| IED ID | IndEnz0002012780 |
| Enzyme Type ID | protease012780 |
| Protein Name |
Basic phospholipase A2 vurtoxin svPLA2 EC 3.1.1.4 Phosphatidylcholine 2-acylhydrolase |
| Gene Name | |
| Organism | Vipera renardi (Steppe viper) (Vipera ursinii renardi) |
| 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 Viperinae (vipers) Vipera Vipera renardi (Steppe viper) (Vipera ursinii renardi) |
| Enzyme Sequence | MRTLWIVAVCLIGVEGSLLEFGMMILEETGKNPLTSYSFYGCYCGVGGKGTPKDATDRCCFVHDCCYGNLPDCNPKIDRYKYHRKNGAIVCGKGTSCENRICECDRAAAICFRKNLKTYNHIYKYYPDFLCKKESEKC |
| Enzyme Length | 138 |
| Uniprot Accession Number | F8QN54 |
| Absorption | |
| Active Site | ACT_SITE 63; /evidence=ECO:0000250|UniProtKB:P14418; ACT_SITE 105; /evidence=ECO:0000250|UniProtKB:P14418 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036, ECO:0000269|PubMed:25522251}; |
| DNA Binding | |
| EC Number | 3.1.1.4 |
| Enzyme Function | FUNCTION: Snake venom phospholipase A2 that may have a strong anticoagulant activity (PubMed:21185324). Is able to suppress the acetylcholine (ACh)-evoked current mediated by alpha-7-similar nAChRs in L.stagnalis neurons (IC(50)=10.5 uM) and to compete with alpha-bungarotoxin for binding to muscle- and alpha-7 neuronal nAChR types, as well as to AChBPs (PubMed:25522251). In inhibition of alpha-bungarotoxin binding, this toxin is mostly active against T.californica nAChR (IC(50)=0.26 uM), it is moderately active against human alpha-7 nAChR (IC(50)=14 uM), and is not active against L.stagnalis and A.californica AChBP (IC(50)>30 uM) (PubMed:25522251). {ECO:0000269|PubMed:21185324, ECO:0000269|PubMed:25522251}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (7); Metal binding (4); Signal peptide (1) |
| Keywords | Acetylcholine receptor inhibiting toxin;Blood coagulation cascade inhibiting toxin;Disulfide bond;Hemostasis impairing toxin;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Neurotoxin;Postsynaptic neurotoxin;Secreted;Signal;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21185324}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000269|PubMed:21185324 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 15,636 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=0.7 mmol/min/umol enzyme {ECO:0000269|PubMed:25522251}; |
| Metal Binding | METAL 43; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P59071; METAL 45; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P59071; METAL 47; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P59071; METAL 64; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P59071 |
| Rhea ID | RHEA:15801 |
| Cross Reference Brenda |