| IED ID | IndEnz0002006126 |
| Enzyme Type ID | protease006126 |
| Protein Name |
Phospholipase A2 taicatoxin TCX svPLA2 EC 3.1.1.4 Phosphatidylcholine 2-acylhydrolase Fragment |
| Gene Name | |
| Organism | Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan) |
| 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 Elapidae Acanthophiinae Oxyuranus Oxyuranus scutellatus (Coastal taipan) Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan) |
| Enzyme Sequence | NLAQFGFMIRCANGGSRSALDYADYGC |
| Enzyme Length | 27 |
| Uniprot Accession Number | Q7LZG2 |
| Absorption | |
| Active Site | |
| 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}; |
| DNA Binding | |
| EC Number | 3.1.1.4 |
| Enzyme Function | FUNCTION: Heterotrimer: blocks the voltage-dependent L-type calcium channels from the heart, and the small conductance calcium-activated potassium channels in the chromaffin cells and in the brain. Is very toxic to mice.; FUNCTION: Monomer: Snake venom phospholipase A2 (PLA2) that has neurotoxic activities. Voltage-dependently affects ionic currents in chick (Gallus domesticus) dorsal root ganglion cells. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Non-terminal residue (2) |
| Keywords | Calcium;Calcium-activated potassium channel impairing toxin;Direct protein sequencing;Disulfide bond;Hydrolase;Ion channel impairing toxin;Lipid degradation;Lipid metabolism;Metal-binding;Neurotoxin;Potassium channel impairing toxin;Secreted;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1373076, ECO:0000269|PubMed:1485334}. |
| Modified Residue | |
| Post Translational Modification | PTM: Contains 7 disulfide bonds. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 2,901 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:15801 |
| Cross Reference Brenda |