Detail Information for IndEnz0002019308
IED ID IndEnz0002019308
Enzyme Type ID protease019308
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 Cf7
Organism Mus musculus (Mouse)
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) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MVPQAHGLLLLCFLLQLQGPLGTAVFITQEEAHGVLHRQRRANSLLEELWPGSLERECNEEQCSFEEAREIFKSPERTKQFWIVYSDGDQCASNPCQNGGTCQDHLKSYVCFCLLDFEGRNCEKSKNEQLICANENGDCDQYCRDHVGTKRTCSCHEDYTLQPDEVSCKPKVEYPCGRIPVVEKRNSSSRQGRIVGGNVCPKGECPWQAVLKINGLLLCGAVLLDARWIVTAAHCFDNIRYWGNITVVMGEHDFSEKDGDEQVRRVTQVIMPDKYIRGKINHDIALLRLHRPVTFTDYVVPLCLPEKSFSENTLARIRFSRVSGWGQLLDRGATALELMSIEVPRLMTQDCLEHAKHSSNTPKITENMFCAGYMDGTKDACKGDSGGPHATHYHGTWYLTGVVSWGEGCAAIGHIGVYTRVSQYIDWLVRHMDSKLQVGVFRLPLL
Enzyme Length 446
Uniprot Accession Number P70375
Absorption
Active Site ACT_SITE 234; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 283; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 385; /note=Charge relay system; /evidence=ECO:0000250
Activity Regulation
Binding Site BINDING 379; /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); Beta strand (3); Binding site (1); Chain (2); Disulfide bond (12); Domain (4); Glycosylation (4); Helix (1); Modified residue (11); Propeptide (1); Sequence conflict (1); Signal peptide (1); Site (1)
Keywords 3D-structure;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 INDUCTION: Expression in the liver and plasma oscillates in a circadian manner. {ECO:0000269|PubMed:18316400}.
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue MOD_RES 47; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P22457, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 48; /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 57; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P22457, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 60; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P22457, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 61; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P22457, ECO:0000255|PROSITE-ProRule:PRU00463"; 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 70; /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 104; /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: Can be either O-glucosylated or O-xylosylated at Ser-93 by POGLUT1. {ECO:0000250}.
Signal Peptide SIGNAL 1..24; /evidence=ECO:0000255
Structure 3D X-ray crystallography (3)
Cross Reference PDB 5KXH; 5KY2; 5KY3;
Mapped Pubmed ID 10021455; 10749569; 11154109; 11171545; 11841337; 12466851; 15604416; 16141072; 16268461; 16524747; 17054310; 18398505; 18802482; 18973189; 19286924; 19404533; 19943873; 20454518; 20504328; 21252090; 21267068; 21325603; 21366858; 22134170; 22370814; 22950420; 23472758; 24194600; 24977291; 27614059; 27626380; 28035745; 28530709; 29321368; 30870413; 9384381; 9442072; 9759642;
Motif
Gene Encoded By
Mass 50,276
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda