Factor X

Factor X, also known by the eponym Stuart–Prower factor, is an enzyme (EC 3.4.21.6) of the coagulation cascade. It is a serine endopeptidase (protease group S1, PA clan). Factor X is synthesized in the liver and requires vitamin K for its synthesis.

F10
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesF10, FX, FXA, coagulation factor X
External IDsOMIM: 613872 MGI: 103107 HomoloGene: 30976 GeneCards: F10
Orthologs
SpeciesHumanMouse
Entrez

2159

14058

Ensembl

ENSG00000126218

ENSMUSG00000031444

UniProt

P00742

O88947

RefSeq (mRNA)

NM_000504
NM_001312674
NM_001312675

NM_001242368
NM_007972

RefSeq (protein)

NP_000495
NP_001299603
NP_001299604

NP_001229297
NP_031998

Location (UCSC)Chr 13: 113.12 – 113.15 MbChr 8: 13.09 – 13.11 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

Factor X is activated, by hydrolysis, into factor Xa by both factor IX (with its cofactor, factor VIII in a complex known as intrinsic tenase) and factor VII with its cofactor, tissue factor (a complex known as extrinsic tenase). It is therefore the first member of the final common pathway or thrombin pathway.

It acts by cleaving prothrombin in two places (an Arg-Thr and then an Arg-Ile bond), which yields the active thrombin. This process is optimized when factor Xa is complexed with activated co-factor V in the prothrombinase complex.

Factor Xa is inactivated by protein Z-dependent protease inhibitor (ZPI), a serine protease inhibitor (serpin). The affinity of this protein for factor Xa is increased 1000-fold by the presence of protein Z, while it does not require protein Z for inactivation of factor XI. Defects in protein Z lead to increased factor Xa activity and a propensity for thrombosis.

The half life of factor X is 40–45 hours.

This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.