PLAT3_PONAB
ID PLAT3_PONAB Reviewed; 162 AA.
AC Q5R611;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Phospholipase A and acyltransferase 3 {ECO:0000250|UniProtKB:P53816};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:P53816};
DE EC=3.1.1.32 {ECO:0000250|UniProtKB:P53816};
DE EC=3.1.1.4 {ECO:0000250|UniProtKB:P53816};
DE AltName: Full=Group XVI phospholipase A2 {ECO:0000250|UniProtKB:P53816};
DE AltName: Full=H-rev 107 protein homolog {ECO:0000250|UniProtKB:P53816};
DE AltName: Full=HRAS-like suppressor 3 {ECO:0000250|UniProtKB:P53816};
DE Short=HRSL3 {ECO:0000250|UniProtKB:P53816};
GN Name=PLAAT3 {ECO:0000250|UniProtKB:P53816};
GN Synonyms=HRASLS3 {ECO:0000250|UniProtKB:P53816},
GN HREV107 {ECO:0000250|UniProtKB:P53816},
GN PLA2G16 {ECO:0000250|UniProtKB:P53816};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Exhibits both phospholipase A1/2 and acyltransferase
CC activities (By similarity). Shows phospholipase A1 (PLA1) and A2
CC (PLA2), catalyzing the calcium-independent release of fatty acids from
CC the sn-1 or sn-2 position of glycerophospholipids (By similarity). For
CC most substrates, PLA1 activity is much higher than PLA2 activity (By
CC similarity). Shows O-acyltransferase activity, catalyzing the transfer
CC of a fatty acyl group from glycerophospholipid to the hydroxyl group of
CC lysophospholipid (By similarity). Shows N-acyltransferase activity,
CC catalyzing the calcium-independent transfer of a fatty acyl group at
CC the sn-1 position of phosphatidylcholine (PC) and other
CC glycerophospholipids to the primary amine of phosphatidylethanolamine
CC (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as
CC precursor for N-acylethanolamines (NAEs) (By similarity). Exhibits high
CC N-acyltransferase activity and low phospholipase A1/2 activity (By
CC similarity). Required for complete organelle rupture and degradation
CC that occur during eye lens terminal differentiation, when fiber cells
CC that compose the lens degrade all membrane-bound organelles in order to
CC provide lens with transparency to allow the passage of light. Organelle
CC membrane degradation is probably catalyzed by the phospholipase
CC activity (By similarity). {ECO:0000250|UniProtKB:P53816,
CC ECO:0000250|UniProtKB:Q8R3U1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 2-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:40487, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72999, ChEBI:CHEBI:76078;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40488;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:38783, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73001,
CC ChEBI:CHEBI:76071; Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38784;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73001; Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:40571, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73003, ChEBI:CHEBI:76079;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40572;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + H2O = 2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-
CC phosphoethanolamine + H(+) + hexadecanoate; Xref=Rhea:RHEA:45164,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:73008, ChEBI:CHEBI:76090;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45165;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phosphoethanolamine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41348, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73009, ChEBI:CHEBI:76091;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41349;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexanoyl-2-acyl-sn-glycero-3-phosphocholine + H2O = a 2-
CC acyl-sn-glycero-3-phosphocholine + H(+) + hexanoate;
CC Xref=Rhea:RHEA:53496, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17120, ChEBI:CHEBI:57875, ChEBI:CHEBI:137403;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53497;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexanoyl-2-acyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexanoyl-sn-glycero-3-phosphocholine + a fatty acid + H(+);
CC Xref=Rhea:RHEA:53500, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:78215, ChEBI:CHEBI:137403;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53501;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diheptadecanoyl-sn-glycero-3-phosphoethanolamine + 1-(9Z-
CC octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine = 1,2-
CC diheptadecanoyl-sn-glycero-3-phospho-N-hexadecanoyl-ethanolamine + 1-
CC (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:53524, ChEBI:CHEBI:15378, ChEBI:CHEBI:28610,
CC ChEBI:CHEBI:74667, ChEBI:CHEBI:138218, ChEBI:CHEBI:138220;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53525;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diheptadecanoyl-sn-glycero-3-phosphoethanolamine + 1-(9Z-
CC octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine = 1,2-
CC diheptadecanoyl-sn-glycero-3-phospho-N-(9Z-octadecenoyl)-ethanolamine
CC + 2-hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:53528, ChEBI:CHEBI:15378, ChEBI:CHEBI:74667,
CC ChEBI:CHEBI:76078, ChEBI:CHEBI:138218, ChEBI:CHEBI:138222;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53529;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine + 2-heptanoyl-
CC sn-glycero-3-phosphocholine = 1-hexanoyl-2-heptanoyl-sn-glycero-3-
CC phosphocholine + hexanoyl-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:54544, ChEBI:CHEBI:138197, ChEBI:CHEBI:138216,
CC ChEBI:CHEBI:138266, ChEBI:CHEBI:138267;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54545;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-octadecanoyl-sn-glycero-3-phosphocholine +
CC H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) +
CC octadecanoate; Xref=Rhea:RHEA:56432, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73000; Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56433;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-octadecanoyl-sn-glycero-3-phosphocholine +
CC H2O = 2-octadecanoyl-sn-glycero-3-phosphocholine + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:56436, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73000,
CC ChEBI:CHEBI:76076; Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56437;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine +
CC H2O = 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:56440, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73858,
CC ChEBI:CHEBI:75026; Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56441;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine +
CC H2O = 2-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) +
CC octadecanoate; Xref=Rhea:RHEA:56444, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:75026,
CC ChEBI:CHEBI:76078; Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56445;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-
CC glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H2O = 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:40971,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:73002, ChEBI:CHEBI:76084;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40972;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O =
CC (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H(+); Xref=Rhea:RHEA:56448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76071;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56449;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + hexadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:41384, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41385;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O =
CC (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H(+); Xref=Rhea:RHEA:40923, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28610, ChEBI:CHEBI:30823, ChEBI:CHEBI:74669;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40924;
CC Evidence={ECO:0000250|UniProtKB:P53816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine +
CC 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine = H(+) + hexadecanoyl-
CC sn-glycero-3-phosphocholine + N-hexadecanoyl-1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:41360,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999,
CC ChEBI:CHEBI:74986, ChEBI:CHEBI:78097;
CC Evidence={ECO:0000250|UniProtKB:P53817};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41361;
CC Evidence={ECO:0000250|UniProtKB:P53817};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine +
CC H2O = (9Z,12Z)-octadecadienoate + 1-(9Z,12Z)-octadecadienoyl-sn-
CC glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:56428,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28733,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:42027;
CC Evidence={ECO:0000250|UniProtKB:Q8R3U1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56429;
CC Evidence={ECO:0000250|UniProtKB:Q8R3U1};
CC -!- SUBUNIT: Interacts with PPP2R1A; this interaction might decrease PP2A
CC activity. {ECO:0000250|UniProtKB:P53816}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P53817};
CC Single-pass membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000250|UniProtKB:P53816}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q8R3U1}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q8R3U1}. Peroxisome membrane
CC {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein
CC {ECO:0000305}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q8R3U1};
CC Single-pass membrane protein {ECO:0000305}. Nucleus envelope
CC {ECO:0000250|UniProtKB:Q8R3U1}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein
CC {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein
CC {ECO:0000305}. Note=During eye lens differentiation, recruited from the
CC cytosol to various organelles, including mitochondria, endoplasmic
CC reticulum, nuclear envelope and lysosomes, immediately before organelle
CC degradation. This translocation is triggered by organelle membrane
CC damage and requires the C-terminal transmembrane domain.
CC {ECO:0000250|UniProtKB:Q8R3U1}.
CC -!- DOMAIN: The C-terminal transmembrane domain is required for the
CC targeting of the protein to damaged organelles.
CC {ECO:0000250|UniProtKB:Q8R3U1}.
CC -!- SIMILARITY: Belongs to the H-rev107 family. {ECO:0000305}.
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DR EMBL; CR860689; CAH92805.1; -; mRNA.
DR RefSeq; NP_001128980.1; NM_001135508.1.
DR AlphaFoldDB; Q5R611; -.
DR BMRB; Q5R611; -.
DR SMR; Q5R611; -.
DR STRING; 9601.ENSPPYP00000004679; -.
DR GeneID; 100190820; -.
DR KEGG; pon:100190820; -.
DR CTD; 11145; -.
DR eggNOG; ENOG502S0JN; Eukaryota.
DR InParanoid; Q5R611; -.
DR OrthoDB; 1602481at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016410; F:N-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; ISS:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; ISS:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; ISS:UniProtKB.
DR GO; GO:0046485; P:ether lipid metabolic process; ISS:UniProtKB.
DR GO; GO:0070306; P:lens fiber cell differentiation; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; ISS:UniProtKB.
DR GO; GO:0030397; P:membrane disassembly; ISS:UniProtKB.
DR GO; GO:0070292; P:N-acylphosphatidylethanolamine metabolic process; ISS:UniProtKB.
DR GO; GO:1903008; P:organelle disassembly; ISS:UniProtKB.
DR GO; GO:0007031; P:peroxisome organization; ISS:UniProtKB.
DR GO; GO:1904177; P:regulation of adipose tissue development; ISS:UniProtKB.
DR GO; GO:0006641; P:triglyceride metabolic process; ISS:UniProtKB.
DR InterPro; IPR007053; LRAT_dom.
DR Pfam; PF04970; LRAT; 1.
DR PROSITE; PS51934; LRAT; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Endoplasmic reticulum; Hydrolase;
KW Lipid degradation; Lipid metabolism; Lysosome; Membrane; Mitochondrion;
KW Nucleus; Peroxisome; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..162
FT /note="Phospholipase A and acyltransferase 3"
FT /id="PRO_0000152486"
FT TOPO_DOM 1..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..162
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 13..129
FT /note="LRAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT ACT_SITE 23
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT ACT_SITE 35
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT ACT_SITE 113
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P53816,
FT ECO:0000255|PROSITE-ProRule:PRU01283"
SQ SEQUENCE 162 AA; 17909 MW; C402BFC756A6DA24 CRC64;
MRAPIPEPKP GDLIEIFRPF YRHWAIYVGD GYVVHLAPPS EVAGAGAASV MSALTDKAIV
KKELLYDVAG SDKYQVNNKH DDKYSPLPCS KIIQRAEELV GQEVLYKLTS ENCEHFVNEL
RYGVARSDQV RDVIIAASAA GMGLAAMSLI GVMFSRNKRQ KQ
