DGAT2_YEAST
ID DGAT2_YEAST Reviewed; 418 AA.
AC Q08650; D6W2U7;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Diacylglycerol O-acyltransferase 1 {ECO:0000305};
DE Short=DGAT;
DE EC=2.3.1.20 {ECO:0000269|PubMed:20225889, ECO:0000269|PubMed:20554061};
DE AltName: Full=Acyl-CoA-dependent diacylglycerol O-acyltransferase;
DE AltName: Full=Acyl-CoA:monoacylglycerol acyltransferase;
DE Short=MGAT;
DE EC=2.3.1.22 {ECO:0000269|PubMed:20554061};
DE AltName: Full=Triacylglycerol synthase;
DE Short=TAG synthase;
GN Name=DGA1; OrderedLocusNames=YOR245C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11751830; DOI=10.1128/jb.184.2.519-524.2002;
RA Sorger D., Daum G.;
RT "Synthesis of triacylglycerols by the acyl-coenzyme A:diacyl-glycerol
RT acyltransferase Dga1p in lipid particles of the yeast Saccharomyces
RT cerevisiae.";
RL J. Bacteriol. 184:519-524(2002).
RN [4]
RP FUNCTION.
RX PubMed=11741946; DOI=10.1074/jbc.m109109200;
RA Sandager L., Gustavsson M.H., Staahl U., Dahlqvist A., Wiberg E., Banas A.,
RA Lenman M., Ronne H., Stymne S.;
RT "Storage lipid synthesis is non-essential in yeast.";
RL J. Biol. Chem. 277:6478-6482(2002).
RN [5]
RP FUNCTION.
RX PubMed=11751875; DOI=10.1074/jbc.m111646200;
RA Oelkers P., Cromley D., Padamsee M., Billheimer J.T., Sturley S.L.;
RT "The DGA1 gene determines a second triglyceride synthetic pathway in
RT yeast.";
RL J. Biol. Chem. 277:8877-8881(2002).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION.
RX PubMed=14640980; DOI=10.1042/bj20031064;
RA Ferreira T., Regnacq M., Alimardani P., Moreau-Vauzelle C., Berges T.;
RT "Lipid dynamics in yeast under haem-induced unsaturated fatty acid and/or
RT sterol depletion.";
RL Biochem. J. 378:899-908(2004).
RN [9]
RP FUNCTION.
RX PubMed=15155725; DOI=10.1074/jbc.m403251200;
RA Sorger D., Athenstaedt K., Hrastnik C., Daum G.;
RT "A yeast strain lacking lipid particles bears a defect in ergosterol
RT formation.";
RL J. Biol. Chem. 279:31190-31196(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=20225889; DOI=10.1021/bi9020499;
RA Liu Q., Siloto R.M., Weselake R.J.;
RT "Role of cysteine residues in thiol modification of acyl-CoA:diacylglycerol
RT acyltransferase 2 from yeast.";
RL Biochemistry 49:3237-3245(2010).
RN [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20554061; DOI=10.1016/j.bbalip.2010.06.001;
RA Heier C., Taschler U., Rengachari S., Oberer M., Wolinski H., Natter K.,
RA Kohlwein S.D., Leber R., Zimmermann R.;
RT "Identification of Yju3p as functional orthologue of mammalian
RT monoglyceride lipase in the yeast Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1801:1063-1071(2010).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=21820081; DOI=10.1016/j.bbalip.2011.07.015;
RA Grillitsch K., Connerth M., Kofeler H., Arrey T.N., Rietschel B.,
RA Wagner B., Karas M., Daum G.;
RT "Lipid particles/droplets of the yeast Saccharomyces cerevisiae revisited:
RT lipidome meets proteome.";
RL Biochim. Biophys. Acta 1811:1165-1176(2011).
RN [14]
RP FUNCTION, TOPOLOGY, AND MUTAGENESIS OF PHE-71; LEU-73; 129-TYR--PRO-131;
RP HIS-193; 193-HIS--GLY-196 AND HIS-195.
RX PubMed=21321129; DOI=10.1074/jbc.m110.204412;
RA Liu Q., Siloto R.M., Snyder C.L., Weselake R.J.;
RT "Functional and topological analysis of yeast acyl-CoA:diacylglycerol
RT acyltransferase 2, an endoplasmic reticulum enzyme essential for
RT triacylglycerol biosynthesis.";
RL J. Biol. Chem. 286:13115-13126(2011).
