Complement Component 1, R Subcomponent (C1r)

C1-r; complement Component 1; Complement component 1 subcomponent r

SPN	V701
HGNC	1246
MGI	1355313
PubMed	1249422
RGD	1309091
UniProt	P00736
Wiki	C1R_(gene

Complement component 1R is a protein involved in the complement system.The complement complexes have multiple subunits: one carrying the active site, one that binds to the cell surface, and one that binds to substrate. The steps in the complement cascade have similarities to those in the coagulation cascade. Furthermore, many enzymes have the same pattern of activation and multimeric structure with specific function of the several subunits. Both C1r and C1s are enzymatic, as is C2, as noted earlier. In the alternate pathway, factors B and D are enzymatic but deficiency states are unknown. C1r is a single-chain glycoprotein with a molecular weight of about 83,000. Upon activation, it is cleaved into an A chain and a B chain which are held together by a disulfide bond. The B chain contains the catalytic portion of the enzyme.

Reference

"Nucleotide sequence of the cDNA coding for human complement C1r."
Biochemistry 25:4855-4863(1986) [PubMed] [Europe PMC] [Abstract]

"Cloning and sequencing of full-length cDNA encoding the precursor of human complement component C1r."
Biochem. J. 240:783-787(1986) [PubMed] [Europe PMC] [Abstract]

"The human complement component C1R gene: the exon-intron structure and the molecular basis of allelic diversity."
Ann. Hum. Genet. 67:207-215(2003) [PubMed] [Europe PMC] [Abstract]

"The full-ORF clone resource of the German cDNA consortium."
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]

"The finished DNA sequence of human chromosome 12."
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Complete amino acid sequence of the A chain of human complement-classical-pathway enzyme C1r."
Biochem. J. 241:711-720(1987) [PubMed] [Europe PMC] [Abstract]

"Complete amino acid sequence of the catalytic chain of human complement subcomponent C1-r."
Biochemistry 22:1758-1764(1983) [PubMed] [Europe PMC] [Abstract]

"Identification of erythro-beta-hydroxyasparagine in the EGF-like domain of human C1r."
FEBS Lett. 222:129-134(1987) [PubMed] [Europe PMC] [Abstract]

"Identification of a cryptic protein kinase CK2 phosphorylation site in human complement protease Clr, and its use to probe intramolecular interaction."
FEBS Lett. 386:15-20(1996) [PubMed] [Europe PMC] [Abstract]

"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]

"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]

"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]

"Solution structure of the epidermal growth factor (EGF)-like module of human complement protease C1r, an atypical member of the EGF family."
Biochemistry 37:1204-1214(1998) [PubMed] [Europe PMC] [Abstract]

"The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex."
EMBO J. 21:231-239(2002) [PubMed] [Europe PMC] [Abstract]

"Monomeric structures of the zymogen and active catalytic domain of complement protease c1r: further insights into the c1 activation mechanism."
Structure 10:1509-1519(2002) [PubMed] [Europe PMC] [Abstract]

"A common amino acid polymorphism in complement component C1R."
Hum. Mol. Genet. 3:217-217(1994) [PubMed] [Europe PMC] [Abstract]

"Quantitative detection of single amino acid polymorphisms by targeted proteomics."
J. Mol. Cell Biol. 3:309-315(2011) [PubMed] [Europe PMC] [Abstract]