| IED ID | IndEnz0002005419 |
| Enzyme Type ID | protease005419 |
| Protein Name |
Coagulation factor X EC 3.4.21.6 Stuart factor Virus-activating protease VAP Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain |
| Gene Name | F10 FX |
| Organism | Gallus gallus (Chicken) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Archelosauria Archosauria Dinosauria Saurischia Theropoda Coelurosauria Aves Neognathae Galloanserae Galliformes Phasianidae (turkeys) Phasianinae Gallus Gallus gallus (Chicken) |
| Enzyme Sequence | MAGRLLLLLLCAALPDELRAEGGVFIKKESADKFLERTKRANSFLEEMKQGNIERECNEERCSKEEAREAFEDNEKTEEFWNIYVDGDQCSSNPCHYGGQCKDGLGSYTCSCLDGYQGKNCEFVIPKYCKINNGDCEQFCSIKKSVQKDVVCSCTSGYELAEDGKQCVSKVKYPCGKVLMKRIKRSVILPTNSNTNATSDQDVPSTNGSILEEVFTTTTESPTPPPRNGSSITDPNVDTRIVGGDECRPGECPWQAVLINEKGEEFCGGTILNEDFILTAAHCINQSKEIKVVVGEVDREKEEHSETTHTAEKIFVHSKYIAETYDNDIALIKLKEPIQFSEYVVPACLPQADFANEVLMNQKSGMVSGFGREFEAGRLSKRLKVLEVPYVDRSTCKQSTNFAITENMFCAGYETEQKDACQGDSGGPHVTRYKDTYFVTGIVSWGEGCARKGKYGVYTKLSRFLRWVRTVMRQK |
| Enzyme Length | 475 |
| Uniprot Accession Number | P25155 |
| Absorption | |
| Active Site | ACT_SITE 282; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 328; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 425; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.; EC=3.4.21.6; |
| DNA Binding | |
| EC Number | 3.4.21.6 |
| Enzyme Function | 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. VAP cleaves the fusion proteins of Sendai virus, NDV, and influenza virus a at a specific single arginine-containing site, and plays a key role in the viral spreading in the allantoic sac. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (4); Disulfide bond (12); Domain (4); Glycosylation (4); Modified residue (12); Propeptide (2); Region (1); Signal peptide (1) |
| Keywords | Blood coagulation;Calcium;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;EGF-like domain;Gamma-carboxyglutamic acid;Glycoprotein;Hemostasis;Hydrolase;Hydroxylation;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | MOD_RES 46; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 47; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 54; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 56; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 59; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 60; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 65; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 66; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 69; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 72; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 79; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 103; /note=(3R)-3-hydroxyaspartate; /evidence=ECO:0000250 |
| Post Translational Modification | PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.; 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. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 53,142 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |