(data stored in ACNUC7421 zone)

SWISSPROT: DGAT2_ASHGO

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   11-DEC-2019, entry version 101.
DE   RecName: Full=Diacylglycerol O-acyltransferase 1;
DE            EC=2.3.1.20;
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 synthesis by using diacylglycerol and fatty acyl CoA as
CC       substrates. Required for storage lipid synthesis. May be involved in
CC       lipid particle synthesis from the endoplasmic reticulum and ergosterol
CC       biosynthesis. Also has monoacylglycerol acyltransferase (MGAT)
CC       activity, catalyzing the acyl-CoA-dependent esterification of
CC       monoacylglycerol to diacylglycerol (By similarity). {ECO:0000250}.
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   -!- 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   -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein. Lipid droplet {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the diacylglycerol acyltransferase family.
CC       {ECO:0000305}.
DR   EMBL; AE016816; AAS51366.1; -; Genomic_DNA.
DR   RefSeq; NP_983542.1; NM_208895.1.
DR   STRING; 33169.AAS51366; -.
DR   EnsemblFungi; AAS51366; AAS51366; AGOS_ACR140C.
DR   GeneID; 4619674; -.
DR   KEGG; ago:AGOS_ACR140C; -.
DR   HOGENOM; HOG000179738; -.
DR   InParanoid; Q75BY0; -.
DR   KO; K14457; -.
DR   OMA; FYCCVFY; -.
DR   UniPathway; UPA00282; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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: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:0019915; P:lipid storage; IEA:EnsemblFungi.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR007130; DAGAT.
DR   Pfam; PF03982; DAGAT; 2.
PE   3: Inferred from homology;
DR   PRODOM; Q75BY0.
DR   SWISS-2DPAGE; Q75BY0.
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"
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
//

If you have problems or comments...

PBIL Back to PBIL home page