Detail Information for IndEnz0002012669
IED ID IndEnz0002012669
Enzyme Type ID protease012669
Protein Name Zinc metalloproteinase/disintegrin
Cleaved into: Snake venom metalloproteinase insularinase-A
SVMP
EC 3.4.24.-
; Disintegrin insularin
Gene Name
Organism Bothrops insularis (Golden lancehead) (Lachesis insularis)
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 insularis (Golden lancehead) (Lachesis insularis)
Enzyme Sequence MIQVLLVTICLAAFPYQGSSIILESGNVNDYEVVYARKVTELPKGAVQQKYEDAMQYEFKVNGEPVVLHLEKNKGLFSEDYSETHYSPDGRQIITYPPFEDHCYYHGRIENDADSTASISACNGLKGHFKLQGETYLIEPLKLPDSEAHAVYKYENVEKEDEAPKMCGVTETNWESYEPIEKASQSNLTPEQQKFSPRYIELAVVADHGMFTKYNSNLNTIRTRVHEMVNTLNGFFRSVNVDASLANLEVWSKKDLIKVEKDSSKTLTSFGEWRERDLLPRISHDHAQLLTTIVFDQQTIGLAYTAGMCDPRQSVAVVMDHSKKNLRVAVTMAHELGHNLGMDHDDTCTCGAKSCIMASTISKGLSFEFSKCSQNQYQTYLTDHNPQCILNKPLTTVSGNELLEAGEECDCGAPENPCCDAATCKLRPRAQCAEGLCCDQCRFKGAGKICRRARGDNPDDRCTGQSADCPRNRFHA
Enzyme Length 476
Uniprot Accession Number Q5XUW8
Absorption
Active Site ACT_SITE 335; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095"
Activity Regulation ACTIVITY REGULATION: Inhibited by EDTA, and 1,10-phenanthroline, but not by PMSF. {ECO:0000269|PubMed:16006246}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function FUNCTION: [Snake venom metalloproteinase insularinase-A]: Non-hemorrhagic proteinase that activates prothrombin (F2) calcium-independently. Activates factor X (F10) and hydrolyzes the Aalpha-chain and more slowly the Bbeta-chain of fibrin and fibrinogen without affecting the gamma chain. It induces neither detachment nor apoptosis of human endothelial cells and is also not able to trigger an endothelial proinflammatory cell response. Nitric oxide and prostacyclin levels released by endothelial cells are significantly increased after treatment with insularinase A. {ECO:0000269|PubMed:16006246}.; FUNCTION: [Disintegrin insularin]: Inhibits platelet aggregation induced by ADP, thrombin, platelet-activating factor and collagen. Acts by inhibiting fibrinogen interaction with platelet receptors GPIIb/GPIIIa (ITGA2B/ITGB3) (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (2); Disulfide bond (7); Domain (2); Metal binding (7); Modified residue (1); Motif (1); Propeptide (2); Signal peptide (1)
Keywords Blood coagulation cascade activating toxin;Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Prothrombin activator;Pyrrolidone carboxylic acid;Secreted;Signal;Toxin;Zinc;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue MOD_RES 193; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250
Post Translational Modification PTM: The N-terminus is blocked.; PTM: Not glycosylated.
Signal Peptide SIGNAL 1..20; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 454..456; /note=Cell attachment site
Gene Encoded By
Mass 53,313
Kinetics
Metal Binding METAL 201; /note=Calcium; /evidence=ECO:0000250; METAL 285; /note=Calcium; /evidence=ECO:0000250; METAL 334; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 338; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 344; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 388; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 391; /note=Calcium; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda