DGAT2_DANRE
ID DGAT2_DANRE Reviewed; 361 AA.
AC Q4V9F0;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Diacylglycerol O-acyltransferase 2 {ECO:0000305};
DE EC=2.3.1.20 {ECO:0000250|UniProtKB:Q96PD7};
DE AltName: Full=Acyl-CoA retinol O-fatty-acyltransferase {ECO:0000250|UniProtKB:Q96PD7};
DE Short=ARAT {ECO:0000250|UniProtKB:Q96PD7};
DE Short=Retinol O-fatty-acyltransferase {ECO:0000250|UniProtKB:Q96PD7};
DE EC=2.3.1.76 {ECO:0000250|UniProtKB:Q96PD7};
DE AltName: Full=Diglyceride acyltransferase 2;
GN Name=dgat2; ORFNames=zgc:113394;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q96PD7}.
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:Q96PD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10869;
CC Evidence={ECO:0000250|UniProtKB:Q96PD7};
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:0000250|UniProtKB:Q96PD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11489;
CC Evidence={ECO:0000250|UniProtKB:Q96PD7};
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=(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:0000250|UniProtKB:Q96PD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38220;
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 -!- 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 -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
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 -!- SIMILARITY: Belongs to the diacylglycerol acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; BC096927; AAH96927.1; -; mRNA.
DR RefSeq; NP_001025367.1; NM_001030196.1.
DR AlphaFoldDB; Q4V9F0; -.
DR STRING; 7955.ENSDARP00000116381; -.
DR PaxDb; Q4V9F0; -.
DR Ensembl; ENSDART00000066793; ENSDARP00000066792; ENSDARG00000018846.
DR GeneID; 565316; -.
DR KEGG; dre:565316; -.
DR CTD; 84649; -.
DR ZFIN; ZDB-GENE-050913-15; dgat2.
DR eggNOG; KOG0831; Eukaryota.
DR GeneTree; ENSGT01030000234582; -.
DR HOGENOM; CLU_023995_0_1_1; -.
DR InParanoid; Q4V9F0; -.
DR OMA; STMFYVP; -.
DR OrthoDB; 1347007at2759; -.
DR PhylomeDB; Q4V9F0; -.
DR Reactome; R-DRE-1482883; Acyl chain remodeling of DAG and TAG.
DR Reactome; R-DRE-2142753; Arachidonic acid metabolism.
DR Reactome; R-DRE-2187335; The retinoid cycle in cones (daylight vision).
DR Reactome; R-DRE-75109; Triglyceride biosynthesis.
DR Reactome; R-DRE-9640463; Wax biosynthesis.
DR UniPathway; UPA00282; -.
DR PRO; PR:Q4V9F0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 10.
DR Bgee; ENSDARG00000018846; Expressed in liver and 14 other tissues.
DR ExpressionAtlas; Q4V9F0; baseline.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR GO; GO:1990578; C:perinuclear endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0050252; F:retinol O-fatty-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0055088; P:lipid homeostasis; IGI:ZFIN.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:1905897; P:regulation of response to endoplasmic reticulum stress; IGI:ZFIN.
DR GO; GO:0061959; P:response to (R)-carnitine; IEP:ZFIN.
DR GO; GO:0019432; P:triglyceride biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR007130; DAGAT.
DR Pfam; PF03982; DAGAT; 1.
PE 2: Evidence at transcript 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..361
FT /note="Diacylglycerol O-acyltransferase 2"
FT /id="PRO_0000249048"
FT TOPO_DOM 1..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..65
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 361 AA; 40865 MW; E0B9A0E8E9D1A8B0 CRC64;
MKTILAAYSG VKKGSGSSIL SALHDLPTVP WLTRSKMVKH LQVISVLQFI MTFLTMGIAC
SLLLMYMFCT DFWVISVLYV AWLIYDWNTP GQGGRRSTWV RDWTVWKYMR DYFPIRLIKT
HNLLPSRNYI FGYHPHGILC FGAFCNFGTE ATGFTKVFPG IKPSLATLAG NFRLPMFREY
LMCGGICPVN RNSIDYLLSS NGTGNAVVIV IGGAAESLDC APGRNSVMLK KRKGFVKLAL
KQGADLVPVY SFGENEVYKQ LIFEEGSWWR TIQRKLQKFL GFAPCLFHGC GLFFPESWGL
VPYCKPITTV VGEPITVPKI EEPTQDVIDM YHAMYIRSLK SLFDNYKTRF GLNESDTLII
H
