PAG15_MOUSE
ID PAG15_MOUSE Reviewed; 412 AA.
AC Q8VEB4; Q3TCB1; Q3U303;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Phospholipase A2 group XV;
DE AltName: Full=1-O-acylceramide synthase {ECO:0000303|PubMed:11790796};
DE Short=ACS;
DE AltName: Full=LCAT-like lysophospholipase;
DE Short=LLPL;
DE EC=3.1.1.5 {ECO:0000250|UniProtKB:Q8NCC3};
DE AltName: Full=Lysophospholipase 3;
DE AltName: Full=Lysosomal phospholipase A and acyltransferase;
DE EC=2.3.1.- {ECO:0000269|PubMed:11790796, ECO:0000269|PubMed:16106046, ECO:0000269|PubMed:16837646, ECO:0000269|PubMed:16880524, ECO:0000269|PubMed:19017977, ECO:0000269|PubMed:20410020, ECO:0000269|PubMed:27993948};
DE EC=3.1.1.32 {ECO:0000269|PubMed:16837646, ECO:0000269|PubMed:27993948};
DE EC=3.1.1.4 {ECO:0000269|PubMed:16837646};
DE AltName: Full=Lysosomal phospholipase A2 {ECO:0000303|PubMed:11790796, ECO:0000303|PubMed:16106046};
DE Short=LPLA2 {ECO:0000303|PubMed:16106046};
DE Flags: Precursor;
GN Name=Pla2g15 {ECO:0000312|MGI:MGI:2178076}; Synonyms=Lypla3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF SER-198, AND GLYCOSYLATION.
RC STRAIN=129/Sv, and C57BL/6J; TISSUE=Kidney;
RX PubMed=11790796; DOI=10.1074/jbc.m111977200;
RA Hiraoka M., Abe A., Shayman J.A.;
RT "Cloning and characterization of a lysosomal phospholipase A2, 1-O-
RT acylceramide synthase.";
RL J. Biol. Chem. 277:10090-10099(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Embryonic stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, DISULFIDE BOND, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF CYS-65; CYS-89; SER-198; ASP-360 AND
RP HIS-392.
RX PubMed=16106046; DOI=10.1194/jlr.m500248-jlr200;
RA Hiraoka M., Abe A., Shayman J.A.;
RT "Structure and function of lysosomal phospholipase A2: identification of
RT the catalytic triad and the role of cysteine residues.";
RL J. Lipid Res. 46:2441-2447(2005).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=16837646; DOI=10.1194/jlr.m600183-jlr200;
RA Abe A., Hiraoka M., Shayman J.A.;
RT "Positional specificity of lysosomal phospholipase A2.";
RL J. Lipid Res. 47:2268-2279(2006).
RN [6]
RP DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=16880524; DOI=10.1128/mcb.00627-06;
RA Hiraoka M., Abe A., Lu Y., Yang K., Han X., Gross R.W., Shayman J.A.;
RT "Lysosomal phospholipase A2 and phospholipidosis.";
RL Mol. Cell. Biol. 26:6139-6148(2006).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17626977; DOI=10.1194/jlr.m700277-jlr200;
RA Abe A., Hiraoka M., Shayman J.A.;
RT "The acylation of lipophilic alcohols by lysosomal phospholipase A2.";
RL J. Lipid Res. 48:2255-2263(2007).
RN [8]
RP SUBCELLULAR LOCATION, FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=19017977; DOI=10.4049/jimmunol.181.11.7873;
RA Abe A., Kelly R., Kollmeyer J., Hiraoka M., Lu Y., Shayman J.A.;
RT "The secretion and uptake of lysosomal phospholipase A2 by alveolar
RT macrophages.";
RL J. Immunol. 181:7873-7881(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20410020; DOI=10.1194/jlr.d007146;
RA Abe A., Kelly R., Shayman J.A.;
RT "The measurement of lysosomal phospholipase A2 activity in plasma.";
RL J. Lipid Res. 51:2464-2470(2010).
RN [11]
RP FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=27993948; DOI=10.1194/jlr.m070730;
RA Abe A., Hiraoka M., Ohguro H., Tesmer J.J., Shayman J.A.;
RT "Preferential hydrolysis of truncated oxidized glycerophospholipids by
RT lysosomal phospholipase A2.";
RL J. Lipid Res. 58:339-349(2017).
CC -!- FUNCTION: Has dual calcium-independent phospholipase and O-
CC acyltransferase activities with a potential role in glycerophospholipid
CC homeostasis and remodeling of acyl groups of lipophilic alcohols
CC present in acidic cellular compartments (PubMed:16837646,
CC PubMed:17626977, PubMed:11790796, PubMed:16106046, PubMed:16880524,
CC PubMed:19017977, PubMed:20410020). Catalyzes hydrolysis of the ester
CC bond of the fatty acyl group attached at sn-1 or sn-2 position of
CC phospholipids (phospholipase A1 or A2 activity) and transfer it to the
CC hydroxyl group at the first carbon of lipophilic alcohols (O-
CC acyltransferase activity). Among preferred fatty acyl donors are
CC phosphatidylcholines, phosphatidylethanolamines, phosphatidylglycerols
CC and phosphatidylserines (PubMed:20410020). Favors sn-2 over sn-1
CC deacylation of unsaturated fatty acyl groups of phosphatidylcholines
CC and phosphatidylethanolamines (PubMed:16837646, PubMed:17626977). Among
CC preferred fatty acyl acceptors are natural lipophilic alcohols
CC including short-chain ceramide N-acetyl-sphingosine (C2 ceramide),
CC alkylacylglycerols, monoacylglycerols, and acylethanolamides such as
CC anandamide and oleoylethanolamide (PubMed:16837646, PubMed:17626977).
CC Selectively hydrolyzes the sn-1 fatty acyl group of truncated oxidized
CC phospholipids and may play a role in detoxification of reactive
CC oxidized phospholipids during oxidative stress (PubMed:27993948).
CC Required for normal phospholipid degradation in alveolar macrophages
CC with potential implications in pulmonary surfactant clearance
CC (PubMed:16880524, PubMed:19017977). At neutral pH, hydrolyzes the sn-1
CC fatty acyl group of the lysophosphatidylcholines (By similarity).
CC {ECO:0000250|UniProtKB:Q8NCC3, ECO:0000269|PubMed:11790796,
CC ECO:0000269|PubMed:16106046, ECO:0000269|PubMed:16837646,
CC ECO:0000269|PubMed:16880524, ECO:0000269|PubMed:17626977,
CC ECO:0000269|PubMed:19017977, ECO:0000269|PubMed:20410020,
CC ECO:0000269|PubMed:27993948}.
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:27993948};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690;
CC Evidence={ECO:0000305|PubMed:27993948};
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:16837646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38784;
CC Evidence={ECO:0000305|PubMed:16837646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-glutaroyl-sn-glycero-3-phosphocholine + H2O =
CC 2-glutaroyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:62480, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:77756, ChEBI:CHEBI:145781;
CC Evidence={ECO:0000269|PubMed:27993948};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62481;
CC Evidence={ECO:0000305|PubMed:27993948};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-nonadioyl-sn-glycero-3-phosphocholine + H2O =
CC 2-nonadioyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:62464, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:78207, ChEBI:CHEBI:145780;
CC Evidence={ECO:0000269|PubMed:27993948};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62465;
CC Evidence={ECO:0000305|PubMed:27993948};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine
CC + H2O = 2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:62484, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:77890,
CC ChEBI:CHEBI:145782; Evidence={ECO:0000269|PubMed:27993948};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62485;
CC Evidence={ECO:0000305|PubMed:27993948};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9-oxononanoyl)-sn-glycero-3-phosphocholine +
CC H2O = 2-(9-oxononanoyl)-sn-glycero-3-phosphocholine + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:62488, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:61042,
CC ChEBI:CHEBI:145783; Evidence={ECO:0000269|PubMed:27993948};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62489;
CC Evidence={ECO:0000305|PubMed:27993948};
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:27993948};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:27993948};
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:16837646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000305|PubMed:16837646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC Evidence={ECO:0000250|UniProtKB:Q8NCC3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC Evidence={ECO:0000250|UniProtKB:Q8NCC3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000250|UniProtKB:Q8NCC3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000250|UniProtKB:Q8NCC3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N-
CC (acetyl)-sphing-4-enine + 2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine; Xref=Rhea:RHEA:38827, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:73007, ChEBI:CHEBI:76077, ChEBI:CHEBI:76088;
CC Evidence={ECO:0000269|PubMed:16837646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38828;
CC Evidence={ECO:0000305|PubMed:16837646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1-(9Z-
CC octadecenoyl)-N-(acetyl)-sphing-4-enine + 1-hexadecanoyl-sn-glycero-
CC 3-phosphoethanolamine; Xref=Rhea:RHEA:38823, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:73004, ChEBI:CHEBI:73007, ChEBI:CHEBI:76054;
CC Evidence={ECO:0000269|PubMed:16837646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38824;
CC Evidence={ECO:0000305|PubMed:16837646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N-
CC (acetyl)-sphing-4-enine + 2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-
CC phosphoethanolamine; Xref=Rhea:RHEA:38831, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:73008, ChEBI:CHEBI:76077, ChEBI:CHEBI:76090;
CC Evidence={ECO:0000269|PubMed:16837646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38832;
CC Evidence={ECO:0000305|PubMed:16837646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1-(9Z,12Z-
CC octadecadienoyl)-N-acetylsphing-4-enine + 1-hexadecanoyl-sn-glycero-
CC 3-phosphoethanolamine; Xref=Rhea:RHEA:38835, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:73004, ChEBI:CHEBI:73008, ChEBI:CHEBI:76086;
CC Evidence={ECO:0000269|PubMed:16837646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38836;
CC Evidence={ECO:0000305|PubMed:16837646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N-
CC (acetyl)-sphing-4-enine + 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:38843,
CC ChEBI:CHEBI:46979, ChEBI:CHEBI:73009, ChEBI:CHEBI:76077,
CC ChEBI:CHEBI:76091; Evidence={ECO:0000269|PubMed:16837646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38844;
CC Evidence={ECO:0000305|PubMed:16837646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1-
CC (5Z,8Z,11Z,14Z)-eicosatetraenoyl-N-(acetyl)-sphing-4-enine + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:38839,
CC ChEBI:CHEBI:46979, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009,
CC ChEBI:CHEBI:76080; Evidence={ECO:0000269|PubMed:16837646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38840;
CC Evidence={ECO:0000305|PubMed:16837646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N-(acetyl)-sphing-4-
CC enine + 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:38759, ChEBI:CHEBI:46979, ChEBI:CHEBI:73001,
CC ChEBI:CHEBI:76071, ChEBI:CHEBI:76077;
CC Evidence={ECO:0000269|PubMed:16837646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38760;
CC Evidence={ECO:0000305|PubMed:16837646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-sphing-
CC 4-enine + 1-hexadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:38755, ChEBI:CHEBI:46979, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73001, ChEBI:CHEBI:76054;
CC Evidence={ECO:0000269|PubMed:16837646, ECO:0000269|PubMed:16880524};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38756;
CC Evidence={ECO:0000305|PubMed:16837646, ECO:0000305|PubMed:16880524};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N-
CC (acetyl)-sphing-4-enine + 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine; Xref=Rhea:RHEA:38811, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:73002, ChEBI:CHEBI:76077, ChEBI:CHEBI:76084;
CC Evidence={ECO:0000269|PubMed:16837646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38812;
CC Evidence={ECO:0000305|PubMed:16837646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + N-(acetyl)-sphing-4-enine = 1-(9Z,12Z-
CC octadecadienoyl)-N-acetylsphing-4-enine + 1-hexadecanoyl-sn-glycero-
CC 3-phosphocholine; Xref=Rhea:RHEA:38807, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002, ChEBI:CHEBI:76086;
CC Evidence={ECO:0000269|PubMed:16837646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38808;
CC Evidence={ECO:0000305|PubMed:16837646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N-
CC (acetyl)-sphing-4-enine + 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phosphocholine; Xref=Rhea:RHEA:38775, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:73003, ChEBI:CHEBI:76077, ChEBI:CHEBI:76079;
CC Evidence={ECO:0000269|PubMed:16837646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38776;
CC Evidence={ECO:0000305|PubMed:16837646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-N-(acetyl)-sphing-4-enine + 1-hexadecanoyl-sn-
CC glycero-3-phosphocholine; Xref=Rhea:RHEA:38771, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73003, ChEBI:CHEBI:76080;
CC Evidence={ECO:0000269|PubMed:16837646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38772;
CC Evidence={ECO:0000305|PubMed:16837646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-
CC hexadecanoyl-N-(acetyl)-sphing-4-enine + 2-(4Z,7Z,10Z,13Z,16Z,19Z-
CC docosahexaenoyl)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38815,
CC ChEBI:CHEBI:46979, ChEBI:CHEBI:74963, ChEBI:CHEBI:76077,
CC ChEBI:CHEBI:76085; Evidence={ECO:0000269|PubMed:16837646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38816;
CC Evidence={ECO:0000305|PubMed:16837646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-
CC (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-N-(acetyl)-sphing-4-enine +
CC 1-hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38819,
CC ChEBI:CHEBI:46979, ChEBI:CHEBI:72998, ChEBI:CHEBI:74963,
CC ChEBI:CHEBI:76087; Evidence={ECO:0000269|PubMed:16837646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38820;
CC Evidence={ECO:0000305|PubMed:16837646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-nonadioyl-sn-glycero-3-phosphocholine + N-
CC (acetyl)-sphing-4-enine = 1-hexadecanoyl-N-(acetyl)-sphing-4-enine +
CC 2-nonadioyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:62472,
CC ChEBI:CHEBI:46979, ChEBI:CHEBI:76077, ChEBI:CHEBI:78207,
CC ChEBI:CHEBI:145780; Evidence={ECO:0000269|PubMed:27993948};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62473;
CC Evidence={ECO:0000305|PubMed:27993948};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + N-(acetyl)-sphing-4-enine = 1-octadecanoyl-N-(acetyl)-sphing-4-
CC enine + 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:38799, ChEBI:CHEBI:46979, ChEBI:CHEBI:75034,
CC ChEBI:CHEBI:76071, ChEBI:CHEBI:76074;
CC Evidence={ECO:0000269|PubMed:16837646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38800;
CC Evidence={ECO:0000305|PubMed:16837646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-sphing-
CC 4-enine + 1-octadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:38795, ChEBI:CHEBI:46979, ChEBI:CHEBI:73858,
CC ChEBI:CHEBI:75034, ChEBI:CHEBI:76054;
CC Evidence={ECO:0000269|PubMed:16837646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38796;
CC Evidence={ECO:0000305|PubMed:16837646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-
CC phosphocholine + N-(acetyl)-sphing-4-enine = 1-(9Z,12Z-
CC octadecadienoyl)-N-acetylsphing-4-enine + 1-octadecanoyl-sn-glycero-
CC 3-phosphocholine; Xref=Rhea:RHEA:57108, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:73858, ChEBI:CHEBI:76086, ChEBI:CHEBI:84822;
CC Evidence={ECO:0000250|UniProtKB:Q8NCC3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57109;
CC Evidence={ECO:0000250|UniProtKB:Q8NCC3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-octadecanoyl-N-
CC (acetyl)-sphing-4-enine + 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phosphocholine; Xref=Rhea:RHEA:57120, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:74965, ChEBI:CHEBI:76074, ChEBI:CHEBI:76079;
CC Evidence={ECO:0000250|UniProtKB:Q8NCC3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57121;
CC Evidence={ECO:0000250|UniProtKB:Q8NCC3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-N-(acetyl)-sphing-4-enine + 1-octadecanoyl-sn-
CC glycero-3-phosphocholine; Xref=Rhea:RHEA:57116, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:73858, ChEBI:CHEBI:74965, ChEBI:CHEBI:76080;
CC Evidence={ECO:0000250|UniProtKB:Q8NCC3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57117;
CC Evidence={ECO:0000250|UniProtKB:Q8NCC3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine
CC + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-sphing-
CC 4-enine + 2-hexadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:38767, ChEBI:CHEBI:46979, ChEBI:CHEBI:74667,
CC ChEBI:CHEBI:76054, ChEBI:CHEBI:76078;
CC Evidence={ECO:0000269|PubMed:16837646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38768;
CC Evidence={ECO:0000305|PubMed:16837646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine
CC + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + 1-hexadecanoyl-N-(acetyl)-sphing-4-enine;
CC Xref=Rhea:RHEA:38763, ChEBI:CHEBI:28610, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:74667, ChEBI:CHEBI:76077;
CC Evidence={ECO:0000269|PubMed:16837646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38764;
CC Evidence={ECO:0000305|PubMed:16837646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z)-octadecenoyl-2-octadecanoyl-sn-glycero-3-phosphocholine
CC + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-sphing-
CC 4-enine + 2-octadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:38791, ChEBI:CHEBI:46979, ChEBI:CHEBI:76054,
CC ChEBI:CHEBI:76073, ChEBI:CHEBI:76076;
CC Evidence={ECO:0000269|PubMed:16837646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38792;
CC Evidence={ECO:0000305|PubMed:16837646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z)-octadecenoyl-2-octadecanoyl-sn-glycero-3-phosphocholine
CC + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + 1-octadecanoyl-N-(acetyl)-sphing-4-enine;
CC Xref=Rhea:RHEA:38803, ChEBI:CHEBI:28610, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:76073, ChEBI:CHEBI:76074;
CC Evidence={ECO:0000269|PubMed:16837646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38804;
CC Evidence={ECO:0000305|PubMed:16837646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + N-
CC (acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-sphing-4-
CC enine + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:38703, ChEBI:CHEBI:28610, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:74669, ChEBI:CHEBI:76054;
CC Evidence={ECO:0000269|PubMed:11790796, ECO:0000269|PubMed:16106046,
CC ECO:0000269|PubMed:16880524, ECO:0000269|PubMed:17626977,
CC ECO:0000269|PubMed:19017977, ECO:0000269|PubMed:20410020,
CC ECO:0000269|PubMed:27993948};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38704;
CC Evidence={ECO:0000305|PubMed:17626977};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-
CC serine + N-(acetyl)-sphing-4-enine = 1-octadecanoyl-N-(acetyl)-
CC sphing-4-enine + 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine;
CC Xref=Rhea:RHEA:57140, ChEBI:CHEBI:46979, ChEBI:CHEBI:76074,
CC ChEBI:CHEBI:77342, ChEBI:CHEBI:78260;
CC Evidence={ECO:0000250|UniProtKB:Q8NCC3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57141;
CC Evidence={ECO:0000250|UniProtKB:Q8NCC3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-
CC serine + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-
CC sphing-4-enine + 1-octadecanoyl-sn-glycero-3-phosphoserine;
CC Xref=Rhea:RHEA:57136, ChEBI:CHEBI:46979, ChEBI:CHEBI:76054,
CC ChEBI:CHEBI:78260, ChEBI:CHEBI:84467;
CC Evidence={ECO:0000250|UniProtKB:Q8NCC3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57137;
CC Evidence={ECO:0000250|UniProtKB:Q8NCC3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-
CC sn-glycerol) + N-(acetyl)-sphing-4-enine = 1-octadecanoyl-N-(acetyl)-
CC sphing-4-enine + 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-
CC glycerol); Xref=Rhea:RHEA:57144, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:72845, ChEBI:CHEBI:76074, ChEBI:CHEBI:141490;
CC Evidence={ECO:0000250|UniProtKB:Q8NCC3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57145;
CC Evidence={ECO:0000250|UniProtKB:Q8NCC3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-
CC sn-glycerol) + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-
CC (acetyl)-sphing-4-enine + 1-octadecanoyl-sn-glycero-3-phospho-(1'-sn-
CC glycerol); Xref=Rhea:RHEA:57148, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:72827, ChEBI:CHEBI:72845, ChEBI:CHEBI:76054;
CC Evidence={ECO:0000250|UniProtKB:Q8NCC3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57149;
CC Evidence={ECO:0000250|UniProtKB:Q8NCC3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + N-
CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine = (9Z-octadecenoyl)-sn-
CC glycero-3-phosphocholine + 2-[(5Z,8Z,11Z,14Z)-
CC eicosatetraenoylamino]ethyl (9Z)-octadecenoate; Xref=Rhea:RHEA:38751,
CC ChEBI:CHEBI:2700, ChEBI:CHEBI:74669, ChEBI:CHEBI:76070,
CC ChEBI:CHEBI:76083; Evidence={ECO:0000269|PubMed:17626977};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38752;
CC Evidence={ECO:0000305|PubMed:17626977};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + N-(9Z-
CC octadecenoyl) ethanolamine = (9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + 2-[(9Z)-octadecenoylamino]ethyl (9Z)-octadecenoate;
CC Xref=Rhea:RHEA:38747, ChEBI:CHEBI:71466, ChEBI:CHEBI:74669,
CC ChEBI:CHEBI:76068, ChEBI:CHEBI:76083;
CC Evidence={ECO:0000269|PubMed:17626977};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38748;
CC Evidence={ECO:0000305|PubMed:17626977};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 3-(9Z-
CC octadecenoyl)-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + 1,3-di-(9Z-octadecenoyl)-glycerol;
CC Xref=Rhea:RHEA:38743, ChEBI:CHEBI:74669, ChEBI:CHEBI:75735,
CC ChEBI:CHEBI:75938, ChEBI:CHEBI:76083;
CC Evidence={ECO:0000269|PubMed:17626977};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38744;
CC Evidence={ECO:0000305|PubMed:17626977};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-(9Z-
CC octadecenoyl)-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + 1,3-di-(9Z-octadecenoyl)-glycerol;
CC Xref=Rhea:RHEA:38739, ChEBI:CHEBI:74669, ChEBI:CHEBI:75735,
CC ChEBI:CHEBI:75757, ChEBI:CHEBI:76083;
CC Evidence={ECO:0000269|PubMed:17626977};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38740;
CC Evidence={ECO:0000305|PubMed:17626977};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 2-
CC hexadecanoylglycerol = (9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + 1-(9Z)-octadecenoyl-2-hexadecanoylglycerol; Xref=Rhea:RHEA:38735,
CC ChEBI:CHEBI:74669, ChEBI:CHEBI:75455, ChEBI:CHEBI:76065,
CC ChEBI:CHEBI:76083; Evidence={ECO:0000269|PubMed:17626977};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38736;
CC Evidence={ECO:0000305|PubMed:17626977};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 3-
CC hexadecanoyl-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + 1-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol;
CC Xref=Rhea:RHEA:38731, ChEBI:CHEBI:64757, ChEBI:CHEBI:74669,
CC ChEBI:CHEBI:75867, ChEBI:CHEBI:76083;
CC Evidence={ECO:0000269|PubMed:17626977};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38732;
CC Evidence={ECO:0000305|PubMed:17626977};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O =
CC (9Z)-octadecenoate + (9Z-octadecenoyl)-sn-glycero-3-phosphocholine +
CC H(+); Xref=Rhea:RHEA:38699, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76083;
CC Evidence={ECO:0000269|PubMed:17626977};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38700;
CC Evidence={ECO:0000305|PubMed:17626977};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-O-
CC hexadecyl-2-acetyl-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + 1-O-hexadecyl-2-acetyl-3-(9Z)-octadecenoyl-sn-
CC glycerol; Xref=Rhea:RHEA:38707, ChEBI:CHEBI:74669, ChEBI:CHEBI:75936,
CC ChEBI:CHEBI:76055, ChEBI:CHEBI:76083;
CC Evidence={ECO:0000269|PubMed:17626977};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38708;
CC Evidence={ECO:0000305|PubMed:17626977};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-O-
CC hexadecylglycerol = (9Z-octadecenoyl)-sn-glycero-3-phosphocholine +
CC 1-O-hexadecyl-3-(9Z)-octadecenoylglycerol; Xref=Rhea:RHEA:38711,
CC ChEBI:CHEBI:74669, ChEBI:CHEBI:76061, ChEBI:CHEBI:76062,
CC ChEBI:CHEBI:76083; Evidence={ECO:0000269|PubMed:17626977};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38712;
CC Evidence={ECO:0000305|PubMed:17626977};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-O-
CC hexadecyl-2-O-methyl-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + 1-O-hexadecyl-2-O-methyl-3-(9Z)-octadecenoyl-sn-
CC glycerol; Xref=Rhea:RHEA:38723, ChEBI:CHEBI:74669, ChEBI:CHEBI:76063,
CC ChEBI:CHEBI:76064, ChEBI:CHEBI:76083;
CC Evidence={ECO:0000269|PubMed:17626977};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38724;
CC Evidence={ECO:0000305|PubMed:17626977};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-
CC hexadecanoyl-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + 1-hexadecanoyl-3-(9Z)-octadecenoyl-sn-glycerol;
CC Xref=Rhea:RHEA:38727, ChEBI:CHEBI:74669, ChEBI:CHEBI:75542,
CC ChEBI:CHEBI:75868, ChEBI:CHEBI:76083;
CC Evidence={ECO:0000269|PubMed:17626977};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38728;
CC Evidence={ECO:0000305|PubMed:17626977};
CC -!- ACTIVITY REGULATION: Phospholipase sn-2 versus sn-1 positional
CC specificity is affected by the phospholipid composition of membranes.
CC Phospholipase A2 activity toward 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phosphocholine (PAPE) is enhanced in the
CC presence of 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC), which
CC promotes lipid bilayer formation (PubMed:16837646). O-acyltransferase
CC activity is inhibited by antiarrhythmic drug amiodarone
CC (PubMed:27993948). {ECO:0000269|PubMed:16837646,
CC ECO:0000269|PubMed:27993948}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=171 uM for 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC (O-acyltransferase activity) {ECO:0000269|PubMed:20410020};
CC Vmax=5.55 umol/min/mg enzyme toward 1,2-di-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphocholine (O-acyltransferase activity)
CC {ECO:0000269|PubMed:20410020};
CC pH dependence:
CC Optimum pH is 4.5. {ECO:0000305|PubMed:27993948};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19017977,
CC ECO:0000269|PubMed:20410020}. Lysosome {ECO:0000269|PubMed:19017977}.
CC Membrane {ECO:0000250|UniProtKB:Q8NCC3}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8NCC3}.
CC -!- TISSUE SPECIFICITY: Detected in blood plasma (PubMed:20410020).
CC Detected in alveolar macrophages (at protein level) (PubMed:16106046,
CC PubMed:16880524, PubMed:19017977). Detected in heart, liver, spleen,
CC kidney, thymus, brain and lung (PubMed:16880524).
CC {ECO:0000269|PubMed:16106046, ECO:0000269|PubMed:16880524,
CC ECO:0000269|PubMed:19017977, ECO:0000269|PubMed:20410020}.
CC -!- PTM: N-glycosylated (PubMed:11790796). N-glycosylation is important for
CC maturation of the enzyme and normal subcellular location (By
CC similarity). {ECO:0000250|UniProtKB:Q8NCC3,
CC ECO:0000269|PubMed:11790796}.
CC -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate, are
CC viable and fertile. They display strongly reduced transacylase activity
CC in lung alveolar macrophages and in peritoneal macrophages, leading to
CC the accumulation of pulmonary surfactant phospholipids with
CC phosphatidylethanolamine and phosphatidylcholine headgroups. Mice
CC display higher numers of alveolar macrophages in the lung, together
CC with a mononuclear cell infiltrate in airways and blood vessels.
CC Alveolar nmacrophages are larger than normal and present lamellar
CC inclusion bodies, indicative of cellular phospholipidosis. Besides,
CC mutant mice display splenomegaly. {ECO:0000269|PubMed:16880524}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AF468958; AAL78651.1; -; mRNA.
DR EMBL; AY179884; AAO49009.1; -; Genomic_DNA.
DR EMBL; AK085194; BAC39387.1; -; mRNA.
DR EMBL; AK155004; BAE32987.1; -; mRNA.
DR EMBL; AK163111; BAE37197.1; -; mRNA.
DR EMBL; AK170814; BAE42046.1; -; mRNA.
DR EMBL; BC019373; AAH19373.1; -; mRNA.
DR CCDS; CCDS22630.1; -.
DR RefSeq; NP_598553.1; NM_133792.2.
DR AlphaFoldDB; Q8VEB4; -.
DR SMR; Q8VEB4; -.
DR BioGRID; 228695; 19.
DR IntAct; Q8VEB4; 1.
DR STRING; 10090.ENSMUSP00000034377; -.
DR ChEMBL; CHEMBL3259497; -.
DR SwissLipids; SLP:000000352; -.
DR ESTHER; mouse-C87498; PC-sterol_acyltransferase.
DR GlyConnect; 2363; 7 N-Linked glycans (4 sites).
DR GlyGen; Q8VEB4; 4 sites, 7 N-linked glycans (4 sites).
DR PhosphoSitePlus; Q8VEB4; -.
DR EPD; Q8VEB4; -.
DR MaxQB; Q8VEB4; -.
DR PaxDb; Q8VEB4; -.
DR PeptideAtlas; Q8VEB4; -.
DR PRIDE; Q8VEB4; -.
DR ProteomicsDB; 294151; -.
DR Antibodypedia; 29747; 106 antibodies from 18 providers.
DR DNASU; 192654; -.
DR Ensembl; ENSMUST00000034377; ENSMUSP00000034377; ENSMUSG00000031903.
DR GeneID; 192654; -.
DR KEGG; mmu:192654; -.
DR UCSC; uc009nfj.1; mouse.
DR CTD; 23659; -.
DR MGI; MGI:2178076; Pla2g15.
DR VEuPathDB; HostDB:ENSMUSG00000031903; -.
DR eggNOG; KOG2369; Eukaryota.
DR GeneTree; ENSGT00940000157499; -.
DR HOGENOM; CLU_037070_1_1_1; -.
DR InParanoid; Q8VEB4; -.
DR OMA; PNENKQF; -.
DR OrthoDB; 828056at2759; -.
DR PhylomeDB; Q8VEB4; -.
DR TreeFam; TF313258; -.
DR Reactome; R-MMU-1483115; Hydrolysis of LPC.
DR BioGRID-ORCS; 192654; 6 hits in 76 CRISPR screens.
DR ChiTaRS; Pla2g15; mouse.
DR PRO; PR:Q8VEB4; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8VEB4; protein.
DR Bgee; ENSMUSG00000031903; Expressed in stroma of bone marrow and 211 other tissues.
DR ExpressionAtlas; Q8VEB4; baseline and differential.
DR Genevisible; Q8VEB4; MM.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016411; F:acylglycerol O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0008374; F:O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
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:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006672; P:ceramide metabolic process; IDA:UniProtKB.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; IDA:UniProtKB.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; ISO:MGI.
DR GO; GO:0046338; P:phosphatidylethanolamine catabolic process; IDA:UniProtKB.
DR GO; GO:0046471; P:phosphatidylglycerol metabolic process; ISS:UniProtKB.
DR GO; GO:0006658; P:phosphatidylserine metabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003386; LACT/PDAT_acylTrfase.
DR Pfam; PF02450; LCAT; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Disulfide bond; Fatty acid metabolism; Glycoprotein;
KW Hydrolase; Lipid metabolism; Lysosome; Membrane; Metal-binding;
KW Reference proteome; Secreted; Signal; Transferase; Zinc.
FT SIGNAL 1..33
FT /evidence="ECO:0000250|UniProtKB:Q8NCC3"
FT CHAIN 34..412
FT /note="Phospholipase A2 group XV"
FT /id="PRO_0000017809"
FT ACT_SITE 198
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:11790796,
FT ECO:0000305|PubMed:16106046"
FT ACT_SITE 360
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8NCC3,
FT ECO:0000305|PubMed:16106046"
FT ACT_SITE 392
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8NCC3,
FT ECO:0000305|PubMed:16106046"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NCC3"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8NCC3"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NCC3"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8NCC3"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8NCC3"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 65..89
FT /evidence="ECO:0000250|UniProtKB:Q8NCC3,
FT ECO:0000305|PubMed:16106046"
FT MUTAGEN 65
FT /note="C->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:16106046"
FT MUTAGEN 89
FT /note="C->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:16106046"
FT MUTAGEN 198
FT /note="S->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:11790796,
FT ECO:0000269|PubMed:16106046"
FT MUTAGEN 360
FT /note="D->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:16106046"
FT MUTAGEN 392
FT /note="H->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:16106046"
FT CONFLICT 342
FT /note="F -> S (in Ref. 2; BAE32987)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 412 AA; 47307 MW; 6544369410C46C9A CRC64;
MDRHLCTCRE TQLRSGLLLP LFLLMMLADL TLPAQRHPPV VLVPGDLGNQ LEAKLDKPKV
VHYLCSKKTD SYFTLWLNLE LLLPVIIDCW IDNIRLVYNR TSRATQFPDG VDVRVPGFGE
TFSMEFLDPS KRNVGSYFYT MVESLVGWGY TRGEDVRGAP YDWRRAPNEN GPYFLALREM
IEEMYQMYGG PVVLVAHSMG NVYMLYFLQR QPQVWKDKYI HAFVSLGAPW GGVAKTLRVL
ASGDNNRIPV IGPLKIREQQ RSAVSTSWLL PYNHTWSHEK VFVYTPTTNY TLRDYHRFFR
DIGFEDGWFM RQDTEGLVEA MTPPGVELHC LYGTGVPTPN SFYYESFPDR DPKICFGDGD
GTVNLESVLQ CQAWQSRQEH RVSLQELPGS EHIEMLANAT TLAYLKRVLL EP
