C1R (gene)

C1R

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1APQ, 1GPZ, 1MD7, 1MD8, 2QY0

Identifiers

Aliases

C1R, complement C1r, EDSPD1

External IDs

MGI: 1355313 HomoloGene: 1313 GeneCards: C1R

Gene ontology
Molecular function	• peptidase activity • serine-type peptidase activity • serine-type endopeptidase activity • protein binding • hydrolase activity • calcium ion binding
Cellular component	• extracellular region • blood microparticle • extracellular exosome • extracellular space
Biological process	• immune response • proteolysis • complement activation, classical pathway • immune system process • innate immune response • complement activation • regulation of complement activation • zymogen activation
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


715


50909

Ensembl


ENSG00000159403


ENSMUSG00000055172

UniProt


P00736


Q8CG16

RefSeq (mRNA)


NM_001733


NM_023143

RefSeq (protein)


NP_001724


NP_075632

Location (UCSC)

Chr 12: 7.08 – 7.09 Mb

Chr 6: 124.51 – 124.52 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Complement C1r subcomponent is a protein that in humans is encoded by the C1R gene.^[3]

Along with C1s and C1q complex it forms C1, the first component of the serum complement system.

Interactions

C1R (gene) has been shown to interact with C1S.^[4]^[5]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ "Entrez Gene: C1R complement component 1, r subcomponent".
↑ Thielens, N M; Enrie K; Lacroix M; Jaquinod M; Hernandez J F; Esser A F; Arlaud G J (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". J. Biol. Chem. UNITED STATES. 274 (14): 9149–59. ISSN 0021-9258. PMID 10092586. doi:10.1074/jbc.274.14.9149.
↑ Thiel, S; Petersen S V; Vorup-Jensen T; Matsushita M; Fujita T; Stover C M; Schwaeble W J; Jensenius J C (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". J. Immunol. UNITED STATES. 165 (2): 878–87. ISSN 0022-1767. PMID 10878362. doi:10.4049/jimmunol.165.2.878.

External links

Human C1R genome location and C1R gene details page in the UCSC Genome Browser.

Lee SL, Wallace SL, Barone R, et al. (1979). "Familial deficiency of two subunits of the first component of complement. C1r and C1s associated with a lupus erythematosus-like disease.". Arthritis Rheum. 21 (8): 958–67. PMID 737019. doi:10.1002/art.1780210813.
Ward SL, Ingham KC (1992). "A calcium-binding monoclonal antibody that recognizes a non-calcium-binding epitope in the short consensus repeat units (SCRs) of complement C1r.". Mol. Immunol. 29 (1): 83–93. PMID 1370572. doi:10.1016/0161-5890(92)90160-Y.
Luo C, Thielens NM, Gagnon J, et al. (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. PMID 1533159. doi:10.1021/bi00132a015.
Busby TF, Ingham KC (1990). "NH2-terminal calcium-binding domain of human complement C1s- mediates the interaction of C1r- with C1q.". Biochemistry. 29 (19): 4613–8. PMID 2372546. doi:10.1021/bi00471a016.
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. PMID 2541966.
Arlaud GJ, Van Dorsselaer A, Bell A, et al. (1987). "Identification of erythro-beta-hydroxyasparagine in the EGF-like domain of human C1r.". FEBS Lett. 222 (1): 129–34. PMID 2820791. doi:10.1016/0014-5793(87)80205-3.
Nguyen VC, Tosi M, Gross MS, et al. (1988). "Assignment of the complement serine protease genes C1r and C1s to chromosome 12 region 12p13.". Hum. Genet. 78 (4): 363–8. PMID 2834284. doi:10.1007/BF00291737.
Leytus SP, Kurachi K, Sakariassen KS, Davie EW (1986). "Nucleotide sequence of the cDNA coding for human complement C1r.". Biochemistry. 25 (17): 4855–63. PMID 3021205. doi:10.1021/bi00365a020.
Journet A, Tosi M (1987). "Cloning and sequencing of full-length cDNA encoding the precursor of human complement component C1r.". Biochem. J. 240 (3): 783–7. PMC 1147487 . PMID 3030286.
Arlaud GJ, Willis AC, Gagnon J (1987). "Complete amino acid sequence of the A chain of human complement-classical-pathway enzyme C1r.". Biochem. J. 241 (3): 711–20. PMC 1147622 . PMID 3036070.
Chesne S, Villiers CL, Arlaud GJ, et al. (1982). "Fluid-phase interaction of C1 inhibitor (C1 Inh) and the subcomponents C1r and C1s of the first component of complement, C1.". Biochem. J. 201 (1): 61–70. PMC 1163609 . PMID 6282262.
Arlaud GJ, Gagnon J (1983). "Complete amino acid sequence of the catalytic chain of human complement subcomponent C1-r.". Biochemistry. 22 (8): 1758–64. PMID 6303394. doi:10.1021/bi00277a003.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene. 138 (1-2): 171–4. PMID 8125298. doi:10.1016/0378-1119(94)90802-8.
Nöthen MM, Dewald G (1994). "A common amino acid polymorphism in complement component C1R.". Hum. Mol. Genet. 3 (1): 217. PMID 8162045. doi:10.1093/hmg/3.1.217-a.
Gasque P, Ischenko A, Legoedec J, et al. (1993). "Expression of the complement classical pathway by human glioma in culture. A model for complement expression by nerve cells.". J. Biol. Chem. 268 (33): 25068–74. PMID 8227070.
Pelloux S, Thielens NM, Hudry-Clergeon G, et al. (1996). "Identification of a cryptic protein kinase CK2 phosphorylation site in human complement protease Clr, and its use to probe intramolecular interaction.". FEBS Lett. 386 (1): 15–20. PMID 8635594. doi:10.1016/0014-5793(96)00403-6.
Bradley K, North J, Saunders D, et al. (1996). "Synthesis of classical pathway complement components by chondrocytes.". Immunology. 88 (4): 648–56. PMC 1456645 . PMID 8881771.
Lacroix M, Rossi V, Gaboriaud C, et al. (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. PMID 9174342. doi:10.1021/bi962719i.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene. 200 (1-2): 149–56. PMID 9373149. doi:10.1016/S0378-1119(97)00411-3.
Bersch B, Hernandez JF, Marion D, Arlaud GJ (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. PMID 9477945. doi:10.1021/bi971851v.

PDB gallery

1apq: STRUCTURE OF THE EGF-LIKE MODULE OF HUMAN C1R, NMR, 19 STRUCTURES

1gpz: THE CRYSTAL STRUCTURE OF THE ZYMOGEN CATALYTIC DOMAIN OF COMPLEMENT PROTEASE C1R

1md7: Monomeric structure of the zymogen of complement protease C1r

1md8: Monomeric structure of the active catalytic domain of complement protease C1r

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C1R (gene)

Interactions

References

External links

Further reading