F7
This gene encodes coagulation factor VII which is a vitamin K-dependent factor essential for hemostasis. This factor circulates in the blood in a zymogen form, and is converted to an active form by either factor IXa, factor Xa, factor XIIa, or thrombin by minor proteolysis. Upon activation of the factor VII, a heavy chain containing a catalytic domain and a light chain containing 2 EGF-like domains are generated, and two chains are held together by a disulfide bond. In the presence of factor III and calcium ions, the activated factor then further activates the coagulation cascade by converting factor IX to factor IXa and/or factor X to factor Xa. Defects in this gene can cause coagulopathy. Alternative splicing results in multiple transcript variants encoding different isoforms that may undergo similar proteolytic processing to generate mature polypeptides. [provided by RefSeq, Aug 2015]
Full Name
Coagulation Factor VII
Research Area
Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium.
Biological Process
Animal organ regeneration Source: Ensembl
Blood coagulation Source: BHF-UCL
Circadian rhythm Source: Ensembl
Positive regulation of blood coagulation Source: Ensembl
Positive regulation of cell migration Source: BHF-UCL
Positive regulation of leukocyte chemotaxis Source: BHF-UCL
Positive regulation of platelet-derived growth factor receptor signaling pathway Source: BHF-UCL
Positive regulation of positive chemotaxis Source: BHF-UCL
Positive regulation of protein kinase B signaling Source: BHF-UCL
Protein processing Source: BHF-UCL
Response to 2,3,7,8-tetrachlorodibenzodioxine Source: Ensembl
Response to anticoagulant Source: Ensembl
Response to astaxanthin Source: Ensembl
Response to carbon dioxide Source: Ensembl
Response to cholesterol Source: Ensembl
Response to estradiol Source: Ensembl
Response to estrogen Source: Ensembl
Response to genistein Source: Ensembl
Response to growth hormone Source: Ensembl
Response to hypoxia Source: Ensembl
Response to Thyroid stimulating hormone Source: Ensembl
Response to thyrotropin-releasing hormone Source: Ensembl
Response to thyroxine Source: Ensembl
Response to vitamin K Source: Ensembl
Cellular Location
Secreted
Involvement in disease
Factor VII deficiency (FA7D):
A hemorrhagic disease with variable presentation. The clinical picture can be very severe, with the early occurrence of intracerebral hemorrhages or repeated hemarthroses, or, in contrast, moderate with cutaneous-mucosal hemorrhages (epistaxis, menorrhagia) or hemorrhages provoked by a surgical intervention. Finally, numerous subjects are completely asymptomatic despite very low factor VII levels.
PTM
The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
O- and N-glycosylated. N-glycosylation at Asn-205 occurs cotranslationally and is mediated by STT3A-containing complexes, while glycosylation at Asn-382 is post-translational and is mediated STT3B-containing complexes before folding. O-fucosylated by POFUT1 on a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines.
Can be either O-glucosylated or O-xylosylated at Ser-112 by POGLUT1 in vitro.
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Datasheet