| IED ID | IndEnz0002012036 |
| Enzyme Type ID | protease012036 |
| Protein Name |
Venom serine protease Bi-VSP EC 3.4.21.- Thrombin-like enzyme |
| Gene Name | |
| Organism | Bombus ignitus (Bumblebee) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Hymenoptera Apocrita (wasps ants and bees) Aculeata Apoidea (bees) Apidae (bumble bees and honey bees) Apinae (honey bees) Bombini Bombus (bumble bees) Bombus Bombus ignitus (Bumblebee) |
| Enzyme Sequence | MTGSKMLFACLALIAFLHPLVHVASAQECTTPNNKAGKCLGIRVCKPLLEMLQTQGHAAADFLRQSVCKYENNNPIVCCPNEESREDRGILVGNEYEPLRPPHCGFSNVSHTRVVGGKPAVLGAWPWIAALGFRYPRNPALEPLWKCGGSLISSRHVLTAAHCAEINELYVVRIGDLNLVRNDDGAHPVQIEIESKIIHPDYISGVTKHDIAILKLVEEVPFSEYVYPICLPVEDNLRNNNFERYYPFVAGWGSLAHHGPGSDDLMEVQVPVISNTECKNSYARFAAAHVTDTVLCAGYTQGGKDACQGDSGGPLMLPKKFTFYQIGVVSYGHKCAAAGYPGVYTRVTSYLDDFILPAMQ |
| Enzyme Length | 360 |
| Uniprot Accession Number | B5U2W0 |
| Absorption | |
| Active Site | ACT_SITE 162; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 210; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 311; /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: Multifunctional venom serine protease. In insects, it acts as an arthropod prophenoloxidase-activating factor, thereby triggering the phenoloxidase cascade. When injected into larvae, it induces a lethal melanization response in target insects by modulating the innate immune response. In mammals, it converts fibrinogen into fibrin, activates prothrombin, and also degrades fibrin. In mammal, it may act in a cooperative manner with the serine protease inhibitor Bi-KTI (AC G3LH89) to promote the spread of bee venom under anti-bleeding conditions. {ECO:0000269|PubMed:20454652, ECO:0000269|PubMed:22359676}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (7); Domain (2); Glycosylation (1); Metal binding (4); Propeptide (1); Signal peptide (1) |
| Keywords | Blood coagulation cascade activating toxin;Calcium;Direct protein sequencing;Disulfide bond;Fibrinolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Protease;Prothrombin activator;Secreted;Serine protease;Signal;Toxin;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 39,461 |
| Kinetics | |
| Metal Binding | METAL 176; /note=Calcium; /evidence=ECO:0000250|UniProtKB:O97366; METAL 178; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:O97366; METAL 181; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:O97366; METAL 184; /note=Calcium; /evidence=ECO:0000250|UniProtKB:O97366 |
| Rhea ID | |
| Cross Reference Brenda |