DGAT2_RAT
ID DGAT2_RAT Reviewed; 388 AA.
AC Q5FVP8; Q8K4Y4;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
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;
DE Short=ARAT;
DE Short=Retinol O-fatty-acyltransferase;
DE EC=2.3.1.76 {ECO:0000250|UniProtKB:Q96PD7};
DE AltName: Full=Diglyceride acyltransferase 2;
GN Name=Dgat2 {ECO:0000312|RGD:620329};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 177-327.
RC STRAIN=Wistar; TISSUE=Liver;
RA Waterman I.J., Zammit V.A., Price N.T.;
RT "Sequencing of a partial rat DGAT2 cDNA.";
RL Submitted (MAY-2002) 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 (By similarity). 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) (By similarity).
CC {ECO:0000250|UniProtKB:Q96PD7, ECO:0000250|UniProtKB:Q9DCV3}.
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 -!- ACTIVITY REGULATION: Inhibited by niacin. {ECO:0000250}.
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q96PD7, ECO:0000250|UniProtKB:Q9DCV3}.
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; BC089846; AAH89846.1; -; mRNA.
DR EMBL; AJ487787; CAD32178.1; -; mRNA.
DR RefSeq; NP_001012345.1; NM_001012345.1.
DR AlphaFoldDB; Q5FVP8; -.
DR STRING; 10116.ENSRNOP00000022557; -.
DR ChEMBL; CHEMBL4295847; -.
DR PhosphoSitePlus; Q5FVP8; -.
DR PaxDb; Q5FVP8; -.
DR PRIDE; Q5FVP8; -.
DR GeneID; 252900; -.
DR KEGG; rno:252900; -.
DR UCSC; RGD:620329; rat.
DR CTD; 84649; -.
DR RGD; 620329; Dgat2.
DR VEuPathDB; HostDB:ENSRNOG00000016573; -.
DR eggNOG; KOG0831; Eukaryota.
DR HOGENOM; CLU_023995_0_1_1; -.
DR InParanoid; Q5FVP8; -.
DR OMA; STMFYVP; -.
DR OrthoDB; 1347007at2759; -.
DR PhylomeDB; Q5FVP8; -.
DR TreeFam; TF314707; -.
DR Reactome; R-RNO-1482883; Acyl chain remodeling of DAG and TAG.
DR Reactome; R-RNO-75109; Triglyceride biosynthesis.
DR UniPathway; UPA00282; -.
DR PRO; PR:Q5FVP8; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000016573; Expressed in liver and 19 other tissues.
DR ExpressionAtlas; Q5FVP8; baseline and differential.
DR Genevisible; Q5FVP8; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:1990578; C:perinuclear endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0003846; F:2-acylglycerol O-acyltransferase activity; ISO:RGD.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IDA:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0050252; F:retinol O-fatty-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0038183; P:bile acid signaling pathway; IEP:RGD.
DR GO; GO:0071400; P:cellular response to oleic acid; ISO:RGD.
DR GO; GO:0035356; P:cellular triglyceride homeostasis; ISO:RGD.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IMP:RGD.
DR GO; GO:0060613; P:fat pad development; ISO:RGD.
DR GO; GO:0055089; P:fatty acid homeostasis; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; ISO:RGD.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; ISO:RGD.
DR GO; GO:0006640; P:monoacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0046322; P:negative regulation of fatty acid oxidation; IMP:RGD.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IMP:RGD.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IMP:RGD.
DR GO; GO:0090181; P:regulation of cholesterol metabolic process; IMP:RGD.
DR GO; GO:0050746; P:regulation of lipoprotein metabolic process; IMP:RGD.
DR GO; GO:0097006; P:regulation of plasma lipoprotein particle levels; ISO:RGD.
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..388
FT /note="Diacylglycerol O-acyltransferase 2"
FT /id="PRO_0000249047"
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"
SQ SEQUENCE 388 AA; 43795 MW; 04DCBB134206F78D CRC64;
MKTLIAAYSG VLRGERRAEA ARSENKNKGS ALSREGSGRW GTGSSILSAL QDIFSVTWLN
RSKVEKHLQV ISVLQWVLSF LVLGVACSVI LMYTFCTDCW LIAALYFTWL AFDWNTPKKG
GRRSQWVRNW AVWRYFRDYF PIQLVKTHNL LTTRNYIFGY HPHGIMGLGA FCNFSTEATE
VSKKFPGIRP YLATLAGNFR MPVLREYLMS GGICPVNRDT IDYLLSKNGS GNAIVIVVGG
AAESLSSMPG KNAVTLRNRK GFVKLALRHG ADLVPTYSFG ENEVYKQVIF EEGSWGRWVQ
KKFQKYIGFA PCIFHGRGLF SSDTWGLVPY SKPITTVVGE PITVPKLEHP TQKDIDLYHT
MYMEALVKLF DNHKTKFGLP ETEVLEVN
