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MGP001013

UniProt Annotations

Entry Information
Gene Namecoagulation factor X
Protein EntryFA10_HUMAN
UniProt IDP00742
SpeciesHuman
Comments
Comment typeDescription
Catalytic ActivitySelective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.
DiseaseFactor X deficiency (FA10D) [MIM:227600]: A hemorrhagic disease with variable presentation. Affected individuals can manifest prolonged nasal and mucosal hemorrhage, menorrhagia, hematuria, and occasionally hemarthrosis. Some patients do not have clinical bleeding diathesis. {ECO:0000269|PubMed:10468877, ECO:0000269|PubMed:10746568, ECO:0000269|PubMed:11248282, ECO:0000269|PubMed:11728527, ECO:0000269|PubMed:12945883, ECO:0000269|PubMed:15650540, ECO:0000269|PubMed:17393015, ECO:0000269|PubMed:19135706, ECO:0000269|PubMed:1973167, ECO:0000269|PubMed:1985698, ECO:0000269|PubMed:2790181, ECO:0000269|PubMed:7669671, ECO:0000269|PubMed:7860069, ECO:0000269|PubMed:8529633, ECO:0000269|PubMed:8845463, ECO:0000269|PubMed:8910490}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Enzyme RegulationInhibited by SERPINA5 and SERPINA10. {ECO:0000269|PubMed:20427285, ECO:0000269|PubMed:6323392}.
FunctionFactor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.
PtmN- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. {ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:8243461}.
PtmThe activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway).
PtmThe iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269|PubMed:6871167}.
PtmThe vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.
SimilarityBelongs to the peptidase S1 family. {ECO:0000255|PROSITE-ProRule:PRU00274}.
SimilarityContains 1 Gla (gamma-carboxy-glutamate) domain. {ECO:0000255|PROSITE-ProRule:PRU00463}.
SimilarityContains 1 peptidase S1 domain. {ECO:0000255|PROSITE- ProRule:PRU00274}.
SimilarityContains 2 EGF-like domains. {ECO:0000255|PROSITE- ProRule:PRU00076}.
Subcellular LocationSecreted.
SubunitThe two chains are formed from a single-chain precursor by the excision of two Arg residues and are held together by 1 or more disulfide bonds. Forms a heterodimer with SERPINA5.
Tissue SpecificityPlasma; synthesized in the liver. {ECO:0000269|PubMed:6587384}.
Web ResourceName=SeattleSNPs; URL="http://pga.gs.washington.edu/data/f10/";
Web ResourceName=Wikipedia; Note=Factor X entry; URL="http://en.wikipedia.org/wiki/Factor_X";
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