| IED ID | IndEnz0002012965 |
| Enzyme Type ID | protease012965 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like bothropasin EC 3.4.24.49 Snake venom metalloproteinase SVMP Cleaved into: Disintegrin-like bothropasin |
| Gene Name | |
| Organism | Bothrops jararaca (Jararaca) (Bothrops jajaraca) |
| 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 jararaca (Jararaca) (Bothrops jajaraca) |
| Enzyme Sequence | MIEVLLVTICLAAFPYQGSSIILESGNVNDYEVVYPRKVTALPKGAVQPKYEDAMQYEFKVNGEPVVLHLEKNKGLFSKDYSETHYSPDGREITTYPAVEDHCYYHGRIENDADSTASISACNGLKGHFKLQRETYFIEPLKLSNSEAHAVFKYENVEKEDEAPKMCGVTQNWKSYEPIKKASQLVVTAEQQKYNPFRYVELFIVVDQGMVTKNNGDLDKIKARMYELANIVNEILRYLYMHAALVGLEIWSNGDKITVKPDVDYTLNSFAEWRKTDLLTRKKHDNAQLLTAIDFNGPTIGYAYIGSMCHPKRSVAIVEDYSPINLVVAVIMAHEMGHNLGIHHDTDFCSCGDYPCIMGPTISNEPSKFFSNCSYIQCWDFIMKENPQCILNEPLGTDIVSPPVCGNELLEVGEECDCGTPENCQNECCDAATCKLKSGSQCGHGDCCEQCKFSKSGTECRASMSECDPAEHCTGQSSECPADVFHKNGQPCLDNYGYCYNGNCPIMYHQCYALFGADVYEAEDSCFKDNQKGNYYGYCRKENGKKIPCAPEDVKCGRLYCKDNSPGQNNPCKMFYSNDDEHKGMVLPGTKCADGKVCSNGHCVDVATAY |
| Enzyme Length | 610 |
| Uniprot Accession Number | O93523 |
| Absorption | |
| Active Site | ACT_SITE 335; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA and EGTA. {ECO:0000269|PubMed:6819660}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of 5-His-|-Leu-6, 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 in insulin B chain.; EC=3.4.24.49; Evidence={ECO:0000269|PubMed:6819660}; |
| DNA Binding | |
| EC Number | 3.4.24.49 |
| Enzyme Function | FUNCTION: [Zinc metalloproteinase-disintegrin-like bothropasin]: Has caseinolytic activity. Causes hemorrhage on rabbit skin and causes myonecrosis in mouse tibialis anterior muscle.; FUNCTION: [Disintegrin-like bothropasin]: Inhibits platelet aggregation. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Disulfide bond (25); Domain (2); Glycosylation (1); Metal binding (18); Modified residue (1); Motif (1); Propeptide (1); Signal peptide (1); Site (1) |
| Keywords | 3D-structure;Calcium;Cell adhesion impairing toxin;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. |
| Modified Residue | MOD_RES 192; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:18831982 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3DSL; |
| Mapped Pubmed ID | - |
| Motif | MOTIF 466..468; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 68,213 |
| Kinetics | |
| Metal Binding | METAL 201; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:18831982, ECO:0000312|PDB:3DSL"; METAL 285; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:18831982, ECO:0000312|PDB:3DSL"; METAL 334; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:18831982, ECO:0000312|PDB:3DSL"; METAL 338; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:18831982, ECO:0000312|PDB:3DSL"; METAL 344; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:18831982, ECO:0000312|PDB:3DSL"; METAL 389; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:18831982, ECO:0000312|PDB:3DSL"; METAL 392; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:18831982, ECO:0000312|PDB:3DSL"; METAL 404; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:18831982, ECO:0000312|PDB:3DSL"; METAL 407; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:18831982, ECO:0000312|PDB:3DSL"; METAL 409; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:18831982, ECO:0000312|PDB:3DSL"; METAL 411; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:18831982, ECO:0000312|PDB:3DSL"; METAL 414; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:18831982, ECO:0000312|PDB:3DSL"; METAL 417; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:18831982, ECO:0000312|PDB:3DSL"; METAL 468; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:18831982, ECO:0000312|PDB:3DSL"; METAL 469; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:18831982, ECO:0000312|PDB:3DSL"; METAL 471; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:18831982, ECO:0000312|PDB:3DSL"; METAL 483; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:18831982, ECO:0000312|PDB:3DSL"; METAL 484; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:18831982, ECO:0000312|PDB:3DSL" |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.49; |