Literature summary for 3.4.21.42 extracted from

Wijeyewickrema, L.C.; Yongqing, T.; Tran, T.P.; Thompson, P.E.; Viljoen, J.E.; Coetzer, T.H.; Duncan, R.C.; Kass, I.; Buckle, A.M.; Pike, R.N.
Molecular determinants of the substrate specificity of the complement-initiating protease, C1r (2013), J. Biol. Chem., 288, 15571-15580.

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P09871	-	-

Subunits

Subunits	Comment	Organism
More	C1r and C1s pro-enzymes form a heterotetrameric structure that associates with the recognition molecule, C1q, in the C1 complex	Homo sapiens

Synonyms

Synonyms	Comment	Organism
C1s	-	Homo sapiens
complement subcomponent 1s	-	Homo sapiens

General Information

General Information	Comment	Organism
metabolism	C1r and C1s pro-enzymes form a heterotetrameric structure that associates with the recognition molecule, C1q, in the C1 complex. Zymogen C1s is cleaved by the C1r protease resulting in C1s activation, kinetics of activation of C1s by C1r protease, overview	Homo sapiens
additional information	synthesis of a series of fluorescence-quenched peptide substrates, comprising residues from the cleavage site in C1s and some peptides found among the phage-displayed peptides, very high concentrations of C1r are required to cleave such peptides	Homo sapiens
physiological function	enzyme C1r is active with the substrate fragment consisting of complement control protein domains, CCP1 and CCP2, plus serine protease domain of wild-type and mutant Q462N, Q462G, I464A, and Q462N/I464A forms of C1s, C1s mutant Q462N/I464A gives very low activity as substrate for C1r	Homo sapiens

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Release 2023.1 (January 2023)