IED ID | IndEnz0002011467 |
Enzyme Type ID | protease011467 |
Protein Name |
Snake venom metalloproteinase-disintegrin-like mocarhagin MOC Mocarhagin-1 SVMP EC 3.4.24.- Zinc metalloproteinase mocarhagin |
Gene Name | |
Organism | Naja mossambica (Mozambique spitting 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 mossambica (Mozambique spitting cobra) |
Enzyme Sequence | MIQALLVAICLAVFPYQGSSIILESGNVNDYEVVYPQKVPALSKGGVQNPQPETKYEDTMQYEFHVNGEPVVLHLERNKGLFSEDYTETHYAPDGREITTSSPVQDHCYYHGYIQNEADSSAVISACDGLKGHFKHQGETYFIEPLELSDSEAHAIYKDENVEEEEEIPKICGVTQTTWESDEPIEKSSQLTNTPEQDRYLQAKKYIEFYVVVDNVMYRKYTGKLHVITRRVYEMVNALNTMYRRLNFHIALIGLEIWSNGNEINVQSDVQATLDLFGEWRENKLLPRKRNDNAQLLTSTEFNGTTTGLGYIGSLCSPKKSVAVVQDHSKSTSMVAITMAHQMGHNLGMNDDRASCTCGSNKCIMSTKYYESLSEFSSCSVQEHREYLLRDRPQCILNKPSRKAIVTPPVCGNYFVERGEECDCGSPEDCQNTCCDAATCKLQHEAQCDSGECCEKCKFKGAGAECRAAKNDCDFPELCTGRSAKCPKDSFQRNGHPCQNNQGYCYNGTCPTLTNQCATLWGPGAKMSPGLCFMLNWNARSCGLCRKENGRKILCAAKDVKCGRLFCKKKNSMICHCPPPSKDPNYGMVAPGTKCGVKKVCRNRQCVKV |
Enzyme Length | 609 |
Uniprot Accession Number | Q10749 |
Absorption | |
Active Site | |
Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA and diisopropyl fluorophosphate (DFP). Also inhibited by an excess of zinc or calcium ions. {ECO:0000269|PubMed:7592904}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.24.- |
Enzyme Function | FUNCTION: Snake venom zinc metalloproteinase that inhibits platelet aggregation by cleaving platelet glycoprotein Ib alpha (GP1BA) at Glu-298/Asp-299, and abolishes binding of von Willebrand factor (VWF) to GPIBA. Cleaves P-selectin glycoprotein ligand-1 (PSGL-1/SELPLG) at Tyr-51/Asp-52, and completely abolishes the binding of PSGL-1 to P-selectin. Anionic amino acid sequences containing sulfated tyrosines are needed for cleavages. Inhibits the thrombin-induced platelet aggregation, and the thrombin-induced release of ATP and ADP. Has lectin activity (inhibited by heparin). {ECO:0000269|PubMed:12598411, ECO:0000269|PubMed:7592904, ECO:0000269|PubMed:8664285, ECO:0000269|PubMed:8931262}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Disulfide bond (17); Domain (2); Glycosylation (2); Metal binding (12); Motif (1); Propeptide (1); Sequence conflict (2); Signal peptide (1) |
Keywords | Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;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:8664285}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | MOTIF 472..474; /note=D/ECD-tripeptide |
Gene Encoded By | |
Mass | 68,176 |
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:0000255|PROSITE-ProRule:PRU00276; METAL 345; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; 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 |
Rhea ID | |
Cross Reference Brenda |