RN [15]
RP FUNCTION.
RX PubMed=22738231; DOI=10.1042/bj20120712;
RA Voynova N.S., Vionnet C., Ejsing C.S., Conzelmann A.;
RT "A novel pathway of ceramide metabolism in Saccharomyces cerevisiae.";
RL Biochem. J. 447:103-114(2012).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=24868093; DOI=10.1194/jlr.m050229;
RA Currie E., Guo X., Christiano R., Chitraju C., Kory N., Harrison K.,
RA Haas J., Walther T.C., Farese R.V. Jr.;
RT "High-confidence proteomic analysis of yeast lipid droplets identifies
RT additional droplet proteins and reveals connections to dolichol synthesis
RT and sterol acetylation.";
RL J. Lipid Res. 55:1465-1477(2014).
RN [17]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=27620384; DOI=10.1007/s00284-016-1127-4;
RA Jain S., Dholakia H., Kirtley W., Oelkers P.;
RT "Energy storage in yeast: Regulation and competition with ethanol
RT production.";
RL Curr. Microbiol. 73:851-858(2016).
RN [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=32349126; DOI=10.1083/jcb.201910177;
RA Choudhary V., El Atab O., Mizzon G., Prinz W.A., Schneiter R.;
RT "Seipin and Nem1 establish discrete ER subdomains to initiate yeast lipid
RT droplet biogenesis.";
RL J. Cell Biol. 219:0-0(2020).
CC -!- FUNCTION: Catalyzes the terminal and only committed step in
CC triacylglycerol (TAG) synthesis by using diacylglycerol (DAG) and fatty
CC acyl-CoA as substrates. Required for storage lipid synthesis. Major DAG
CC esterifying enzyme in stationary phase when TAG production is
CC particularly active. Involved in lipid particle synthesis from the
CC endoplasmic reticulum, promoting localized TAG production at discrete
CC ER subdomains, and in ergosterol biosynthesis (PubMed:11741946,
CC PubMed:11751830, PubMed:11751875, PubMed:14640980, PubMed:15155725,
CC PubMed:21321129, PubMed:32349126). Also has monoacylglycerol
CC acyltransferase (MGAT) activity, catalyzing the acyl-CoA-dependent
CC esterification of monoacylglycerol to diacylglycerol (PubMed:20554061).
CC Can also utilize ceramide instead of DAG, acylating the ceramides by
CC attaching a fatty acid to the hydroxy group on the first carbon atom of
CC the long-chain base to produce 1-O-acylceramides (PubMed:22738231).
CC {ECO:0000269|PubMed:11741946, ECO:0000269|PubMed:11751830,
CC ECO:0000269|PubMed:11751875, ECO:0000269|PubMed:14640980,
CC ECO:0000269|PubMed:15155725, ECO:0000269|PubMed:20554061,
CC ECO:0000269|PubMed:21321129, ECO:0000269|PubMed:22738231,
CC ECO:0000269|PubMed:32349126}.
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:20225889, ECO:0000269|PubMed:20554061};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acylglycerol + an acyl-CoA = a 1,2-diacyl-sn-glycerol +
CC CoA; Xref=Rhea:RHEA:32947, ChEBI:CHEBI:17389, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:58342; EC=2.3.1.22;
CC Evidence={ECO:0000269|PubMed:20554061};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 2-(9Z-octadecenoyl)-glycerol = 1,2-di-
CC (9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:39951,
CC ChEBI:CHEBI:52323, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:73990; Evidence={ECO:0000269|PubMed:20554061,
CC ECO:0000269|PubMed:27620384};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39952;
CC Evidence={ECO:0000305|PubMed:20554061};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17 uM for (9Z)-octadecenoyl-CoA {ECO:0000269|PubMed:27620384};
CC Vmax=5.8 nmol/min/mg enzyme with (9Z)-octadecenoyl-CoA as substrate
CC {ECO:0000269|PubMed:27620384};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:21820081, ECO:0000269|PubMed:24868093}. Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:20225889, ECO:0000269|PubMed:21321129,
CC ECO:0000269|PubMed:32349126}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes to sites of lipid droplet biogenesis in
CC the endoplasmic reticulum. {ECO:0000269|PubMed:32349126}.
CC -!- MISCELLANEOUS: Present with 907 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the diacylglycerol acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; Z75153; CAA99466.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11013.1; -; Genomic_DNA.
DR PIR; S67138; S67138.
DR RefSeq; NP_014888.1; NM_001183664.1.
DR AlphaFoldDB; Q08650; -.
DR BioGRID; 34636; 82.
DR DIP; DIP-2923N; -.
DR IntAct; Q08650; 2.
DR MINT; Q08650; -.
DR STRING; 4932.YOR245C; -.
DR SwissLipids; SLP:000000051; -.
DR iPTMnet; Q08650; -.
DR MaxQB; Q08650; -.
DR PaxDb; Q08650; -.
DR PRIDE; Q08650; -.
DR EnsemblFungi; YOR245C_mRNA; YOR245C; YOR245C.
DR GeneID; 854419; -.
DR KEGG; sce:YOR245C; -.
DR SGD; S000005771; DGA1.
DR VEuPathDB; FungiDB:YOR245C; -.
DR eggNOG; KOG0831; Eukaryota.
DR GeneTree; ENSGT01030000234582; -.
DR HOGENOM; CLU_023995_4_1_1; -.
DR InParanoid; Q08650; -.
DR OMA; PVFREYM; -.
DR BioCyc; MetaCyc:YOR245C-MON; -.
DR BioCyc; YEAST:YOR245C-MON; -.
DR BRENDA; 2.3.1.20; 984.
DR Reactome; R-SCE-1482883; Acyl chain remodeling of DAG and TAG.
DR Reactome; R-SCE-2142753; Arachidonic acid metabolism.
DR Reactome; R-SCE-75109; Triglyceride biosynthesis.
DR Reactome; R-SCE-9640463; Wax biosynthesis.
DR UniPathway; UPA00282; -.
DR PRO; PR:Q08650; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08650; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0003846; F:2-acylglycerol O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IDA:SGD.
DR GO; GO:0035356; P:cellular triglyceride homeostasis; IMP:SGD.
DR GO; GO:0006672; P:ceramide metabolic process; IDA:SGD.
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:SGD.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IDA:SGD.
DR InterPro; IPR007130; DAGAT.
DR Pfam; PF03982; DAGAT; 2.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Glycerol metabolism; Glycoprotein;
KW Lipid biosynthesis; Lipid droplet; Lipid metabolism; Membrane;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..418
FT /note="Diacylglycerol O-acyltransferase 1"
FT /id="PRO_0000233001"
FT TOPO_DOM 1..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21321129"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..186
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:21321129"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21321129"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..289
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:21321129"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..418
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21321129"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 71
FT /note="F->A: Retains more than 40% of the wild-type enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:21321129"
FT MUTAGEN 73
FT /note="L->A: Retains more than 40% of the wild-type enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:21321129"
FT MUTAGEN 129..131
FT /note="YFP->AA: Almost complete loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:21321129"
FT MUTAGEN 193..196
FT /note="HPHG->EPHS: Complete loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:21321129"
FT MUTAGEN 193
FT /note="H->A: Almost complete loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:21321129"
FT MUTAGEN 195
FT /note="H->A: Complete loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:21321129"
SQ SEQUENCE 418 AA; 47711 MW; E6ECAA95219583BD CRC64;
MSGTFNDIRR RKKEEGSPTA GITERHENKS LSSIDKREQT LKPQLESCCP LATPFERRLQ
TLAVAWHTSS FVLFSIFTLF AISTPALWVL AIPYMIYFFF DRSPATGEVV NRYSLRFRSL
PIWKWYCDYF PISLIKTVNL KPTFTLSKNK RVNEKNYKIR LWPTKYSINL KSNSTIDYRN
QECTGPTYLF GYHPHGIGAL GAFGAFATEG CNYSKIFPGI PISLMTLVTQ FHIPLYRDYL
LALGISSVSR KNALRTLSKN QSICIVVGGA RESLLSSTNG TQLILNKRKG FIKLAIQTGN
INLVPVFAFG EVDCYNVLST KKDSVLGKMQ LWFKENFGFT IPIFYARGLF NYDFGLLPFR
APINVVVGRP IYVEKKITNP PDDVVNHFHD LYIAELKRLY YENREKYGVP DAELKIVG
