DGAT2_HUMAN
ID DGAT2_HUMAN Reviewed; 388 AA.
AC Q96PD7; A6ND76; Q5U810; Q68CL3; Q68DJ0; Q8NDB7; Q96BS0; Q9BYE5;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Diacylglycerol O-acyltransferase 2 {ECO:0000305};
DE EC=2.3.1.20 {ECO:0000269|PubMed:16214399, ECO:0000269|PubMed:27184406};
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:0000269|PubMed:16214399};
DE AltName: Full=Diglyceride acyltransferase 2;
GN Name=DGAT2 {ECO:0000312|HGNC:HGNC:16940};
GN ORFNames=HMFN1045, UNQ738/PRO1433;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
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 [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph node, and Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-341 (ISOFORM 2).
RC TISSUE=Adipocyte;
RA Reichwald K., Petz U., Platzer M.;
RT "Evaluation of gene structure of human DGAT2 gene.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 66-388.
RC TISSUE=Hepatoblastoma;
RX PubMed=15221005; DOI=10.1038/sj.onc.1207782;
RA Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S.,
RA Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S.,
RA Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.;
RT "Expression profiling and differential screening between hepatoblastomas
RT and the corresponding normal livers: identification of high expression of
RT the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas.";
RL Oncogene 23:5901-5911(2004).
RN [9]
RP CATALYTIC ACTIVITY.
RX PubMed=16214399; DOI=10.1016/j.bbalip.2005.09.003;
RA Orland M.D., Anwar K., Cromley D., Chu C.H., Chen L., Billheimer J.T.,
RA Hussain M.M., Cheng D.;
RT "Acyl coenzyme A dependent retinol esterification by acyl coenzyme A:
RT diacylglycerol acyltransferase 1.";
RL Biochim. Biophys. Acta 1737:76-82(2005).
RN [10]
RP CATALYTIC ACTIVITY.
RX PubMed=18768481; DOI=10.1074/jbc.m800494200;
RA Cheng D., Iqbal J., Devenny J., Chu C.H., Chen L., Dong J., Seethala R.,
RA Keim W.J., Azzara A.V., Lawrence R.M., Pelleymounter M.A., Hussain M.M.;
RT "Acylation of acylglycerols by acyl coenzyme A:diacylglycerol
RT acyltransferase 1 (DGAT1). Functional importance of DGAT1 in the intestinal
RT fat absorption.";
RL J. Biol. Chem. 283:29802-29811(2008).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=27184406; DOI=10.1016/j.bbrc.2016.05.071;
RA Brandt C., McFie P.J., Stone S.J.;
RT "Biochemical characterization of human acyl coenzyme A: 2-monoacylglycerol
RT acyltransferase-3 (MGAT3).";
RL Biochem. Biophys. Res. Commun. 475:264-270(2016).
RN [12]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=28420705; DOI=10.1194/jlr.m073445;
RA Ma Z., Onorato J.M., Chen L., Nelson D.W., Yen C.E., Cheng D.;
RT "Synthesis of neutral ether lipid monoalkyl-diacylglycerol by lipid
RT acyltransferases.";
RL J. Lipid Res. 58:1091-1099(2017).
RN [13]
RP INTERACTION WITH SLC27A1.
RX PubMed=30970241; DOI=10.1016/j.celrep.2019.03.025;
RA Li D., Zhao Y.G., Li D., Zhao H., Huang J., Miao G., Feng D., Liu P.,
RA Li D., Zhang H.;
RT "The ER-Localized Protein DFCP1 Modulates ER-Lipid Droplet Contact
RT Formation.";
RL Cell Rep. 27:343-358(2019).
RN [14]
RP VARIANT HIS-223.
RX PubMed=26786738; DOI=10.1002/humu.22959;
RA Hong Y.B., Kang J., Kim J.H., Lee J., Kwak G., Hyun Y.S., Nam S.H.,
RA Hong H.D., Choi Y.R., Jung S.C., Koo H., Lee J.E., Choi B.O., Chung K.W.;
RT "DGAT2 mutation in a family with autosomal-dominant early-onset axonal
RT Charcot-Marie-Tooth disease.";
RL Hum. Mutat. 37:473-480(2016).
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 (PubMed:27184406). Probably
CC plays a central role in cytosolic lipid accumulation. In liver, is
CC primarily responsible for incorporating endogenously synthesized fatty
CC acids into triglycerides (By similarity). Functions also as an acyl-CoA
CC retinol acyltransferase (ARAT) (By similarity). Also able to use 1-
CC monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of
CC monoalkyl-monoacylglycerol (MAMAG) (PubMed:28420705).
CC {ECO:0000250|UniProtKB:Q9DCV3, ECO:0000269|PubMed:27184406,
CC ECO:0000269|PubMed:28420705}.
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:16214399, ECO:0000269|PubMed:27184406};
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 Evidence={ECO:0000269|PubMed:16214399};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11489;
CC Evidence={ECO:0000305};
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:0000269|PubMed:18768481};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37912;
CC Evidence={ECO:0000305|PubMed:18768481};
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:18768481};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38220;
CC Evidence={ECO:0000305|PubMed:18768481};
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:0000269|PubMed:16214399};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38176;
CC Evidence={ECO:0000305|PubMed:16214399};
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:0000269|PubMed:28420705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55341;
CC Evidence={ECO:0000305|PubMed:28420705};
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:0000269|PubMed:28420705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37916;
CC Evidence={ECO:0000305|PubMed:28420705};
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:0000250|UniProtKB:Q9DCV3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38164;
CC Evidence={ECO:0000250|UniProtKB:Q9DCV3};
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:0000250|UniProtKB:Q9DCV3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38436;
CC Evidence={ECO:0000250|UniProtKB:Q9DCV3};
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:0000250|UniProtKB:Q9DCV3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38440;
CC Evidence={ECO:0000250|UniProtKB:Q9DCV3};
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:0000250|UniProtKB:Q9DCV3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38072;
CC Evidence={ECO:0000250|UniProtKB:Q9DCV3};
CC -!- ACTIVITY REGULATION: Inhibited by niacin. {ECO:0000250}.
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC {ECO:0000269|PubMed:27184406}.
CC -!- SUBUNIT: Forms multimeric complexes consisting of several DGAT2
CC subunits (By similarity). Interacts with SLC27A1 and this interaction
CC is enhanced in the presence of ZFYVE1 (PubMed:30970241).
CC {ECO:0000250|UniProtKB:Q9DCV3, ECO:0000269|PubMed:30970241}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14521909, ECO:0000269|PubMed:27184406}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:14521909}. Lipid droplet
CC {ECO:0000269|PubMed:27184406}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:27184406}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96PD7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96PD7-2; Sequence=VSP_020356;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in liver and white adipose
CC tissue. Expressed at lower level in mammary gland, testis and
CC peripheral blood leukocytes. Expressed in sebaceous glands of normal
CC skin but decreased psoriatic skin. {ECO:0000269|PubMed:11481335,
CC ECO:0000269|PubMed:14521909}.
CC -!- SIMILARITY: Belongs to the diacylglycerol acyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD38635.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD38961.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF384161; AAK84176.2; -; mRNA.
DR EMBL; AB048286; BAB40641.2; -; mRNA.
DR EMBL; AY358532; AAQ88896.1; -; mRNA.
DR EMBL; AL834287; CAD38961.1; ALT_INIT; mRNA.
DR EMBL; CR749377; CAH18230.1; -; mRNA.
DR EMBL; AP001922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015234; AAH15234.1; -; mRNA.
DR EMBL; AY780647; AAV35727.1; -; mRNA.
DR EMBL; AB073384; BAD38635.1; ALT_INIT; mRNA.
DR CCDS; CCDS31642.1; -. [Q96PD7-1]
DR CCDS; CCDS58162.1; -. [Q96PD7-2]
DR RefSeq; NP_001240820.1; NM_001253891.1. [Q96PD7-2]
DR RefSeq; NP_115953.2; NM_032564.4. [Q96PD7-1]
DR AlphaFoldDB; Q96PD7; -.
DR BioGRID; 124172; 6.
DR CORUM; Q96PD7; -.
DR IntAct; Q96PD7; 2.
DR MINT; Q96PD7; -.
DR STRING; 9606.ENSP00000228027; -.
DR BindingDB; Q96PD7; -.
DR ChEMBL; CHEMBL5853; -.
DR DrugBank; DB13961; Fish oil.
DR DrugBank; DB08949; Inositol nicotinate.
DR DrugBank; DB09568; Omega-3-carboxylic acids.
DR SwissLipids; SLP:000000304; -.
DR iPTMnet; Q96PD7; -.
DR PhosphoSitePlus; Q96PD7; -.
DR BioMuta; DGAT2; -.
DR DMDM; 74732654; -.
DR EPD; Q96PD7; -.
DR jPOST; Q96PD7; -.
DR MassIVE; Q96PD7; -.
DR PaxDb; Q96PD7; -.
DR PeptideAtlas; Q96PD7; -.
DR PRIDE; Q96PD7; -.
DR Antibodypedia; 1632; 315 antibodies from 36 providers.
DR DNASU; 84649; -.
DR Ensembl; ENST00000228027.12; ENSP00000228027.6; ENSG00000062282.15. [Q96PD7-1]
DR Ensembl; ENST00000376262.7; ENSP00000365438.3; ENSG00000062282.15. [Q96PD7-2]
DR GeneID; 84649; -.
DR KEGG; hsa:84649; -.
DR MANE-Select; ENST00000228027.12; ENSP00000228027.6; NM_032564.5; NP_115953.2.
DR UCSC; uc001oxa.4; human. [Q96PD7-1]
DR CTD; 84649; -.
DR DisGeNET; 84649; -.
DR GeneCards; DGAT2; -.
DR GeneReviews; DGAT2; -.
DR HGNC; HGNC:16940; DGAT2.
DR HPA; ENSG00000062282; Group enriched (adipose tissue, breast, liver, skin).
DR MalaCards; DGAT2; -.
DR MIM; 606983; gene.
DR neXtProt; NX_Q96PD7; -.
DR OpenTargets; ENSG00000062282; -.
DR Orphanet; 487814; Autosomal dominant Charcot-Marie-Tooth disease type 2 due to DGAT2 mutation.
DR PharmGKB; PA27304; -.
DR VEuPathDB; HostDB:ENSG00000062282; -.
DR eggNOG; KOG0831; Eukaryota.
DR GeneTree; ENSGT01030000234582; -.
DR HOGENOM; CLU_023995_0_1_1; -.
DR InParanoid; Q96PD7; -.
DR OMA; STMFYVP; -.
DR OrthoDB; 1347007at2759; -.
DR PhylomeDB; Q96PD7; -.
DR TreeFam; TF314707; -.
DR BRENDA; 2.3.1.20; 2681.
DR PathwayCommons; Q96PD7; -.
DR Reactome; R-HSA-1482883; Acyl chain remodeling of DAG and TAG.
DR Reactome; R-HSA-75109; Triglyceride biosynthesis.
DR SABIO-RK; Q96PD7; -.
DR SignaLink; Q96PD7; -.
DR UniPathway; UPA00282; -.
DR BioGRID-ORCS; 84649; 15 hits in 1081 CRISPR screens.
DR ChiTaRS; DGAT2; human.
DR GenomeRNAi; 84649; -.
DR Pharos; Q96PD7; Tchem.
DR PRO; PR:Q96PD7; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96PD7; protein.
DR Bgee; ENSG00000062282; Expressed in upper arm skin and 150 other tissues.
DR ExpressionAtlas; Q96PD7; baseline and differential.
DR Genevisible; Q96PD7; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IDA:BHF-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:1990578; C:perinuclear endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:BHF-UCL.
DR GO; GO:0003846; F:2-acylglycerol O-acyltransferase activity; IEA:Ensembl.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS: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; ISS:BHF-UCL.
DR GO; GO:0035356; P:cellular triglyceride homeostasis; ISS:BHF-UCL.
DR GO; GO:0042632; P:cholesterol homeostasis; ISS:BHF-UCL.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IDA:BHF-UCL.
DR GO; GO:0060613; P:fat pad development; ISS:BHF-UCL.
DR GO; GO:0055089; P:fatty acid homeostasis; ISS: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; ISS: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; ISS:BHF-UCL.
DR GO; GO:0006640; P:monoacylglycerol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0046322; P:negative regulation of fatty acid oxidation; IEA:Ensembl.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IEA:Ensembl.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IEA:Ensembl.
DR GO; GO:0090181; P:regulation of cholesterol metabolic process; IEA:Ensembl.
DR GO; GO:0050746; P:regulation of lipoprotein metabolic process; IEA:Ensembl.
DR GO; GO:0097006; P:regulation of plasma lipoprotein particle levels; ISS:BHF-UCL.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR007130; DAGAT.
DR Pfam; PF03982; DAGAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Cytoplasm; Endoplasmic reticulum;
KW Glycerol metabolism; Lipid biosynthesis; Lipid droplet; Lipid metabolism;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..388
FT /note="Diacylglycerol O-acyltransferase 2"
FT /id="PRO_0000249045"
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"
FT REGION 16..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 41..83
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_020356"
FT VARIANT 223
FT /note="Y -> H (found in patients with Charcot-Marie-Tooth
FT disease; unknown pathological significance;
FT dbSNP:rs869025595)"
FT /evidence="ECO:0000269|PubMed:26786738"
FT /id="VAR_077236"
FT VARIANT 317
FT /note="R -> G (in dbSNP:rs34421064)"
FT /id="VAR_033864"
FT VARIANT 361
FT /note="M -> I (in dbSNP:rs34113941)"
FT /id="VAR_033865"
FT CONFLICT 295
FT /note="W -> C (in Ref. 7; AAV35727)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="Q -> H (in Ref. 7; AAV35727)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 388 AA; 43831 MW; 39EE7783A3F06593 CRC64;
MKTLIAAYSG VLRGERQAEA DRSQRSHGGP ALSREGSGRW GTGSSILSAL QDLFSVTWLN
RSKVEKQLQV ISVLQWVLSF LVLGVACSAI LMYIFCTDCW LIAVLYFTWL VFDWNTPKKG
GRRSQWVRNW AVWRYFRDYF PIQLVKTHNL LTTRNYIFGY HPHGIMGLGA FCNFSTEATE
VSKKFPGIRP YLATLAGNFR MPVLREYLMS GGICPVSRDT IDYLLSKNGS GNAIIIVVGG
AAESLSSMPG KNAVTLRNRK GFVKLALRHG ADLVPIYSFG ENEVYKQVIF EEGSWGRWVQ
KKFQKYIGFA PCIFHGRGLF SSDTWGLVPY SKPITTVVGE PITIPKLEHP TQQDIDLYHT
MYMEALVKLF DKHKTKFGLP ETEVLEVN
