| IED ID | IndEnz0002012590 |
| Enzyme Type ID | protease012590 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like cobrin EC 3.4.24.- Snake venom metalloproteinase SVMP |
| Gene Name | |
| Organism | Naja kaouthia (Monocled cobra) (Naja siamensis) |
| 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 Elapidae Elapinae Naja Naja kaouthia (Monocled cobra) (Naja siamensis) |
| Enzyme Sequence | MIQLSWSSIILESGNVNDYEVVYPQKVPALLKGGVQNPQPETKYEDTMQYEFQVNGEPVVLHLERNKGLFSEDYTETHYAPDGREITTSPPVQDHCYYHGYFQNEADSSAVISACDGLKGHFKLQGEIYFIEPLKISDSEAHAIYKDENVEEEDETPKICGVTDTTWESDEPIKKTSLLTNTPEQDRYLQAEKYIEFYMVVDNIMYRHYKRNQLVIKRKVYEMINTMNMIYRRLNFHIALIGLEIWSNINEINVQSDVKATLDLFGEWREKKLLPRKRNDNAQLLTGIDFNGTPVGLAYIGSICNPKTSAAVVQDYSKSTRMVAITMAHEMGHNLGMNHDKGFCTCGFNKCVMSTRRTKPAYQFSSCSVREHQRYLLRDRPQCILNKPLSTDIVSPPICGNYFVEVGEECDCGSPADCQSACCNATTCKLQHEAQCDSEECCEKCKFKGAGAECRAAKDDCDLPELCTGQSAECPTDVFQRNGLPCQNNGYCYNGKCPIMTNQCIALRGPGVKVSRDSCFTLNQRTRGCGLCRMEYGRKIPCAAKDVKCGRLFCKKRNSMICNCSISPRDPSYGMVEPGTKCGDGMVCSNRQCVDVKTAY |
| Enzyme Length | 600 |
| Uniprot Accession Number | Q9PVK7 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc metalloproteinase that may cleave complement protein C3 into C3c-like (C3o). {ECO:0000269|PubMed:3045125}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (17); Domain (2); Glycosylation (1); Metal binding (18); Motif (1); Propeptide (1); Signal peptide (1) |
| Keywords | Calcium;Complement system impairing toxin;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..8; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 460..462; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 67,662 |
| Kinetics | |
| Metal Binding | METAL 196; /note=Calcium 1; /evidence=ECO:0000250; METAL 280; /note=Calcium 1; /evidence=ECO:0000250; METAL 329; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 333; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 339; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 383; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 386; /note=Calcium 1; /evidence=ECO:0000250; METAL 398; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 401; /note=Calcium 2; /evidence=ECO:0000250; METAL 403; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 405; /note=Calcium 2; /evidence=ECO:0000250; METAL 408; /note=Calcium 2; /evidence=ECO:0000250; METAL 411; /note=Calcium 2; /evidence=ECO:0000250; METAL 462; /note=Calcium 3; /evidence=ECO:0000250; METAL 463; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 465; /note=Calcium 3; /evidence=ECO:0000250; METAL 477; /note=Calcium 3; /evidence=ECO:0000250; METAL 478; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |