ID  Q5R611;
PN  Phospholipase A and acyltransferase 3;
GN  PLAAT3;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P53817}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P53816}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8R3U1}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8R3U1}. Peroxisome membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein {ECO:0000305}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250|UniProtKB:Q8R3U1}. Lysosome membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein {ECO:0000305}. Note=During eye lens differentiation, recruited from the cytosol to various organelles, including mitochondria, endoplasmic reticulum, nuclear envelope and lysosomes, immediately before organelle degradation. This translocation is triggered by organelle membrane damage and requires the C-terminal transmembrane domain. {ECO:0000250|UniProtKB:Q8R3U1}.
DR  UNIPROT: Q5R611;
DR  Pfam: PF04970;
DR  PROSITE: PS51934;
DE  Function: Exhibits both phospholipase A1/2 and acyltransferase activities (By similarity). Shows phospholipase A1 (PLA1) and A2 (PLA2), catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (By similarity). For most substrates, PLA1 activity is much higher than PLA2 activity (By similarity). Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (By similarity). Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) (By similarity). Exhibits high N-acyltransferase activity and low phospholipase A1/2 activity (By similarity). Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light. Organelle membrane degradation is probably catalyzed by the phospholipase activity (By similarity). {ECO:0000250|UniProtKB:P53816, ECO:0000250|UniProtKB:Q8R3U1}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005765;
GO  GO:0005764;
GO  GO:0031966;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0005778;
GO  GO:0005777;
GO  GO:0005886;
GO  GO:0052740;
GO  GO:0016410;
GO  GO:0052739;
GO  GO:0008970;
GO  GO:0004623;
GO  GO:0004620;
GO  GO:0046485;
GO  GO:0070306;
GO  GO:0016042;
GO  GO:0030397;
GO  GO:0070292;
GO  GO:1903008;
GO  GO:0007031;
GO  GO:1904177;
GO  GO:0006641;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRAPIPEPKPGDLIEIFRPFYRHWAIYVGDGYVVHLAPPSEVAGAGAASVMSALTDKAIVKKELLYDVAGSDKYQVNNKH
SQ  DDKYSPLPCSKIIQRAEELVGQEVLYKLTSENCEHFVNELRYGVARSDQVRDVIIAASAAGMGLAAMSLIGVMFSRNKRQ
SQ  KQ
//