ID   DGAT2_ASHGO             Reviewed;         461 AA.
AC   Q75BY0;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Diacylglycerol O-acyltransferase 1;
DE            EC=2.3.1.20 {ECO:0000250|UniProtKB:Q08650};
GN   Name=DGA1; OrderedLocusNames=ACR140C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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. {ECO:0000250|UniProtKB:Q08650}.
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:0000250|UniProtKB:Q08650};
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;
CC         Evidence={ECO:0000250|UniProtKB:Q08650};
CC   -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC       {ECO:0000250|UniProtKB:Q08650}.
CC   -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:Q08650}.
CC       Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q08650}; Multi-
CC       pass membrane protein {ECO:0000255}. Note=Localizes to sites of lipid
CC       droplet biogenesis in the endoplasmic reticulum.
CC       {ECO:0000250|UniProtKB:Q08650}.
CC   -!- SIMILARITY: Belongs to the diacylglycerol acyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AE016816; AAS51366.1; -; Genomic_DNA.
DR   RefSeq; NP_983542.1; NM_208895.1.
DR   AlphaFoldDB; Q75BY0; -.
DR   STRING; 33169.AAS51366; -.
DR   EnsemblFungi; AAS51366; AAS51366; AGOS_ACR140C.
DR   GeneID; 4619674; -.
DR   KEGG; ago:AGOS_ACR140C; -.
DR   eggNOG; KOG0831; Eukaryota.
DR   HOGENOM; CLU_023995_4_1_1; -.
DR   InParanoid; Q75BY0; -.
DR   OMA; PVFREYM; -.
DR   UniPathway; UPA00282; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0032541; C:cortical endoplasmic reticulum; IEA:EnsemblFungi.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR   GO; GO:0097038; C:perinuclear endoplasmic reticulum; IEA:EnsemblFungi.
DR   GO; GO:0003846; F:2-acylglycerol O-acyltransferase activity; IEA:RHEA.
DR   GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0035356; P:cellular triglyceride homeostasis; IEA:EnsemblFungi.
DR   GO; GO:0006672; P:ceramide metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0140042; P:lipid droplet formation; IEA:EnsemblFungi.
DR   GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR007130; DAGAT.
DR   Pfam; PF03982; DAGAT; 2.
PE   3: Inferred from homology;
KW   Acyltransferase; Endoplasmic reticulum; Glycerol metabolism;
KW   Lipid biosynthesis; Lipid droplet; Lipid metabolism; Membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..461
FT                   /note="Diacylglycerol O-acyltransferase 1"
FT                   /id="PRO_0000233000"
FT   TOPO_DOM        1..112
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        134..230
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        252..258
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        280..332
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        333..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        354..461
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   461 AA;  52241 MW;  A2E6EC619934ABF1 CRC64;
     MQDSMDDSLR EAEGRQDDSE VSSGTTLGSS TPEDSGVTAK LRKKYQMASA LLRRELEELS
     VYDAKTAGVS GRSSGSGSGG LALLGGRFHV APLRIPARRR LQTLVVAWHT SSFIYMTVLV
     LFLAANPLMW WFMVPYMVYY VWNRSPANGG VVRRYSPRLR SLALWRYYCE YYPISLHKSE
     DLAPTFVPDP RGAEPREWKL RLWLWPTRVE LLNLTLQWTR ARPQVATGPR YIFGYHPHGV
     GALGAFGAIA TEGCNWSKVF AGIPACLCTL VNQFQIPIYR DYLLGLGCTS VARKNVLKVL
     EQNYSVCIVV GGAQEALLSR VGSTELVLNK RKGFIKLALE TGNVNLVPIY AFGETDCFNV
     LDTGNESYLR KFQLWIKKTY GFTIPFFFAR GVFNYDFGFL PFRNPINVVV GKPVYVDKRR
     TNPTMEEIDH YHDLYVQELR NVFDKNKHKF GYAGKELKIV E