| IED ID | IndEnz0002010741 |
| Enzyme Type ID | protease010741 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like ACLD EC 3.4.24.- Snake venom metalloproteinase SVMP VMP-III AclVMP-III |
| Gene Name | |
| Organism | Agkistrodon contortrix laticinctus (Broad-banded copperhead) (Agkistrodon mokasen laticinctus) |
| 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) Agkistrodon Agkistrodon contortrix (Copperhead) Agkistrodon contortrix laticinctus (Broad-banded copperhead) (Agkistrodon mokasen laticinctus) |
| Enzyme Sequence | MIQVLLVTLCLAVFPYQGSSIILESGNVNDYEVVYPRKVTVLPKGAVQPKYEDAMQYEFKVNGEPVVLHLEKNKQLFSKDYSETHYSPDGREITTYPLVEDHCYYHGRIENDADSTASISACNGLKGHFKLQGEMYLIDPLKLPDSEAHAVFKYENVEKEDEAPKMCGVTQNWESYEPIKKASQLNLTPEQQAYLDAKKYVEFVVVLDHGMYTKYKDNLDKIKTRIFEIVNTMNEMFIPLNIRVALICLEIWSDKDKFNMTSAANVTSISFRNWRATDLLKRKSHDNAQLLTVIDFDGPTIGKAYMASMCDPKRSVGIIQDHSTINLMMAVTMAHEMGHNLGMDHDEKYCTCGAKSCVMAKALSRQPSKLFSNCSQEDYRKYLIKRRPKCILNEPNGTDIVSPPVCGNELLEVGEECDCGSPTNCQNPCCDAATCKLTPGSQCADGVCCDQCRFTRAGTECRQAKDDCDMADLCTGQSAECPTDRFQRNGHPCLNDNGYCYNRTCPTLKNQCIYFFGPNAAVAKDSCFKGNQKSNNHTYCRKENGKKIPCAPQDIKCGRLYCFRNLPGKKNICSVIYTPTDEDIGMVLPGTKCEDGKVCSNGHCVDVNIAYKSTTGFSQI |
| Enzyme Length | 620 |
| Uniprot Accession Number | O42138 |
| 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 O-phenanthroline. Not inhibited by PMSF, benzamidine, irreversible serine-proteinase inhibitors and cysteine proteinase inhibitor E-64 (By similarity). {ECO:0000250}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Is a potent activator of prothrombin (F2). Does not elicit any hemorrhagic response. Barely inhibits collagen-induced platelet aggregation. Binds neither collagen, nor the jararhagin-monoclonal antibody MAJar3. Hydrolyzes the Aalpha-chain of fibrin and fibrinogen, without affecting the Bbeta- and gamma-chains. Is capable of triggering endothelial proinflammatory and procoagulant cell responses, but fails to trigger apoptosis. Induces von Willebrand factor release, and the expression of both ICAM1 and E-selectin (SELE) (without increase in VCAM1) in endothelial cells (HUVEC). Is also able to up-regulate the synthesis of the coagulation factor TF (F3). Enhances nitric oxide (NO) generation, prostacyclin production and interleukin-8 release (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (17); Domain (2); Glycosylation (6); Metal binding (13); Motif (1); Propeptide (1); Sequence conflict (5); Signal peptide (1) |
| Keywords | Blood coagulation cascade activating toxin;Calcium;Cell adhesion impairing toxin;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Prothrombin activator;Secreted;Signal;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| 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 | 69,512 |
| Kinetics | |
| Metal Binding | METAL 202; /note=Calcium 1; /evidence=ECO:0000250; METAL 286; /note=Calcium 1; /evidence=ECO:0000250; 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 390; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 393; /note=Calcium 1; /evidence=ECO:0000250; METAL 405; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 408; /note=Calcium 2; /evidence=ECO:0000250; METAL 410; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 412; /note=Calcium 2; /evidence=ECO:0000250; METAL 415; /note=Calcium 2; /evidence=ECO:0000250; METAL 418; /note=Calcium 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |