Leu Glu Ala Tyr Ala Glu Leu Cys Arg Ala Arg Gly Val
5330 5335 5340
Cys Ser Asp Trp Arg Gly Ala Thr Gly Gly Leu Cys Asp Leu Thr
5345 5350 5355
Cys Pro Pro Thr Lys Val Tyr Lys Pro Cys Gly Pro Ile Gln Pro
5360 5365 5370
Ala Thr Cys Asn Ser Arg Asn Gln Ser Pro Gln Leu Glu Gly Met
5375 5380 5385
Ala Glu Gly Cys Phe Cys Pro Glu Asp Gln Ile Leu Phe Asn Ala
5390 5395 5400
His Met Gly Ile Cys Val Gln Ala Cys Pro Cys Val Gly Pro Asp
5405 5410 5415
Gly Phe Pro Lys Phe Pro Gly Glu Arg Trp Val Ser Asn Cys Gln
5420 5425 5430
Ser Cys Val Cys Asp Glu Gly Ser Val Ser Val Gln Cys Lys Pro
5435 5440 5445
Leu Pro Cys Asp Ala Gln Gly Gln Pro Pro Pro Cys Asn Arg Pro
5450 5455 5460
Gly Phe Val Thr Val Thr Arg Pro Arg Ala Glu Asn Pro Cys Cys
5465 5470 5475
Pro Glu Thr Val Cys Val Cys Asn Thr Thr Thr Cys Pro Gln Ser
5480 5485 5490
Leu Pro Val Cys Pro Pro Gly Gln Glu Ser Ile Cys Thr Gln Glu
5495 5500 5505
Glu Gly Asp Cys Cys Pro Thr Phe Arg Cys Arg Pro Gln Leu Cys
5510 5515 5520
Ser Tyr Asn Gly Thr Phe Tyr Gly Val Gly Ala Thr Phe Pro Gly
5525 5530 5535
Ala Leu Pro Cys His Met Cys Thr Cys Leu Ser Gly Asp Thr Gln
5540 5545 5550
Asp Pro Thr Val Gln Cys Gln Glu Asp Ala Cys Asn Asn Thr Thr
5555 5560 5565
Cys Pro Gln Gly Phe Glu Tyr Lys Arg Val Ala Gly Gln Cys Cys
5570 5575 5580
Gly Glu Cys Val Gln Thr Ala Cys Leu Thr Pro Asp Gly Gln Pro
5585 5590 5595
Val Gln Leu Asn Glu Thr Trp Val Asn Ser His Val Asp Asn Cys
5600 5605 5610
Thr Val Tyr Leu Cys Glu Ala Glu Gly Gly Val His Leu Leu Thr
5615 5620 5625
Pro Gln Pro Ala Ser Cys Pro Asp Val Ser Ser Cys Arg Gly Ser
5630 5635 5640
Leu Arg Lys Thr Gly Cys Cys Tyr Ser Cys Glu Glu Asp Ser Cys
5645 5650 5655
Gln Val Arg Ile Asn Thr Thr Ile Leu Trp His Gln Gly Cys Glu
5660 5665 5670
Thr Glu Val Asn Ile Thr Phe Cys Glu Gly Ser Cys Pro Gly Ala
5675 5680 5685
Ser Lys Tyr Ser Ala Glu Ala Gln Ala Met Gln His Gln Cys Thr
5690 5695 5700
Cys Cys Gln Glu Arg Arg Val His Glu Glu Thr Val Pro Leu His
5705 5710 5715
Cys Pro Asn Gly Ser Ala Ile Leu His Thr Tyr Thr His Val Asp
5720 5725 5730
Glu Cys Gly Cys Thr Pro Phe Cys Val Pro Ala Pro Met Ala Pro
5735 5740 5745
Pro His Thr Arg Gly Phe Pro Ala Gln Glu Ala Thr Ala Val
5750 5755 5760
<210> 15
<211> 217
<212> PRT
<213> Homo sapiens
<400> 15
Met Glu Ala Ile Ala Lys Tyr Asp Phe Lys Ala Thr Ala Asp Asp Glu
1 5 10 15
Leu Ser Phe Lys Arg Gly Asp Ile Leu Lys Val Leu Asn Glu Glu Cys
20 25 30
Asp Gln Asn Trp Tyr Lys Ala Glu Leu Asn Gly Lys Asp Gly Phe Ile
35 40 45
Pro Lys Asn Tyr Ile Glu Met Lys Pro His Pro Trp Phe Phe Gly Lys
50 55 60
Ile Pro Arg Ala Lys Ala Glu Glu Met Leu Ser Lys Gln Arg His Asp
65 70 75 80
Gly Ala Phe Leu Ile Arg Glu Ser Glu Ser Ala Pro Gly Asp Phe Ser
85 90 95
Leu Ser Val Lys Phe Gly Asn Asp Val Gln His Phe Lys Val Leu Arg
100 105 110
Asp Gly Ala Gly Lys Tyr Phe Leu Trp Val Val Lys Phe Asn Ser Leu
115 120 125
Asn Glu Leu Val Asp Tyr His Arg Ser Thr Ser Val Ser Arg Asn Gln
130 135 140
Gln Ile Phe Leu Arg Asp Ile Glu Gln Val Pro Gln Gln Pro Thr Tyr
145 150 155 160
Val Gln Ala Leu Phe Asp Phe Asp Pro Gln Glu Asp Gly Glu Leu Gly
165 170 175
Phe Arg Arg Gly Asp Phe Ile His Val Met Asp Asn Ser Asp Pro Asn
180 185 190
Trp Trp Lys Gly Ala Cys His Gly Gln Thr Gly Met Phe Pro Arg Asn
195 200 205
Tyr Val Thr Pro Val Asn Arg Asn Val
210 215
<210> 16
<211> 320
<212> PRT
<213> Homo sapiens
<400> 16
Met Ala Gln Val Leu Arg Gly Thr Val Thr Asp Phe Pro Gly Phe Asp
1 5 10 15
Glu Arg Ala Asp Ala Glu Thr Leu Arg Lys Ala Met Lys Gly Leu Gly
20 25 30
Thr Asp Glu Glu Ser Ile Leu Thr Leu Leu Thr Ser Arg Ser Asn Ala
35 40 45
Gln Arg Gln Glu Ile Ser Ala Ala Phe Lys Thr Leu Phe Gly Arg Asp
50 55 60
Leu Leu Asp Asp Leu Lys Ser Glu Leu Thr Gly Lys Phe Glu Lys Leu
65 70 75 80
Ile Val Ala Leu Met Lys Pro Ser Arg Leu Tyr Asp Ala Tyr Glu Leu
85 90 95
Lys His Ala Leu Lys Gly Ala Gly Thr Asn Glu Lys Val Leu Thr Glu
100 105 110
Ile Ile Ala Ser Arg Thr Pro Glu Glu Leu Arg Ala Ile Lys Gln Val
115 120 125
Tyr Glu Glu Glu Tyr Gly Ser Ser Leu Glu Asp Asp Val Val Gly Asp
130 135 140
Thr Ser Gly Tyr Tyr Gln Arg Met Leu Val Val Leu Leu Gln Ala Asn
145 150 155 160
Arg Asp Pro Asp Ala Gly Ile Asp Glu Ala Gln Val Glu Gln Asp Ala
165 170 175
Gln Ala Leu Phe Gln Ala Gly Glu Leu Lys Trp Gly Thr Asp Glu Glu
180 185 190
Lys Phe Ile Thr Ile Phe Gly Thr Arg Ser Val Ser His Leu Arg Lys
195 200 205
Val Phe Asp Lys Tyr Met Thr Ile Ser Gly Phe Gln Ile Glu Glu Thr
210 215 220
Ile Asp Arg Glu Thr Ser Gly Asn Leu Glu Gln Leu Leu Leu Ala Val
225 230 235 240
Val Lys Ser Ile Arg Ser Ile Pro Ala Tyr Leu Ala Glu Thr Leu Tyr
245 250 255
Tyr Ala Met Lys Gly Ala Gly Thr Asp Asp His Thr Leu Ile Arg Val
260 265 270
Met Val Ser Arg Ser Glu Ile Asp Leu Phe Asn Ile Arg Lys Glu Phe
275 280 285
Arg Lys Asn Phe Ala Thr Ser Leu Tyr Ser Met Ile Lys Gly Asp Thr
290 295 300
Ser Gly Asp Tyr Lys Lys Ala Leu Leu Leu Leu Cys Gly Glu Asp Asp
305 310 315 320
<210> 17
<211> 510
<212> PRT
<213> Homo sapiens
<400> 17
Met Arg Pro Gly Leu Ser Phe Leu Leu Ala Leu Leu Phe Phe Leu Gly
1 5 10 15
Gln Ala Ala Gly Asp Leu Gly Asp Val Gly Pro Pro Ile Pro Ser Pro
20 25 30
Gly Phe Ser Ser Phe Pro Gly Val Asp Ser Ser Ser Ser Phe Ser Ser
35 40 45
Ser Ser Arg Ser Gly Ser Ser Ser Ser Arg Ser Leu Gly Ser Gly Gly
50 55 60
Ser Val Ser Gln Leu Phe Ser Asn Phe Thr Gly Ser Val Asp Asp Arg
65 70 75 80
Gly Thr Cys Gln Cys Ser Val Ser Leu Pro Asp Thr Thr Phe Pro Val
85 90 95
Asp Arg Val Glu Arg Leu Glu Phe Thr Ala His Val Leu Ser Gln Lys
100 105 110
Phe Glu Lys Glu Leu Ser Lys Val Arg Glu Tyr Val Gln Leu Ile Ser
115 120 125
Val Tyr Glu Lys Lys Leu Leu Asn Leu Thr Val Arg Ile Asp Ile Met
130 135 140
Glu Lys Asp Thr Ile Ser Tyr Thr Glu Leu Asp Phe Glu Leu Ile Lys
145 150 155 160
Val Glu Val Lys Glu Met Glu Lys Leu Val Ile Gln Leu Lys Glu Ser
165 170 175
Phe Gly Gly Ser Ser Glu Ile Val Asp Gln Leu Glu Val Glu Ile Arg
180 185 190
Asn Met Thr Leu Leu Val Glu Lys Leu Glu Thr Leu Asp Lys Asn Asn
195 200 205
Val Leu Ala Ile Arg Arg Glu Ile Val Ala Leu Lys Thr Lys Leu Lys
210 215 220
Glu Cys Glu Ala Ser Lys Asp Gln Asn Thr Pro Val Val His Pro Pro
225 230 235 240
Pro Thr Pro Gly Ser Cys Gly His Gly Gly Val Val Asn Ile Ser Lys
245 250 255
Pro Ser Val Val Gln Leu Asn Trp Arg Gly Phe Ser Tyr Leu Tyr Gly
260 265 270
Ala Trp Gly Arg Asp Tyr Ser Pro Gln His Pro Asn Lys Gly Leu Tyr
275 280 285
Trp Val Ala Pro Leu Asn Thr Asp Gly Arg Leu Leu Glu Tyr Tyr Arg
290 295 300
Leu Tyr Asn Thr Leu Asp Asp Leu Leu Leu Tyr Ile Asn Ala Arg Glu
305 310 315 320
Leu Arg Ile Thr Tyr Gly Gln Gly Ser Gly Thr Ala Val Tyr Asn Asn
325 330 335
Asn Met Tyr Val Asn Met Tyr Asn Thr Gly Asn Ile Ala Arg Val Asn
340 345 350
Leu Thr Thr Asn Thr Ile Ala Val Thr Gln Thr Leu Pro Asn Ala Ala
355 360 365
Tyr Asn Asn Arg Phe Ser Tyr Ala Asn Val Ala Trp Gln Asp Ile Asp
370 375 380
Phe Ala Val Asp Glu Asn Gly Leu Trp Val Ile Tyr Ser Thr Glu Ala
385 390 395 400
Ser Thr Gly Asn Met Val Ile Ser Lys Leu Asn Asp Thr Thr Leu Gln
405 410 415
Val Leu Asn Thr Trp Tyr Thr Lys Gln Tyr Lys Pro Ser Ala Ser Asn
420 425 430
Ala Phe Met Val Cys Gly Val Leu Tyr Ala Thr Arg Thr Met Asn Thr
435 440 445
Arg Thr Glu Glu Ile Phe Tyr Tyr Tyr Asp Thr Asn Thr Gly Lys Glu
450 455 460
Gly Lys Leu Asp Ile Val Met His Lys Met Gln Glu Lys Val Gln Ser
465 470 475 480
Ile Asn Tyr Asn Pro Phe Asp Gln Lys Leu Tyr Val Tyr Asn Asp Gly
485 490 495
Tyr Leu Leu Asn Tyr Asp Leu Ser Val Leu Gln Lys Pro Gln
500 505 510
<210> 18
<211> 541
<212> PRT
<213> Homo sapiens
<400> 18
Met Val Ala Asp Pro Pro Arg Asp Ser Lys Gly Leu Ala Ala Ala Glu
1 5 10 15
Pro Thr Ala Asn Gly Gly Leu Ala Leu Ala Ser Ile Glu Asp Gln Gly
20 25 30
Ala Ala Ala Gly Gly Tyr Cys Gly Ser Arg Asp Gln Val Arg Arg Cys
35 40 45
Leu Arg Ala Asn Leu Leu Val Leu Leu Thr Val Val Ala Val Val Ala
50 55 60
Gly Val Ala Leu Gly Leu Gly Val Ser Gly Ala Gly Gly Ala Leu Ala
65 70 75 80
Leu Gly Pro Glu Arg Leu Ser Ala Phe Val Phe Pro Gly Glu Leu Leu
85 90 95
Leu Arg Leu Leu Arg Met Ile Ile Leu Pro Leu Val Val Cys Ser Leu
100 105 110
Ile Gly Gly Ala Ala Ser Leu Asp Pro Gly Ala Leu Gly Arg Leu Gly
115 120 125
Ala Trp Ala Leu Leu Phe Phe Leu Val Thr Thr Leu Leu Ala Ser Ala
130 135 140
Leu Gly Val Gly Leu Ala Leu Ala Leu Gln Pro Gly Ala Ala Ser Ala
145 150 155 160
Ala Ile Asn Ala Ser Val Gly Ala Ala Gly Ser Ala Glu Asn Ala Pro
165 170 175
Ser Lys Glu Val Leu Asp Ser Phe Leu Asp Leu Ala Arg Asn Ile Phe
180 185 190
Pro Ser Asn Leu Val Ser Ala Ala Phe Arg Ser Tyr Ser Thr Thr Tyr
195 200 205
Glu Glu Arg Asn Ile Thr Gly Thr Arg Val Lys Val Pro Val Gly Gln
210 215 220
Glu Val Glu Gly Met Asn Ile Leu Gly Leu Val Val Phe Ala Ile Val
225 230 235 240
Phe Gly Val Ala Leu Arg Lys Leu Gly Pro Glu Gly Glu Leu Leu Ile
245 250 255
Arg Phe Phe Asn Ser Phe Asn Glu Ala Thr Met Val Leu Val Ser Trp
260 265 270
Ile Met Trp Tyr Ala Pro Val Gly Ile Met Phe Leu Val Ala Gly Lys
275 280 285
Ile Val Glu Met Glu Asp Val Gly Leu Leu Phe Ala Arg Leu Gly Lys
290 295 300
Tyr Ile Leu Cys Cys Leu Leu Gly His Ala Ile His Gly Leu Leu Val
305 310 315 320
Leu Pro Leu Ile Tyr Phe Leu Phe Thr Arg Lys Asn Pro Tyr Arg Phe
325 330 335
Leu Trp Gly Ile Val Thr Pro Leu Ala Thr Ala Phe Gly Thr Ser Ser
340 345 350
Ser Ser Ala Thr Leu Pro Leu Met Met Lys Cys Val Glu Glu Asn Asn
355 360 365
Gly Val Ala Lys His Ile Ser Arg Phe Ile Leu Pro Ile Gly Ala Thr
370 375 380
Val Asn Met Asp Gly Ala Ala Leu Phe Gln Cys Val Ala Ala Val Phe
385 390 395 400
Ile Ala Gln Leu Ser Gln Gln Ser Leu Asp Phe Val Lys Ile Ile Thr
405 410 415
Ile Leu Val Thr Ala Thr Ala Ser Ser Val Gly Ala Ala Gly Ile Pro
420 425 430
Ala Gly Gly Val Leu Thr Leu Ala Ile Ile Leu Glu Ala Val Asn Leu
435 440 445
Pro Val Asp His Ile Ser Leu Ile Leu Ala Val Asp Trp Leu Val Asp
450 455 460
Arg Ser Cys Thr Val Leu Asn Val Glu Gly Asp Ala Leu Gly Ala Gly
465 470 475 480
Leu Leu Gln Asn Tyr Val Asp Arg Thr Glu Ser Arg Ser Thr Glu Pro
485 490 495
Glu Leu Ile Gln Val Lys Ser Glu Leu Pro Leu Asp Pro Leu Pro Val
500 505 510
Pro Thr Glu Glu Gly Asn Pro Leu Leu Lys His Tyr Arg Gly Pro Ala
515 520 525
Gly Asp Ala Thr Val Ala Ser Glu Lys Glu Ser Val Met
530 535 540
<210> 19
<211> 563
<212> PRT
<213> Homo sapiens
<400> 19
Met Gly Leu Gln Ala Cys Leu Leu Gly Leu Phe Ala Leu Ile Leu Ser
1 5 10 15
Gly Lys Cys Ser Tyr Ser Pro Glu Pro Asp Gln Arg Arg Thr Leu Pro
20 25 30
Pro Gly Trp Val Ser Leu Gly Arg Ala Asp Pro Glu Glu Glu Leu Ser
35 40 45
Leu Thr Phe Ala Leu Arg Gln Gln Asn Val Glu Arg Leu Ser Glu Leu
50 55 60
Val Gln Ala Val Ser Asp Pro Ser Ser Pro Gln Tyr Gly Lys Tyr Leu
65 70 75 80
Thr Leu Glu Asn Val Ala Asp Leu Val Arg Pro Ser Pro Leu Thr Leu
85 90 95
His Thr Val Gln Lys Trp Leu Leu Ala Ala Gly Ala Gln Lys Cys His
100 105 110
Ser Val Ile Thr Gln Asp Phe Leu Thr Cys Trp Leu Ser Ile Arg Gln
115 120 125
Ala Glu Leu Leu Leu Pro Gly Ala Glu Phe His His Tyr Val Gly Gly
130 135 140
Pro Thr Glu Thr His Val Val Arg Ser Pro His Pro Tyr Gln Leu Pro
145 150 155 160
Gln Ala Leu Ala Pro His Val Asp Phe Val Gly Gly Leu His Arg Phe
165 170 175
Pro Pro Thr Ser Ser Leu Arg Gln Arg Pro Glu Pro Gln Val Thr Gly
180 185 190
Thr Val Gly Leu His Leu Gly Val Thr Pro Ser Val Ile Arg Lys Arg
195 200 205
Tyr Asn Leu Thr Ser Gln Asp Val Gly Ser Gly Thr Ser Asn Asn Ser
210 215 220
Gln Ala Cys Ala Gln Phe Leu Glu Gln Tyr Phe His Asp Ser Asp Leu
225 230 235 240
Ala Gln Phe Met Arg Leu Phe Gly Gly Asn Phe Ala His Gln Ala Ser
245 250 255
Val Ala Arg Val Val Gly Gln Gln Gly Arg Gly Arg Ala Gly Ile Glu
260 265 270
Ala Ser Leu Asp Val Gln Tyr Leu Met Ser Ala Gly Ala Asn Ile Ser
275 280 285
Thr Trp Val Tyr Ser Ser Pro Gly Arg His Glu Gly Gln Glu Pro Phe
290 295 300
Leu Gln Trp Leu Met Leu Leu Ser Asn Glu Ser Ala Leu Pro His Val
305 310 315 320
His Thr Val Ser Tyr Gly Asp Asp Glu Asp Ser Leu Ser Ser Ala Tyr
325 330 335
Ile Gln Arg Val Asn Thr Glu Leu Met Lys Ala Ala Ala Arg Gly Leu
340 345 350
Thr Leu Leu Phe Ala Ser Gly Asp Ser Gly Ala Gly Cys Trp Ser Val
355 360 365
Ser Gly Arg His Gln Phe Arg Pro Thr Phe Pro Ala Ser Ser Pro Tyr
370 375 380
Val Thr Thr Val Gly Gly Thr Ser Phe Gln Glu Pro Phe Leu Ile Thr
385 390 395 400
Asn Glu Ile Val Asp Tyr Ile Ser Gly Gly Gly Phe Ser Asn Val Phe
405 410 415
Pro Arg Pro Ser Tyr Gln Glu Glu Ala Val Thr Lys Phe Leu Ser Ser
420 425 430
Ser Pro His Leu Pro Pro Ser Ser Tyr Phe Asn Ala Ser Gly Arg Ala
435 440 445
Tyr Pro Asp Val Ala Ala Leu Ser Asp Gly Tyr Trp Val Val Ser Asn
450 455 460
Arg Val Pro Ile Pro Trp Val Ser Gly Thr Ser Ala Ser Thr Pro Val
465 470 475 480
Phe Gly Gly Ile Leu Ser Leu Ile Asn Glu His Arg Ile Leu Ser Gly
485 490 495
Arg Pro Pro Leu Gly Phe Leu Asn Pro Arg Leu Tyr Gln Gln His Gly
500 505 510
Ala Gly Leu Phe Asp Val Thr Arg Gly Cys His Glu Ser Cys Leu Asp
515 520 525
Glu Glu Val Glu Gly Gln Gly Phe Cys Ser Gly Pro Gly Trp Asp Pro
530 535 540
Val Thr Gly Trp Gly Thr Pro Asn Phe Pro Ala Leu Leu Lys Thr Leu
545 550 555 560
Leu Asn Pro
<210> 20
<211> 639
<212> PRT
<213> Homo sapiens
<400> 20
Met Ser Ala Arg Gly Pro Ala Ile Gly Ile Asp Leu Gly Thr Thr Tyr
1 5 10 15
Ser Cys Val Gly Val Phe Gln His Gly Lys Val Glu Ile Ile Ala Asn
20 25 30
Asp Gln Gly Asn Arg Thr Thr Pro Ser Tyr Val Ala Phe Thr Asp Thr
35 40 45
Glu Arg Leu Ile Gly Asp Ala Ala Lys Asn Gln Val Ala Met Asn Pro
50 55 60
Thr Asn Thr Ile Phe Asp Ala Lys Arg Leu Ile Gly Arg Lys Phe Glu
65 70 75 80
Asp Ala Thr Val Gln Ser Asp Met Lys His Trp Pro Phe Arg Val Val
85 90 95
Ser Glu Gly Gly Lys Pro Lys Val Gln Val Glu Tyr Lys Gly Glu Thr
100 105 110
Lys Thr Phe Phe Pro Glu Glu Ile Ser Ser Met Val Leu Thr Lys Met
115 120 125
Lys Glu Ile Ala Glu Ala Tyr Leu Gly Gly Lys Val His Ser Ala Val
130 135 140
Ile Thr Val Pro Ala Tyr Phe Asn Asp Ser Gln Arg Gln Ala Thr Lys
145 150 155 160
Asp Ala Gly Thr Ile Thr Gly Leu Asn Val Leu Arg Ile Ile Asn Glu
165 170 175
Pro Thr Ala Ala Ala Ile Ala Tyr Gly Leu Asp Lys Lys Gly Cys Ala
180 185 190
Gly Gly Glu Lys Asn Val Leu Ile Phe Asp Leu Gly Gly Gly Thr Phe
195 200 205
Asp Val Ser Ile Leu Thr Ile Glu Asp Gly Ile Phe Glu Val Lys Ser
210 215 220
Thr Ala Gly Asp Thr His Leu Gly Gly Glu Asp Phe Asp Asn Arg Met
225 230 235 240
Val Ser His Leu Ala Glu Glu Phe Lys Arg Lys His Lys Lys Asp Ile
245 250 255
Gly Pro Asn Lys Arg Ala Val Arg Arg Leu Arg Thr Ala Cys Glu Arg
260 265 270
Ala Lys Arg Thr Leu Ser Ser Ser Thr Gln Ala Ser Ile Glu Ile Asp
275 280 285
Ser Leu Tyr Glu Gly Val Asp Phe Tyr Thr Ser Ile Thr Arg Ala Arg
290 295 300
Phe Glu Glu Leu Asn Ala Asp Leu Phe Arg Gly Thr Leu Glu Pro Val
305 310 315 320
Glu Lys Ala Leu Arg Asp Ala Lys Leu Asp Lys Gly Gln Ile Gln Glu
325 330 335
Ile Val Leu Val Gly Gly Ser Thr Arg Ile Pro Lys Ile Gln Lys Leu
340 345 350
Leu Gln Asp Phe Phe Asn Gly Lys Glu Leu Asn Lys Ser Ile Asn Pro
355 360 365
Asp Glu Ala Val Ala Tyr Gly Ala Ala Val Gln Ala Ala Ile Leu Ile
370 375 380
Gly Asp Lys Ser Glu Asn Val Gln Asp Leu Leu Leu Leu Asp Val Thr
385 390 395 400
Pro Leu Ser Leu Gly Ile Glu Thr Ala Gly Gly Val Met Thr Pro Leu
405 410 415
Ile Lys Arg Asn Thr Thr Ile Pro Thr Lys Gln Thr Gln Thr Phe Thr
420 425 430
Thr Tyr Ser Asp Asn Gln Ser Ser Val Leu Val Gln Val Tyr Glu Gly
435 440 445
Glu Arg Ala Met Thr Lys Asp Asn Asn Leu Leu Gly Lys Phe Asp Leu
450 455 460
Thr Gly Ile Pro Pro Ala Pro Arg Gly Val Pro Gln Ile Glu Val Thr
465 470 475 480
Phe Asp Ile Asp Ala Asn Gly Ile Leu Asn Val Thr Ala Ala Asp Lys
485 490 495
Ser Thr Gly Lys Glu Asn Lys Ile Thr Ile Thr Asn Asp Lys Gly Arg
500 505 510
Leu Ser Lys Asp Asp Ile Asp Arg Met Val Gln Glu Ala Glu Arg Tyr
515 520 525
Lys Ser Glu Asp Glu Ala Asn Arg Asp Arg Val Ala Ala Lys Asn Ala
530 535 540
Leu Glu Ser Tyr Thr Tyr Asn Ile Lys Gln Thr Val Glu Asp Glu Lys
545 550 555 560
Leu Arg Gly Lys Ile Ser Glu Gln Asp Lys Asn Lys Ile Leu Asp Lys
565 570 575
Cys Gln Glu Val Ile Asn Trp Leu Asp Arg Asn Gln Met Ala Glu Lys
580 585 590
Asp Glu Tyr Glu His Lys Gln Lys Glu Leu Glu Arg Val Cys Asn Pro
595 600 605
Ile Ile Ser Lys Leu Tyr Gln Gly Gly Pro Gly Gly Gly Ser Gly Gly
610 615 620
Gly Gly Ser Gly Ala Ser Gly Gly Pro Thr Ile Glu Glu Val Asp
625 630 635
<210> 21
<211> 241
<212> PRT
<213> Homo sapiens
<400> 21
Met Phe Leu Thr Arg Ser Glu Tyr Asp Arg Gly Val Asn Thr Phe Ser
1 5 10 15
Pro Glu Gly Arg Leu Phe Gln Val Glu Tyr Ala Ile Glu Ala Ile Lys
20 25 30
Leu Gly Ser Thr Ala Ile Gly Ile Gln Thr Ser Glu Gly Val Cys Leu
35 40 45
Ala Val Glu Lys Arg Ile Thr Ser Pro Leu Met Glu Pro Ser Ser Ile
50 55 60
Glu Lys Ile Val Glu Ile Asp Ala His Ile Gly Cys Ala Met Ser Gly
65 70 75 80
Leu Ile Ala Asp Ala Lys Thr Leu Ile Asp Lys Ala Arg Val Glu Thr
85 90 95
Gln Asn His Trp Phe Thr Tyr Asn Glu Thr Met Thr Val Glu Ser Val
100 105 110
Thr Gln Ala Val Ser Asn Leu Ala Leu Gln Phe Gly Glu Glu Asp Ala
115 120 125
Asp Pro Gly Ala Met Ser Arg Pro Phe Gly Val Ala Leu Leu Phe Gly
130 135 140
Gly Val Asp Glu Lys Gly Pro Gln Leu Phe His Met Asp Pro Ser Gly
145 150 155 160
Thr Phe Val Gln Cys Asp Ala Arg Ala Ile Gly Ser Ala Ser Glu Gly
165 170 175
Ala Gln Ser Ser Leu Gln Glu Val Tyr His Lys Ser Met Thr Leu Lys
180 185 190
Glu Ala Ile Lys Ser Ser Leu Ile Ile Leu Lys Gln Val Met Glu Glu
195 200 205
Lys Leu Asn Ala Thr Asn Ile Glu Leu Ala Thr Val Gln Pro Gly Gln
210 215 220
Asn Phe His Met Phe Thr Lys Glu Glu Leu Glu Glu Val Ile Lys Asp
225 230 235 240
Ile
<210> 22
<211> 198
<212> PRT
<213> Homo sapiens
<400> 22
Met Pro Leu Gly Leu Leu Trp Leu Gly Leu Ala Leu Leu Gly Ala Leu
1 5 10 15
His Ala Gln Ala Gln Asp Ser Thr Ser Asp Leu Ile Pro Ala Pro Pro
20 25 30
Leu Ser Lys Val Pro Leu Gln Gln Asn Phe Gln Asp Asn Gln Phe Gln
35 40 45
Gly Lys Trp Tyr Val Val Gly Leu Ala Gly Asn Ala Ile Leu Arg Glu
50 55 60
Asp Lys Asp Pro Gln Lys Met Tyr Ala Thr Ile Tyr Glu Leu Lys Glu
65 70 75 80
Asp Lys Ser Tyr Asn Val Thr Ser Val Leu Phe Arg Lys Lys Lys Cys
85 90 95
Asp Tyr Trp Ile Arg Thr Phe Val Pro Gly Cys Gln Pro Gly Glu Phe
100 105 110
Thr Leu Gly Asn Ile Lys Ser Tyr Pro Gly Leu Thr Ser Tyr Leu Val
115 120 125
Arg Val Val Ser Thr Asn Tyr Asn Gln His Ala Met Val Phe Phe Lys
130 135 140
Lys Val Ser Gln Asn Arg Glu Tyr Phe Lys Ile Thr Leu Tyr Gly Arg
145 150 155 160
Thr Lys Glu Leu Thr Ser Glu Leu Lys Glu Asn Phe Ile Arg Phe Ser
165 170 175
Lys Ser Leu Gly Leu Pro Glu Asn His Ile Val Phe Pro Val Pro Ile
180 185 190
Asp Gln Cys Ile Asp Gly
195
<210> 23
<211> 13
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 23
Gly Thr Ile Thr Asp Ala Pro Gly Phe Asp Pro Leu Arg
1 5 10
<210> 24
<211> 9
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 24
Ser Glu Thr Asp Leu Leu Asp Ile Arg
1 5
<210> 25
<211> 16
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 25
Gly Ala Gly Thr Asn Glu Asp Ala Leu Ile Glu Ile Leu Thr Thr Arg
1 5 10 15
<210> 26
<211> 13
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 26
Ser Asp Thr Ser Gly Asp Tyr Glu Ile Thr Leu Leu Lys
1 5 10
<210> 27
<211> 16
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 27
Gly Ala Gly Thr Asp Glu Gly Cys Leu Ile Glu Ile Leu Ala Ser Arg
1 5 10 15
<210> 28
<211> 12
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 28
Asp Glu Gly Asn Tyr Leu Asp Asp Ala Leu Val Arg
1 5 10
<210> 29
<211> 8
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 29
Glu Glu Gln Asn Ile Ile Phe Arg
1 5
<210> 30
<211> 9
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 30
Ala Gln Thr Glu Ile Asp Gly Pro Lys
1 5
<210> 31
<211> 10
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 31
Leu Leu Asn Glu Asn Ser Tyr Val Pro Arg
1 5 10
<210> 32
<211> 13
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 32
Val Ser Ala Ser Pro Leu Leu Tyr Thr Leu Ile Glu Lys
1 5 10
<210> 33
<211> 8
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 33
Val Thr Ile Leu Glu Leu Phe Arg
1 5
<210> 34
<211> 10
