Detail Information for IndEnz0002011467
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