| IED ID | IndEnz0002011945 |
| Enzyme Type ID | protease011945 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like HV1 EC 3.4.24.- Snake venom metalloproteinase SVMP Vascular apoptosis-inducing protein VAP |
| Gene Name | |
| 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 | MIQVLLVTICLAVFPYQGSSIILESGNVNDYEVVYPRKVTALPKGAVQQKYEDAMQYEFTVNGEPVVLHLEKNKGLFSEDYSETHYSPDGREITTNPPVEDHCYYHGRIQNDADLTASISACDGLKGHFKLQGETYIIEPLKLPDSEAHAVFKYENVEKEDEAPKMCGVTQSNWESDESIKEDSQSNLTPAQQKYLNAKKYVKFFLVADHIMYLKYGRNLTTLRTRMFDTVNIVNQILQRINIHVALIGIEIWSKEDKIIVQSVPDVTLKLFATWRESVLLKRKNHDNAHLLTGINFNGPTAGLAYLGGICKPMYSAGIVQDHNKIHHLVAIAMAHEMGHNLGMDHDKDTCTCRAKACVMAGTLSCDASYLFSDCSRQEHRAFLIKNMPQCILKKPLKTDVVSPPVCGNYFVEVGEDCDCGSPATCRDPCCDAATCKLRQGAQCAEGLCCDQCRFKAAGTECRAATDECDMADLCTGRSAECTDRFQRNGQPCQNNNGYCYNRTCPTMNNQCIALFGPNAAVSQDACFQFNRQGNYYGYCRKEQNTKIACEPQNVKCGRLYCIDSSPAKKNPCNIIYSPNDEDKGMVLPGTKCADGMACNSNGQCVDVNRTY |
| Enzyme Length | 612 |
| Uniprot Accession Number | Q90ZI3 |
| Absorption | |
| Active Site | ACT_SITE 337; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA and EGTA. {ECO:0000269|PubMed:11389737}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc metalloproteinase-disintegrin-like that potently activates prothrombin (F2). Does not elicit any hemorrhagic response. Barely inhibits collagen-induced platelet aggregation. Hydrolyzes the alpha-chain of fibrin and fibrinogen (FGA), without affecting the Bbeta- and gamma-chains (By similarity). Induces apoptosis in cultured vascular endothelial cells. {ECO:0000250, ECO:0000269|PubMed:11389737}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (18); Domain (2); Glycosylation (3); Metal binding (14); Motif (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) |
| Keywords | Apoptosis;Blood coagulation cascade activating toxin;Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Prothrombin activator;Secreted;Signal;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11389737}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 468..470; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 68,191 |
| Kinetics | |
| Metal Binding | METAL 336; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 340; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 346; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 406; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 409; /note=Calcium 1; /evidence=ECO:0000250; METAL 411; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 413; /note=Calcium 1; /evidence=ECO:0000250; METAL 416; /note=Calcium 1; /evidence=ECO:0000250; METAL 419; /note=Calcium 1; /evidence=ECO:0000250; METAL 470; /note=Calcium 2; /evidence=ECO:0000250; METAL 471; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 473; /note=Calcium 2; /evidence=ECO:0000250; METAL 484; /note=Calcium 2; /evidence=ECO:0000250; METAL 485; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |