| IED ID | IndEnz0002013240 |
| Enzyme Type ID | protease013240 |
| Protein Name |
Zinc metalloproteinase/disintegrin Long ocellatusin precursor Eo-00006 EOC00006 Cleaved into: Snake venom metalloproteinase Eoc6 SVMP EC 3.4.24.- ; Disintegrin ocellatusin |
| Gene Name | |
| Organism | Echis ocellatus (Ocellated saw-scaled viper) |
| 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 Viperinae (vipers) Echis Echis ocellatus (Ocellated saw-scaled viper) |
| Enzyme Sequence | MIQVLLVTICLAVFPFQGSSKTLKSGNVNDYEVVNPQKITGLPVGAFKQPEKKYEDAVQYEFEVNGEPVVLHLEKNKGLFSEDYSETHYSPDGSEITTNPPVEDHCYYHGRVQNDADSTASISTCNGLKGFFTLRGETYLIEPLKVPDSESHAVYKYEDAKKKDEAPKMCGVTLTNWESDEPIKKASHLVATSEQQHFHPRYVQLVIVADHSMVTKNNNDLTALTTWIHQIVNDMIVMYRILNIHITLANVEIWSSGDLIAVTSSAPTTLRSFGEWRARNLVNRITHDNAQLITAVHLDNLIGYGYLGTMCDPQSSVAITEDHSTDHLWVAATMAHEMGHNLGMNHDGNQCNCGAAGCIMSAIISQYRSYQFSDCSMNEYRNYITTHNPPCILNQALRTDTVSTPVSENELLQNSVNPCYDPVTCQPKEKEDCESGPCCDNCKFLKEGTICKMARGDNMHDYCNGKTCDCPRNPYKGEHDPMEWPAPAKGSVLM |
| Enzyme Length | 494 |
| Uniprot Accession Number | Q14FJ4 |
| Absorption | |
| Active Site | ACT_SITE 337; /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 metalloproteinase Eoc6]: Impairs hemostasis in the envenomed animal. {ECO:0000250}.; FUNCTION: [Disintegrin ocellatusin]: Inhibits ADP-induced platelet aggregation (IC(50)=168nM). Inhibits alpha-5/beta-1 (ITGA5/ITGB1) integrin and induces the expression of a ligand-induced binding site epitope on beta-1 integrin subunit. Has a direct chemotactic stimulus on human neutrophils in vitro. {ECO:0000269|PubMed:11852062}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Disulfide bond (8); Domain (2); Metal binding (3); Motif (1); Propeptide (3); Sequence conflict (1); Signal peptide (1) |
| Keywords | Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;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 {ECO:0000269|PubMed:11852062}. |
| 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=Cell attachment site |
| Gene Encoded By | |
| Mass | 55,165 |
| Kinetics | |
| Metal Binding | METAL 336; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 340; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 346; /note=Zinc; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |