| IED ID | IndEnz0002013360 |
| Enzyme Type ID | protease013360 |
| Protein Name |
Thrombin-like enzyme gyroxin B1.7 SVTLE gyroxin B1.7 EC 3.4.21.- Fibrinogen-clotting enzyme Snake venom serine protease SVSP |
| Gene Name | |
| Organism | Crotalus durissus terrificus (South American rattlesnake) |
| 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) Crotalus Crotalus durissus (tropical rattlesnake) Crotalus durissus terrificus (South American rattlesnake) |
| Enzyme Sequence | MVLIRVLANLLILQLSYAQKSSELVIGGDECNINEHRLLAIVYTNSSQCAGTLINQEWVLTAAHCDGENMDIYLGVHNESVQYDDEEGRVAAEKFFCLSSRNYTKWDKDIMLIRLNIPVRNSTHIAPLSLPSSPPSVGSVCRVMGWGTITSPNETYPDVPHCANINLFDYEVCLAAYPEFGLPATSRTLCAGIQQGGKDTCGSDSGGSLICNGQFQGIVSWGDNPCAQPHKPALYTKVLDDTEWIQSIIAGNTAVTCPP |
| Enzyme Length | 259 |
| Uniprot Accession Number | B0FXM3 |
| Absorption | |
| Active Site | ACT_SITE 64; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 109; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 205; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Thrombin-like snake venom serine protease. Displays a specificity similar to trypsin. Releases only fibrinopeptide A in the conversion of fibrinogen to fibrin. Shows coagulant, esterase and amidase activities (By similarity). Reversibly increases the permeability of the blood brain barrier (BBB) in mice. Induces the barrel rotation syndrome in mice, which is manifested by gyroxin-like, rapid rolling motions. This syndrome may be due to its effect on BBB permeability, and certainly also to other actions affecting endogenous substrates present in the endothelium, nervous tissues or blood. {ECO:0000250, ECO:0000269|PubMed:11137545, ECO:0000269|PubMed:20637222}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (1); Propeptide (1); Signal peptide (1) |
| Keywords | Blood coagulation cascade activating toxin;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Signal;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 28,184 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |