| IED ID | IndEnz0002010633 |
| Enzyme Type ID | protease010633 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like jerdohagin EC 3.4.24.- Snake venom metalloproteinase SVMP Fragments |
| Gene Name | |
| Organism | Protobothrops jerdonii (Jerdon's pitviper) (Trimeresurus jerdonii) |
| 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 jerdonii (Jerdon's pitviper) (Trimeresurus jerdonii) |
| Enzyme Sequence | YLNNFRYLYIRHDREACTCHANSCIMSAYFSNSHVQYENYINDCKPQCILNELHSWVECESGECCEQCRSECDIAESCTNGQPLHNFGYCYNGNCPIMYHQCYLYCYNSLGNQFPCVPYYTPR |
| Enzyme Length | 123 |
| Uniprot Accession Number | P0DM88 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Its proteolytic and hemorrhagic activities are inhibited by EDTA, but not by PMSF. {ECO:0000269|PubMed:15302534}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom metalloproteinase that has high hemorrhagic activity and degrades the alpha-chain of fibrinogen (FGA), leaving the beta- and the gamma-chain intact. It may also inhibit platelet aggregation. Cleaves insulin B chain at '25-Phe-|-Val-26', '26-Val-|-Asn-27', '29-His-|-Leu-30', '30-Leu-|-Cys-31', '33-Ser-|-His-34', '35-Leu-|-Val-36', '40-Tyr-|-Leu-41', '41-Leu-|-Val-42', '42-Val-|-Cys-43', '43-Cys-|-Gly-44', '44-Gly-|-Glu-45', '46-Arg-|-Gly-47', '47-Gly-|-Phe-48', '49-Phe-|-Tyr-50' and '52-Pro-|-Lys-53' bonds. Also cleaves human prothrombin (72 kDa) and activation fragment F1 (27 kDa) of activated human prothrombin, to generate two new proteins of 68 and 23 kDa. {ECO:0000269|PubMed:15302534}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (5); Domain (2); Metal binding (3); Motif (1); Non-adjacent residues (7); Non-terminal residue (2) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: The N-terminus is blocked. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 71..73; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 14,489 |
| Kinetics | |
| Metal Binding | METAL 12; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 48; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000250"; METAL 51; /note="Calcium 1"; /evidence="ECO:0000250" |
| Rhea ID | |
| Cross Reference Brenda |