Detail Information for IndEnz0002010047
IED ID IndEnz0002010047
Enzyme Type ID protease010047
Protein Name Zinc metalloproteinase-disintegrin-like BaG
EC 3.4.24.-
Snake venom metalloproteinase
SVMP
Fragments
Gene Name
Organism Bothrops alternatus (Urutu) (Rhinocerophis alternatus)
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 Crotalinae (pit vipers) Bothrops Bothrops alternatus (Urutu) (Rhinocerophis alternatus)
Enzyme Sequence SISACNGLKGHFLIEPLKLSDSEKTDLLNRSHDNAQLSPINLVVAVIMAHEMGHGMVLPGTK
Enzyme Length 62
Uniprot Accession Number P0C7B1
Absorption
Active Site ACT_SITE 51; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095"
Activity Regulation ACTIVITY REGULATION: Inhibited by EDTA, and 1,10-phenanthroline. {ECO:0000269|PubMed:12893294}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function FUNCTION: Snake venom Zinc metalloproteinase that inhibits ADP-induced platelet aggregation and inhibits the alpha-5/beta-1 (ITGA5/ITGB1) integrin, a fibronectin receptor. Has caseinolytic activity. Induces the detachment of cells that are bound to fibronectin. {ECO:0000269|PubMed:12893294}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Domain (1); Glycosylation (1); Metal binding (2); Non-adjacent residues (4); Non-terminal residue (2)
Keywords Cell adhesion impairing toxin;Direct protein sequencing;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Secreted;Toxin;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12893294}.
Modified Residue
Post Translational Modification PTM: The N-terminus is blocked.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 6,650
Kinetics
Metal Binding METAL 50; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 54; /note=Zinc; catalytic; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda