Detail Information for IndEnz0002010304
IED ID IndEnz0002010304
Enzyme Type ID protease010304
Protein Name Zinc metalloproteinase/disintegrin
Cleaved into: Snake venom metalloproteinase graminelysin
SVMP
EC 3.4.24.-
Graminelysin I
; Disintegrin-like
Fragment
Gene Name
Organism Trimeresurus gramineus (Bamboo pit viper) (Indian green tree viper)
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) Trimeresurus Trimeresurus gramineus (Bamboo pit viper) (Indian green tree viper)
Enzyme Sequence KMCGVTQNWESYESTKKASQLNLTPEQQRFPQRYIKLGIFVDHGMYTKYSGNSERITKRVHQMINNINMMCRALNIVTTLSLLEIWSEKDLITVQASAPTTLTLFGAWRETVLLNRTSHDHAQLLTATIFNGNVIGRAPVGGMCDPKRSVAIVRDHNAIVFVVAVTMTHEMGHNLGNHHDEDKCNCNTCIMSKVLSRQPSKYFSECSKDYYQTFLTNHNFQCILNAPLRTDTVSTPVSGNELLEAGEDCDCGSPANPCCDAATCKLRPGAQCGEGLCCDQCRFTSAGTECRAARSECDIAESCAGQSADCPTDDFHRNGQPCLNNHGYCYNGNCPIMFYQCIALFGSNATVGQDGCFDANDIGHKYFHCRKDNEKYIPCAPQDVKCGRLFCTYIYDIDLCRYDDSANGMVAQGTKCADGKVCNSNRQCADVNTAY
Enzyme Length 435
Uniprot Accession Number P0C6E8
Absorption
Active Site ACT_SITE 170; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095"
Activity Regulation ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:11463342}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function FUNCTION: [Snake venom metalloproteinase graminelysin]: Cleaves the alpha chain of fibrinogen (FGA) preferentially and cleaves the beta chain (FGB) either on longer incubation or at high concentrations. Induces apoptosis of endothelial cells (prior to cell detachment). {ECO:0000269|PubMed:11463342, ECO:0000269|PubMed:11776320, ECO:0000269|PubMed:12878166}.; FUNCTION: Disintegrin: 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 (9); Domain (2); Glycosylation (1); Metal binding (9); Modified residue (1); Motif (1); Non-terminal residue (1); Propeptide (2)
Keywords Apoptosis;Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Pyrrolidone carboxylic acid;Secreted;Toxin;Zinc;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue MOD_RES 27; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250
Post Translational Modification PTM: The N-terminus of the metalloproteinase is blocked.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 296..298; /note=D/ECD-tripeptide
Gene Encoded By
Mass 48,204
Kinetics
Metal Binding METAL 169; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 173; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 179; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 237; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 240; /note=Calcium; /evidence=ECO:0000250; METAL 242; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 244; /note=Calcium; /evidence=ECO:0000250; METAL 247; /note=Calcium; /evidence=ECO:0000250; METAL 250; /note=Calcium; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda