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Protein

Diacylglycerol O-acyltransferase 1

Gene

Dgat1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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. 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. In liver, plays a role in esterifying exogenous fatty acids to glycerol.By similarity

Catalytic activityi

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

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 – 4261By similarity

GO - Molecular functioni

  • diacylglycerol binding Source: RGD
  • diacylglycerol O-acyltransferase activity Source: RGD
  • fatty acid binding Source: RGD
  • retinol O-fatty-acyltransferase activity Source: UniProtKB-EC
  • transferase activity, transferring acyl groups Source: RGD

GO - Biological processi

  • glycerolipid metabolic process Source: RGD
  • insulin secretion Source: RGD
  • ketone body metabolic process Source: RGD
  • positive regulation of fatty acid oxidation Source: RGD
  • positive regulation of hepatic stellate cell activation Source: RGD
  • positive regulation of triglyceride biosynthetic process Source: RGD
  • regulation of eating behavior Source: RGD
  • regulation of intestinal lipid absorption Source: RGD
  • regulation of vitamin A metabolic process Source: RGD
  • response to human chorionic gonadotropin Source: RGD
  • triglyceride biosynthetic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

UniPathwayiUPA00230.

Names & Taxonomyi

Protein namesi
Recommended name:
Diacylglycerol O-acyltransferase 1 (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
Gene namesi
Name:Dgat1
Synonyms:Dgat
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi628673. Dgat1.

Subcellular locationi

  • Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity

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: UniProtKB-KW
  • intracellular membrane-bounded organelle Source: RGD
  • plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL6129.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 498498Diacylglycerol O-acyltransferase 1PRO_0000207656Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9ERM3.
PeptideAtlasiQ9ERM3.
PRIDEiQ9ERM3.

Interactioni

Subunit structurei

Homodimer or homotetramer.By similarity

Protein-protein interaction databases

MINTiMINT-4569730.
STRINGi10116.ENSRNOP00000035110.

Chemistry

BindingDBiQ9ERM3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 9696Involved in homomerizationBy similarityAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0380. Eukaryota.
COG5056. LUCA.
HOVERGENiHBG051341.
InParanoidiQ9ERM3.
KOiK11155.
PhylomeDBiQ9ERM3.

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.

Q9ERM3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDRGGAGSS RRRRTGSRVS VQGGSGPKVE EDEVREAAVS PDLGAGGDAP
60 70 80 90 100
APAPAPAHTR DKDRQTSVGD GHWELRCHRL QDSLFSSDSG FSNYRGILNW
110 120 130 140 150
CVVMLILSNA RLSLENLIKY GILVDPIQVV SLFLKDPYSW PAPCLIIASN
160 170 180 190 200
IFIVATFQIE KRLSVGALTE QMGLLLHVVN LATIICFPAA VALLVESITP
210 220 230 240 250
VGSLFALASY SIIFLKLSSY RDVNLWCRQR RVKAKAVSAG KKVSGAAAQN
260 270 280 290 300
TVSYPDNLTY RDLYYFIFAP TLCYELNFPR SPRIRKRFLL RRVLEMLFFT
310 320 330 340 350
QLQVGLIQQW MVPTIQNSMK PFKDMDYSRI IERLLKLAVP NHLIWLIFFY
360 370 380 390 400
WLFHSCLNAV AELLQFGDRE FYRDWWNAES VTYFWQNWNI PVHKWCIRHF
410 420 430 440 450
YKPMLRLGSN KWMARTGVFW ASAFFHEYLV SIPLRMFRLW AFTAMMAQVP
460 470 480 490
LAWIVNRFFQ GNYGNAAVWV TLIIGQPVAV LMYVHDYYVL NYDAPVGA
Length:498
Mass (Da):56,870
Last modified:March 1, 2001 - v1
Checksum:i5B24DD4AEB87CB4D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF296131 mRNA. Translation: AAG10084.1.
RefSeqiNP_445889.1. NM_053437.1.
UniGeneiRn.252.

Genome annotation databases

GeneIDi84497.
KEGGirno:84497.
UCSCiRGD:628673. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF296131 mRNA. Translation: AAG10084.1.
RefSeqiNP_445889.1. NM_053437.1.
UniGeneiRn.252.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4569730.
STRINGi10116.ENSRNOP00000035110.

Chemistry

BindingDBiQ9ERM3.
ChEMBLiCHEMBL6129.

Proteomic databases

PaxDbiQ9ERM3.
PeptideAtlasiQ9ERM3.
PRIDEiQ9ERM3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi84497.
KEGGirno:84497.
UCSCiRGD:628673. rat.

Organism-specific databases

CTDi8694.
RGDi628673. Dgat1.

Phylogenomic databases

eggNOGiKOG0380. Eukaryota.
COG5056. LUCA.
HOVERGENiHBG051341.
InParanoidiQ9ERM3.
KOiK11155.
PhylomeDBiQ9ERM3.

Enzyme and pathway databases

UniPathwayiUPA00230.

Miscellaneous databases

PROiQ9ERM3.

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_RAT
AccessioniPrimary (citable) accession number: Q9ERM3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 101 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.