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 34
Thr Phe Asp Glu Ile Ala Ser Gly Phe Arg
1 5 10
<210> 35
<211> 11
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 35
Leu Ser Pro Ile Tyr Asn Leu Val Pro Val Lys
1 5 10
<210> 36
<211> 12
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 36
Ala Ile Glu Asp Tyr Ile Asn Glu Phe Ser Val Arg
1 5 10
<210> 37
<211> 7
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 37
Ser Leu Pro Ser Leu Leu Arg
1 5
<210> 38
<211> 10
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 38
Asn Val Leu Thr Glu Glu Ser Val Val Arg
1 5 10
<210> 39
<211> 8
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 39
Val Leu Glu Asp Ser Asp Leu Lys
1 5
<210> 40
<211> 14
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 40
Ser Asp Ile Asp Glu Ile Val Leu Val Gly Gly Ser Thr Arg
1 5 10
<210> 41
<211> 15
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 41
Tyr Val Gly Gly Gln Glu His Phe Ala His Leu Leu Ile Leu Arg
1 5 10 15
<210> 42
<211> 14
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 42
Glu Gln Leu Gly Glu Phe Tyr Glu Ala Leu Asp Cys Leu Arg
1 5 10
<210> 43
<211> 12
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 43
Gln Ser Thr Leu Val Leu Phe Pro Gly Asp Leu Arg
1 5 10
<210> 44
<211> 9
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 44
Phe Gln Thr Phe Glu Gly Asp Leu Lys
1 5
<210> 45
<211> 14
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 45
Leu Glu Ile Gln Leu Leu Glu Asn Ser Leu Ser Thr Tyr Lys
1 5 10
<210> 46
<211> 9
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 46
Glu Asn Leu Gln Gly Leu Val Thr Arg
1 5
<210> 47
<211> 14
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 47
Glu Val Leu Leu Leu Val His Asn Leu Pro Gln Asp Pro Arg
1 5 10
<210> 48
<211> 9
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 48
Leu Phe Ile Pro Asn Ile Thr Thr Lys
1 5
<210> 49
<211> 16
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 49
Ala Ala Gly Gly Ala Val Cys Glu Gln Pro Leu Gly Leu Glu Cys Arg
1 5 10 15
<210> 50
<211> 19
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 50
Val Cys Gly Leu Cys Gly Asn Phe Asp Asp Asn Ala Ile Asn Asp Phe
1 5 10 15
Ala Thr Arg
<210> 51
<211> 7
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 51
Tyr Phe Leu Trp Val Val Lys
1 5
<210> 52
<211> 7
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 52
Asn Gln Gln Ile Phe Leu Arg
1 5
<210> 53
<211> 9
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 53
Ser Glu Ile Asp Leu Phe Asn Ile Arg
1 5
<210> 54
<211> 12
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 54
Val Gln Ser Ile Asn Tyr Asn Pro Phe Asp Gln Lys
1 5 10
<210> 55
<211> 12
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 55
Gly Pro Ala Gly Asp Ala Thr Val Ala Ser Glu Lys
1 5 10
<210> 56
<211> 14
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 56
Leu Phe Gly Gly Asn Phe Ala His Gln Ala Ser Val Ala Arg
1 5 10
<210> 57
<211> 11
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 57
Asn Ala Leu Glu Ser Tyr Thr Tyr Asn Ile Lys
1 5 10
<210> 58
<211> 14
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 58
Pro Phe Gly Val Ala Leu Leu Phe Gly Gly Val Asp Glu Lys
1 5 10
<210> 59
<211> 7
<212> PRT
<213> Artificial
<220>
<223> Synthetic
<400> 59
