MBOA5_MOUSE
ID MBOA5_MOUSE Reviewed; 487 AA.
AC Q91V01; B1B362; O35131; Q8BNH6;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Lysophospholipid acyltransferase 5;
DE Short=LPLAT 5;
DE EC=2.3.1.- {ECO:0000269|PubMed:18287005, ECO:0000269|PubMed:25898003};
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
DE EC=2.3.1.23 {ECO:0000269|PubMed:18287005, ECO:0000269|PubMed:25898003};
DE AltName: Full=1-acylglycerophosphoethanolamine O-acyltransferase;
DE EC=2.3.1.n7 {ECO:0000269|PubMed:18287005};
DE AltName: Full=1-acylglycerophosphoserine O-acyltransferase;
DE EC=2.3.1.n6 {ECO:0000269|PubMed:18287005};
DE AltName: Full=Lysophosphatidylcholine acyltransferase;
DE Short=LPCAT;
DE Short=Lyso-PC acyltransferase;
DE AltName: Full=Lysophosphatidylcholine acyltransferase 3;
DE Short=Lyso-PC acyltransferase 3;
DE Short=mLPCAT3;
DE AltName: Full=Lysophosphatidylethanolamine acyltransferase;
DE Short=LPEAT;
DE Short=Lyso-PE acyltransferase;
DE AltName: Full=Lysophosphatidylserine acyltransferase;
DE Short=LPSAT;
DE Short=Lyso-PS acyltransferase;
DE AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 5;
DE Short=O-acyltransferase domain-containing protein 5;
GN Name=Lpcat3; Synonyms=Grcc3f {ECO:0000312|MGI:MGI:1315211}, Mboat5, Oact5;
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] {ECO:0000312|EMBL:AAK20915.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAK20915.1};
RC TISSUE=Liver {ECO:0000312|EMBL:AAK20915.1};
RA Zhu Y., Han Y., Reddy J.K.;
RT "Cloning and initial characterization of mouse PTG cDNA, whose expression
RT is in a PPAR alpha dependent manner.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=18287005; DOI=10.1073/pnas.0712245105;
RA Hishikawa D., Shindou H., Kobayashi S., Nakanishi H., Taguchi R.,
RA Shimizu T.;
RT "Discovery of a lysophospholipid acyltransferase family essential for
RT membrane asymmetry and diversity.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2830-2835(2008).
RN [3] {ECO:0000312|EMBL:AAK20915.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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] {ECO:0000312|EMBL:AAH06753.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH06753.2};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH06753.2};
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 [5] {ECO:0000305, ECO:0000312|EMBL:AAC36007.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-487.
RX PubMed=9445485;
RA Ansari-Lari M.A., Oeltjen J.C., Schwartz S., Zhang Z., Muzny D.M., Lu J.,
RA Gorrell J.H., Chinault A.C., Belmont J.W., Miller W., Gibbs R.A.;
RT "Comparative sequence analysis of a gene-rich cluster at human chromosome
RT 12p13 and its syntenic region in mouse chromosome 6.";
RL Genome Res. 8:29-40(1998).
RN [6] {ECO:0000305, ECO:0000312|EMBL:BAC38993.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 114-487.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC38993.1};
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
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 [8]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=24206663; DOI=10.1016/j.cmet.2013.10.002;
RA Rong X., Albert C.J., Hong C., Duerr M.A., Chamberlain B.T., Tarling E.J.,
RA Ito A., Gao J., Wang B., Edwards P.A., Jung M.E., Ford D.A., Tontonoz P.;
RT "LXRs regulate ER stress and inflammation through dynamic modulation of
RT membrane phospholipid composition.";
RL Cell Metab. 18:685-697(2013).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, INDUCTION,
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-374.
RX PubMed=25898003; DOI=10.7554/elife.06328;
RA Hashidate-Yoshida T., Harayama T., Hishikawa D., Morimoto R., Hamano F.,
RA Tokuoka S.M., Eto M., Tamura-Nakano M., Yanobu-Takanashi R., Mukumoto Y.,
RA Kiyonari H., Okamura T., Kita Y., Shindou H., Shimizu T.;
RT "Fatty acid remodeling by LPCAT3 enriches arachidonate in phospholipid
RT membranes and regulates triglyceride transport.";
RL Elife 4:0-0(2015).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25806685; DOI=10.7554/elife.06557;
RA Rong X., Wang B., Dunham M.M., Hedde P.N., Wong J.S., Gratton E.,
RA Young S.G., Ford D.A., Tontonoz P.;
RT "Lpcat3-dependent production of arachidonoyl phospholipids is a key
RT determinant of triglyceride secretion.";
RL Elife 4:0-0(2015).
RN [11]
RP FUNCTION.
RX PubMed=26833026; DOI=10.1016/j.cmet.2016.01.001;
RA Wang B., Rong X., Duerr M.A., Hermanson D.J., Hedde P.N., Wong J.S.,
RA Vallim T.Q., Cravatt B.F., Gratton E., Ford D.A., Tontonoz P.;
RT "Intestinal Phospholipid Remodeling Is Required for Dietary-Lipid Uptake
RT and Survival on a High-Fat Diet.";
RL Cell Metab. 23:492-504(2016).
RN [12]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=28846071; DOI=10.1172/jci93616;
RA Rong X., Wang B., Palladino E.N., de Aguiar Vallim T.Q., Ford D.A.,
RA Tontonoz P.;
RT "ER phospholipid composition modulates lipogenesis during feeding and in
RT obesity.";
RL J. Clin. Invest. 127:3640-3651(2017).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29395055; DOI=10.1016/j.stem.2017.12.017;
RA Wang B., Rong X., Palladino E.N.D., Wang J., Fogelman A.M., Martin M.G.,
RA Alrefai W.A., Ford D.A., Tontonoz P.;
RT "Phospholipid Remodeling and Cholesterol Availability Regulate Intestinal
RT Stemness and Tumorigenesis.";
RL Cell Stem Cell 22:206-220(2018).
CC -!- FUNCTION: Lysophospholipid O-acyltransferase (LPLAT) that catalyzes the
CC reacylation step of the phospholipid remodeling process also known as
CC the Lands cycle (PubMed:18287005, PubMed:25898003). Catalyzes transfer
CC of the fatty acyl chain from fatty acyl-CoA to 1-acyl lysophospholipid
CC to form various classes of phospholipids. Converts 1-acyl
CC lysophosphatidylcholine (LPC) into phosphatidylcholine (PC) (LPCAT
CC activity), 1-acyl lysophosphatidylserine (LPS) into phosphatidylserine
CC (PS) (LPSAT activity) and 1-acyl lysophosphatidylethanolamine (LPE)
CC into phosphatidylethanolamine (PE) (LPEAT activity). Favors
CC polyunsaturated fatty acyl-CoAs as acyl donors compared to saturated
CC fatty acyl-CoAs (PubMed:18287005, PubMed:25898003). Has higher activity
CC for LPC acyl acceptors compared to LPEs and LPSs (PubMed:18287005). Can
CC also transfer the fatty acyl chain from fatty acyl-CoA to 1-O-alkyl
CC lysophospholipid or 1-O-alkenyl lysophospholipid with lower efficiency
CC (PubMed:18287005). Acts as a major LPC O-acyltransferase in liver and
CC intestine (PubMed:25898003, PubMed:26833026). As a component of the
CC liver X receptor/NR1H3 or NR1H2 signaling pathway, mainly catalyzes the
CC incorporation of arachidonate into PCs of endoplasmic reticulum (ER)
CC membranes, increasing membrane dynamics and enabling triacylglycerols
CC transfer to nascent very low-density lipoprotein (VLDL) particles
CC (PubMed:25806685). Promotes processing of sterol regulatory protein
CC SREBF1 in hepatocytes, likely by facilitating the translocation of
CC SREBF1-SCAP complex from ER to the Golgi apparatus (PubMed:28846071).
CC Participates in mechanisms by which the liver X receptor/NR1H3 or NR1H2
CC signaling pathway counteracts lipid-induced ER stress response and
CC inflammation (PubMed:24206663). Down-regulates hepatic inflammation by
CC limiting arachidonic acid availability for synthesis of inflammatory
CC eicosanoids, such as prostaglandins (PubMed:24206663). In enterocytes,
CC acts as a component of a gut-brain feedback loop that coordinates
CC dietary lipid absorption and food intake. Regulates the abundance of
CC PCs containing linoleate and arachidonate in enterocyte membranes,
CC enabling passive diffusion of fatty acids and cholesterol across the
CC membrane for efficient chylomicron assembly (PubMed:26833026). In the
CC intestinal crypt, acts as a component of dietary-responsive
CC phospholipid-cholesterol axis, regulating the biosynthesis of
CC cholesterol and its mitogenic effects on intestinal stem cells
CC (PubMed:29395055). {ECO:0000269|PubMed:18287005,
CC ECO:0000269|PubMed:24206663, ECO:0000269|PubMed:25806685,
CC ECO:0000269|PubMed:25898003, ECO:0000269|PubMed:26833026,
CC ECO:0000269|PubMed:28846071, ECO:0000269|PubMed:29395055}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:58342; EC=2.3.1.23;
CC Evidence={ECO:0000269|PubMed:18287005, ECO:0000269|PubMed:25898003};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12938;
CC Evidence={ECO:0000305|PubMed:18287005, ECO:0000305|PubMed:25898003};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + an acyl-CoA = a
CC 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:32995, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:64612; EC=2.3.1.n7;
CC Evidence={ECO:0000269|PubMed:18287005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32996;
CC Evidence={ECO:0000305|PubMed:18287005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phospho-L-serine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:33191,
CC ChEBI:CHEBI:57262, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64379; EC=2.3.1.n6;
CC Evidence={ECO:0000269|PubMed:18287005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33192;
CC Evidence={ECO:0000305|PubMed:18287005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + a 1-acyl-sn-glycero-3-
CC phosphocholine = 1-acyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37563, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:58168, ChEBI:CHEBI:60000;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37564;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + a 1-acyl-sn-glycero-3-
CC phosphocholine = 1-acyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-
CC glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:37559,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:75063; Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37560;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + dodecanoyl-CoA =
CC 1-hexadecanoyl-2-dodecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37515, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:75018;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37516;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + octadecanoyl-CoA
CC = 1-hexadecanoyl-2-octadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:35987, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73000;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35988;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-dodecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA =
CC 1-dodecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37511, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:74966, ChEBI:CHEBI:75017;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37512;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-tetradecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA
CC = 1-tetradecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37655, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:64489, ChEBI:CHEBI:75062;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37656;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA
CC = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:35983, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35984;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA
CC = 1-octadecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37527, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:73858, ChEBI:CHEBI:75026;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37528;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine +
CC hexadecanoyl-CoA = 1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37383, ChEBI:CHEBI:28610,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74667;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37384;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z-hexadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37207, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:72998, ChEBI:CHEBI:74000;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37208;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:35991, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001;
CC Evidence={ECO:0000269|PubMed:18287005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35992;
CC Evidence={ECO:0000305|PubMed:18287005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:35995,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73002; Evidence={ECO:0000269|PubMed:18287005,
CC ECO:0000269|PubMed:25898003};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35996;
CC Evidence={ECO:0000305|PubMed:18287005, ECO:0000305|PubMed:25898003};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-dodecanoyl-sn-
CC glycero-3-phosphocholine = 1-dodecanoyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37483, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:74966, ChEBI:CHEBI:74967;
CC Evidence={ECO:0000269|PubMed:18287005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37484;
CC Evidence={ECO:0000305|PubMed:18287005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-hexadecanoyl-sn-
CC glycero-3-phosphocholine = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:35999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC Evidence={ECO:0000269|PubMed:18287005, ECO:0000269|PubMed:25898003};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36000;
CC Evidence={ECO:0000305|PubMed:18287005, ECO:0000305|PubMed:25898003};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-octadecanoyl-sn-
CC glycero-3-phosphocholine = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37479, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:73858, ChEBI:CHEBI:74965;
CC Evidence={ECO:0000269|PubMed:18287005, ECO:0000269|PubMed:25898003};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37480;
CC Evidence={ECO:0000305|PubMed:18287005, ECO:0000305|PubMed:25898003};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-eicosanoyl-sn-
CC glycero-3-phosphocholine = 1-eicosanoyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37487, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:74968, ChEBI:CHEBI:74970;
CC Evidence={ECO:0000269|PubMed:18287005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37488;
CC Evidence={ECO:0000305|PubMed:18287005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + CoA; Xref=Rhea:RHEA:37387, ChEBI:CHEBI:28610, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:74669;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37388;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphocholine = 1-(9Z)-octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn-
CC glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:37391,
CC ChEBI:CHEBI:28610, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:74670; Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37392;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphocholine = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-
CC icosatetraenoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37395, ChEBI:CHEBI:28610, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57368, ChEBI:CHEBI:74671;
CC Evidence={ECO:0000269|PubMed:18287005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37396;
CC Evidence={ECO:0000305|PubMed:18287005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + a 1-acyl-sn-glycero-3-
CC phosphoethanolamine = 1-acyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:37579, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:64381, ChEBI:CHEBI:75069;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37580;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphoethanolamine = 1-(9Z)-octadecenoyl-2-(9Z,12Z)-
CC octadecadienoyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:37503, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:74971, ChEBI:CHEBI:74977;
CC Evidence={ECO:0000269|PubMed:18287005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37504;
CC Evidence={ECO:0000305|PubMed:18287005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(10Z-heptadecenoyl)-sn-
CC glycero-3-phosphoethanolamine = 1-(10Z-heptadecenoyl)-2-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:64228, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:149768, ChEBI:CHEBI:149770;
CC Evidence={ECO:0000269|PubMed:25898003};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64229;
CC Evidence={ECO:0000305|PubMed:25898003};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + a 1-acyl-sn-glycero-3-
CC phosphoethanolamine = 1-acyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:37575,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:64381,
CC ChEBI:CHEBI:75067; Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37576;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-hexadecanoyl-sn-
CC glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:36023, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:73004, ChEBI:CHEBI:73009;
CC Evidence={ECO:0000269|PubMed:18287005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36024;
CC Evidence={ECO:0000305|PubMed:18287005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphoethanolamine = 1-(9Z)-octadecenoyl-2-
CC (5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine +
CC CoA; Xref=Rhea:RHEA:37495, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:74971, ChEBI:CHEBI:74975;
CC Evidence={ECO:0000269|PubMed:18287005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37496;
CC Evidence={ECO:0000305|PubMed:18287005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(10Z-heptadecenoyl)-
CC sn-glycero-3-phosphoethanolamine = 1-(10Z-heptadecenoyl)-2-
CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine +
CC CoA; Xref=Rhea:RHEA:64204, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:149768, ChEBI:CHEBI:149769;
CC Evidence={ECO:0000269|PubMed:25898003};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64205;
CC Evidence={ECO:0000305|PubMed:25898003};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-O-(1Z-alkenyl)-sn-
CC glycero-3-phosphoethanolamine = 1-O-(1Z)-alkenyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:37635, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:77288, ChEBI:CHEBI:77295;
CC Evidence={ECO:0000269|PubMed:18287005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37636;
CC Evidence={ECO:0000305|PubMed:18287005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + a 1-acyl-sn-glycero-3-phospho-
CC L-serine = 1-acyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho-L-
CC serine + CoA; Xref=Rhea:RHEA:37567, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:64379, ChEBI:CHEBI:75066;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37568;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + a 1-acyl-sn-glycero-3-
CC phospho-L-serine = 1-acyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-
CC glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:37571,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:64379,
CC ChEBI:CHEBI:75065; Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37572;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phospho-L-
CC serine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-
CC serine + CoA; Xref=Rhea:RHEA:37531, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:75020, ChEBI:CHEBI:75029;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37532;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-L-serine = 1,2-di-(9Z)-octadecenoyl-sn-glycero-3-phospho-L-
CC serine + CoA; Xref=Rhea:RHEA:37407, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:74617, ChEBI:CHEBI:74905;
CC Evidence={ECO:0000269|PubMed:18287005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37408;
CC Evidence={ECO:0000305|PubMed:18287005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phospho-L-serine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:37535,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:75020,
CC ChEBI:CHEBI:75031; Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37536;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-
CC 3-phospho-L-serine = 1-(9Z-octadecenoyl)-2-(9Z,12Z-octadienoyl)-sn-
CC glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:37375,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:74617,
CC ChEBI:CHEBI:74892; Evidence={ECO:0000269|PubMed:18287005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37376;
CC Evidence={ECO:0000305|PubMed:18287005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-hexadecanoyl-sn-
CC glycero-3-phospho-L-serine = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phospho-L-serine + CoA;
CC Xref=Rhea:RHEA:37539, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:75020, ChEBI:CHEBI:75032;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37540;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phospho-L-serine = 1-(9Z-octadecenoyl)-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phospho-L-serine + CoA;
CC Xref=Rhea:RHEA:37379, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:74617, ChEBI:CHEBI:74897;
CC Evidence={ECO:0000269|PubMed:18287005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37380;
CC Evidence={ECO:0000305|PubMed:18287005};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.8 uM for arachidonoyl-CoA (in the presence of LPC C16:0 as
CC cosubstrate) {ECO:0000269|PubMed:18287005};
CC KM=44.1 uM for arachidonoyl-CoA (in the presence of LPE C18:1 as
CC cosubstrate) {ECO:0000269|PubMed:18287005};
CC KM=28 uM for arachidonoyl-CoA (in the presence of LPS C18:1 as
CC cosubstrate) {ECO:0000269|PubMed:18287005};
CC KM=34.5 uM for LPC C16:0 (in the presence of arachidonoyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:18287005};
CC KM=29.7 uM for LPE C18:1 (in the presence of arachidonoyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:18287005};
CC KM=22.3 uM for LPS C18:1 (in the presence of arachidonoyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:18287005};
CC Vmax=1085.5 nmol/min/mg enzyme with arachidonoyl-CoA and LPC C16:0 as
CC substrates {ECO:0000269|PubMed:18287005};
CC Vmax=389.25 nmol/min/mg enzyme with arachidonoyl-CoA and LPE C18:1 as
CC substrates {ECO:0000269|PubMed:18287005};
CC Vmax=335.75 nmol/min/mg enzyme with arachidonoyl-CoA and LPS C18:1 as
CC substrates {ECO:0000269|PubMed:18287005};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000269|PubMed:18287005, ECO:0000269|PubMed:25898003}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18287005}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Detected ubiquitously, with high expression levels
CC in small intestine, brown adipose tissue, liver, kidney and testis
CC (PubMed:18287005, PubMed:28846071, PubMed:25898003, PubMed:25806685,
CC PubMed:24206663). Expressed in liver and both proximal and distal small
CC intestine (at protein level) (PubMed:25898003). Expressed in peritoneal
CC macrophages (PubMed:24206663). {ECO:0000269|PubMed:18287005,
CC ECO:0000269|PubMed:24206663, ECO:0000269|PubMed:25806685,
CC ECO:0000269|PubMed:25898003, ECO:0000269|PubMed:28846071}.
CC -!- DEVELOPMENTAL STAGE: Expressed at late embryonic stages between 18.5
CC and 19.5 dpc in intestine and liver. {ECO:0000269|PubMed:25898003}.
CC -!- INDUCTION: Up-regulated in response to liver X receptor/NR1H3 or NR1H2
CC agonist GW3965 (PubMed:28846071, PubMed:25898003, PubMed:25806685,
CC PubMed:24206663). Up-regulated in peritoneal macrophages upon exposure
CC to 22(R)-hydroxycholesterol (PubMed:24206663).
CC {ECO:0000269|PubMed:24206663, ECO:0000269|PubMed:25806685,
CC ECO:0000269|PubMed:25898003, ECO:0000269|PubMed:28846071}.
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are born at the expected Mendelian
CC frequency, but none survives beyond day 2 due to an extensive
CC triacylglycerol accumulation in enterocytes associated with very low
CC blood glucose levels at birth (P1.5) (PubMed:25806685,
CC PubMed:25898003). Conditional knockdown in intestine results in
CC hyperproliferation of the intestinal crypt and increased susceptibility
CC to intestinal tumorigenesis (PubMed:29395055).
CC {ECO:0000269|PubMed:25806685, ECO:0000269|PubMed:25898003,
CC ECO:0000269|PubMed:29395055}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000255}.
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DR EMBL; AY028317; AAK20915.1; -; mRNA.
DR EMBL; AB294194; BAG12120.1; -; mRNA.
DR EMBL; CH466523; EDK99746.1; -; Genomic_DNA.
DR EMBL; BC006753; AAH06753.2; -; mRNA.
DR EMBL; AC002397; AAC36007.1; -; Genomic_DNA.
DR EMBL; AK083687; BAC38993.1; -; mRNA.
DR CCDS; CCDS20523.1; -.
DR RefSeq; NP_660112.1; NM_145130.2.
DR AlphaFoldDB; Q91V01; -.
DR SMR; Q91V01; -.
DR BioGRID; 200053; 4.
DR IntAct; Q91V01; 1.
DR MINT; Q91V01; -.
DR STRING; 10090.ENSMUSP00000004381; -.
DR ChEMBL; CHEMBL1255159; -.
DR SwissLipids; SLP:000000286; -.
DR GlyGen; Q91V01; 3 sites.
DR iPTMnet; Q91V01; -.
DR PhosphoSitePlus; Q91V01; -.
DR EPD; Q91V01; -.
DR jPOST; Q91V01; -.
DR MaxQB; Q91V01; -.
DR PaxDb; Q91V01; -.
DR PeptideAtlas; Q91V01; -.
DR PRIDE; Q91V01; -.
DR ProteomicsDB; 295971; -.
DR Antibodypedia; 67641; 75 antibodies from 11 providers.
DR DNASU; 14792; -.
DR Ensembl; ENSMUST00000004381; ENSMUSP00000004381; ENSMUSG00000004270.
DR GeneID; 14792; -.
DR KEGG; mmu:14792; -.
DR UCSC; uc009drf.2; mouse.
DR CTD; 10162; -.
DR MGI; MGI:1315211; Lpcat3.
DR VEuPathDB; HostDB:ENSMUSG00000004270; -.
DR eggNOG; KOG2705; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_011340_6_1_1; -.
DR InParanoid; Q91V01; -.
DR OMA; CILVLRM; -.
DR OrthoDB; 881262at2759; -.
DR PhylomeDB; Q91V01; -.
DR TreeFam; TF106143; -.
DR BRENDA; 2.3.1.23; 3474.
DR Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
DR Reactome; R-MMU-1482801; Acyl chain remodelling of PS.
DR Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
DR UniPathway; UPA00085; -.
DR BioGRID-ORCS; 14792; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Lpcat3; mouse.
DR PRO; PR:Q91V01; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q91V01; protein.
DR Bgee; ENSMUSG00000004270; Expressed in yolk sac and 256 other tissues.
DR ExpressionAtlas; Q91V01; baseline and differential.
DR Genevisible; Q91V01; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0106262; F:1-acylglycerophosphoethanolamine O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0106263; F:1-acylglycerophosphoserine O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0071617; F:lysophospholipid acyltransferase activity; IBA:GO_Central.
DR GO; GO:0034378; P:chylomicron assembly; IMP:UniProtKB.
DR GO; GO:0090158; P:endoplasmic reticulum membrane organization; IMP:UniProtKB.
DR GO; GO:0036335; P:intestinal stem cell homeostasis; IMP:UniProtKB.
DR GO; GO:0030258; P:lipid modification; IBA:GO_Central.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:UniProtKB.
DR GO; GO:1903573; P:negative regulation of response to endoplasmic reticulum stress; IDA:UniProtKB.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IMP:UniProtKB.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IBA:GO_Central.
DR GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; IMP:UniProtKB.
DR GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; IMP:UniProtKB.
DR GO; GO:0045797; P:positive regulation of intestinal cholesterol absorption; IMP:UniProtKB.
DR GO; GO:1901310; P:positive regulation of sterol regulatory element binding protein cleavage; IMP:UniProtKB.
DR GO; GO:1905885; P:positive regulation of triglyceride transport; IMP:UniProtKB.
DR GO; GO:0045540; P:regulation of cholesterol biosynthetic process; IMP:UniProtKB.
DR GO; GO:0097006; P:regulation of plasma lipoprotein particle levels; IMP:MGI.
DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; IMP:UniProtKB.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Endoplasmic reticulum; Glycoprotein;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6P1A2"
FT CHAIN 2..487
FT /note="Lysophospholipid acyltransferase 5"
FT /id="PRO_0000233383"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 484..487
FT /note="Di-lysine motif"
FT ACT_SITE 338
FT /evidence="ECO:0000250"
FT ACT_SITE 374
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q6P1A2"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 374
FT /note="H->A: Loss of O-acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:25898003"
FT CONFLICT 48..49
FT /note="IF -> SH (in Ref. 5; AAC36007)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 487 AA; 56147 MW; EBC51DB3734B17C7 CRC64;
MASTADGDMG ETLEQMRGLW PGVEDLSLNK LATSLGASEQ ALRLIFSIFL GYPLALFYRH
YLFYKDSYLI HLFHTFTGLS IAYFNFGHQF YHSLLCVVLQ FLILRLMGRT VTAVITTLCF
QMAYLLAGYY YTATGDYDIK WTMPHCVLTL KLIGLCIDYY DGGKDGNSLT SEQQKYAIRG
VPSLLEVAGF SYFYGAFLVG PQFSMNHYMK LVRGQLTDIP GKMPNSTIPA LKRLSLGLVY
LVGYTLLSPH ITDDYLLTED YDNRPFWFRC MYMLIWGKFV LYKYVTCWLV TEGVCILSGL
GFNGFDENGT VRWDACANMK VWLFETTPRF NGTIASFNIN TNAWVARYIF KRLKFLGNKE
LSQGLSLLFL ALWHGLHSGY LICFQMEFLI VIVEKQVSSL IRDSPALSSL ASITALQPFY
YLVQQTIHWL FMGYSMTAFC LFTWDKWLKV YRSIYFLGHV FFLSLLFILP YIHKAMVPRK
EKLKKRE
