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Protein

Diacylglycerol O-acyltransferase 2

Gene

Dgat2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides. Probably plays a central role in cytosolic lipid accumulation. In liver, is primarily responsible for incorporating endogenously synthesized fatty acids into triglycerides. Functions also as an acyl-CoA retinol acyltransferase (ARAT) (By similarity).By similarity4 Publications

Catalytic activityi

Acyl-CoA + 1,2-diacylglycerol = CoA + triacylglycerol.
Acyl-CoA + retinol = CoA + retinyl ester.

Enzyme regulationi

Inhibited by niacin.By similarity

Pathwayi: triacylglycerol biosynthesis

This protein is involved in the pathway triacylglycerol biosynthesis, which is part of Glycerolipid metabolism.
View all proteins of this organism that are known to be involved in the pathway triacylglycerol biosynthesis and in Glycerolipid metabolism.

GO - Molecular functioni

GO - Biological processi

  • cellular response to oleic acid Source: BHF-UCL
  • cellular triglyceride homeostasis Source: BHF-UCL
  • cholesterol homeostasis Source: BHF-UCL
  • diacylglycerol metabolic process Source: BHF-UCL
  • fat pad development Source: BHF-UCL
  • fatty acid homeostasis Source: BHF-UCL
  • glycerol metabolic process Source: UniProtKB-KW
  • lipid storage Source: BHF-UCL
  • long-chain fatty-acyl-CoA metabolic process Source: BHF-UCL
  • low-density lipoprotein particle clearance Source: BHF-UCL
  • negative regulation of fatty acid oxidation Source: Ensembl
  • positive regulation of gluconeogenesis Source: Ensembl
  • positive regulation of triglyceride biosynthetic process Source: Ensembl
  • regulation of cholesterol metabolic process Source: Ensembl
  • regulation of lipoprotein metabolic process Source: Ensembl
  • regulation of plasma lipoprotein particle levels Source: BHF-UCL
  • triglyceride biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Glycerol metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BRENDAi2.3.1.20. 3474.
ReactomeiR-MMU-1482883. Acyl chain remodeling of DAG and TAG.
R-MMU-75109. Triglyceride Biosynthesis.
UniPathwayiUPA00282.

Chemistry

SwissLipidsiSLP:000000303.

Names & Taxonomyi

Protein namesi
Recommended name:
Diacylglycerol O-acyltransferase 2 (EC:2.3.1.20)
Alternative name(s):
Acyl-CoA retinol O-fatty-acyltransferase (EC:2.3.1.76)
Short name:
ARAT
Short name:
Retinol O-fatty-acyltransferase
Diglyceride acyltransferase 2
Gene namesi
Name:Dgat2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1915050. Dgat2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6969CytoplasmicSequence analysisAdd
BLAST
Transmembranei70 – 8819HelicalSequence analysisAdd
BLAST
Topological domaini89 – 924LumenalSequence analysis
Transmembranei93 – 11220HelicalSequence analysisAdd
BLAST
Topological domaini113 – 388276CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: BHF-UCL
  • integral component of endoplasmic reticulum membrane Source: BHF-UCL
  • integral component of membrane Source: MGI
  • lipid particle Source: UniProtKB-SubCell
  • membrane Source: MGI
  • perinuclear region of cytoplasm Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Lipid droplet, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice are lipopenic and die soon after birth, apparently from profound reductions in substrates for energy metabolism and from impaired permeability barrier function in the skin.1 Publication

Chemistry

ChEMBLiCHEMBL1075285.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 388388Diacylglycerol O-acyltransferase 2PRO_0000249046Add
BLAST

Proteomic databases

MaxQBiQ9DCV3.
PaxDbiQ9DCV3.
PRIDEiQ9DCV3.

PTM databases

iPTMnetiQ9DCV3.
PhosphoSiteiQ9DCV3.

Expressioni

Tissue specificityi

Predominantly expressed in liver. Also expressed in testis.1 Publication

Inductioni

In white adipose tissue, it is regulated by leptin. By insulin. Up-regulated in diabetic mice. Down-regulated upon fasting and replenished upon refeeding in adipose tissue and liver. Down-regulation in obese animals can reduce hepatic lipogenesis and hepatic steatosis as well as attenuate hyperlipidemia, thereby leading to an improvement in metabolic syndrome.3 Publications

Gene expression databases

BgeeiENSMUSG00000030747.
CleanExiMM_DGAT2.
GenevisibleiQ9DCV3. MM.

Interactioni

Subunit structurei

Forms multimeric complexes consisting of several DGAT2 subunits.By similarity

GO - Molecular functioni

  • protein homodimerization activity Source: BHF-UCL

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033001.

Structurei

3D structure databases

ProteinModelPortaliQ9DCV3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0831. Eukaryota.
ENOG410XTG3. LUCA.
GeneTreeiENSGT00750000117391.
HOGENOMiHOG000179738.
HOVERGENiHBG065791.
InParanoidiQ9DCV3.
KOiK11160.
OMAiAILMYTF.
OrthoDBiEOG091G0BGQ.
PhylomeDBiQ9DCV3.
TreeFamiTF314707.

Family and domain databases

InterProiIPR007130. DAGAT.
[Graphical view]
PfamiPF03982. DAGAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9DCV3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTLIAAYSG VLRGERRAEA ARSENKNKGS ALSREGSGRW GTGSSILSAL
60 70 80 90 100
QDIFSVTWLN RSKVEKQLQV ISVLQWVLSF LVLGVACSVI LMYTFCTDCW
110 120 130 140 150
LIAVLYFTWL AFDWNTPKKG GRRSQWVRNW AVWRYFRDYF PIQLVKTHNL
160 170 180 190 200
LTTRNYIFGY HPHGIMGLGA FCNFSTEATE VSKKFPGIRP YLATLAGNFR
210 220 230 240 250
MPVLREYLMS GGICPVNRDT IDYLLSKNGS GNAIIIVVGG AAESLSSMPG
260 270 280 290 300
KNAVTLKNRK GFVKLALRHG ADLVPTYSFG ENEVYKQVIF EEGSWGRWVQ
310 320 330 340 350
KKFQKYIGFA PCIFHGRGLF SSDTWGLVPY SKPITTVVGE PITVPKLEHP
360 370 380
TQKDIDLYHA MYMEALVKLF DNHKTKFGLP ETEVLEVN
Length:388
Mass (Da):43,770
Last modified:June 1, 2001 - v1
Checksum:i9C35C37DCAF61D55
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF384160 mRNA. Translation: AAK84175.1.
AK002443 mRNA. Translation: BAB22105.1.
BC043447 mRNA. Translation: AAH43447.1.
CCDSiCCDS21477.1.
RefSeqiNP_080660.1. NM_026384.3.
UniGeneiMm.180189.
Mm.491108.

Genome annotation databases

EnsembliENSMUST00000033001; ENSMUSP00000033001; ENSMUSG00000030747.
GeneIDi67800.
KEGGimmu:67800.
UCSCiuc009ile.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF384160 mRNA. Translation: AAK84175.1.
AK002443 mRNA. Translation: BAB22105.1.
BC043447 mRNA. Translation: AAH43447.1.
CCDSiCCDS21477.1.
RefSeqiNP_080660.1. NM_026384.3.
UniGeneiMm.180189.
Mm.491108.

3D structure databases

ProteinModelPortaliQ9DCV3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033001.

Chemistry

ChEMBLiCHEMBL1075285.
SwissLipidsiSLP:000000303.

PTM databases

iPTMnetiQ9DCV3.
PhosphoSiteiQ9DCV3.

Proteomic databases

MaxQBiQ9DCV3.
PaxDbiQ9DCV3.
PRIDEiQ9DCV3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033001; ENSMUSP00000033001; ENSMUSG00000030747.
GeneIDi67800.
KEGGimmu:67800.
UCSCiuc009ile.1. mouse.

Organism-specific databases

CTDi84649.
MGIiMGI:1915050. Dgat2.

Phylogenomic databases

eggNOGiKOG0831. Eukaryota.
ENOG410XTG3. LUCA.
GeneTreeiENSGT00750000117391.
HOGENOMiHOG000179738.
HOVERGENiHBG065791.
InParanoidiQ9DCV3.
KOiK11160.
OMAiAILMYTF.
OrthoDBiEOG091G0BGQ.
PhylomeDBiQ9DCV3.
TreeFamiTF314707.

Enzyme and pathway databases

UniPathwayiUPA00282.
BRENDAi2.3.1.20. 3474.
ReactomeiR-MMU-1482883. Acyl chain remodeling of DAG and TAG.
R-MMU-75109. Triglyceride Biosynthesis.

Miscellaneous databases

ChiTaRSiDgat2. mouse.
PROiQ9DCV3.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000030747.
CleanExiMM_DGAT2.
GenevisibleiQ9DCV3. MM.

Family and domain databases

InterProiIPR007130. DAGAT.
[Graphical view]
PfamiPF03982. DAGAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDGAT2_MOUSE
AccessioniPrimary (citable) accession number: Q9DCV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 2001
Last modified: September 7, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.