구성 요소 1r 보완

C1R
사용 가능한 구조물
PDB	직교 검색: PDBe RCSB
PDB ID 코드 목록
	1APQ, 1GPZ, 1MD7, 1MD8, 2QY0
식별자
별칭	C1R, C1r, EDSPD1 보완
외부 ID	OMIM: 613785 MGI: 3779804 HomoloGene: 1313 GeneCard: C1R
유전자 위치(인간)
쳇.	12번 염색체(인간)
끝	7,092,540 bp
유전자 위치(마우스)
쳇.	6번 염색체(쥐)
끝	124,558,130 bp
RNA 표현 패턴
	표현된 상단
	간; ; 심막염; ; 간 우엽; ; 난소의; ; 비뇨기 방광; ; 담낭;
	추가 참조 표현식 데이터
	n/a
유전자 온톨로지
분자함수	펩티다아제 활성; 세린형 펩티다아제 활성; 세린형내막증제작용; GO:0001948 단백질 결합; 수산화효소 활동; 칼슘 이온 결합;
셀룰러 컴포넌트	세포외 지역; 혈액 미세조립물; 세포외 외성체; 세포외 공간;
생물학적 과정	면역 반응; 단백질 분해; 활성화 보완, 고전적 경로; 면역 체계 과정; 선천적인 면역 반응; 활성화를 보완하다; 보완 활성화 규정; 지모겐 활성화;
	출처:아미고 / 퀵고
직교체
	715
	667277
	ENSG00000159403; ENSG00000288512
	ENSMUSG00000098470
	P00736
	Q8CFG9
	NM_001733; NM_001354346
	NM_001113356
	NP_001724; NP_001341275
	NP_001106827
	위키다타
인간 보기/편집	마우스 보기/편집

보충 C1r 하위 성분(EC 3.4.21.41, 활성화 보충제 C1r, C overbar 1r esterase, C1r)은 선천적 면역 체계의 보완 시스템에 관여하는 단백질이다.^[5]^[6]^[7]인간에서 C1R은 C1R 유전자에 의해 암호화된다.^[8]

C1r과 함께 C1q, C1s와 함께 C1 콤플렉스를 형성하는데, 이는 혈청보완 시스템의 첫 번째 성분이다.C1r은 단백질 분해능에 의해 C1을 활성 형태로 활성화시키는 효소다.

임상적 유의성

Ehlers-Danlos 증후군 Beridontal 타입은 CR1 유전자의 돌연변이와 관련이 있다.

함수

C1r은 C1s와 상호작용하는 것으로 나타났다.C1r는 C1을 분할하여 C1의 활성 형태를 형성한다.^[9]^[10]

참조

^ ^a ^b ^c ENSG00000288512 GRCh38: 앙상블 릴리스 89: ENSG00000159403, ENSG00000288512 - 앙상블, 2017년 5월
^ ^a ^b ^c GRCm38: 앙상블 릴리스 89: ENSMUSG000098470 - 앙상블, 2017년 5월
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Sim RB (1981). "The human complement system serine proteases C1r and C1s and their proenzymes". Methods in Enzymology. 80 Pt C: 26–42. doi:10.1016/s0076-6879(81)80006-7. PMID 6281620.
^ Leytus SP, Kurachi K, Sakariassen KS, Davie EW (August 1986). "Nucleotide sequence of the cDNA coding for human complement C1r". Biochemistry. 25 (17): 4855–63. doi:10.1021/bi00365a020. PMID 3021205.
^ Müller-Eberhard HJ (1988). "Molecular organization and function of the complement system". Annual Review of Biochemistry. 57: 321–47. doi:10.1146/annurev.bi.57.070188.001541. PMID 3052276.
^ "Entrez Gene: C1R complement component 1, r subcomponent".
^ Thielens NM, Enrie K, Lacroix M, Jaquinod M, Hernandez JF, Esser AF, Arlaud GJ (April 1999). "The N-terminal CUB-epidermal growth factor module pair of human complement protease C1r binds Ca2+ with high affinity and mediates Ca2+-dependent interaction with C1s". The Journal of Biological Chemistry. 274 (14): 9149–59. doi:10.1074/jbc.274.14.9149. PMID 10092586.
^ Thiel S, Petersen SV, Vorup-Jensen T, Matsushita M, Fujita T, Stover CM, Schwaeble WJ, Jensenius JC (July 2000). "Interaction of C1q and mannan-binding lectin (MBL) with C1r, C1s, MBL-associated serine proteases 1 and 2, and the MBL-associated protein MAp19". Journal of Immunology. 165 (2): 878–87. doi:10.4049/jimmunol.165.2.878. PMID 10878362.

추가 읽기

Lee SL, Wallace SL, Barone R, Blum L, Chase PH (1979). "Familial deficiency of two subunits of the first component of complement. C1r and C1s associated with a lupus erythematosus-like disease". Arthritis and Rheumatism. 21 (8): 958–67. doi:10.1002/art.1780210813. PMID 737019.
Ward SL, Ingham KC (January 1992). "A calcium-binding monoclonal antibody that recognizes a non-calcium-binding epitope in the short consensus repeat units (SCRs) of complement C1r". Molecular Immunology. 29 (1): 83–93. doi:10.1016/0161-5890(92)90160-Y. PMID 1370572.
Luo C, Thielens NM, Gagnon J, Gal P, Sarvari M, Tseng Y, Tosi M, Zavodszky P, Arlaud GJ, Schumaker VN (May 1992). "Recombinant human complement subcomponent C1s lacking beta-hydroxyasparagine, sialic acid, and one of its two carbohydrate chains still reassembles with C1q and C1r to form a functional C1 complex". Biochemistry. 31 (17): 4254–62. doi:10.1021/bi00132a015. PMID 1533159.
Busby TF, Ingham KC (May 1990). "NH2-terminal calcium-binding domain of human complement C1s- mediates the interaction of C1r- with C1q". Biochemistry. 29 (19): 4613–8. doi:10.1021/bi00471a016. PMID 2372546.
Lyons LA, Kamboh MI, Ferrell RE (1989). "Genetic studies of low-abundance human plasma proteins. XI. Linkage analysis and population genetics of the C1S subcomponent of the first complement component". Complement and Inflammation. 6 (2): 81–7. doi:10.1159/000463078. PMID 2541966.
Arlaud GJ, Van Dorsselaer A, Bell A, Mancini M, Aude C, Gagnon J (September 1987). "Identification of erythro-beta-hydroxyasparagine in the EGF-like domain of human C1r". FEBS Letters. 222 (1): 129–34. doi:10.1016/0014-5793(87)80205-3. PMID 2820791. S2CID 36194093.
Nguyen VC, Tosi M, Gross MS, Cohen-Haguenauer O, Jegou-Foubert C, de Tand MF, Meo T, Frézal J (April 1988). "Assignment of the complement serine protease genes C1r and C1s to chromosome 12 region 12p13". Human Genetics. 78 (4): 363–8. doi:10.1007/BF00291737. PMID 2834284. S2CID 30582112.
Leytus SP, Kurachi K, Sakariassen KS, Davie EW (August 1986). "Nucleotide sequence of the cDNA coding for human complement C1r". Biochemistry. 25 (17): 4855–63. doi:10.1021/bi00365a020. PMID 3021205.
Journet A, Tosi M (December 1986). "Cloning and sequencing of full-length cDNA encoding the precursor of human complement component C1r". The Biochemical Journal. 240 (3): 783–7. doi:10.1042/bj2400783. PMC 1147487. PMID 3030286.
Arlaud GJ, Willis AC, Gagnon J (February 1987). "Complete amino acid sequence of the A chain of human complement-classical-pathway enzyme C1r". The Biochemical Journal. 241 (3): 711–20. doi:10.1042/bj2410711. PMC 1147622. PMID 3036070.
Chesne S, Villiers CL, Arlaud GJ, Lacroix MB, Colomb MG (January 1982). "Fluid-phase interaction of C1 inhibitor (C1 Inh) and the subcomponents C1r and C1s of the first component of complement, C1". The Biochemical Journal. 201 (1): 61–70. doi:10.1042/bj2010061. PMC 1163609. PMID 6282262.
Arlaud GJ, Gagnon J (April 1983). "Complete amino acid sequence of the catalytic chain of human complement subcomponent C1-r". Biochemistry. 22 (8): 1758–64. doi:10.1021/bi00277a003. PMID 6303394.
Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Nöthen MM, Dewald G (January 1994). "A common amino acid polymorphism in complement component C1R". Human Molecular Genetics. 3 (1): 217. doi:10.1093/hmg/3.1.217-a. PMID 8162045.
Gasque P, Ischenko A, Legoedec J, Mauger C, Schouft MT, Fontaine M (November 1993). "Expression of the complement classical pathway by human glioma in culture. A model for complement expression by nerve cells". The Journal of Biological Chemistry. 268 (33): 25068–74. PMID 8227070.
Pelloux S, Thielens NM, Hudry-Clergeon G, Pétillot Y, Filhol O, Arlaud GJ (May 1996). "Identification of a cryptic protein kinase CK2 phosphorylation site in human complement protease Clr, and its use to probe intramolecular interaction". FEBS Letters. 386 (1): 15–20. doi:10.1016/0014-5793(96)00403-6. PMID 8635594. S2CID 28372780.
Bradley K, North J, Saunders D, Schwaeble W, Jeziorska M, Woolley DE, Whaley K (August 1996). "Synthesis of classical pathway complement components by chondrocytes". Immunology. 88 (4): 648–56. PMC 1456645. PMID 8881771.
Lacroix M, Rossi V, Gaboriaud C, Chevallier S, Jaquinod M, Thielens NM, Gagnon J, Arlaud GJ (May 1997). "Structure and assembly of the catalytic region of human complement protease C1r: a three-dimensional model based on chemical cross-linking and homology modeling". Biochemistry. 36 (21): 6270–82. doi:10.1021/bi962719i. PMID 9174342.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Bersch B, Hernandez JF, Marion D, Arlaud GJ (February 1998). "Solution structure of the epidermal growth factor (EGF)-like module of human complement protease C1r, an atypical member of the EGF family". Biochemistry. 37 (5): 1204–14. doi:10.1021/bi971851v. PMID 9477945.

