DGAT2_MOUSE
ID DGAT2_MOUSE Reviewed; 388 AA.
AC Q9DCV3;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Diacylglycerol O-acyltransferase 2 {ECO:0000305};
DE EC=2.3.1.20 {ECO:0000269|PubMed:15834126, ECO:0000269|PubMed:16106050};
DE AltName: Full=Acyl-CoA retinol O-fatty-acyltransferase;
DE Short=ARAT;
DE Short=Retinol O-fatty-acyltransferase;
DE EC=2.3.1.76 {ECO:0000250|UniProtKB:Q96PD7};
DE AltName: Full=Diglyceride acyltransferase 2;
GN Name=Dgat2 {ECO:0000312|MGI:MGI:1915050};
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], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=11481335; DOI=10.1074/jbc.m106219200;
RA Cases S., Stone S.J., Zhou P., Yen C.-L.E., Tow B., Lardizabal K.D.,
RA Voelker T., Farese R.V. Jr.;
RT "Cloning of DGAT2, a second mammalian diacylglycerol acyltransferase, and
RT related family members.";
RL J. Biol. Chem. 276:38870-38876(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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=Liver;
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 INDUCTION.
RX PubMed=12413942; DOI=10.1016/s0006-291x(02)02466-x;
RA Meegalla R.L., Billheimer J.T., Cheng D.;
RT "Concerted elevation of acyl-coenzyme A:diacylglycerol acyltransferase
RT (DGAT) activity through independent stimulation of mRNA expression of DGAT1
RT and DGAT2 by carbohydrate and insulin.";
RL Biochem. Biophys. Res. Commun. 298:317-323(2002).
RN [5]
RP INDUCTION.
RX PubMed=14521909; DOI=10.1016/j.bbrc.2003.09.015;
RA Wakimoto K., Chiba H., Michibata H., Seishima M., Kawasaki S., Okubo K.,
RA Mitsui H., Torii H., Imai Y.;
RT "A novel diacylglycerol acyltransferase (DGAT2) is decreased in human
RT psoriatic skin and increased in diabetic mice.";
RL Biochem. Biophys. Res. Commun. 310:296-302(2003).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=14668353; DOI=10.1074/jbc.m311000200;
RA Stone S.J., Myers H.M., Watkins S.M., Brown B.E., Feingold K.R.,
RA Elias P.M., Farese R.V. Jr.;
RT "Lipopenia and skin barrier abnormalities in DGAT2-deficient mice.";
RL J. Biol. Chem. 279:11767-11776(2004).
RN [7]
RP ACTIVITY REGULATION.
RX PubMed=15258194; DOI=10.1194/jlr.m300403-jlr200;
RA Ganji S.H., Tavintharan S., Zhu D., Xing Y., Kamanna V.S., Kashyap M.L.;
RT "Niacin noncompetitively inhibits DGAT2 but not DGAT1 activity in HepG2
RT cells.";
RL J. Lipid Res. 45:1835-1845(2004).
RN [8]
RP INDUCTION.
RX PubMed=16001399; DOI=10.1002/hep.20783;
RA Yu X.X., Murray S.F., Pandey S.K., Booten S.L., Bao D., Song X.Z.,
RA Kelly S., Chen S., McKay R., Monia B.P., Bhanot S.;
RT "Antisense oligonucleotide reduction of DGAT2 expression improves hepatic
RT steatosis and hyperlipidemia in obese mice.";
RL Hepatology 42:362-371(2005).
RN [9]
RP FUNCTION.
RX PubMed=15797871; DOI=10.1074/jbc.m412989200;
RA Yamazaki T., Sasaki E., Kakinuma C., Yano T., Miura S., Ezaki O.;
RT "Increased very low density lipoprotein secretion and gonadal fat mass in
RT mice overexpressing liver DGAT1.";
RL J. Biol. Chem. 280:21506-21514(2005).
RN [10]
RP CATALYTIC ACTIVITY.
RX PubMed=15834126; DOI=10.1194/jlr.m500036-jlr200;
RA Yen C.L., Monetti M., Burri B.J., Farese R.V. Jr.;
RT "The triacylglycerol synthesis enzyme DGAT1 also catalyzes the synthesis of
RT diacylglycerols, waxes, and retinyl esters.";
RL J. Lipid Res. 46:1502-1511(2005).
RN [11]
RP CATALYTIC ACTIVITY.
RX PubMed=16106050; DOI=10.1194/jlr.m500168-jlr200;
RA Yen C.-L.E., Brown C.H. IV, Monetti M., Farese R.V. Jr.;
RT "A human skin multifunctional O-acyltransferase that catalyzes the
RT synthesis of acylglycerols, waxes, and retinyl esters.";
RL J. Lipid Res. 46:2388-2397(2005).
RN [12]
RP SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY.
RX PubMed=17035227; DOI=10.1074/jbc.m607986200;
RA Stone S.J., Levin M.C., Farese R.V. Jr.;
RT "Membrane topology and identification of key functional amino acid residues
RT of murine acyl-CoA:diacylglycerol acyltransferase-2.";
RL J. Biol. Chem. 281:40273-40282(2006).
RN [13]
RP SUBUNIT, FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=21680734; DOI=10.1074/jbc.m111.256008;
RA McFie P.J., Banman S.L., Kary S., Stone S.J.;
RT "Murine diacylglycerol acyltransferase-2 (DGAT2) can catalyze
RT triacylglycerol synthesis and promote lipid droplet formation independent
RT of its localization to the endoplasmic reticulum.";
RL J. Biol. Chem. 286:28235-28246(2011).
RN [14]
RP CATALYTIC ACTIVITY.
RX PubMed=23066022; DOI=10.1074/jbc.m112.400416;
RA Eichmann T.O., Kumari M., Haas J.T., Farese R.V. Jr., Zimmermann R.,
RA Lass A., Zechner R.;
RT "Studies on the substrate and stereo/regioselectivity of adipose
RT triglyceride lipase, hormone-sensitive lipase, and diacylglycerol-O-
RT acyltransferases.";
RL J. Biol. Chem. 287:41446-41457(2012).
RN [15]
RP FUNCTION.
RX PubMed=22493088; DOI=10.1194/jlr.m020156;
RA Qi J., Lang W., Geisler J.G., Wang P., Petrounia I., Mai S., Smith C.,
RA Askari H., Struble G.T., Williams R., Bhanot S., Monia B.P., Bayoumy S.,
RA Grant E., Caldwell G.W., Todd M.J., Liang Y., Gaul M.D., Demarest K.T.,
RA Connelly M.A.;
RT "The use of stable isotope-labeled glycerol and oleic acid to differentiate
RT the hepatic functions of DGAT1 and -2.";
RL J. Lipid Res. 53:1106-1116(2012).
CC -!- FUNCTION: Essential acyltransferase that catalyzes the terminal and
CC only committed step in triacylglycerol synthesis by using
CC diacylglycerol and fatty acyl CoA as substrates. Required for synthesis
CC and storage of intracellular triglycerides. Probably plays a central
CC role in cytosolic lipid accumulation. In liver, is primarily
CC responsible for incorporating endogenously synthesized fatty acids into
CC triglycerides. Functions also as an acyl-CoA retinol acyltransferase
CC (ARAT) (By similarity). Also able to use 1-monoalkylglycerol (1-MAkG)
CC as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol
CC (MAMAG) (By similarity). {ECO:0000250|UniProtKB:Q96PD7,
CC ECO:0000269|PubMed:11481335, ECO:0000269|PubMed:15797871,
CC ECO:0000269|PubMed:21680734, ECO:0000269|PubMed:22493088}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol
CC + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20;
CC Evidence={ECO:0000269|PubMed:15834126, ECO:0000269|PubMed:16106050};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10869;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + an acyl-CoA = an all-trans-retinyl ester +
CC CoA; Xref=Rhea:RHEA:11488, ChEBI:CHEBI:17336, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:63410; EC=2.3.1.76;
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11489;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + hexadecanoyl-CoA = 1,2-
CC di-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol + CoA;
CC Xref=Rhea:RHEA:38163, ChEBI:CHEBI:52333, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:75583;
CC Evidence={ECO:0000269|PubMed:15834126, ECO:0000269|PubMed:16106050};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38164;
CC Evidence={ECO:0000269|PubMed:15834126, ECO:0000305|PubMed:16106050};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1,2-di-(9Z-octadecenoyl)-sn-glycerol =
CC 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38219,
CC ChEBI:CHEBI:52333, ChEBI:CHEBI:53753, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387; Evidence={ECO:0000269|PubMed:21680734,
CC ECO:0000269|PubMed:23066022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38220;
CC Evidence={ECO:0000305|PubMed:21680734, ECO:0000305|PubMed:23066022};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1,3-di-(9Z-octadecenoyl)-glycerol =
CC 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38435,
CC ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:75735; Evidence={ECO:0000269|PubMed:23066022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38436;
CC Evidence={ECO:0000305|PubMed:23066022};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 2,3-di-(9Z)-octadecenoyl-sn-glycerol =
CC 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38439,
CC ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:75824; Evidence={ECO:0000269|PubMed:23066022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38440;
CC Evidence={ECO:0000305|PubMed:23066022};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + hexadecanoyl-CoA = 1-
CC hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CoA;
CC Xref=Rhea:RHEA:38071, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:73990, ChEBI:CHEBI:75466;
CC Evidence={ECO:0000269|PubMed:15834126};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38072;
CC Evidence={ECO:0000305|PubMed:15834126};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 2-(9Z-octadecenoyl)-glycerol = 1,2-di-
CC (9Z-octadecenoyl)-sn-glycerol + CoA; Xref=Rhea:RHEA:37911,
CC ChEBI:CHEBI:52333, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:Q96PD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37912;
CC Evidence={ECO:0000250|UniProtKB:Q96PD7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + hexadecanoyl-CoA = all-trans-retinyl
CC hexadecanoate + CoA; Xref=Rhea:RHEA:38175, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17616, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379;
CC Evidence={ECO:0000250|UniProtKB:Q96PD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38176;
CC Evidence={ECO:0000250|UniProtKB:Q96PD7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecenyl)-glycerol = 1-O-
CC (9Z-octadecenyl)-mono-(9Z-octadecenoyl)-glycerol + CoA;
CC Xref=Rhea:RHEA:55340, ChEBI:CHEBI:34116, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:138734;
CC Evidence={ECO:0000250|UniProtKB:Q96PD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55341;
CC Evidence={ECO:0000250|UniProtKB:Q96PD7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-glycerol = 1,2-di-
CC (9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:37915,
CC ChEBI:CHEBI:52323, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:Q96PD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37916;
CC Evidence={ECO:0000250|UniProtKB:Q96PD7};
CC -!- ACTIVITY REGULATION: Inhibited by niacin. {ECO:0000250}.
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC -!- SUBUNIT: Forms multimeric complexes consisting of several DGAT2
CC subunits (PubMed:21680734). Interacts with SLC27A1 and this interaction
CC is enhanced in the presence of ZFYVE1 (By similarity).
CC {ECO:0000250|UniProtKB:Q96PD7, ECO:0000269|PubMed:21680734}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96PD7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q96PD7}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q96PD7}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q96PD7}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in liver. Also expressed in
CC testis. {ECO:0000269|PubMed:11481335}.
CC -!- INDUCTION: In white adipose tissue, it is regulated by leptin. By
CC insulin. Up-regulated in diabetic mice. Down-regulated upon fasting and
CC replenished upon refeeding in adipose tissue and liver. Down-regulation
CC in obese animals can reduce hepatic lipogenesis and hepatic steatosis
CC as well as attenuate hyperlipidemia, thereby leading to an improvement
CC in metabolic syndrome. {ECO:0000269|PubMed:12413942,
CC ECO:0000269|PubMed:14521909, ECO:0000269|PubMed:16001399}.
CC -!- DISRUPTION PHENOTYPE: Mice are lipopenic and die soon after birth,
CC apparently from profound reductions in substrates for energy metabolism
CC and from impaired permeability barrier function in the skin.
CC {ECO:0000269|PubMed:14668353}.
CC -!- SIMILARITY: Belongs to the diacylglycerol acyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF384160; AAK84175.1; -; mRNA.
DR EMBL; AK002443; BAB22105.1; -; mRNA.
DR EMBL; BC043447; AAH43447.1; -; mRNA.
DR CCDS; CCDS21477.1; -.
DR RefSeq; NP_080660.1; NM_026384.3.
DR AlphaFoldDB; Q9DCV3; -.
DR BioGRID; 212449; 2.
DR STRING; 10090.ENSMUSP00000033001; -.
DR ChEMBL; CHEMBL1075285; -.
DR SwissLipids; SLP:000000303; -.
DR iPTMnet; Q9DCV3; -.
DR PhosphoSitePlus; Q9DCV3; -.
DR MaxQB; Q9DCV3; -.
