| IED ID | IndEnz0002011049 |
| Enzyme Type ID | protease011049 |
| Protein Name |
Zinc metalloproteinase-disintegrin BlatH1 EC 3.4.24.- Snake venom metalloproteinase SVMP |
| Gene Name | |
| Organism | Bothriechis lateralis (Side-striped palm pitviper) |
| 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) Bothriechis Bothriechis lateralis (Side-striped palm pitviper) |
| Enzyme Sequence | MIQVLLVTICLAALPYQGSSIILESGNVNDYEVVYPRKVTALPKGAGQPKYEDAMQYEFKVNGEPVVLHLEKNKGLFSKDYSETHYSSDGRKITTNPPVEDHCYYHGRIENDADSTGSISACNGLKGHFKLQGEMYLIEPLKLSDSEAHAIYKYENVEKEDEAPKMCGVTETNWESYEPIKKASQSNLTPEQQRFNPFKYVELVIVADHRMFTKYNGDLEKIRIKIYEIVNILNEMFRYLYIRIALVDLEIWSNRDLINVTSVAGDTLDSFGNWRETDLLKRKSHDNAQLLTGIDFNGTTIGIAYIASMCNPYLSVGIVQDHSEINFLIAVTMAHEMGHNLGMRHDTDYCTCGGYSCIMCAVLSDQPSKFFSNCSYIQYGKFIMNQNSQCILNEPLGTDIVSPPVCGNEILEVGEECDCGCPTNCQDPCCNAATCKQYSWVQCESGECCEQCRFRAAGTVCRRATDNDMDNRCTGQSADCPSNG |
| Enzyme Length | 484 |
| Uniprot Accession Number | U5PZ28 |
| Absorption | |
| Active Site | ACT_SITE 336; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Platelet aggregation in inhibited by the metalloproteinase inhibitors EDTA and Batimastat. The hemorrhagic activity is not inhibited by the plasma proteinase inhibitor alpha2-macroglobulin, although the SVMP is able to cleave this plasma inhibitor, generating a 90 kDa product. {ECO:0000269|PubMed:24457155}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc metalloprotease-disintegrin that hydrolyzes azocasein, gelatin and fibrinogen (Aalpha and Bbeta chains and partially gamma-chain), and exerts a potent local and systemic hemorrhagic activity in mice. It inhibits ADP- and collagen-induced human platelet aggregation (IC(50) = 0.3 uM and 0.7 uM for ADP and collagen, respectively). This inhibition is dependent of protease activity, and probably occurs through the degradation of an unknown platelet receptor. {ECO:0000269|PubMed:24457155}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (11); Domain (2); Glycosylation (3); Metal binding (12); Modified residue (1); Motif (1); Propeptide (1); Signal peptide (1) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Pyrrolidone carboxylic acid;Secreted;Signal;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | MOD_RES 191; /note=Pyrrolidone carboxylic acid (Glu); /evidence=ECO:0000250 |
| Post Translational Modification | PTM: The N-terminus is blocked. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 465..467; /note=TDN-tripeptide |
| Gene Encoded By | |
| Mass | 54,298 |
| 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 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 |