IED ID | IndEnz0002012906 |
Enzyme Type ID | protease012906 |
Protein Name |
Acidic phospholipase A2 Vur-PL3 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 | MRTLWIVAVCLIGVEGNLFQFGKMIKYKTGKSALLSYSAYGCYCGWGGQGKPQDPTDRCCFVHDCCYGRVNGCNPKMDTYSYSFLNGDIVCGDDDPCLRAICECDRAAAICFGENVNTYDKKYKYYSSSHCTETEQC |
Enzyme Length | 137 |
Uniprot Accession Number | F8QN51 |
Absorption | |
Active Site | ACT_SITE 63; /evidence=ECO:0000250; ACT_SITE 105; /evidence=ECO:0000250 |
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 | |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Disulfide bond (7); Metal binding (4); Signal peptide (1) |
Keywords | Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Secreted;Signal;Toxin |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..16 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 15,318 |
Kinetics | |
Metal Binding | METAL 43; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 45; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 47; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 64; /note=Calcium; /evidence=ECO:0000250 |
Rhea ID | RHEA:15801 |
Cross Reference Brenda |