GPAT3_MOUSE
ID GPAT3_MOUSE Reviewed; 438 AA.
AC Q8C0N2; A6H5X0;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Glycerol-3-phosphate acyltransferase 3 {ECO:0000250|UniProtKB:Q53EU6};
DE Short=GPAT-3;
DE EC=2.3.1.15 {ECO:0000269|PubMed:17170135};
DE AltName: Full=1-acyl-sn-glycerol-3-phosphate O-acyltransferase 10 {ECO:0000250|UniProtKB:Q53EU6};
DE Short=AGPAT 10 {ECO:0000250|UniProtKB:Q53EU6};
DE AltName: Full=1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9;
DE Short=1-AGP acyltransferase 9;
DE Short=1-AGPAT 9;
DE EC=2.3.1.51 {ECO:0000250|UniProtKB:Q53EU6};
DE AltName: Full=Acyl-CoA:glycerol-3-phosphate acyltransferase 3 {ECO:0000303|PubMed:17170135};
DE Short=mGPAT3;
DE AltName: Full=Lysophosphatidic acid acyltransferase theta;
DE Short=LPAAT-theta;
GN Name=Gpat3 {ECO:0000250|UniProtKB:Q53EU6}; Synonyms=Agpat9;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CD-1; TISSUE=Brain, Neural stem cell, and Testis;
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 [3]
RP CATALYTIC ACTIVITY.
RX PubMed=11003606; DOI=10.1152/ajpcell.2000.279.4.c1259;
RA Starodub O., Jolly C.A., Atshaves B.P., Roths J.B., Murphy E.J., Kier A.B.,
RA Schroeder F.;
RT "Sterol carrier protein-2 localization in endoplasmic reticulum and role in
RT phospholipid formation.";
RL Am. J. Physiol. 279:C1259-C1269(2000).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=17170135; DOI=10.1073/pnas.0609140103;
RA Cao J., Li J.-L., Li D., Tobin J.F., Gimeno R.E.;
RT "Molecular identification of microsomal acyl-CoA:glycerol-3-phosphate
RT acyltransferase, a key enzyme in de novo triacylglycerol synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:19695-19700(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, 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).
CC -!- FUNCTION: Converts glycerol-3-phosphate to 1-acyl-sn-glycerol-3-
CC phosphate (lysophosphatidic acid or LPA) by incorporating an acyl
CC moiety at the sn-1 position of the glycerol backbone (PubMed:17170135).
CC Also converts LPA into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic
CC acid or PA) by incorporating an acyl moiety at the sn-2 position of the
CC glycerol backbone (By similarity). Protects cells against lipotoxicity
CC (By similarity). {ECO:0000250|UniProtKB:Q53EU6,
CC ECO:0000269|PubMed:17170135}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC Evidence={ECO:0000269|PubMed:17170135};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15326;
CC Evidence={ECO:0000305|PubMed:17170135};
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:0000250|UniProtKB:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + sn-glycerol 3-phosphate = 1-dodecanoyl-sn-
CC glycerol 3-phosphate + CoA; Xref=Rhea:RHEA:35727, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57375, ChEBI:CHEBI:57597, ChEBI:CHEBI:72682;
CC Evidence={ECO:0000269|PubMed:17170135};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35728;
CC Evidence={ECO:0000305|PubMed:17170135};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + sn-glycerol 3-phosphate = 1-hexadecanoyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:35723,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57518,
CC ChEBI:CHEBI:57597; Evidence={ECO:0000269|PubMed:11003606};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35724;
CC Evidence={ECO:0000269|PubMed:11003606};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + sn-glycerol 3-phosphate = 1-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37199,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:74544; Evidence={ECO:0000269|PubMed:11003606};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37200;
CC Evidence={ECO:0000269|PubMed:11003606};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + sn-glycerol 3-phosphate = 1-
CC (9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37203, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:74547;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37204;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-tetradecanoyl-sn-glycerol 3-
CC phosphate = 1-tetradecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:37187, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:72683, ChEBI:CHEBI:74586;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37188;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
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:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
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:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(6Z,9Z,12Z-octadecatrienoyl)-sn-
CC glycero-3-phosphate = (6Z,9Z,12Z)-octadecatrienoyl-2-(9Z)-
CC octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37179,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74581,
CC ChEBI:CHEBI:74582; Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37180;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z,12Z,15Z)-octadecatrienoyl-sn-
CC glycero-3-phosphate = 1-(9Z,12Z,15Z)-octadecatrienoyl-2-(9Z)-
CC octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37139,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74549,
CC ChEBI:CHEBI:74550; Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37140;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
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:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37172;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37143, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74551;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
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:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37148;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphate = 1-(9Z)-octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn-
CC glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37159, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:74544, ChEBI:CHEBI:74563;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37160;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
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:Q53EU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37456;
CC Evidence={ECO:0000250|UniProtKB:Q53EU6};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17170135}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Most abundant in epididymal fat, followed by small
CC intestine, brown adipose tissue, kidney, heart and colon.
CC {ECO:0000269|PubMed:17170135}.
CC -!- INDUCTION: During adipocyte differentiation.
CC {ECO:0000269|PubMed:17170135}.
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}.
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DR EMBL; AK030171; BAC26820.1; -; mRNA.
DR EMBL; AK160261; BAE35719.1; -; mRNA.
DR EMBL; AK138410; BAE23647.1; -; mRNA.
DR EMBL; BC096769; AAH96769.1; -; mRNA.
DR EMBL; BC138228; AAI38229.1; -; mRNA.
DR EMBL; BC145669; AAI45670.1; -; mRNA.
DR CCDS; CCDS19470.1; -.
DR RefSeq; NP_766303.1; NM_172715.3.
DR RefSeq; XP_011247733.1; XM_011249431.2.
DR RefSeq; XP_011247734.1; XM_011249432.1.
DR RefSeq; XP_011247735.1; XM_011249433.2.
DR AlphaFoldDB; Q8C0N2; -.
DR STRING; 10090.ENSMUSP00000031255; -.
DR SwissLipids; SLP:000000103; -.
DR iPTMnet; Q8C0N2; -.
DR PhosphoSitePlus; Q8C0N2; -.
DR EPD; Q8C0N2; -.
DR jPOST; Q8C0N2; -.
DR MaxQB; Q8C0N2; -.
DR PaxDb; Q8C0N2; -.
DR PeptideAtlas; Q8C0N2; -.
DR PRIDE; Q8C0N2; -.
DR ProteomicsDB; 267755; -.
DR Antibodypedia; 25231; 214 antibodies from 27 providers.
DR DNASU; 231510; -.
DR Ensembl; ENSMUST00000031255; ENSMUSP00000031255; ENSMUSG00000029314.
DR Ensembl; ENSMUST00000092990; ENSMUSP00000090667; ENSMUSG00000029314.
DR Ensembl; ENSMUST00000112887; ENSMUSP00000108508; ENSMUSG00000029314.
DR GeneID; 231510; -.
DR KEGG; mmu:231510; -.
DR UCSC; uc008yih.1; mouse.
DR CTD; 84803; -.
DR MGI; MGI:3603816; Gpat3.
DR VEuPathDB; HostDB:ENSMUSG00000029314; -.
DR eggNOG; KOG2898; Eukaryota.
DR GeneTree; ENSGT01030000234574; -.
DR HOGENOM; CLU_031080_0_1_1; -.
DR InParanoid; Q8C0N2; -.
DR OMA; YMRILVK; -.
DR OrthoDB; 526132at2759; -.
DR PhylomeDB; Q8C0N2; -.
DR TreeFam; TF315039; -.
DR BRENDA; 2.3.1.15; 3474.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR UniPathway; UPA00282; -.
DR UniPathway; UPA00557; UER00612.
DR BioGRID-ORCS; 231510; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Gpat3; mouse.
DR PRO; PR:Q8C0N2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8C0N2; protein.
DR Bgee; ENSMUSG00000029314; Expressed in small intestine Peyer's patch and 137 other tissues.
DR ExpressionAtlas; Q8C0N2; baseline and differential.
DR Genevisible; Q8C0N2; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
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:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IDA:UniProtKB.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0032006; P:regulation of TOR signaling; ISO:MGI.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IDA:UniProtKB.
DR CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR InterPro; IPR045252; LPCAT1-like.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
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; Phospholipid biosynthesis;
KW Phospholipid metabolism; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..438
FT /note="Glycerol-3-phosphate acyltransferase 3"
FT /id="PRO_0000291571"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 229..234
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q9D517"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53EU6"
SQ SEQUENCE 438 AA; 49000 MW; 29B4ED7405DCC8BD CRC64;
MEGADLAVKL LSTWLTLVGG LILLPSAFGL SLGISEIYMK ILVKTLEWAT LRIQKGAPKE
SALKNSASVG IIQRDESPME KGLSGLRGRD FELSDVFYFS KKGLEAIVED EVTQRFSSEE
LVSWNLLTRT NVNFQYISPR LTMVWVLGVL VRYCFLLPLR VTLAFIGISL LIIGTTLVGQ
LPDSSLKNWL SELVHLTCCR ICVRSLSGTI HYHNKQYRPQ KGGICVANHT SPIDVLILAT
DGCYAMVGQV HGGLMGIIQR AMVKACPHVW FERSEIKDRH LVTKRLKEHI ADKKKLPILI
FPEGTCINNT SVMMFKKGSF EIGGTIYPVA IKYNPQFGDA FWNSSKYNLV SYLLRIMTSW
AIVCDVWYMP PMTREEGEDA VQFANRVKSA IAVQGGLTEL PWDGGLKRAK VKDTFKEEQQ
KNYSKMIVGN GSPNLARD
