| IED ID | IndEnz0002009201 |
| Enzyme Type ID | protease009201 |
| Protein Name |
Thrombin EC 3.4.21.5 Cleaved into: Thrombin light chain; Thrombin heavy chain Fragments |
| Gene Name | |
| Organism | Salmo salar (Atlantic salmon) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Actinopterygii Actinopteri Neopterygii Teleostei Osteoglossocephalai Clupeocephala Euteleosteomorpha Protacanthopterygii Salmoniformes (salmons and trouts) Salmonidae (salmonids) Salmoninae (trouts salmons & chars) Salmo Salmo salar (Atlantic salmon) |
| Enzyme Sequence | SFGSGELVXGEXPXFEKIIVKGIDAEVASAPMQVML |
| Enzyme Length | 36 |
| Uniprot Accession Number | P84122 |
| Absorption | |
| Active Site | |
| 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; Evidence={ECO:0000269|PubMed:15236909}; |
| 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 (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (2); Domain (1); Non-adjacent residues (1); Non-terminal residue (1) |
| Keywords | Blood coagulation;Calcium;Direct protein sequencing;Gamma-carboxyglutamic acid;Glycoprotein;Hemostasis;Hydrolase;Protease;Reference proteome;Secreted;Serine protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15236909}. |
| Modified Residue | |
| 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. {ECO:0000305}.; PTM: N-glycosylated. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 3,784 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |