| IED ID | IndEnz0002005418 |
| Enzyme Type ID | protease005418 |
| Protein Name |
Coagulation factor X EC 3.4.21.6 Stuart factor Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain |
| Gene Name | F10 |
| Organism | Bos taurus (Bovine) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine) |
| Enzyme Sequence | MAGLLHLVLLSTALGGLLRPAGSVFLPRDQAHRVLQRARRANSFLEEVKQGNLERECLEEACSLEEAREVFEDAEQTDEFWSKYKDGDQCEGHPCLNQGHCKDGIGDYTCTCAEGFEGKNCEFSTREICSLDNGGCDQFCREERSEVRCSCAHGYVLGDDSKSCVSTERFPCGKFTQGRSRRWAIHTSEDALDASELEHYDPADLSPTESSLDLLGLNRTEPSAGEDGSQVVRIVGGRDCAEGECPWQALLVNEENEGFCGGTILNEFYVLTAAHCLHQAKRFTVRVGDRNTEQEEGNEMAHEVEMTVKHSRFVKETYDFDIAVLRLKTPIRFRRNVAPACLPEKDWAEATLMTQKTGIVSGFGRTHEKGRLSSTLKMLEVPYVDRSTCKLSSSFTITPNMFCAGYDTQPEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKFGVYTKVSNFLKWIDKIMKARAGAAGSRGHSEAPATWTVPPPLPL |
| Enzyme Length | 492 |
| Uniprot Accession Number | P00743 |
| Absorption | |
| Active Site | ACT_SITE 275; /note=Charge relay system; /evidence=ECO:0000269|PubMed:4264286; ACT_SITE 321; /note=Charge relay system; /evidence=ECO:0000269|PubMed:4264286; ACT_SITE 418; /note=Charge relay system; /evidence=ECO:0000269|PubMed:4264286 |
| 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. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (25); Chain (4); Disulfide bond (12); Domain (4); Glycosylation (3); Helix (8); Modified residue (14); Propeptide (3); Region (1); Sequence conflict (7); Signal peptide (1); Site (1); Turn (5) |
| Keywords | 3D-structure;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;Sulfation;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | MOD_RES 46; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6766735"; MOD_RES 47; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6766735"; MOD_RES 54; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6766735"; MOD_RES 56; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6766735"; MOD_RES 59; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6766735"; MOD_RES 60; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6766735"; MOD_RES 65; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6766735"; MOD_RES 66; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6766735"; MOD_RES 69; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6766735"; MOD_RES 72; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6766735"; MOD_RES 75; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6766735"; MOD_RES 79; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6766735"; MOD_RES 103; /note="(3R)-3-hydroxyaspartate"; /evidence="ECO:0000269|PubMed:6688526"; MOD_RES 200; /note="Sulfotyrosine"; /evidence="ECO:0000269|PubMed:3949800" |
| Post Translational Modification | PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.; PTM: N- and O-glycosylated. {ECO:0000269|PubMed:1059093, ECO:0000269|PubMed:8243461}.; PTM: Proteolytically cleaved and activated by cathepsin CTSG (By similarity). The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway) (PubMed:1059122). {ECO:0000250|UniProtKB:P00742, ECO:0000269|PubMed:1059122}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269|PubMed:6688526}. |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | NMR spectroscopy (4); X-ray crystallography (2) |
| Cross Reference PDB | 1APO; 1CCF; 1IOD; 1KIG; 1WHE; 1WHF; |
| Mapped Pubmed ID | 11404471; 18045667; 18296445; 25572019; 28782177; 34831181; 9761680; |
| Motif | |
| Gene Encoded By | |
| Mass | 54,510 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |