| IED ID | IndEnz0002011820 |
| Enzyme Type ID | protease011820 |
| Protein Name |
Snake venom metalloproteinase atrolysin-C SVMP EC 3.4.24.42 Hemorrhagic metalloproteinase atrolysin C Hemorrhagic toxin C HT-C |
| Gene Name | |
| Organism | Crotalus atrox (Western diamondback rattlesnake) |
| 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) Crotalus Crotalus atrox (Western diamondback rattlesnake) |
| Enzyme Sequence | MIEVVLVTICLAVFPYQGSSIILESGNVNDYEVVYPRKVTALPKGAVQPKYEDAMQYELKVNGEPVVLHLEKNKELFSKDYSETHYSPDGRKITTNPSVEDHCYYRGRIENDADSTASISACNGLKGHFKLQGELYLIEPLELSDSEAHAVFKLENVEKEDEAPKMCGVTQNWESYEPIKKASDLNLNPDQQNLPQRYIELVVVADHRVFMKYNSDLNTIRTRVHEIVNFINGFYRSLNIHVSLTDLEIWSNEDQINIQSASSDTLNAFAEWRETDLLNRKSHDNAQLLTAIELDEETLGLAPLGTMCDPKLSIGIVQDHSPINLLMGVTMAHELGHNLGMEHDGKDCLRGASLCIMRPGLTKGRSYEFSADSMHYYERFLKQYKPQCILNKPLRIDPVSTPVSGNELLEAGEE |
| Enzyme Length | 414 |
| Uniprot Accession Number | Q90392 |
| Absorption | |
| Active Site | ACT_SITE 334; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | |
| 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 23-Gly-|-Phe-24 of insulin B chain. With small molecule substrates prefers hydrophobic residue at P2' and small residue such as Ala, Gly at P1.; EC=3.4.24.42; |
| DNA Binding | |
| EC Number | 3.4.24.42 |
| Enzyme Function | FUNCTION: Snake venom zinc metalloproteinase that causes hemorrhage by provoking the degradation of the sub-endothelial matrix proteins (fibronectin, laminin, type IV collagen, nidogen, and gelatins). {ECO:0000269|PubMed:2817904, ECO:0000269|Ref.2}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (2); Domain (1); Metal binding (12); Modified residue (1); Propeptide (2); Signal peptide (1) |
| Keywords | Calcium;Collagen degradation;Direct protein sequencing;Disulfide bond;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Pyrrolidone carboxylic acid;Secreted;Signal;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | MOD_RES 191; /note=Pyrrolidone carboxylic acid; /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 | |
| Gene Encoded By | |
| Mass | 46,769 |
| Kinetics | |
| Metal Binding | METAL 200; /note=Calcium 1; /evidence=ECO:0000250; METAL 284; /note=Calcium 1; /evidence=ECO:0000250; METAL 333; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 337; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 343; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 388; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 391; /note=Calcium 1; /evidence=ECO:0000250; METAL 403; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 406; /note=Calcium 2; /evidence=ECO:0000250; METAL 408; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 410; /note=Calcium 2; /evidence=ECO:0000250; METAL 413; /note=Calcium 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.42; |