MGP Database

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MGP000347

UniProt Annotations

Entry Information
Gene Nameserpin peptidase inhibitor, clade G (C1 inhibitor), member 1
Protein EntryIC1_HUMAN
UniProt IDP05155
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=3; Name=1; IsoId=P05155-1; Sequence=Displayed; Name=2; IsoId=P05155-2; Sequence=VSP_056662; Note=No experimental confirmation available.; Name=3; IsoId=P05155-3; Sequence=VSP_056663; Note=No experimental confirmation available.;
DiseaseHereditary angioedema (HAE) [MIM:106100]: 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. {ECO:0000269|PubMed:12773530, ECO:0000269|PubMed:1363816, ECO:0000269|PubMed:1451784, ECO:0000269|PubMed:14635117, ECO:0000269|PubMed:16409206, ECO:0000269|PubMed:2118657, ECO:0000269|PubMed:2296585, ECO:0000269|PubMed:22994404, ECO:0000269|PubMed:2365061, ECO:0000269|PubMed:24456027, ECO:0000269|PubMed:3178731, ECO:0000269|PubMed:7814636, ECO:0000269|PubMed:7883978, ECO:0000269|PubMed:8172583, ECO:0000269|PubMed:8529136, ECO:0000269|PubMed:8755917, ECO:0000269|Ref.40}. Note=The disease is caused by mutations affecting the gene represented in this entry.
FunctionActivation 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. {ECO:0000269|PubMed:8495195}.
PolymorphismChymotrypsin uses Ala-465 as its reactive site in normal plasma protease C1 inhibitor, and His-466 as its reactive site in the variant His-466.
PtmCan be proteolytically cleaved by E.coli stcE. {ECO:0000269|PubMed:12123444, ECO:0000269|PubMed:15096536}.
PtmHighly 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). {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16040958, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17488724, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:23234360, ECO:0000269|PubMed:3756141}.
Sequence CautionSequence=AAA53096.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
SimilarityBelongs to the serpin family. {ECO:0000305}.
Subcellular LocationSecreted.
SubunitBinds to E.coli stcE which allows localization of SERPING1 to cell membranes thus protecting the bacteria against complement-mediated lysis. Interacts with MASP1. {ECO:0000269|PubMed:10946292, ECO:0000269|PubMed:12123444, ECO:0000269|PubMed:15096536}.
Web ResourceName=SeattleSNPs; URL="http://pga.gs.washington.edu/data/serping1/";
Web ResourceName=SERPING1base; Note=SERPING1 mutation db; URL="http://structure.bmc.lu.se/idbase/SERPING1base/";
Web ResourceName=Wikipedia; Note=C1-inhibitor entry; URL="http://en.wikipedia.org/wiki/C1-inhibitor";
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