외부 링크

UCSC 게놈 브라우저의 인간 C1R 게놈 위치 및 C1R 유전자 세부 정보 페이지.
미국 국립 의학 도서관의 보완책 +C1r(MesH)

12번 염색체의 유전자에 관한 이 기사는 단조롭다.위키피디아를 확장하여 도울 수 있다.

이 단백질 관련 기사는 단조롭다.위키피디아를 확장하여 도울 수 있다.

[refGRCh38Ensembl-1] ENSG00000288512 GRCh38: 앙상블 릴리스 89: ENSG00000159403, ENSG00000288512 - 앙상블, 2017년 5월

[refGRCm38Ensembl-2] GRCm38: 앙상블 릴리스 89: ENSMUSG000098470 - 앙상블, 2017년 5월

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[5] Sim RB (1981). "The human complement system serine proteases C1r and C1s and their proenzymes". Methods in Enzymology. 80 Pt C: 26–42. doi:10.1016/s0076-6879(81)80006-7. PMID 6281620.

[6] Leytus SP, Kurachi K, Sakariassen KS, Davie EW (August 1986). "Nucleotide sequence of the cDNA coding for human complement C1r". Biochemistry. 25 (17): 4855–63. doi:10.1021/bi00365a020. PMID 3021205.

[7] Müller-Eberhard HJ (1988). "Molecular organization and function of the complement system". Annual Review of Biochemistry. 57: 321–47. doi:10.1146/annurev.bi.57.070188.001541. PMID 3052276.

[entrez-8] "Entrez Gene: C1R complement component 1, r subcomponent".

[pmid10092586-9] Thielens NM, Enrie K, Lacroix M, Jaquinod M, Hernandez JF, Esser AF, Arlaud GJ (April 1999). "The N-terminal CUB-epidermal growth factor module pair of human complement protease C1r binds Ca2+ with high affinity and mediates Ca2+-dependent interaction with C1s". The Journal of Biological Chemistry. 274 (14): 9149–59. doi:10.1074/jbc.274.14.9149. PMID 10092586.

[pmid10878362-10] Thiel S, Petersen SV, Vorup-Jensen T, Matsushita M, Fujita T, Stover CM, Schwaeble WJ, Jensenius JC (July 2000). "Interaction of C1q and mannan-binding lectin (MBL) with C1r, C1s, MBL-associated serine proteases 1 and 2, and the MBL-associated protein MAp19". Journal of Immunology. 165 (2): 878–87. doi:10.4049/jimmunol.165.2.878. PMID 10878362.

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v t 내시경 검사: 세린 프로테아제/세린내시경 검사(EC 3.4.21)
소화효소	엔토펩티다아제 트립신 키모트립신 엘라스타아제 중성미자 췌장
응고	요인: 트롬빈 인자 VIIA 인자 IXa 인자 사 인자 XIA 인자 XIIA 칼리크레인 PSA KLK1 KLK2 KLK3 KLK4 KLK5 KLK6 KLK7 KLK8 KLK9 KLK10 KLK11 KLK12 KLK13 KLK14 KLK15 섬유소 분해: 플라스민 플라스미노겐 활성제 조직 플라스미노겐 활성제 비뇨기 플라스미노겐 활성제
보완체계	요인 B 요인 D 인자 I MASP MASP1 MASP2 C3 변환효소
기타 면역 체계	키마세 그란지메 트립타제 단백질 분해효소 3/미엘로블라스틴
베놈빈	앤크로드 바트록소빈
기타	아크로신 프롤릴엔도펩티다아제 프로나아제 프로프로테인 변환 1 2 프로스타신 릴린 서브틸리신/퓨린/S1P4 세돌리신/TPP1 스트렙토키나아제 카테신 A G

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구성 요소 1r 보완

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임상적 유의성

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