| IED ID | IndEnz0002011110 |
| Enzyme Type ID | protease011110 |
| Protein Name |
Thrombin-like enzyme flavoxobin SVTLE EC 3.4.21.74 Fibrinogen-clotting enzyme Habutobin Snake venom serine protease 1 SVSP |
| Gene Name | TLF1 |
| Organism | Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Lepidosauria (lepidosaurs) Squamata (squamates) Bifurcata (split-tongued squamates) Unidentata Episquamata Toxicofera Serpentes (snakes) Colubroidea Viperidae Crotalinae (pit vipers) Protobothrops Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis) |
| Enzyme Sequence | MVLIRVLANLLILQLSYAQKSSELVIGGDECNINEHPFLVALYDAWSGRFLCGGTLINPEWVLTAAHCDSKNFKMKLGAHSKKVLNEDEQIRNPKEKFICPNKKNDEVLDKDIMLIKLDSPVSYSEHIAPLSLPSSPPSVGSVCRIMGWGSITPVEETFPDVPHCANINLLDDVECKPGYPELLPEYRTLCAGVLQGGIDTCGFDSGTPLICNGQFQGIVSYGGHPCGQSRKPGIYTKVFDYNAWIQSIIAGNTAATCLP |
| Enzyme Length | 260 |
| Uniprot Accession Number | P05620 |
| Absorption | |
| Active Site | ACT_SITE 67; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 112; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 206; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by alpha(2)-macroglobulin, diisopropylfluorophosphate (DFP) and PMSF. Low inhibition by tosyl-L-lysine chloromethyl ketone. {ECO:0000269|PubMed:3910643, ECO:0000269|PubMed:8875777}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Xaa bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme.; EC=3.4.21.74; |
| DNA Binding | |
| EC Number | 3.4.21.74 |
| Enzyme Function | FUNCTION: Thrombin-like snake venom serine protease that clots fibrinogen (FGA) by releasing fibrinopeptide A. According to PubMed:8585090, only cleaves rabbit fibrinogen, whereas no specificity is described in PubMed:3910643 (tests done on bovine fibrinogen). Also acts as a C3 convertase that independently cleaves human C3 and kick-starts the complement cascade. Also increases urokinase-type plasminogen activator (PLAU) and plasminogen activator inhibitor (SERPINE1) in cultured bovine pulmonary artery endothelial cells. Dose-dependently inhibits collagen-induced platelet aggregation. {ECO:0000269|PubMed:10708795, ECO:0000269|PubMed:12225369, ECO:0000269|PubMed:3910643, ECO:0000269|PubMed:8585090, ECO:0000269|PubMed:8817813, ECO:0000269|PubMed:9241744}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Domain (1); Propeptide (1); Sequence conflict (8); Signal peptide (1) |
| Keywords | Blood coagulation cascade activating toxin;Complement system impairing toxin;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Hydrolase;Platelet aggregation inhibiting toxin;Protease;Secreted;Serine protease;Signal;Toxin;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 28,398 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |