| IED ID | IndEnz0002009854 |
| Enzyme Type ID | protease009854 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like halysase EC 3.4.24.- Snake venom metalloproteinase SVMP Vascular apoptosis-inducing protein VAP |
| Gene Name | |
| Organism | Gloydius halys (Chinese water mocassin) (Agkistrodon halys) |
| 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) Gloydius Gloydius halys (Chinese water mocassin) (Agkistrodon halys) |
| Enzyme Sequence | MIQVLLVTICLAVFPYQGSSIILESGNVNDYEVVYPRKVPALPKGAVQPKYEDAMQYEFKVNGEPVVLHLEKNKGLFSEDYSETHYSPDGREITTNPPVEDHCYYHGRIQNDADSTASISACNGLKGHFTLQGETYLIEPLKLPDSEAHAVFKYENVEKEDEAPKMCGVTQNWESYEPIKKASQSNLTPEQQRYLNAKKYVKLVMVADYIMYLKYDRNLTTVRTRMYDIVNVINVIYQRMNIHVALVGLEIWSNKDKFILRSAADVTLKLFATWRETDLLKRKSHDNAQLLTGINFNGPTAGLGYLGGICNPMYSAGIVQDHNKIHHLVAIAMAHEMGHNLGIDHDKDTCTCGAKSCVMAGTLSCEASYLFSDCSRKEHQAFLIKDMPQCILKKPLKTDVVSPPVCGNYFVEVGEDCDCGSPATCRDSCCDAATCKLRQGAQCAEGLCCDQCRFKGAGTECRAATDECDMADLCTGRSAECTDRFQRNGQPCQNNNGYCYNGKCPIMTDQCIALFGPNAAVSEDACFQFNLEGNHYGYCRKEQNTKIACEPQNVKCGRLYCIDSSPANKNPCNIYYSPGDEDKGMVLPGTKCADGKACSNGQCVDVNRAS |
| Enzyme Length | 610 |
| Uniprot Accession Number | Q8AWI5 |
| Absorption | |
| Active Site | ACT_SITE 336; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA and EGTA. Not inhibited by PMSF, antipain, pepstatin, and iodoacetamide. {ECO:0000269|PubMed:16329990}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Strongly inhibits the collagen-induced human platelet aggregation (inhibition of alpha-2/beta-1 (ITGA2/ITGB1) integrin). Hydrolyzes the Aalpha-chain of fibrinogen, without cleavage of Bbeta- and gamma-chains. Degrades type IV collagen (but not types I, II and V), fibronectin and vitronectin and also integrins alpha-1/beta-1 (ITGA1/ITGB1) and alpha-5/beta/1 (ITGA5/ITGB1) (but not alpha-V/beta-3 (ITGAV/ITGB3) and alpha-V/beta-5 (ITGAV/ITGB5) integrins). Both metalloproteinase (peptidase M12B) and disintegrin-like domains (recombinantly expressed and named halydin) play characteristic roles to inhibit human platelet aggregation. Induces apoptosis and strongly inhibits proliferation of endothelial cells as well as adhesion of the cells to extracellular matrix proteins. The apoptosis is closely associated with activation of caspase-3 and decreased level of Bcl-X(L)/Bax. Apohalysase, which lacks metalloprotease activity, is also able to induce the apoptosis. Cleaves insulin B chain at '34-His-|-Leu-35', '37-Glu-|-Ala-38', '38-Ala-|-Leu-39', '39-Leu-|-Tyr-40', '40-Tyr-|-Leu-41', '47-Gly-|-Phe-48' and '48-Phe-|-Phe-49' bonds (PubMed:16329990). {ECO:0000269|PubMed:12963038, ECO:0000269|PubMed:14688240, ECO:0000269|PubMed:16329990}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (17); Domain (2); Glycosylation (1); Metal binding (9); Motif (1); Propeptide (1); Signal peptide (1) |
| Keywords | Apoptosis;Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Secreted;Signal;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 467..469; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 67,652 |
| Kinetics | |
| Metal Binding | METAL 335; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 339; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 345; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 405; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 408; /note=Calcium; /evidence=ECO:0000250; METAL 410; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 412; /note=Calcium; /evidence=ECO:0000250; METAL 415; /note=Calcium; /evidence=ECO:0000250; METAL 418; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |