C1R (gene)

C1R

Available structures

Ortholog search: PDBe RCSB

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

Identifiers

Aliases

C1R

External IDs

MGI: 3779804 HomoloGene: 1313 GeneCards: C1R

Targeted by Drug

nafamostat^[1]

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

Orthologs

Species

Human

Mouse

Entrez


715


667277

Ensembl


ENSG00000159403


ENSMUSG00000098470

UniProt


P00736


Q8CFG9

RefSeq (mRNA)


NM_001733


NM_001113356

RefSeq (protein)


NP_001724.3


NP_001106827.1

Location (UCSC)

Chr 12: 7.08 – 7.09 Mb

Chr 6: 124.57 – 124.58 Mb

PubMed search

^[2]

^[3]

Wikidata

View/Edit Human

View/Edit Mouse

Complement C1r subcomponent is a protein that in humans is encoded by the C1R gene.^[4]

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.^[5]^[6]

References

↑ "Drugs that physically interact with Complement C1r subcomponent view/edit references on wikidata".
↑ "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. doi:10.1074/jbc.274.14.9149. ISSN 0021-9258. PMID 10092586.
↑ 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. doi:10.4049/jimmunol.165.2.878. ISSN 0022-1767. PMID 10878362.

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. doi:10.1002/art.1780210813. PMID 737019.
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. doi:10.1016/0161-5890(92)90160-Y. PMID 1370572.
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. doi:10.1021/bi00132a015. PMID 1533159.
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. 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. 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. doi:10.1016/0014-5793(87)80205-3. PMID 2820791.
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. doi:10.1007/BF00291737. PMID 2834284.
Leytus SP, Kurachi K, Sakariassen KS, Davie EW (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 (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. doi:10.1021/bi00277a003. PMID 6303394.
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. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Nöthen MM, Dewald G (1994). "A common amino acid polymorphism in complement component C1R.". Hum. Mol. Genet. 3 (1): 217. doi:10.1093/hmg/3.1.217-a. PMID 8162045.
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. doi:10.1016/0014-5793(96)00403-6. PMID 8635594.
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. doi:10.1021/bi962719i. PMID 9174342.
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. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
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. doi:10.1021/bi971851v. PMID 9477945.

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

Further reading