Glu Leu Thr Ser Glu Leu Lys
1 5
Claims (15)
- 하기 1∼22의 22개의 단백질 중 적어도 1개의 단백질, 또는 1∼22의 단백질의 부분 펩티드 중 적어도 1개의 펩티드로 이루어지는, 대장암 검출을 위한 대장암 바이오마커:
1. 아넥신 A11(Annexin A11)(ANXA 11)(서열번호 1);
2. 아넥신 A3(Annexin A3)(ANXA 3)(서열번호 2);
3. 아넥신 A4(Annexin A4)(ANXA 4)(서열번호 3);
4. 테나신-N(Tanascin-N)(TNN)(서열번호 4);
5. 트랜스페린 수용체 단백질 1(Transferrin receptor protein 1)(TFRC)(서열번호 5);
6. 글루코오스 트랜스포터 1(GLUT-1)(SLC2A1)(서열번호 6);
7. 보체 성분 C9(Complement component C9)(C9)(서열번호 7);
8. CD88 항원(CD88 antigen)(C5AR1)(서열번호 8);
9. 78kDa 글루코오스 제어 단백질(78kDa glucose-regulated protein)(HSPA5)(서열번호 9);
10. α-1-산성 글리코프로테인(α-1-acid glycoprotein)(ORM1)(서열번호 10);
11. 매트릭스 메탈로프로테아제 9(Matrix metalloproteinase-9)(MMP9)(서열번호 11);
12. 앙기오포이에틴-1(Angiopoietin-1)(ANGPT1)(서열번호 12);
13. CD67 항원(CD67 antigen)(CEACAM8)(서열번호 13);
14. 뮤신-5B(Mucin-5B)(MUC5B)(서열번호 14);
15. 어댑터 단백질 GRB2(Adapter protein GRB2)(GRB2)(서열번호 15);
16. 아넥신 A5(Annexin A5)(ANXA 5)(서열번호 16);
17. 올팍토메딘-4(Olfactomedin-4)(OLFM4)(서열번호 17);
18. 중성 아미노산 트랜스포터 B(0)(Neutral amino acid transporter B(0))(SLC1A5)(서열번호 18);
19. 트리펩티딜펩티다제 1(Tripeptidyl-peptidase 1)(TPP1)(서열번호 19);
20. 열쇼크 관련 70kDa 단백질 2(Heat shock-related 70kDa protein 2)(HSPA2)(서열번호 20);
21. 프로테아좀 서브유닛 α 타입-5(Proteasome subunit alpha type-5)(PSMA5)(서열번호 21); 또는
22. 호중구(好中球) 젤라티나아제 관련 리포칼린(Neutrophil gelatinase-associated lipocalin)(LCN2)(서열번호 22). - 제1항에 있어서,
제1항에 기재된 1∼22의 22개의 단백질 중 2개 이상의 단백질, 또는 상기 1∼22의 단백질의 부분 펩티드 중 2개 이상의 펩티드를 조합하여 이루어지는, 대장암 검출을 위한 대장암 바이오마커. - 제1항 또는 제2항에 있어서,
제1항에 기재된 1∼22의 단백질의 부분 펩티드가 서열번호 23∼59로 표시되는 아미노산서열로 이루어지는 펩티드인, 대장암 검출을 위한 대장암 바이오마커. - 제1항에 있어서,
하기 12개의 단백질 중 적어도 1개의 단백질, 또는 하기 12개의 단백질의 부분 펩티드 중 적어도 1개의 펩티드로 이루어지는, 대장암 검출을 위한 대장암 바이오마커:
1. 아넥신 A11(서열번호 1);
2. 아넥신 A3(서열번호 2);
3. 아넥신 A4(서열번호 3);
4. 테나신-N (서열번호 4);
5. 트랜스페린 수용체 단백질 1(서열번호 5);
6. 글루코오스 트랜스포터 1(서열번호 6);
8. CD88 항원(서열번호 8);
11. 매트릭스 메탈로프로테아제 9(서열번호 11);
16. 아넥신 A5(서열번호 16);
17. 올팍토메딘-4(서열번호 17);
19. 트리펩티딜펩티다제 1(서열번호 19); 또는
22. 호중구 젤라티나아제 관련 리포칼린(서열번호 22). - 제4항에 있어서,
제4항에 기재된 12개의 단백질 중 2개 이상의 단백질, 또는 상기 12개의 단백질의 부분 펩티드 중 2개 이상의 펩티드를 조합하여 이루어지는, 대장암 검출을 위한 대장암 바이오마커. - 제4항 또는 제5항에 있어서,
제4항에 기재된 12개의 단백질의 부분 펩티드가 서열번호 23∼34, 37, 38, 43, 44, 53, 54, 56 및 59로 표시되는 아미노산서열로 이루어지는 펩티드인, 대장암 검출을 위한 대장암 바이오마커. - 제1항에 있어서,
아넥신 A4 혹은 아넥신 A11, 또는 이들의 부분 펩티드로 이루어지는, 대장암 검출을 위한 대장암 바이오마커. - 제7항에 있어서,
아넥신 A4와 아넥신 A11, 또는 아넥신 A4의 부분 펩티드와 아넥신 A11의 부분 펩티드를 조합하여 이루어지는, 대장암 검출을 위한 대장암 바이오마커. - 제7항 또는 제8항에 있어서,
아넥신 A4 및 아넥신 A11의 부분 펩티드가 서열번호 23, 24, 27 및 28로 표시되는 아미노산서열로 이루어지는 펩티드인, 대장암 검출을 위한 대장암 바이오마커. - 제1항 내지 제9항 중 어느 한 항에 기재된 대장암 바이오마커와 CEA를 조합하여 이루어지는, 대장암 검출을 위한 대장암 바이오마커.
- 생체시료 중의 제1항 내지 제10항 중 어느 한 항에 기재된 대장암 바이오마커를 측정하는 것을 포함하는, 대장암 검출 방법.
- 생체시료 중의 제1항 내지 제10항 중 어느 한 항에 기재된 대장암 바이오마커를 측정하고, 상기 바이오마커가 정상인과 비교하여 고농도로 존재하는 경우에, 대장암에 이환(罹患)되어 있는 것으로 판단하는, 대장암 검출 방법.
- 제11항 또는 제12항에 있어서,
생체시료가 혈액 중의 세포외소포(EV)인, 대장암 검출 방법. - 제11항 내지 제13항 중 어느 한 항에 있어서,
검출이 면역학적 측정법 또는 질량분석법에 의해 행해지는, 대장암 검출 방법. - 생체시료 중의 제1항 내지 제10항 중 어느 한 항에 기재된 대장암 바이오마커에 대한 항체를 포함하는, 대장암 검출 키트.
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WO2019004430A1 (ja) | 2019-01-03 |
TW201905461A (zh) | 2019-02-01 |
EP3647788A4 (en) | 2021-07-14 |
JP7285215B2 (ja) | 2023-06-01 |
CA3068688A1 (en) | 2019-01-03 |
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