| IED ID | IndEnz0002005396 |
| Enzyme Type ID | protease005396 |
| 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 | Pan paniscus (Pygmy chimpanzee) (Bonobo) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Pan (chimpanzees) Pan paniscus (Pygmy chimpanzee) (Bonobo) |
| Enzyme Sequence | MVSQALRLLCLLLGLQGCLAAGGVAEASGGETRDMPWKPGPHRVFITQEEAHGVLHRRRRANAFLEELRPGSLERECKEEQCSFEEAREIFKDLERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETYKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILENRNASKPQGRIVGGKVCPKGECPWQXLLXVNGAQLCGGTLINTIWVASAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYIPGTTNHDIALLRLHQPVVLTDHVVPLCLPERAFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCASVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP |
| Enzyme Length | 466 |
| Uniprot Accession Number | Q2F9P4 |
| Absorption | |
| Active Site | ACT_SITE 253; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 302; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 404; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 398; /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 (5); Modified residue (11); Propeptide (1); Signal peptide (1); Site (2) |
| 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 66; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P22457, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 67; /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 76; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P22457, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 79; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P22457, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 80; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P22457, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 85; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P22457, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 86; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P22457, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 89; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P22457, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 95; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P22457, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 123; /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-112 by POGLUT1. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 51,615 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |