| IED ID | IndEnz0002011345 |
| Enzyme Type ID | protease011345 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like atrase-B EC 3.4.24.- Snake venom metalloproteinase SVMP |
| Gene Name | |
| Organism | Naja atra (Chinese cobra) |
| 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 atra (Chinese cobra) |
| Enzyme Sequence | MIQALLVIICLAVFPHQGSSIILESGNVNDYEVVYPQKVPALLKGGVQNPQPETKYEDTMRYEFQVNGEPVVLHLERNKGLFSEDYTETHYAPDGREITTSPPVQDHCYYHGYIQNEADSSAVISACDGLKGHFEHQGETYFIEPLKISNSEAHAIYKDENVENEDETPEICGVTETTWESDESIEKTSQLTNTPEQDRYLQDKKYIEFYVIVDNRMYRYYNNDKPAIKIRVYEMINAVNTKFRPLKIHIALIGLEIWSNKDKFEVKPAASVTLKSFGEWRETVLLPRKRNDNAQLLTGIDFNGNTVGRAYIGSLCKTNESVAIVQDYNRRISLVASTMTHELGHNLGIHHDKASCICIPGPCIMLKKRTAPAFQFSSCSIREYREYLLRDRPQCILNKPLSTDIVSPPICGNYFVEVGEECDCGSPQACQSACCNAATCQFKGAETECRVAKDDCDLPELCTGQSAECPTDSLQRNGHPCQNNQGYCYNRTCPTLTNQCITLLGPHFTVSPKGCFDLNMRGDDGSFCGMEDGTKIPCAAKDVKCGRLYCTEKNTMSCLIPPNPDGIMAEPGTKCGDGMVCSKGQCVDVQTAY |
| Enzyme Length | 593 |
| Uniprot Accession Number | D6PXE8 |
| Absorption | |
| Active Site | ACT_SITE 342; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA, EGTA, 1,10-phenanthroline and DTT. Not inhibited by PMSF and SBTI. {ECO:0000269|PubMed:20837040}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc protease that inhibits the classical and alternative pathways of complement by cleaving factor B, C6, C7, and C8. Also slowly and selectively degrades alpha-chain of fibrinogen (FGA), and shows edema-inducing activity. {ECO:0000269|PubMed:20837040}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (14); Domain (2); Glycosylation (2); Metal binding (17); Motif (1); Propeptide (1); Signal peptide (1) |
| Keywords | Calcium;Complement system impairing toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 455..457; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 66,246 |
| Kinetics | |
| Metal Binding | METAL 208; /note=Calcium 1; /evidence=ECO:0000250; METAL 292; /note=Calcium 1; /evidence=ECO:0000250; METAL 341; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 345; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 351; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 395; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 398; /note=Calcium 1; /evidence=ECO:0000250; METAL 410; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 413; /note=Calcium 2; /evidence=ECO:0000250; METAL 415; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 417; /note=Calcium 2; /evidence=ECO:0000250; METAL 420; /note=Calcium 2; /evidence=ECO:0000250; METAL 423; /note=Calcium 2; /evidence=ECO:0000250; METAL 457; /note=Calcium 3; /evidence=ECO:0000250; METAL 458; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 460; /note=Calcium 3; /evidence=ECO:0000250; METAL 472; /note=Calcium 3; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |