IED ID | IndEnz0002011190 |
Enzyme Type ID | protease011190 |
Protein Name |
Zinc metalloproteinase-disintegrin-like atrase-A EC 3.4.24.- Snake venom metalloproteinase SVMP |
Gene Name | |
Organism | Naja atra (Chinese 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 atra (Chinese cobra) |
Enzyme Sequence | MIQALLVIICLAVFPHQGSSIILESGNVNDYEVVYPQKVPALLKGGVQNPQPETKYEDTMRYEFQVNGEPVVLHLERNKGLFSEDYTETHYAPDGREITTSPPVQDHCYYHGYIQNEADSSAVISACNGLKGHFKHQGETYFIEPLELSESEAHAIYKDENVEKEDETPKICAVTQTTWESDESIEKTSQLTNTPEQDRYLQVKKYIEFYLVVDNKMYKNHTSNQELRTRVYEMVNYLNTKYRRLNFHIALIGLEIWSNQDKVDMDPGANVTLKSFAEWRAKLPPHKRNDNAQLLTGIDFNGTTVGLAYTGTLCTWGSVAVVQDYSRRTILMASTMAHELGHNMGIHHDKANCRCSHSPCIMSDTISDEPFYEFSSCSVREHQEYLLRERPQCILNKPSRKAIVSRPVCGNNFVEVGEQCDCGSLQDCQSTCCNATTCKLQPHAQCDSEECCEKCKFKGAETECRAAKDDCDLPEFCTGQSAECPTDSLQRNGHPCQNNQGYCYNGKCPTMENQCITLLGPNYTVGPAGCFKNNRKGDDVSHCRKENGAKIPCAAKDEKCGTLYCTEIKKTGCIVPVSPRDPDSRMVEPGTKCEDKKVCSKSQCVKV |
Enzyme Length | 607 |
Uniprot Accession Number | D5LMJ3 |
Absorption | |
Active Site | |
Activity Regulation | |
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. {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Disulfide bond (17); Domain (2); Glycosylation (5); Metal binding (17); Motif (1); Propeptide (1); Signal peptide (1) |
Keywords | Calcium;Cell adhesion impairing toxin;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:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | MOTIF 470..472; /note=D/ECD-tripeptide |
Gene Encoded By | |
Mass | 68,254 |
Kinetics | |
Metal Binding | METAL 208; /note=Calcium 1; /evidence=ECO:0000250; METAL 290; /note=Calcium 1; /evidence=ECO:0000250; METAL 338; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 342; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 348; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 393; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 396; /note=Calcium 1; /evidence=ECO:0000250; METAL 411; /note=Calcium 2; /evidence=ECO:0000250; METAL 413; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 415; /note=Calcium 2; /evidence=ECO:0000250; METAL 418; /note=Calcium 2; /evidence=ECO:0000250; METAL 421; /note=Calcium 2; /evidence=ECO:0000250; METAL 472; /note=Calcium 3; /evidence=ECO:0000250; METAL 473; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 475; /note=Calcium 3; /evidence=ECO:0000250; METAL 487; /note=Calcium 3; /evidence=ECO:0000250; METAL 488; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |