| IED ID | IndEnz0002013021 |
| Enzyme Type ID | protease013021 |
| Protein Name |
Zinc metalloproteinase-disintegrin jerdonitin EC 3.4.24.- Snake venom metalloproteinase SVMP |
| 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 | MIQVLLVTICLAVFPYQGSSIILESGNIDDYEVVYPRKVTALPKGAVQQKYEDTMQYEFKVNEEPVVLHLEKNKGLFSKDYSETHYSPDGREITTYPPVEDHCYYHGRIQNDADSTASISACNGLKGHFKLQGETYFIEPLKLPDSEAHAVFKYENVEKEDEAPKMCGVTETNWESDEPIKKLSQIMIPPEQQRYIELVIVADHRMYTKYDGDKTEISSKIYETANNLNEIYRHLKIHVVLIGLEMWSSGELSKVTLSADETLDSFGEWRERDLLQRKRHDNAQLLTGMIFNEKIEGRAYKESMCDPKRSVGIVRDHRTRPHLVANRMAHELGHNLGFHHDGDSCTCGANSCIMSATVSNEPSSRFSDCSLFQYSSDIIHNPFTSRCLYNEPSKTDIVSPSVCGNYYMEVGEDCDCGPPANCQNPCCDAATCRLTPGSQCADGLCCDQCRFMKKGTICRIARGDDLDDYCNGISAGCPRNPFHA |
| Enzyme Length | 484 |
| Uniprot Accession Number | P83912 |
| Absorption | |
| Active Site | ACT_SITE 331; /evidence="ECO:0000250|UniProtKB:P18619, ECO:0000255|PROSITE-ProRule:PRU00276" |
| Activity Regulation | ACTIVITY REGULATION: Fibrinogenolytic is completely inhibited by EDTA, but not by PMSF. {ECO:0000269|Ref.2}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc metalloproteinase that inhibits ADP-induced human platelet aggregation with an IC(50) of 120 nM (248 nM for the recombinant protein). May act by binding to the receptor GPIIb/GPIIIa (ITGA2B/ITGB3) on the platelet surface (PubMed:14511668). Degrades the alpha-chain of fibrinogen completely and the beta-chain partially, leaving the gamma chain intact (Ref.2). Also inhibits the growth of several cell lines, including human liver cancer cells (Bel7402), human leukemia cells (K562) and human gastric carcinoma cells (BGC823) (PubMed:19732785). {ECO:0000269|PubMed:14511668, ECO:0000269|PubMed:19732785, ECO:0000269|Ref.2}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (10); Domain (2); Metal binding (12); Modified residue (1); Motif (1); Propeptide (1); Signal peptide (1) |
| Keywords | Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic 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. |
| Modified Residue | MOD_RES 192; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000305|PubMed:14511668 |
| Post Translational Modification | PTM: The N-terminus is blocked. {ECO:0000269|PubMed:14511668}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 462..464; /note=Cell attachment site |
| Gene Encoded By | |
| Mass | 54,613 |
| Kinetics | |
| Metal Binding | METAL 197; /note=Calcium 1; /evidence=ECO:0000250; METAL 281; /note=Calcium 1; /evidence=ECO:0000250; METAL 330; /note=Zinc; catalytic; /evidence=ECO:0000305; METAL 334; /note=Zinc; catalytic; /evidence=ECO:0000305; METAL 340; /note=Zinc; catalytic; /evidence=ECO:0000305; METAL 387; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 390; /note=Calcium 1; /evidence=ECO:0000250; METAL 402; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 405; /note=Calcium 2; /evidence=ECO:0000250; METAL 409; /note=Calcium 2; /evidence=ECO:0000250; METAL 412; /note=Calcium 2; /evidence=ECO:0000250; METAL 415; /note=Calcium 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |