UniProt functional annotation for P08709



	UniProt functional annotation for P08709

UniProt code: P08709.

Organism: Homo sapiens (Human).

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

Function: 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.

Catalytic activity: Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.; EC=3.4.21.21;

Subunit: Heterodimer of a light chain and a heavy chain linked by a disulfide bond. {ECO:0000269|PubMed:8598903, ECO:0000269|PubMed:9925787}.

Subcellular location: Secreted.

Tissue specificity: Plasma.

Ptm: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.

Ptm: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269|PubMed:3264725}.

Ptm: 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. {ECO:0000269|PubMed:1904059, ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:21949356, ECO:0000269|PubMed:3264725, ECO:0000269|PubMed:9023546}.

Ptm: Can be either O-glucosylated or O-xylosylated at Ser-112 by POGLUT1 in vitro.

Disease: Factor VII deficiency (FA7D) [MIM:227500]: 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. {ECO:0000269|PubMed:10862079, ECO:0000269|PubMed:11091194, ECO:0000269|PubMed:11129332, ECO:0000269|PubMed:12472587, ECO:0000269|PubMed:14717781, ECO:0000269|PubMed:1634227, ECO:0000269|PubMed:18976247, ECO:0000269|PubMed:19432927, ECO:0000269|PubMed:19751712, ECO:0000269|PubMed:2070047, ECO:0000269|PubMed:21206266, ECO:0000269|PubMed:21372693, ECO:0000269|PubMed:26761581, ECO:0000269|PubMed:7974346, ECO:0000269|PubMed:7981691, ECO:0000269|PubMed:8043443, ECO:0000269|PubMed:8204879, ECO:0000269|PubMed:8242057, ECO:0000269|PubMed:8364544, ECO:0000269|PubMed:8652821, ECO:0000269|PubMed:8844208, ECO:0000269|PubMed:8883260, ECO:0000269|PubMed:8940045, ECO:0000269|PubMed:9414278, ECO:0000269|PubMed:9452082, ECO:0000269|PubMed:9576180}. Note=The disease is caused by variants affecting the gene represented in this entry.

Pharmaceutical: Available under the names Niastase or Novoseven (Novo Nordisk). Used for the treatment of bleeding episodes in hemophilia A or B patients with antibodies to coagulation factors VIII or IX.

Similarity: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE- ProRule:PRU00274}.

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:		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.


Catalytic activity:		Reaction=Selective cleavage of Arg-\|-Ile bond in factor X to form factor Xa.; EC=3.4.21.21;
Subunit:		Heterodimer of a light chain and a heavy chain linked by a disulfide bond. {ECO:0000269\|PubMed:8598903, ECO:0000269\|PubMed:9925787}.
Subcellular location:		Secreted.
Tissue specificity:		Plasma.
Ptm:		The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.
Ptm:		The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269\|PubMed:3264725}.
Ptm:		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. {ECO:0000269\|PubMed:1904059, ECO:0000269\|PubMed:19167329, ECO:0000269\|PubMed:21949356, ECO:0000269\|PubMed:3264725, ECO:0000269\|PubMed:9023546}.
Ptm:		Can be either O-glucosylated or O-xylosylated at Ser-112 by POGLUT1 in vitro.
Disease:		Factor VII deficiency (FA7D) [MIM:227500]: 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. {ECO:0000269\|PubMed:10862079, ECO:0000269\|PubMed:11091194, ECO:0000269\|PubMed:11129332, ECO:0000269\|PubMed:12472587, ECO:0000269\|PubMed:14717781, ECO:0000269\|PubMed:1634227, ECO:0000269\|PubMed:18976247, ECO:0000269\|PubMed:19432927, ECO:0000269\|PubMed:19751712, ECO:0000269\|PubMed:2070047, ECO:0000269\|PubMed:21206266, ECO:0000269\|PubMed:21372693, ECO:0000269\|PubMed:26761581, ECO:0000269\|PubMed:7974346, ECO:0000269\|PubMed:7981691, ECO:0000269\|PubMed:8043443, ECO:0000269\|PubMed:8204879, ECO:0000269\|PubMed:8242057, ECO:0000269\|PubMed:8364544, ECO:0000269\|PubMed:8652821, ECO:0000269\|PubMed:8844208, ECO:0000269\|PubMed:8883260, ECO:0000269\|PubMed:8940045, ECO:0000269\|PubMed:9414278, ECO:0000269\|PubMed:9452082, ECO:0000269\|PubMed:9576180}. Note=The disease is caused by variants affecting the gene represented in this entry.
Pharmaceutical:		Available under the names Niastase or Novoseven (Novo Nordisk). Used for the treatment of bleeding episodes in hemophilia A or B patients with antibodies to coagulation factors VIII or IX.
Similarity:		Belongs to the peptidase S1 family. {ECO:0000255\|PROSITE- ProRule:PRU00274}.