Detail Information for IndEnz0002013695
IED ID IndEnz0002013695
Enzyme Type ID protease013695
Protein Name Zinc metalloproteinase/disintegrin VMP-II
AplVMP2

Cleaved into: Snake venom metalloproteinase
SVMP
EC 3.4.24.-
; Disintegrin beta subunit
Gene Name
Organism Agkistrodon piscivorus leucostoma (Western cottonmouth) (Acontias leucostoma)
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) Agkistrodon Agkistrodon piscivorus (cottonmouth) Agkistrodon piscivorus leucostoma (Western cottonmouth) (Acontias leucostoma)
Enzyme Sequence MIQVLLVTLCLAAFPYQGNSIILESGNVNDYEVLYPQKVTALPKGAVQPKYEDTMQYEFKVNGEPVVLHLEKNKGLFSKDYSETHYSSDGRKITTNPPVEDHCYYHGRIQNDADSTASISACNGLKGHFKLQGETYLIEPLKLSDSEAHAVYKYENVEKGDEAPKMCGVTQTNWKSDKPIKKASQLNLTPEQQRFPQRYIELVVVADHRMFTKYNGNLNTIRIWVHELVNTMNVFYRPLNIHVSLTDLEVWSDQDLINVQPAAADTLEAFGDWRETVLLNRISHDNAQLLTAIELDGETIGLANRGTMCDPKLSTGIVQDHSAINLWVAVTMAHEMGHNLGISHDGNQCHCDANSCIMSEELRQQLSFEFSDCSQNQYQTFLTDHNPQCMLNEPLRTDIVSTPVSGNELWETGEESDFDAPANPCCDAETCKLRPGAQCAEGLCCDQCKFMKEGTVCHRAKGDDLDDYCNGISAGCPRNPFHA
Enzyme Length 483
Uniprot Accession Number C9E1S1
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:19375443}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function FUNCTION: [Snake venom metalloproteinase]: Has fibrinolytic activity. The recombinant enzyme cleaves both alpha- (FGA) and beta-chains (FGB) of fibrinogen, but not the gamma-chain. The recombinant protein does not produce hemorrhage in mice and does not have effect on ADP- or collagen-stimulated platelet aggregation. {ECO:0000269|PubMed:19375443}.; FUNCTION: [Disintegrin beta subunit]: 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); Metal binding (7); Motif (1); Propeptide (2); Sequence conflict (4); Signal peptide (1)
Keywords Calcium;Cell adhesion impairing toxin;Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic toxin;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 461..463; /note=Cell attachment site; atypical (KGD)
Gene Encoded By
Mass 54,098
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 389; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 392; /note=Calcium; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda