| IED ID | IndEnz0002012326 |
| Enzyme Type ID | protease012326 |
| Protein Name |
Snake venom serine protease HS114 SVSP EC 3.4.21.- BjSP Thrombin-like enzyme HS114 SVTLE |
| Gene Name | |
| Organism | Bothrops jararaca (Jararaca) (Bothrops jajaraca) |
| 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) Bothrops Bothrops jararaca (Jararaca) (Bothrops jajaraca) |
| Enzyme Sequence | MVLVRVVANLLILQLSYAQKVSELVVGGDECNINEHRSLVAIFNSTGFFCSGILLNQEWVLTASHCDSTNFQMKIGVHSKKTLNQDEQTRNPKEKIFCPNKKNDDALDKDLMLVRLDSPVSDSEHIAPLSLPSSPPSVGSVCRIMGWGSITPIQKTNPDVPHCANINLLDDAVCRAAYPELPAEYRTLCAGVPEGGIDTCNGDSGGPLICNGQFQGIVFYGAHPCGQAPKPGLYTKVIDYNTWIESVIAGNTAATCPP |
| Enzyme Length | 258 |
| Uniprot Accession Number | Q5W959 |
| Absorption | |
| Active Site | ACT_SITE 65; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q7SZE1; ACT_SITE 110; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q7SZE1; ACT_SITE 204; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q7SZE1 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by benzamidine, PMSF, leupeptin, SDS and DTT, but not by EDTA, and commercial antivenom. {ECO:0000269|PubMed:30145175}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Snake venom serine protease that shows non-specific action on fibrinogen (PubMed:30145175). It preferentially degrades fibrinogen Aalpha (FGA), releasing fibrinopeptide A, and shows a lower activity on fibrinogen Bbeta (FGB), releasing fibrinopeptide B and other uncommon fibrinopeptides (PubMed:30145175). Also shows low fibrinolytic activity compared to plasmin (PubMed:30145175). Has high enzymatic activity on the substrates for activated protein C and factor XIa, and for thrombin (PubMed:30145175). Shows a wide activity spectrum at different peptide sequences, with a preferential cleavage at Lys-|-Xaa over Arg-|-Xaa bonds (PubMed:30145175). {ECO:0000269|PubMed:30145175}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:30145175}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:30145175}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (1); Propeptide (1); Signal peptide (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Signal;Toxin;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30145175}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. Contains approximately 10% carbohydrates. {ECO:0000269|PubMed:30145175}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 27,843 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |