| IED ID | IndEnz0002005398 |
| Enzyme Type ID | protease005398 |
| Protein Name |
Coagulation factor VII EC 3.4.21.21 Serum prothrombin conversion accelerator Cleaved into: Factor VII light chain; Factor VII heavy chain |
| Gene Name | F7 |
| 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 | MAPQARGLGLCSLLALQASLAAVFITQEEAHSVLRRQRRANSFLEELRPGSLERECKEELCSFEEAREVFQSTERTKQFWITYNDGDQCASNPCQNGGSCEDQIQSYICFCLADFEGRNCEKNKNDQLICMYENGGCEQYCSDHVGSQRSCRCHEGYTLLPNGVSCTPTVDYPCGKVPALEKRGASNPQGRIVGGKVCPKGECPWQAALMNGSTLLCGGSLLDTHWVVSAAHCFDKLSSLRNLTIVLGEHDLSEHEGDEQVRHVAQLIMPDKYVPGKTDHDIALLRLLQPAALTNNVVPLCLPERNFSESTLATIRFSRVSGWGQLLYRGALARELMAIDVPRLMTQDCVEQSEHKPGSPEVTGNMFCAGYLDGSKDACKGDSGGPHATSYHGTWYLTGVVSWGEGCAAVGHVGVYTRVSRYTEWLSRLMRSKLHHGIQRHPFP |
| Enzyme Length | 444 |
| Uniprot Accession Number | P98139 |
| Absorption | |
| Active Site | ACT_SITE 232; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 281; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 383; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 377; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.; EC=3.4.21.21; |
| DNA Binding | |
| EC Number | 3.4.21.21 |
| Enzyme Function | FUNCTION: Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (1); Chain (2); Disulfide bond (12); Domain (4); Glycosylation (6); Modified residue (11); Propeptide (1); Signal peptide (1); Site (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 45; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P22457, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 46; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P22457, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 53; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P22457, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 55; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P22457, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 58; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P22457, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 59; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P22457, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 64; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P22457, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 65; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P22457, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 68; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P22457, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 74; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P22457, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 102; /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: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.; PTM: O-glycosylated. O-fucosylated by POFUT1 on a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. {ECO:0000250}.; PTM: Can be either O-glucosylated or O-xylosylated at Ser-91 by POGLUT1. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 49,011 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |