| IED ID | IndEnz0002006930 |
| Enzyme Type ID | protease006930 |
| 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 | Oryctolagus cuniculus (Rabbit) |
| 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 Euarchontoglires Glires (Rodents and rabbits) Lagomorpha Leporidae (rabbits and hares) Oryctolagus Oryctolagus cuniculus (Rabbit) |
| Enzyme Sequence | MANPLHLVLLGAALAGLLLSGSSVFISRRAANDVLARTRRANSFLEELKKGNLERECMEENCSYEEALEVFEDREKTNEFWNKYVDGDQCESNPCQNQGTCKDGLGMYTCSCVEGYEGQDCEPVTRKLCSLDNGGCDQFCKEEENSVLCSCASGYTLGDNGKSCISTELFPCGKVTLGRWRRSPATNSSEGPPEAPGPEQQDDGNLTATENPFNLLDSPEPPPEDDSSSLVRIVGGQDCRDGECPWQALLVNEENEGFCGGTILSEYHVLTAAHCLHQAKRFKVRVGDRDTEHEEGNEETHEVEVVVKHNRFVKETYDFDIAVLRLKTPITFRRNVAPACLPQKDWAESTLMAQKTGIVSGFGRTHEMGRLSTTLKMLEVPYVDRNSCKRSSSFTITQNMFCAGYDARPEDACQGDSGGPHVTRFRDTYFVTGIVSWGEGCARKGKFGVYTKVSNFLKWIEKSMRARAVPVAEAAGTPGPTQPTIKGSPS |
| Enzyme Length | 490 |
| Uniprot Accession Number | O19045 |
| Absorption | |
| Active Site | ACT_SITE 274; /note=Charge relay system; ACT_SITE 320; /note=Charge relay system; ACT_SITE 417; /note=Charge relay system |
| 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); Chain (4); Disulfide bond (12); Domain (4); Glycosylation (3); Modified residue (13); Propeptide (2); Region (1); Signal peptide (1) |
| Keywords | Blood coagulation;Calcium;Cleavage on pair of basic residues;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 {ECO:0000250}. |
| Modified Residue | MOD_RES 46; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00743, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 47; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00743, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 54; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00743, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 56; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00743, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 59; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00743, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 60; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00743, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 65; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00743, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 66; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00743, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 69; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00743, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 72; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00743, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 75; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00743, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 79; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00743, 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. {ECO:0000250}.; PTM: N- and O-glycosylated. {ECO:0000250}.; 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) (By similarity). {ECO:0000250|UniProtKB:P00742, ECO:0000250|UniProtKB:P00743}.; 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 | 53,965 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |