| IED ID | IndEnz0002011116 |
| Enzyme Type ID | protease011116 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like ohanin EC 3.4.24.- Snake venom metalloproteinase SVMP |
| Gene Name | |
| Organism | Ophiophagus hannah (King cobra) (Naja hannah) |
| 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 Ophiophagus Ophiophagus hannah (King cobra) (Naja hannah) |
| Enzyme Sequence | MIQVLLVTICLVVFPYQGSSIILESGKVNDYEVVYPQKIPVLPKSKIQRREQKMYEDTMKYEFKVNGEPVVLHLERNKELFSKDYTETHYSPDGREITTSPPVEDHCYYHGYIQSDIDSTAILNACNGLKGYFRHHGEAYHIEPLKFSDSEAHAVYKYENIEKEDETPKICGVKHSTWESDEPIEKISQKKDFLEEKKYLELYIVADYVMFRKYGRNVTTIRMRVFDMVNYITVVYKALNIHVALIGFEIWSLKDKFVINASTKNNLLHFSIWRSTVLRKRNDNAQLLTGVDLNGYTLGSAYLKAMCDVLQSVGIVQDYSKSPYLVGAAMAHEIGHNLGMEHDTKTCSCMRGNCIMSPEEEGSDFPMEFSSCSLYDFQNYMLTDTPQCLINKPSNTSIIKNAVCGNYVEEEGEECDCGSPEQCENNCCEAATCKLKPGAKCAKGACCKKCQFKKAGAECRAARNECDLPEFCIGQSAECPMDRFHKNGHSCQNDQGYCFRGYCPTLAKQCITLWGSDAKVAPDECFQNNTNGNEYDYCKKTNNVIIPCKPTDVKCGRLYCTGGTENPSEGEKISSDPCKASYSEIEDIGMVDHRTKCGEKMVCSDGKCIPL |
| Enzyme Length | 611 |
| Uniprot Accession Number | A3R0T9 |
| Absorption | |
| Active Site | ACT_SITE 333; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA, but not by PMSF. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc metalloproteinase that has hemorrhagic activity. Inhibits ADP-, TMVA- and stejnulxin-induced platelet aggregation in a dose-dependent manner (on washed platelet, but not on platelet rich plasm). Also specifically degrades alpha-chain of fibrinogen (FGA). {ECO:0000269|PubMed:17337026}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (17); Domain (2); Glycosylation (4); Metal binding (3); Motif (1); Propeptide (1); Signal peptide (1) |
| Keywords | Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Secreted;Signal;Toxin;Zinc;Zymogen |
| 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 465..467; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 69,049 |
| Kinetics | |
| Metal Binding | METAL 332; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 336; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 342; /note=Zinc; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.51; |