Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P09871 | - |
- |
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 | Comment | Organism |
---|---|---|
C1s | - |
Homo sapiens |
complement subcomponent 1s | - |
Homo sapiens |
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 |