SERPING1
This gene encodes a highly glycosylated plasma protein involved in the regulation of the complement cascade. Its protein inhibits activated C1r and C1s of the first complement component and thus regulates complement activation. Deficiency of this protein is associated with hereditary angioneurotic oedema (HANE). Alternative splicing results in multiple transcript variants encoding the same isoform. [provided by RefSeq, Jul 2008]
Full Name
Serpin Family G Member 1
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.
Biological Process
Biological Process agingIEA:Ensembl
Biological Process blood circulationManual Assertion Based On ExperimentTAS:ProtInc
Biological Process blood coagulationIEA:UniProtKB-KW
Biological Process complement activation, classical pathwayIEA:UniProtKB-KW
Biological Process fibrinolysisIEA:UniProtKB-KW
Biological Process innate immune responseIEA:UniProtKB-KW
Biological Process negative regulation of complement activation, lectin pathwayManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process negative regulation of endopeptidase activityManual Assertion Based On ExperimentIBA:GO_Central
Cellular Location
Secreted
Involvement in disease
Angioedema, hereditary (HAE):
An autosomal dominant disorder characterized by episodic local swelling involving subcutaneous or submucous tissue of the upper respiratory and gastrointestinal tracts, face, extremities, and genitalia. Hereditary angioedema due to C1 esterase inhibitor deficiency is comprised of two clinically indistinguishable forms. In hereditary angioedema type 1, serum levels of C1 esterase inhibitor are decreased, while in type 2, the levels are normal or elevated, but the protein is non-functional.
PTM
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.
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