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Protein

Diacylglycerol O-acyltransferase 2

Gene

Dgat2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at transcript 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 similarity

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: RGD
  • cellular triglyceride homeostasis Source: RGD
  • cholesterol homeostasis Source: RGD
  • diacylglycerol metabolic process Source: RGD
  • fat pad development Source: RGD
  • fatty acid homeostasis Source: RGD
  • glycerol metabolic process Source: UniProtKB-KW
  • lipid storage Source: RGD
  • long-chain fatty-acyl-CoA metabolic process Source: RGD
  • low-density lipoprotein particle clearance Source: RGD
  • negative regulation of fatty acid oxidation Source: RGD
  • positive regulation of gluconeogenesis Source: RGD
  • positive regulation of triglyceride biosynthetic process Source: RGD
  • regulation of cholesterol metabolic process Source: RGD
  • regulation of lipoprotein metabolic process Source: RGD
  • regulation of plasma lipoprotein particle levels Source: RGD
  • triglyceride biosynthetic process Source: RGD

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processGlycerol metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

ReactomeiR-RNO-1482883 Acyl chain remodeling of DAG and TAG
R-RNO-75109 Triglyceride biosynthesis
UniPathwayiUPA00282

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi620329 Dgat2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 69CytoplasmicSequence analysisAdd BLAST69
Transmembranei70 – 88HelicalSequence analysisAdd BLAST19
Topological domaini89 – 92LumenalSequence analysis4
Transmembranei93 – 112HelicalSequence analysisAdd BLAST20
Topological domaini113 – 388CytoplasmicSequence analysisAdd BLAST276

Keywords - Cellular componenti

Endoplasmic reticulum, Lipid droplet, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002490471 – 388Diacylglycerol O-acyltransferase 2Add BLAST388

Proteomic databases

PaxDbiQ5FVP8
PRIDEiQ5FVP8

PTM databases

PhosphoSitePlusiQ5FVP8

Expressioni

Gene expression databases

BgeeiENSRNOG00000016573
ExpressionAtlasiQ5FVP8 baseline and differential
GenevisibleiQ5FVP8 RN

Interactioni

Subunit structurei

Forms multimeric complexes consisting of several DGAT2 subunits.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022557

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0831 Eukaryota
ENOG410XTG3 LUCA
GeneTreeiENSGT00750000117391
HOGENOMiHOG000179738
HOVERGENiHBG065791
InParanoidiQ5FVP8
KOiK11160
OMAiLMYTFCT
OrthoDBiEOG091G0BGQ
PhylomeDBiQ5FVP8
TreeFamiTF314707

Family and domain databases

InterProiView protein in InterPro
IPR007130 DAGAT
PfamiView protein in Pfam
PF03982 DAGAT, 1 hit

Sequencei

Sequence statusi: Complete.

Q5FVP8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTLIAAYSG VLRGERRAEA ARSENKNKGS ALSREGSGRW GTGSSILSAL
60 70 80 90 100
QDIFSVTWLN RSKVEKHLQV ISVLQWVLSF LVLGVACSVI LMYTFCTDCW
110 120 130 140 150
LIAALYFTWL AFDWNTPKKG GRRSQWVRNW AVWRYFRDYF PIQLVKTHNL
160 170 180 190 200
LTTRNYIFGY HPHGIMGLGA FCNFSTEATE VSKKFPGIRP YLATLAGNFR
210 220 230 240 250
MPVLREYLMS GGICPVNRDT IDYLLSKNGS GNAIVIVVGG AAESLSSMPG
260 270 280 290 300
KNAVTLRNRK GFVKLALRHG ADLVPTYSFG ENEVYKQVIF EEGSWGRWVQ
310 320 330 340 350
KKFQKYIGFA PCIFHGRGLF SSDTWGLVPY SKPITTVVGE PITVPKLEHP
360 370 380
TQKDIDLYHT MYMEALVKLF DNHKTKFGLP ETEVLEVN
Length:388
Mass (Da):43,795
Last modified:March 1, 2005 - v1
Checksum:i04DCBB134206F78D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC089846 mRNA Translation: AAH89846.1
AJ487787 mRNA Translation: CAD32178.1
RefSeqiNP_001012345.1, NM_001012345.1
UniGeneiRn.9523

Genome annotation databases

EnsembliENSRNOT00000022557; ENSRNOP00000022557; ENSRNOG00000016573
GeneIDi252900
KEGGirno:252900
UCSCiRGD:620329 rat

Similar proteinsi

Entry informationi

Entry nameiDGAT2_RAT
AccessioniPrimary (citable) accession number: Q5FVP8
Secondary accession number(s): Q8K4Y4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: March 1, 2005
Last modified: March 28, 2018
This is version 93 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health