DR PaxDb; Q9DCV3; -.
DR PRIDE; Q9DCV3; -.
DR ProteomicsDB; 279858; -.
DR Antibodypedia; 1632; 315 antibodies from 36 providers.
DR DNASU; 67800; -.
DR Ensembl; ENSMUST00000033001; ENSMUSP00000033001; ENSMUSG00000030747.
DR GeneID; 67800; -.
DR KEGG; mmu:67800; -.
DR UCSC; uc009ile.1; mouse.
DR CTD; 84649; -.
DR MGI; MGI:1915050; Dgat2.
DR VEuPathDB; HostDB:ENSMUSG00000030747; -.
DR eggNOG; KOG0831; Eukaryota.
DR GeneTree; ENSGT01030000234582; -.
DR HOGENOM; CLU_023995_0_1_1; -.
DR InParanoid; Q9DCV3; -.
DR OMA; STMFYVP; -.
DR OrthoDB; 1347007at2759; -.
DR PhylomeDB; Q9DCV3; -.
DR TreeFam; TF314707; -.
DR BRENDA; 2.3.1.20; 3474.
DR Reactome; R-MMU-1482883; Acyl chain remodeling of DAG and TAG.
DR Reactome; R-MMU-75109; Triglyceride biosynthesis.
DR UniPathway; UPA00282; -.
DR BioGRID-ORCS; 67800; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Dgat2; mouse.
DR PRO; PR:Q9DCV3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9DCV3; protein.
DR Bgee; ENSMUSG00000030747; Expressed in epithelium of small intestine and 252 other tissues.
DR ExpressionAtlas; Q9DCV3; baseline and differential.
DR Genevisible; Q9DCV3; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:1990578; C:perinuclear endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0003846; F:2-acylglycerol O-acyltransferase activity; IDA:MGI.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR GO; GO:0050252; F:retinol O-fatty-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0038183; P:bile acid signaling pathway; IEA:Ensembl.
DR GO; GO:0071400; P:cellular response to oleic acid; IMP:BHF-UCL.
DR GO; GO:0035356; P:cellular triglyceride homeostasis; IMP:BHF-UCL.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IDA:BHF-UCL.
DR GO; GO:0060613; P:fat pad development; IMP:BHF-UCL.
DR GO; GO:0055089; P:fatty acid homeostasis; IGI:BHF-UCL.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0019915; P:lipid storage; IMP:BHF-UCL.
DR GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IDA:BHF-UCL.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; IMP:BHF-UCL.
DR GO; GO:0006640; P:monoacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0046322; P:negative regulation of fatty acid oxidation; ISO:MGI.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; ISO:MGI.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISO:MGI.
DR GO; GO:0090181; P:regulation of cholesterol metabolic process; ISO:MGI.
DR GO; GO:0050746; P:regulation of lipoprotein metabolic process; ISO:MGI.
DR GO; GO:0097006; P:regulation of plasma lipoprotein particle levels; IMP:BHF-UCL.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IDA:MGI.
DR InterPro; IPR007130; DAGAT.
DR Pfam; PF03982; DAGAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Endoplasmic reticulum; Glycerol metabolism;
KW Lipid biosynthesis; Lipid droplet; Lipid metabolism; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..388
FT /note="Diacylglycerol O-acyltransferase 2"
FT /id="PRO_0000249046"
FT TOPO_DOM 1..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..92
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 388 AA; 43770 MW; 9C35C37DCAF61D55 CRC64;
MKTLIAAYSG VLRGERRAEA ARSENKNKGS ALSREGSGRW GTGSSILSAL QDIFSVTWLN
RSKVEKQLQV ISVLQWVLSF LVLGVACSVI LMYTFCTDCW LIAVLYFTWL AFDWNTPKKG
GRRSQWVRNW AVWRYFRDYF PIQLVKTHNL LTTRNYIFGY HPHGIMGLGA FCNFSTEATE
VSKKFPGIRP YLATLAGNFR MPVLREYLMS GGICPVNRDT IDYLLSKNGS GNAIIIVVGG
AAESLSSMPG KNAVTLKNRK GFVKLALRHG ADLVPTYSFG ENEVYKQVIF EEGSWGRWVQ
KKFQKYIGFA PCIFHGRGLF SSDTWGLVPY SKPITTVVGE PITVPKLEHP TQKDIDLYHA
MYMEALVKLF DNHKTKFGLP ETEVLEVN
