| Predicate | Object |
|---|---|
| rdf:type | |
| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
Coagulation factor X
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| http://www.biopax.org/relea... |
FA10_HUMAN
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| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
3.4.21.6,
Activated factor Xa heavy chain,
Factor X heavy chain,
Factor X light chain,
Stuart factor,
Stuart-Prower factor
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| http://www.biopax.org/relea... |
FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting. CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin. SUBUNIT: The 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. SUBCELLULAR LOCATION: Secreted. TISSUE SPECIFICITY: Plasma; synthesized in the liver. PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium. PTM: N- and O-glycosylated. PTM: The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway). PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. DISEASE: Defects in F10 are the cause of factor 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. SIMILARITY: Belongs to the peptidase S1 family. SIMILARITY: Contains 2 EGF-like domains. SIMILARITY: Contains 1 Gla (gamma-carboxy-glutamate) domain. SIMILARITY: Contains 1 peptidase S1 domain. WEB RESOURCE: Name=Wikipedia; Note=Factor X entry; URL="http://en.wikipedia.org/wiki/Factor_X"; WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/f10/"; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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