Detail Information for IndEnz0002012165
IED ID IndEnz0002012165
Enzyme Type ID protease012165
Protein Name Zinc metalloproteinase/disintegrin
Cleaved into: Snake venom metalloproteinase HR2a
SVMP
EC 3.4.24.53
Snake venom metalloproteinase HR2b
Trimerelysin II
; Disintegrin flavostatin
Platelet aggregation activation inhibitor
Gene Name
Organism Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis)
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) Protobothrops Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis)
Enzyme Sequence MIEVLLVTICLAVFPYPGSSIILESGNVDDYEVVYPQKLTALPKGAVQPKYEDAMQYEFKVNGEPVVLHLEKNKGLFSEDYSETHYSPDGREITTYPSVEDHCYYHGRIQNDADSTASISACDGLKGYFKLQGETYLIEPLELSDSEAHAVFKYENVEKEDEAPKMCGVTQNWESDESIKKASQLYLTPEQQRFPQRYIELAIVVDHGMYTKYSSNFKKIRKRVHQMVNNINEMYRPLNIAITLSLLDVWSEKDLITMQAVAPTTARLFGDWRETVLLKQKDHDHAQLLTDINFTGNTIGWAYMGGMCNAKNSVGIVKDHSSNVFMVAVTMTHEIGHNLGMEHDDKDKCKCEACIMSAVISDKPSKLFSDCSKDYYQTFLTNSKPQCIINAPLRTDTVSTPVSGNEFLEAGEECDCGSPSNPCCDAATCKLRPGAQCADGLCCDQCRFKKKRTICRRARGDNPDDRCTGQSADCPRNS
Enzyme Length 478
Uniprot Accession Number P14530
Absorption
Active Site ACT_SITE 334
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Cleavage of 3-Asn-|-Gln-4, 10-His-|-Leu-11 and 14-Ala-|-Leu-15 in the insulin B chain, and the bond Z-Gly-Pro-|-Leu-Gly-Pro in a small molecule substrate of microbial collagenase.; EC=3.4.24.53;
DNA Binding
EC Number 3.4.24.53
Enzyme Function FUNCTION: [Snake venom metalloproteinase HR2a]: Zinc protease that induces hemorrhage. {ECO:0000269|PubMed:9114455}.; FUNCTION: [Disintegrin flavostatin]: Inhibits platelet aggregation induced by ADP, thrombin, and collagen. Acts by inhibiting fibrinogen interaction with platelet receptors GPIIb/GPIIIa (ITGA2B/ITGB3). {ECO:0000269|PubMed:9114455}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (2); Disulfide bond (9); Domain (2); Metal binding (7); Modified residue (1); Motif (1); Natural variant (3); Propeptide (2); Region (1); Signal peptide (1); Site (1)
Keywords Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Pyrrolidone carboxylic acid;Secreted;Signal;Toxin;Zinc;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue MOD_RES 191; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:2753880, ECO:0000269|PubMed:7597726"
Post Translational Modification PTM: Not N-glycosylated. {ECO:0000269|PubMed:2753880}.
Signal Peptide SIGNAL 1..20; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 459..461; /note=Cell attachment site
Gene Encoded By
Mass 53,646
Kinetics
Metal Binding METAL 200; /note=Calcium; /evidence=ECO:0000250; METAL 284; /note=Calcium; /evidence=ECO:0000250; METAL 333; /note=Zinc; catalytic; METAL 337; /note=Zinc; catalytic; METAL 343; /note=Zinc; catalytic; METAL 387; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 390; /note=Calcium; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda