UniProt functional annotation for P05155



	UniProt functional annotation for P05155

UniProt code: P05155.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

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. {ECO:0000269|PubMed:8495195}.

Subunit: Binds 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}.

Subcellular location: Secreted.

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). {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}.

Ptm: Can be proteolytically cleaved by E.coli stcE. {ECO:0000269|PubMed:12123444, ECO:0000269|PubMed:15096536}.

Polymorphism: Chymotrypsin 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.

Disease: Hereditary 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.41}. Note=The disease is caused by variants affecting the gene represented in this entry.

Similarity: Belongs to the serpin family. {ECO:0000305}.

Sequence caution: Sequence=AAA53096.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



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. {ECO:0000269\|PubMed:8495195}.


Subunit:		Binds 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}.
Subcellular location:		Secreted.
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). {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}.
Ptm:		Can be proteolytically cleaved by E.coli stcE. {ECO:0000269\|PubMed:12123444, ECO:0000269\|PubMed:15096536}.
Polymorphism:		Chymotrypsin 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.
Disease:		Hereditary 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.41}. Note=The disease is caused by variants affecting the gene represented in this entry.
Similarity:		Belongs to the serpin family. {ECO:0000305}.
Sequence caution:		Sequence=AAA53096.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};