Post Translational Modifications | Highly glycosylated (49%) with N- and O-glycosylation. O-glycosylated with core 1 or possibly core 8 glycans. N-glycan heterogeneity at Asn-25: Hex5HexNAc4 (minor), dHex1Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor). Can be proteolytically cleaved by E.coli stcE. |
Function | Activation of the C1 complex is under control of the C1-inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. Inhibits chymotrypsin and kallikrein. |
Protein Name | Plasma Protease C1 InhibitorC1 InhC1inhC1 Esterase InhibitorC1-Inhibiting FactorSerpin G1 |
Database Links | Reactome: R-HSA-114608Reactome: R-HSA-140837Reactome: R-HSA-9657689Reactome: R-HSA-977606 |
Cellular Localisation | Secreted |
Alternative Protein Names | Plasma Protease C1 Inhibitor proteinC1 Inh proteinC1inh proteinC1 Esterase Inhibitor proteinC1-Inhibiting Factor proteinSerpin G1 proteinSERPING1 proteinC1IN proteinC1NH protein |
Information sourced from Uniprot.org