| IED ID | IndEnz0002013635 |
| Enzyme Type ID | protease013635 |
| Protein Name |
Hemorrhagic metalloproteinase-disintegrin-like kaouthiagin 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 | TNTPEQDRYLQAEKYIEFYVIVDNRMYRYYNYDKPAIKIRVYEMINAVNTKFRPLKIHIALIGLEIWSNEDKFEVKPAASVTLKSFREWRQTVLLPRKRNDNAQLLTGINLNGTAVGIAYPGSLCTQRSVFVVQDYNRRMSLVASTMTHELGHNLGIHHDEASCICIPGPCIMLKKRTAPAFQFSSCSIRDYQEYLLRDRPQCILNKPLSTDIVSPAICGNYFVEEGEECDCGSPAACQSACCDAATCKFNGAGAECRAAKHDCDLPELCTGQSAECPTDSLQRNGHPCQNNQGYCYNGKCPTLTNQCIALLGPHFTVSPKGCFDLNMRGDDGSFCRMEDGTKIPCAAKDVKCGRLYCTEKNTMSCLIPPNPDGIMAEPGTKCGDGMVCSKGQCVDVQTAY |
| Enzyme Length | 401 |
| Uniprot Accession Number | P82942 |
| Absorption | |
| Active Site | ACT_SITE 150; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc protease that inhibits hemostasis by binding and cleaving the vWF in humans. Has also and inhibitory effect on the collagen-induced platelet aggregation. {ECO:0000269|PubMed:11284707}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (14); Domain (2); Glycosylation (1); Metal binding (17); Motif (1) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 263..265; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 44,493 |
| Kinetics | |
| Metal Binding | METAL 17; /note=Calcium 1; /evidence=ECO:0000250; METAL 101; /note=Calcium 1; /evidence=ECO:0000250; METAL 149; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 153; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 159; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 203; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 206; /note=Calcium 1; /evidence=ECO:0000250; METAL 218; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 221; /note=Calcium 2; /evidence=ECO:0000250; METAL 223; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 225; /note=Calcium 2; /evidence=ECO:0000250; METAL 228; /note=Calcium 2; /evidence=ECO:0000250; METAL 231; /note=Calcium 2; /evidence=ECO:0000250; METAL 265; /note=Calcium 3; /evidence=ECO:0000250; METAL 266; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 268; /note=Calcium 3; /evidence=ECO:0000250; METAL 280; /note=Calcium 3; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |