| IED ID | IndEnz0005000788 |
| Enzyme Type ID | lipase000788 |
| Protein Name |
Platelet-activating factor acetylhydrolase PAF acetylhydrolase EC 3.1.1.47 1-alkyl-2-acetylglycerophosphocholine esterase 2-acetyl-1-alkylglycerophosphocholine esterase LDL-associated phospholipase A2 LDL-PLA 2 PAF 2-acylhydrolase |
| Gene Name | PLA2G7 |
| Organism | Gallus gallus (Chicken) |
| 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) Archelosauria Archosauria Dinosauria Saurischia Theropoda Coelurosauria Aves Neognathae Galloanserae Galliformes Phasianidae (turkeys) Phasianinae Gallus Gallus gallus (Chicken) |
| Enzyme Sequence | MASLWVRARRVFMKSRASGFSAKAATEMGSGGAEKGYRIPAGKGPHAVGCTDLMTGDAAEGSFLRLYYLSCDDTDTEETPWIPDKEYYQGLSDFLNVYRALGERLFQYYVGSVTCPAKSNAAFKPGEKYPLLVFSHGLGAFRTIYSAICIEMASQGFLVAAVEHRDESASATYFCKKKADSEPEEDQTSGVEKEWIYYRKLRAGEEERCLRHKQVQQRAQECIKALNLILKISSGEEVMNVLNSDFDWNHLKDSVDTSRIAVMGHSFGGATVIESLSKEIRFRCGIALDAWMLPVGDDTYQSSVQQPLLFINSEKFQWAANILKMKKLSSNDTNKKMITIKGSVHQSFPDFTFVSGEIIGKFFKLKGEIDPNEAIDICNHASLAFLQKHLSLKRDFDKWDSLVDGIGPNVISGTNIDLSPTE |
| Enzyme Length | 422 |
| Uniprot Accession Number | Q90678 |
| Absorption | |
| Active Site | ACT_SITE 266; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 289; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 345; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycero-3-phosphocholine + acetate + H(+); Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47; |
| DNA Binding | |
| EC Number | 3.1.1.47 |
| Enzyme Function | FUNCTION: Modulates the action of platelet-activating factor (PAF) by hydrolyzing the sn-2 ester bond to yield the biologically inactive lyso-PAF. Has a specificity for substrates with a short residue at the sn-2 position. It is inactive against long-chain phospholipids. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Glycosylation (1); Signal peptide (1) |
| Keywords | Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 47,046 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:17777 |
| Cross Reference Brenda |