| IED ID | IndEnz0002012328 |
| Enzyme Type ID | protease012328 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like berythractivase EC 3.4.24.- Snake venom metalloproteinase SVMP ery1 |
| Gene Name | |
| Organism | Bothrops erythromelas (Caatinga lance head) |
| 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 neuwiedi group Bothrops erythromelas (Caatinga lance head) |
| Enzyme Sequence | MIQVLLVIICLEAFPYQGSSIILESGNVNDYEVVYPRKVTALSKGAVHPKYEDAMQYEFKVNGEPVVLHLEKNKGLFSEDYSEIHYSPDGREITTYPLVEDHCYYHGRIQNDADSSASISACNGLKGHFKLQGEMYLIEPFKLPDSEAHAVFKYENVEKEDEAPKMCGVTETNWESDEPIKKASLLNLTPEQQAYLDAKKYVEFVVVLDHGMYKKYKDDLDKIKRRIYEIVNTMNEMFIPLNICVALTGLEIWSKGDKINVTSESWFTLILFTNWRGADLLKRKSHDNAQLLTNTDFDGSTIGRAHIGSMCHPYLSVGIIQDYSPVNLLVASTMAHEMGHNLGMHHDNDTCTCGAPSCVMAAAISKDPSKLFSNCSQEYQRKYLIKNRPQCLLNKPLRTDIISPPVCGNELLEVGEECDCGTPENCRDPCCNATTCKLTPGSQCVEGLCCDQCRFRKTGTECRAAKHDCDLPESCTGQSADCPMDDFQRNGHPCQNNNGYCYNGKCPTMENQCIDLVGPKATVAEDSCFKDNQKGNDYGYCRKENGKKIPCEPQDVKCGRLYCNDNSPGQNNPCKCIYFPRNEDRGMVLPGTKCADGKVCSNRHCVDVATAY |
| Enzyme Length | 612 |
| Uniprot Accession Number | Q8UVG0 |
| 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 o-phenanthroline. Not inhibited by PMSF, benzamidine, irreversible serine-proteinase inhibitors and cysteine proteinase inhibitor E-64. {ECO:0000269|PubMed:12225292}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: 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. {ECO:0000269|PubMed:15899699, ECO:0000269|PubMed:16626772, ECO:0000269|PubMed:18096518}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-9.0. {ECO:0000269|PubMed:12225292}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (17); Domain (2); Glycosylation (4); Metal binding (17); Motif (1); Propeptide (1); Signal peptide (1) |
| Keywords | Blood coagulation cascade activating toxin;Calcium;Direct protein sequencing;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. |
| Modified Residue | |
| Post Translational Modification | PTM: Highly glycosylated. {ECO:0000305}. |
| 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 | 68,532 |
| Kinetics | |
| Metal Binding | METAL 203; /note=Calcium 1; /evidence=ECO:0000250; METAL 287; /note=Calcium 1; /evidence=ECO:0000250; 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 391; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 394; /note=Calcium 1; /evidence=ECO:0000250; METAL 406; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 409; /note=Calcium 2; /evidence=ECO:0000250; METAL 411; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 413; /note=Calcium 2; /evidence=ECO:0000250; METAL 416; /note=Calcium 2; /evidence=ECO:0000250; METAL 419; /note=Calcium 2; /evidence=ECO:0000250; METAL 470; /note=Calcium 3; /evidence=ECO:0000250; METAL 471; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 473; /note=Calcium 3; /evidence=ECO:0000250; METAL 485; /note=Calcium 3; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |