Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Diacylglycerol O-acyltransferase 1

Gene

Dgat1

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

Functioni

Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. In contrast to DGAT2 it is not essential for survival. May be involved in VLDL (very low density lipoprotein) assembly. In liver, plays a role in esterifying exogenous fatty acids to glycerol. Functions as the major acyl-CoA retinol acyltransferase (ARAT) in the skin, where it acts to maintain retinoid homeostasis and prevent retinoid toxicity leading to skin and hair disorders.3 Publications

Catalytic activityi

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

Pathwayi: glycerolipid metabolism

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei426 – 4261Curated

GO - Molecular functioni

  • 2-acylglycerol O-acyltransferase activity Source: MGI
  • diacylglycerol O-acyltransferase activity Source: BHF-UCL
  • retinol O-fatty-acyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  • diacylglycerol metabolic process Source: BHF-UCL
  • fatty acid homeostasis Source: BHF-UCL
  • lipid storage Source: BHF-UCL
  • long-chain fatty-acyl-CoA metabolic process Source: BHF-UCL
  • triglyceride biosynthetic process Source: BHF-UCL
  • very-low-density lipoprotein particle assembly Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.3.1.20. 3474.
ReactomeiR-MMU-1482883. Acyl chain remodeling of DAG and TAG.
R-MMU-75109. Triglyceride Biosynthesis.
UniPathwayiUPA00230.

Chemistry

SwissLipidsiSLP:000000302.

Names & Taxonomyi

Protein namesi
Recommended name:
Diacylglycerol O-acyltransferase 1 (EC:2.3.1.202 Publications)
Alternative name(s):
Acyl-CoA retinol O-fatty-acyltransferase (EC:2.3.1.762 Publications)
Short name:
ARAT
Short name:
Retinol O-fatty-acyltransferase
Diglyceride acyltransferase
Gene namesi
Name:Dgat1
Synonyms:Dgat
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1333825. Dgat1.

Subcellular locationi

  • Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 9696CytoplasmicSequence analysisAdd
BLAST
Transmembranei97 – 11822HelicalSequence analysisAdd
BLAST
Topological domaini119 – 230112LumenalSequence analysisAdd
BLAST
Transmembranei231 – 24010HelicalSequence analysis
Topological domaini241 – 2411CytoplasmicSequence analysis
Transmembranei242 – 2509HelicalSequence analysis
Topological domaini251 – 498248LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: GO_Central
  • integral component of membrane Source: BHF-UCL
  • intracellular membrane-bounded organelle Source: BHF-UCL
  • membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice live well but display reduced postabsorptive chylomicronemia and accumulate neutral-lipid droplets in the cytoplasm of enterocytes when chronically fed a high fat diet.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi426 – 4261H → A: Impairs the ability to synthesize triacylglycerols, as well as retinyl and wax esters, in an in vitro acyltransferase assay. 1 Publication

Chemistry

ChEMBLiCHEMBL1075284.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 498498Diacylglycerol O-acyltransferase 1PRO_0000207655Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9Z2A7.
MaxQBiQ9Z2A7.
PaxDbiQ9Z2A7.
PRIDEiQ9Z2A7.

PTM databases

iPTMnetiQ9Z2A7.
PhosphoSiteiQ9Z2A7.

Expressioni

Gene expression databases

BgeeiENSMUSG00000022555.
CleanExiMM_DGAT1.
ExpressionAtlasiQ9Z2A7. baseline and differential.
GenevisibleiQ9Z2A7. MM.

Interactioni

Subunit structurei

Homodimer or homotetramer.1 Publication

Protein-protein interaction databases

IntActiQ9Z2A7. 2 interactions.
STRINGi10090.ENSMUSP00000023214.

Chemistry

BindingDBiQ9Z2A7.

Structurei

3D structure databases

ProteinModelPortaliQ9Z2A7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 100100Involved in homomerizationAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0380. Eukaryota.
COG5056. LUCA.
GeneTreeiENSGT00530000063122.
HOGENOMiHOG000213917.
HOVERGENiHBG051341.
InParanoidiQ9Z2A7.
KOiK11155.
OMAiGMMAQVP.
OrthoDBiEOG091G0GW2.
PhylomeDBiQ9Z2A7.
TreeFamiTF314921.

Family and domain databases

InterProiIPR027251. Diacylglycerol_acylTrfase1.
IPR004299. MBOAT_fam.
IPR014371. Oat_ACAT_DAG_ARE.
[Graphical view]
PANTHERiPTHR10408. PTHR10408. 1 hit.
PfamiPF03062. MBOAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000439. Oat_ACAT_DAG_ARE. 1 hit.
PIRSF500231. Oat_dag. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9Z2A7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDRGGAGSS RRRRTGSRVS VQGGSGPKVE EDEVRDAAVS PDLGAGGDAP
60 70 80 90 100
APAPAPAHTR DKDGRTSVGD GYWDLRCHRL QDSLFSSDSG FSNYRGILNW
110 120 130 140 150
CVVMLILSNA RLFLENLIKY GILVDPIQVV SLFLKDPYSW PAPCVIIASN
160 170 180 190 200
IFVVAAFQIE KRLAVGALTE QMGLLLHVVN LATIICFPAA VALLVESITP
210 220 230 240 250
VGSVFALASY SIMFLKLYSY RDVNLWCRQR RVKAKAVSTG KKVSGAAAQQ
260 270 280 290 300
AVSYPDNLTY RDLYYFIFAP TLCYELNFPR SPRIRKRFLL RRVLEMLFFT
310 320 330 340 350
QLQVGLIQQW MVPTIQNSMK PFKDMDYSRI IERLLKLAVP NHLIWLIFFY
360 370 380 390 400
WFFHSCLNAV AELLQFGDRE FYRDWWNAES VTYFWQNWNI PVHKWCIRHF
410 420 430 440 450
YKPMLRHGSS KWVARTGVFL TSAFFHEYLV SVPLRMFRLW AFTAMMAQVP
460 470 480 490
LAWIVGRFFQ GNYGNAAVWV TLIIGQPVAV LMYVHDYYVL NYDAPVGV
Length:498
Mass (Da):56,790
Last modified:May 1, 1999 - v1
Checksum:iE7B0DD6DDCF1EC2B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF078752 mRNA. Translation: AAC72917.1.
AK008995 mRNA. No translation available.
BC003717 mRNA. Translation: AAH03717.1.
CCDSiCCDS27573.1.
RefSeqiNP_034176.1. NM_010046.2.
UniGeneiMm.22633.

Genome annotation databases

EnsembliENSMUST00000023214; ENSMUSP00000023214; ENSMUSG00000022555.
GeneIDi13350.
KEGGimmu:13350.
UCSCiuc007wkn.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF078752 mRNA. Translation: AAC72917.1.
AK008995 mRNA. No translation available.
BC003717 mRNA. Translation: AAH03717.1.
CCDSiCCDS27573.1.
RefSeqiNP_034176.1. NM_010046.2.
UniGeneiMm.22633.

3D structure databases

ProteinModelPortaliQ9Z2A7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9Z2A7. 2 interactions.
STRINGi10090.ENSMUSP00000023214.

Chemistry

BindingDBiQ9Z2A7.
ChEMBLiCHEMBL1075284.
SwissLipidsiSLP:000000302.

PTM databases

iPTMnetiQ9Z2A7.
PhosphoSiteiQ9Z2A7.

Proteomic databases

EPDiQ9Z2A7.
MaxQBiQ9Z2A7.
PaxDbiQ9Z2A7.
PRIDEiQ9Z2A7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023214; ENSMUSP00000023214; ENSMUSG00000022555.
GeneIDi13350.
KEGGimmu:13350.
UCSCiuc007wkn.1. mouse.

Organism-specific databases

CTDi8694.
MGIiMGI:1333825. Dgat1.

Phylogenomic databases

eggNOGiKOG0380. Eukaryota.
COG5056. LUCA.
GeneTreeiENSGT00530000063122.
HOGENOMiHOG000213917.
HOVERGENiHBG051341.
InParanoidiQ9Z2A7.
KOiK11155.
OMAiGMMAQVP.
OrthoDBiEOG091G0GW2.
PhylomeDBiQ9Z2A7.
TreeFamiTF314921.

Enzyme and pathway databases

UniPathwayiUPA00230.
BRENDAi2.3.1.20. 3474.
ReactomeiR-MMU-1482883. Acyl chain remodeling of DAG and TAG.
R-MMU-75109. Triglyceride Biosynthesis.

Miscellaneous databases

PROiQ9Z2A7.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022555.
CleanExiMM_DGAT1.
ExpressionAtlasiQ9Z2A7. baseline and differential.
GenevisibleiQ9Z2A7. MM.

Family and domain databases

InterProiIPR027251. Diacylglycerol_acylTrfase1.
IPR004299. MBOAT_fam.
IPR014371. Oat_ACAT_DAG_ARE.
[Graphical view]
PANTHERiPTHR10408. PTHR10408. 1 hit.
PfamiPF03062. MBOAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000439. Oat_ACAT_DAG_ARE. 1 hit.
PIRSF500231. Oat_dag. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDGAT1_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2A7
Secondary accession number(s): Q9D7Q5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: May 1, 1999
Last modified: September 7, 2016
This is version 130 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.