IED ID | IndEnz0002010737 |
Enzyme Type ID | protease010737 |
Protein Name |
Zinc metalloproteinase/disintegrin Cleaved into: Snake venom metalloproteinase SVMP EC 3.4.24.- ; Disintegrin piscivostatin-beta PVS-beta |
Gene Name | |
Organism | Agkistrodon piscivorus piscivorus (Eastern cottonmouth) |
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 piscivorus (Eastern cottonmouth) |
Enzyme Sequence | MIQVLLVTLCLAAFPYQGNSIILESGNVNDYEVLYPQKVTALPKGAVQPKYEDTMQYEFKVNGEPVVLHLEKNKGLFSKDYSETHYSSDGRKITTNPPVEDHCYYHGRIQNDADSTASISACNGLKGHFKLQGETYLIEPLKLSDSEAHAVYKYENVEKEDEAPKMCGVTQTNWKSDKPIKKASQLNLTPEQQRFPQRYIELVVVADHRMFTKYNGNLNTIRIWVHELVNTMNVFYRPLNIHVSLTDLEVWSDQDLINVQPAAADTLEAFGDWRETVLLNRISHDNAQLLTAIELDGETIGLANRGTMCDPKLSTGIVQDHSAINLWVAVTMAHEMGHNLGISHDGNQCHCDANSCIMSEELRQQLSFEFSDCSQNQYQTFLTDHNPQCMLNEPLRTDIVSTPVSGNELWETGEESDFDAPANPCCDAATCKLTPGSQCAEGLCCDQCKFMKEGTVCHRAKGDDLDDYCNGISAGCPRNPFHA |
Enzyme Length | 483 |
Uniprot Accession Number | Q805F4 |
Absorption | |
Active Site | ACT_SITE 335; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.24.- |
Enzyme Function | FUNCTION: [Snake venom metalloproteinase]: Impairs hemostasis in the envenomed animal. {ECO:0000250}.; FUNCTION: [Disintegrin piscivostatin-beta]: Inhibits platelet aggregation induced by ADP. Acts by inhibiting fibrinogen interaction with platelet receptors GPIIb/GPIIIa (ITGA2B/ITGB3). Also inhibits platelet aggregate dissociation in human platelet-rich plasma. {ECO:0000269|PubMed:11530017}. |
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); Signal peptide (1) |
Keywords | Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;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. |
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 | 54,073 |
Kinetics | |
Metal Binding | METAL 201; /note=Calcium; /evidence=ECO:0000250; METAL 285; /note=Calcium; /evidence=ECO:0000250; METAL 334; /note=Zinc; catalytic; METAL 338; /note=Zinc; catalytic; METAL 344; /note=Zinc; catalytic; METAL 389; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 392; /note=Calcium; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |