PLCE_MOUSE
ID PLCE_MOUSE Reviewed; 365 AA.
AC Q9D1E8; Q3U702; Q8BG61; Q8CGN6;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon;
DE EC=2.3.1.51 {ECO:0000269|PubMed:15367102};
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 5;
DE Short=1-AGP acyltransferase 5;
DE Short=1-AGPAT 5;
DE AltName: Full=Lysophosphatidic acid acyltransferase epsilon;
DE Short=LPAAT-epsilon;
GN Name=Agpat5; Synonyms=D8Ertd319e;
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 [MRNA].
RC STRAIN=NMRI;
RA Lu B., Jiang Y.J., Chan M., Choy P.C.;
RT "Identification and characterization of 1-acylglycerolphosphate
RT acyltransferase-epsilon.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Cerebellum, Dendritic cell, Embryo, and Spleen;
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=Czech II; TISSUE=Mammary gland;
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, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=15367102; DOI=10.1042/bj20041348;
RA Lu B., Jiang Y.J., Zhou Y., Xu F.Y., Hatch G.M., Choy P.C.;
RT "Cloning and characterization of murine 1-acyl-sn-glycerol 3-phosphate
RT acyltransferases and their regulation by PPARalpha in murine heart.";
RL Biochem. J. 385:469-477(2005).
CC -!- FUNCTION: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic
CC acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid
CC or PA) by incorporating an acyl moiety at the sn-2 position of the
CC glycerol backbone (PubMed:15367102). Acts on LPA containing saturated
CC or unsaturated fatty acids C15:0-C20:4 at the sn-1 position using
CC C18:1-CoA as the acyl donor (By similarity). Also acts on
CC lysophosphatidylethanolamine using oleoyl-CoA, but not arachidonoyl-
CC CoA, and lysophosphatidylinositol using arachidonoyl-CoA, but not
CC oleoyl-CoA (By similarity). Activity toward lysophosphatidylglycerol
CC not detectable (By similarity). {ECO:0000250|UniProtKB:Q9NUQ2,
CC ECO:0000269|PubMed:15367102}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000269|PubMed:15367102};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000305|PubMed:15367102};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + tetradecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-tetradecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37171, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74579;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37172;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + pentadecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-pentadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37175, ChEBI:CHEBI:57287, ChEBI:CHEBI:74309,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74578;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37176;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + octadecanoyl-CoA
CC = 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37147, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74552;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37148;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + nonadecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-nonadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37595, ChEBI:CHEBI:57287, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:75104, ChEBI:CHEBI:75105;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37596;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:37499, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:74971, ChEBI:CHEBI:74986;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37500;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
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:Q9NUQ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37388;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phospho-(1D-myo-inositol) = 1-(9Z-octadecenoyl)-2-
CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-1D-myo-inositol
CC + CoA; Xref=Rhea:RHEA:42216, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:78762, ChEBI:CHEBI:78765;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42217;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
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:0000250|UniProtKB:Q9NUQ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37408;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
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:0000250|UniProtKB:Q9NUQ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37380;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate
CC = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:33187, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:64839;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-heptadecanoyl-sn-glycero-3-phosphate
CC = 1-heptadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37151, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74554, ChEBI:CHEBI:74556;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37152;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-
CC glycero-3-phosphate = 1-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-2-(9Z)-
CC octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37455,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74938,
CC ChEBI:CHEBI:74941; Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37456;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-phosphate
CC = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37163, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74560, ChEBI:CHEBI:74565;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37164;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37443,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:74928; Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37444;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + heptadecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-heptadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37155, ChEBI:CHEBI:57287, ChEBI:CHEBI:74307,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74558;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37156;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
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:0000250|UniProtKB:Q9NUQ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37396;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74546;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA
CC = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:42592, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:64839, ChEBI:CHEBI:74544;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42593;
CC Evidence={ECO:0000250|UniProtKB:Q9NUQ2};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9NUQ2}; Multi-pass membrane protein
CC {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q9NUQ2}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q9NUQ2}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15367102}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000250|UniProtKB:Q9D517}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-12 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AY161042; AAN75571.1; -; mRNA.
DR EMBL; AK003649; BAB22915.2; -; mRNA.
DR EMBL; AK082137; BAC38421.1; -; mRNA.
DR EMBL; AK089885; BAC40983.1; -; mRNA.
DR EMBL; AK152709; BAE31436.1; -; mRNA.
DR EMBL; AK152889; BAE31572.1; -; mRNA.
DR EMBL; AK155378; BAE33229.1; -; mRNA.
DR EMBL; BC031987; AAH31987.2; -; mRNA.
DR CCDS; CCDS22126.1; -.
DR RefSeq; NP_081068.1; NM_026792.3.
DR AlphaFoldDB; Q9D1E8; -.
DR BioGRID; 206392; 3.
DR IntAct; Q9D1E8; 1.
DR STRING; 10090.ENSMUSP00000117025; -.
DR iPTMnet; Q9D1E8; -.
DR PhosphoSitePlus; Q9D1E8; -.
DR EPD; Q9D1E8; -.
DR MaxQB; Q9D1E8; -.
DR PaxDb; Q9D1E8; -.
DR PRIDE; Q9D1E8; -.
DR ProteomicsDB; 289924; -.
DR Antibodypedia; 2138; 320 antibodies from 27 providers.
DR Ensembl; ENSMUST00000149565; ENSMUSP00000117025; ENSMUSG00000031467.
DR GeneID; 52123; -.
DR KEGG; mmu:52123; -.
DR UCSC; uc009kzv.1; mouse.
DR CTD; 55326; -.
DR MGI; MGI:1196345; Agpat5.
DR VEuPathDB; HostDB:ENSMUSG00000031467; -.
DR eggNOG; KOG1505; Eukaryota.
DR GeneTree; ENSGT00950000182836; -.
DR InParanoid; Q9D1E8; -.
DR OMA; KAETPMY; -.
DR OrthoDB; 959325at2759; -.
DR PhylomeDB; Q9D1E8; -.
DR TreeFam; TF314346; -.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR UniPathway; UPA00557; UER00613.
DR BioGRID-ORCS; 52123; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Agpat5; mouse.
DR PRO; PR:Q9D1E8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9D1E8; protein.
DR Bgee; ENSMUSG00000031467; Expressed in triceps brachii and 267 other tissues.
DR ExpressionAtlas; Q9D1E8; baseline and differential.
DR Genevisible; Q9D1E8; MM.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IDA:MGI.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0006639; P:acylglycerol metabolic process; IDA:MGI.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:MGI.
DR InterPro; IPR032098; Acyltransf_C.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF16076; Acyltransf_C; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Mitochondrion; Nucleus;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..365
FT /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
FT epsilon"
FT /id="PRO_0000208201"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 93..98
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q9D517"
FT CONFLICT 80
FT /note="L -> W (in Ref. 1; AAN75571)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="L -> M (in Ref. 1; AAN75571)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 365 AA; 42202 MW; C13E14759610E19B CRC64;
MLLSLVLHTY SMRYLLPSVL LLGSAPTYLL AWTLWRVLSA LMPARLYQRV DDRLYCVYQN
MVLFFFENYT GVQILLYGDL PKNKENVIYL ANHQSTVDWI VADMLAARQD ALGHVRYVLK
DKLKWLPLYG FYFAQHGGIY VKRSAKFNDK EMRSKLQSYV NAGTPMYLVI FPEGTRYNAT
YTKLLSASQA FAAQRGLAVL KHVLTPRIKA THVAFDSMKS HLDAIYDVTV VYEGNEKGSG
KYSNPPSMTE FLCKQCPKLH IHFDRIDRNE VPEEQEHMKK WLHERFEIKD RLLIEFYDSP
DPERRNKFPG KSVHSRLSVK KTLPSVLILG SLTAVMLMTE SGRKLYMGTW LYGTLLGCLW
FVIKA
