PLAT3_RAT
ID PLAT3_RAT Reviewed; 160 AA.
AC P53817; B7X6T2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Phospholipase A and acyltransferase 3 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:17158102, ECO:0000269|PubMed:19047760};
DE EC=3.1.1.32 {ECO:0000269|PubMed:19047760};
DE EC=3.1.1.4 {ECO:0000269|PubMed:19047760};
DE AltName: Full=Group XVI phospholipase A2 {ECO:0000312|RGD:2829};
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};
DE AltName: Full=Rat LRAT-like protein-3 {ECO:0000303|PubMed:17158102};
DE Short=RLP-3 {ECO:0000303|PubMed:17158102};
GN Name=Plaat3 {ECO:0000312|RGD:2829};
GN Synonyms=H-rev107 {ECO:0000250|UniProtKB:P53816},
GN Hrasls3 {ECO:0000250|UniProtKB:P53816},
GN Hrev107 {ECO:0000250|UniProtKB:P53816}, Pla2g16 {ECO:0000312|RGD:2829},
GN Rlp-3 {ECO:0000303|PubMed:17158102};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8290259;
RA Hajnal A., Klemenz R., Schaefer R.;
RT "Subtraction cloning of H-rev107, a gene specifically expressed in H-ras
RT resistant fibroblasts.";
RL Oncogene 9:479-490(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Morishita J., Okamoto Y., Jin X.H., Tsuboi K., Ueda N.;
RT "Purification and characterization of LRAT-like protein 3.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17158102; DOI=10.1074/jbc.m606369200;
RA Jin X.H., Okamoto Y., Morishita J., Tsuboi K., Tonai T., Ueda N.;
RT "Discovery and characterization of a Ca2+-independent
RT phosphatidylethanolamine N-acyltransferase generating the anandamide
RT precursor and its congeners.";
RL J. Biol. Chem. 282:3614-3623(2007).
RN [5]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=18614531; DOI=10.1074/jbc.m804146200;
RA Duncan R.E., Sarkadi-Nagy E., Jaworski K., Ahmadian M., Sul H.S.;
RT "Identification and functional characterization of adipose-specific
RT phospholipase A2 (AdPLA).";
RL J. Biol. Chem. 283:25428-25436(2008).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-21 AND CYS-111.
RX PubMed=19047760; DOI=10.1194/jlr.m800453-jlr200;
RA Uyama T., Morishita J., Jin X.H., Okamoto Y., Tsuboi K., Ueda N.;
RT "The tumor suppressor gene H-Rev107 functions as a novel Ca2+-independent
RT cytosolic phospholipase A1/2 of the thiol hydrolase type.";
RL J. Lipid Res. 50:685-693(2009).
CC -!- FUNCTION: Exhibits both phospholipase A1/2 and acyltransferase
CC activities (PubMed:19047760). Shows phospholipase A1 (PLA1) and A2
CC (PLA2), ccatalyzing the calcium-independent release of fatty acids from
CC the sn-1 or sn-2 position of glycerophospholipids (PubMed:19047760).
CC For most substrates, PLA1 activity is much higher than PLA2 activity
CC (By similarity). Shows O-acyltransferase activity,catalyzing the
CC transfer of a fatty acyl group from glycerophospholipid to the hydroxyl
CC group of lysophospholipid (By similarity). Shows N-acyltransferase
CC activity, catalyzing the calcium-independent transfer of a fatty acyl
CC group at 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) (PubMed:17158102,
CC PubMed:19047760). Exhibits high N-acyltransferase activity and low
CC phospholipase A1/2 activity (By similarity). Required for complete
CC organelle rupture and degradation that occur during eye lens terminal
CC differentiation, when fiber cells that compose the lens degrade all
CC membrane-bound organelles in order to provide lens with transparency to
CC allow the passage of light. Organelle membrane degradation is probably
CC catalyzed by the phospholipase activity (By similarity).
CC {ECO:0000250|UniProtKB:P53816, ECO:0000250|UniProtKB:Q8R3U1,
CC ECO:0000269|PubMed:17158102, ECO:0000269|PubMed:19047760}.
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:0000269|PubMed:19047760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000269|PubMed:19047760};
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:0000269|PubMed:19047760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690;
CC Evidence={ECO:0000269|PubMed:19047760};
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:0000269|PubMed:19047760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000269|PubMed:19047760};
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:0000269|PubMed:19047760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40488;
CC Evidence={ECO:0000269|PubMed:19047760};
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:0000269|PubMed:19047760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38784;
CC Evidence={ECO:0000269|PubMed:19047760};
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:0000269|PubMed:19047760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000269|PubMed:19047760};
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:0000269|PubMed:19047760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000269|PubMed:19047760};
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:0000269|PubMed:19047760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40572;
CC Evidence={ECO:0000269|PubMed:19047760};
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:0000269|PubMed:19047760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000269|PubMed:19047760};
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:0000269|PubMed:19047760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45165;
CC Evidence={ECO:0000269|PubMed:19047760};
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:0000269|PubMed:19047760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000269|PubMed:19047760};
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:0000269|PubMed:19047760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41349;
CC Evidence={ECO:0000269|PubMed:19047760};
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:0000269|PubMed:17158102};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41361;
CC Evidence={ECO:0000269|PubMed:17158102};
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:0000269|PubMed:8290259};
CC Single-pass membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000269|PubMed:8290259}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q8R3U1}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:8290259}. Peroxisome membrane
CC {ECO:0000250|UniProtKB:Q8R3U1}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein
CC {ECO:0000305}. Nucleus envelope {ECO:0000250|UniProtKB:Q8R3U1}.
CC Lysosome membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane
CC protein {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 -!- TISSUE SPECIFICITY: Specifically expressed in H-ras resistant
CC fibroblasts. {ECO:0000269|PubMed:18614531, ECO:0000269|PubMed:8290259}.
CC -!- INDUCTION: Induced during preadipocyte differentiation into adipocytes.
CC {ECO:0000269|PubMed:18614531}.
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; X76453; CAA53991.1; -; mRNA.
DR EMBL; AB298805; BAH08634.1; -; mRNA.
DR EMBL; CH473953; EDM12684.1; -; Genomic_DNA.
DR EMBL; CH473953; EDM12685.1; -; Genomic_DNA.
DR PIR; S42794; S42794.
DR RefSeq; NP_058756.2; NM_017060.2.
DR AlphaFoldDB; P53817; -.
DR SMR; P53817; -.
DR STRING; 10116.ENSRNOP00000038045; -.
DR SwissLipids; SLP:000001906; -.
DR PhosphoSitePlus; P53817; -.
DR PaxDb; P53817; -.
DR GeneID; 24913; -.
DR KEGG; rno:24913; -.
DR UCSC; RGD:2829; rat.
DR CTD; 11145; -.
DR RGD; 2829; Plaat3.
DR VEuPathDB; HostDB:ENSRNOG00000021206; -.
DR eggNOG; ENOG502S0JN; Eukaryota.
DR InParanoid; P53817; -.
DR OMA; VRDAIMV; -.
DR OrthoDB; 1602481at2759; -.
DR PhylomeDB; P53817; -.
DR TreeFam; TF330836; -.
DR BRENDA; 3.1.1.32; 5301.
DR Reactome; R-RNO-1482788; Acyl chain remodelling of PC.
DR Reactome; R-RNO-1482801; Acyl chain remodelling of PS.
DR Reactome; R-RNO-1482839; Acyl chain remodelling of PE.
DR Reactome; R-RNO-1482922; Acyl chain remodelling of PI.
DR PRO; PR:P53817; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000021206; Expressed in duodenum and 20 other tissues.
DR ExpressionAtlas; P53817; baseline and differential.
DR Genevisible; P53817; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
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:0016020; C:membrane; IDA:RGD.
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; ISO:RGD.
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; IDA:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; ISO:RGD.
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:0045786; P:negative regulation of cell cycle; IMP:RGD.
DR GO; GO:1903008; P:organelle disassembly; ISS:UniProtKB.
DR GO; GO:0007031; P:peroxisome organization; ISS:UniProtKB.
DR GO; GO:0008654; P:phospholipid biosynthetic process; ISO:RGD.
DR GO; GO:0006644; P:phospholipid metabolic process; ISO:RGD.
DR GO; GO:1904177; P:regulation of adipose tissue development; ISS:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
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 1: Evidence at protein 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..160
FT /note="Phospholipase A and acyltransferase 3"
FT /id="PRO_0000152487"
FT TOPO_DOM 1..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..160
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 11..127
FT /note="LRAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT ACT_SITE 21
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283,
FT ECO:0000305|PubMed:19047760"
FT ACT_SITE 33
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT ACT_SITE 111
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283,
FT ECO:0000305|PubMed:19047760"
FT MUTAGEN 21
FT /note="H->L: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:19047760"
FT MUTAGEN 111
FT /note="C->S: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:19047760"
FT CONFLICT 131
FT /note="A -> T (in Ref. 1; CAA53991)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 160 AA; 17749 MW; A0B32D6FA0A943A3 CRC64;
MPIPEPKPGD LIEIFRPMYS HWAIYVGDGY VIHLAPPSEI PGAGAASIMS ALTDKAIVKK
ELLRDVAGKD KYQVNNKHDK EYTPLPLNKI IQRAEELVGQ EVLYRLTSEN CEHFVNELRY
GVPRSDQVRD AVKVATVTGV GLAALGLIGV MLSRNKKQKQ
