| IED ID | IndEnz0002003027 |
| Enzyme Type ID | protease003027 |
| Protein Name |
Coagulation factor X EC 3.4.21.6 Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain |
| Gene Name | F10 TrFX |
| Organism | Tropidechis carinatus (Australian rough-scaled snake) |
| 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) Lepidosauria (lepidosaurs) Squamata (squamates) Bifurcata (split-tongued squamates) Unidentata Episquamata Toxicofera Serpentes (snakes) Colubroidea Elapidae Notechinae Tropidechis Tropidechis carinatus (Australian rough-scaled snake) |
| Enzyme Sequence | MAPQLLLCLILTFLWSLSEAESNVFLKSKVANRFLQRTKRANSLFEEFKAGNIERECIEERCSKEEAREAFEDNEKTETFWNVYVDGDQCSSNPCHYGGTCKDGIGSYTCTCLAGYEGKNCQYVLYQSCRVDNGNCWHFCKPVQNEIQCSCAESYLLGDDGYSCVAGGDFSCGRNIKARNKREASLPDFQTDFSDDYDAIDENNFVETPTNFSGLVPTVQSQNATLLKKSDNPSPDIRVVNGTDCKLGECPWQALLINDQGDGFCGGTILSPIYVLTAAHCINQTKYIRVVVGEIDISRKKTGRLLSVDKIYVHQKFVPSTYDYDIALIQMKTPIQFSENVVPACLPTADFANQVLMKQDFGIVSGFGRTRERGQTSNTLKVVTLPYVDRHTCMLSSNFPITQNMFCAGYNTLPQDACQGDSGGPHITAYRDTHFITGIISWGEGCAQTGKYGAYTKVSRFILWIKRIMRLKLPSTESSTGRL |
| Enzyme Length | 483 |
| Uniprot Accession Number | Q4QXT9 |
| Absorption | |
| Active Site | ACT_SITE 280; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 325; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 422; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250}. |
| 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. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (4); Disulfide bond (12); Domain (4); Glycosylation (5); Modified residue (12); Propeptide (2); Signal peptide (1) |
| Keywords | Calcium;Cleavage on pair of basic residues;Disulfide bond;EGF-like domain;Gamma-carboxyglutamic acid;Glycoprotein;Hemostasis;Hydrolase;Hydroxylation;Protease;Prothrombin activator;Repeat;Secreted;Serine protease;Signal;Toxin;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| 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 75; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 103; /note=(3R)-3-hydroxyaspartate; /evidence=ECO:0000250 |
| Post Translational Modification | PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium.; PTM: The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway). {ECO:0000250}.; 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 | 53,901 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |