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UniProt functional annotation for P16293 | ||
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| UniProt code: P16293. |
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| Organism: | |
Sus scrofa (Pig). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. |
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| Function: | |
Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa. {ECO:0000250|UniProtKB:P00740}. |
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| Catalytic activity: | |
Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.; EC=3.4.21.22; Evidence={ECO:0000250|UniProtKB:P00740}; |
| Subunit: | |
Heterodimer of a light chain and a heavy chain; disulfide- linked. Interacts with SERPINC1. {ECO:0000269|PubMed:7568220}. |
| Subcellular location: | |
Secreted {ECO:0000250|UniProtKB:P00740}. |
| Domain: | |
Calcium binds to the gamma-carboxyglutamic acid (Gla) residues in the Gla domain. Calcium can also bind, with stronger affinity, to another site beyond the Gla domain. Under physiological ion concentrations, Ca(2+) is displaced by Mg(2+) from some of the gammaglutamate residues in the N-terminal Gla domain. This leads to a subtle conformation change that may affect the interaction with its binding protein. {ECO:0000250|UniProtKB:P00741}. |
| Ptm: | |
Activated by factor XIa, which excises the activation peptide. The propeptide can also be removed by snake venom protease. {ECO:0000250|UniProtKB:P00740}. |
| Ptm: | |
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250|UniProtKB:P00740}. |
| Similarity: | |
Belongs to the peptidase S1 family. {ECO:0000255|PROSITE- ProRule:PRU00274}. |
Annotations taken from UniProtKB at the EBI.