Detail Information for IndEnz0002012906
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