| IED ID | IndEnz0002013393 |
| Enzyme Type ID | protease013393 |
| Protein Name |
Prothrombin EC 3.4.21.5 Coagulation factor II Cleaved into: Activation peptide fragment 1; Activation peptide fragment 2; Thrombin light chain; Thrombin heavy chain |
| Gene Name | F2 |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MLHVRGLGLPGCLALAALASLVHSQHVFLAPQQALSLLQRVRRANSGFLEELRKGNLERECVEEQCSYEEAFEALESPQDTDVFWAKYTVCDSVRKPRETFMDCLEGRCAMDLGLNYHGNVSVTHTGIECQLWRSRYPHRPDINSTTHPGADLKENFCRNPDSSTSGPWCYTTDPTVRREECSIPVCGQEGRTTVKMTPRSRGSKENLSPPLGECLLERGRLYQGNLAVTTLGSPCLAWDSLPTKTLSKYQNFDPEVKLVQNFCRNPDRDEEGAWCFVAQQPGFEYCSLNYCDEAVGEENHDGDESIAGRTTDAEFHTFFDERTFGLGEADCGLRPLFEKKSLTDKTEKELLDSYIDGRIVEGWDAEKGIAPWQVMLFRKSPQELLCGASLISDRWVLTAAHCILYPPWDKNFTENDLLVRIGKHSRTRYERNVEKISMLEKIYIHPRYNWRENLDRDIALLKLKKPVPFSDYIHPVCLPDKQTVTSLLQAGYKGRVTGWGNLRETWTTNINEIQPSVLQVVNLPIVERPVCKASTRIRITDNMFCAGFKVNDTKRGDACEGDSGGPFVMKSPYNHRWYQMGIVSWGEGCDRNGKYGFYTHVFRLKRWMQKVIDQHR |
| Enzyme Length | 617 |
| Uniprot Accession Number | P18292 |
| Absorption | |
| Active Site | ACT_SITE 402; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 458; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 564; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.; EC=3.4.21.5; |
| DNA Binding | |
| EC Number | 3.4.21.5 |
| Enzyme Function | FUNCTION: Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (3); Disulfide bond (12); Domain (4); Glycosylation (4); Modified residue (10); Peptide (2); Propeptide (1); Region (1); Signal peptide (1); Site (3) |
| Keywords | Acute phase;Blood coagulation;Calcium;Cleavage on pair of basic residues;Disulfide bond;Gamma-carboxyglutamic acid;Glycoprotein;Hemostasis;Hydrolase;Kringle;Protease;Reference proteome;Repeat;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 50; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00735, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 51; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00735, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 58; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00735, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 60; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00735, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 63; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00735, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 64; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00735, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 69; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00735, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 70; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00735, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 73; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00735, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 76; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00735, ECO:0000255|PROSITE-ProRule:PRU00463" |
| Post Translational Modification | PTM: The gamma-carboxyglutamyl residues, which bind calcium ions, result from the carboxylation of glutamyl residues by a microsomal enzyme, the vitamin K-dependent carboxylase. The modified residues are necessary for the calcium-dependent interaction with a negatively charged phospholipid surface, which is essential for the conversion of prothrombin to thrombin (By similarity). {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10048754; 11186232; 12165407; 12383911; 12479881; 14753426; 15975137; 16046705; 16078333; 16344894; 16981243; 17293494; 18083763; 18336749; 18474218; 18541230; 18622025; 18636965; 18667434; 19103257; 19383433; 19705256; 19719823; 20150433; 20519137; 20541575; 20664909; 20705928; 20806126; 20819545; 20926146; 20979870; 21191574; 21209875; 21232185; 21396682; 21550061; 21736902; 21897338; 22015349; 22227956; 22229668; 22402172; 22473220; 22804886; 22915765; 23103417; 23338707; 23481505; 23535565; 23628972; 23737601; 24916589; 25396762; 28059686; 28489922; |
| Motif | |
| Gene Encoded By | |
| Mass | 70,412 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |