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O75907 (DGAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Diacylglycerol O-acyltransferase 1

EC=2.3.1.20
Alternative name(s):
ACAT-related gene product 1
Acyl-CoA retinol O-fatty-acyltransferase
Short name=ARAT
Short name=Retinol O-fatty-acyltransferase
EC=2.3.1.76
Diglyceride acyltransferase
Gene names
Name:DGAT1
Synonyms:AGRP1, DGAT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

Acyl-CoA + 1,2-diacylglycerol = CoA + triacylglycerol. Ref.5

Acyl-CoA + retinol = CoA + retinyl ester. Ref.5

Enzyme regulation

XP620 is a selective DGAT1 inhibitor. Ref.5

Pathway

Lipid metabolism; glycerolipid metabolism.

Subunit structure

Homodimer or homotetramer By similarity.

Subcellular location

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

Sequence similarities

Belongs to the membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=25.9 µM for retinol Ref.5

KM=13.9 µM for palmitoyl coenzyme A

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacylglycerol acyl-chain remodeling

Traceable author statement. Source: Reactome

cellular lipid metabolic process

Traceable author statement. Source: Reactome

diacylglycerol metabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

fatty acid homeostasis

Inferred from electronic annotation. Source: Ensembl

glycerophospholipid biosynthetic process

Traceable author statement. Source: Reactome

lipid storage

Inferred from sequence or structural similarity. Source: BHF-UCL

long-chain fatty-acyl-CoA metabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

phospholipid metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

triglyceride biosynthetic process

Inferred from direct assay PubMed 18238778. Source: UniProtKB

triglyceride metabolic process

Traceable author statement Ref.1. Source: ProtInc

very-low-density lipoprotein particle assembly

Inferred from mutant phenotype PubMed 15308631. Source: BHF-UCL

   Cellular_componentendoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_function2-acylglycerol O-acyltransferase activity

Inferred from electronic annotation. Source: Ensembl

diacylglycerol O-acyltransferase activity

Inferred from experiment. Source: Reactome

retinol O-fatty-acyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

transferase activity, transferring acyl groups

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q99IB82EBI-3906527,EBI-6931023From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 488488Diacylglycerol O-acyltransferase 1
PRO_0000207654

Regions

Topological domain1 – 8787Cytoplasmic Potential
Transmembrane88 – 10922Helical; Potential
Topological domain110 – 220111Lumenal Potential
Transmembrane221 – 2299Helical; Potential
Topological domain2301Cytoplasmic Potential
Transmembrane231 – 2399Helical; Potential
Topological domain240 – 488249Lumenal Potential
Region1 – 9191Involved in homomerization By similarity

Sites

Active site4151 By similarity

Experimental info

Sequence conflict1291Y → H in AAC63997. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O75907 [UniParc].

Last modified July 25, 2003. Version 2.
Checksum: 6574D5DBF15D6171

FASTA48855,278
        10         20         30         40         50         60 
MGDRGSSRRR RTGSRPSSHG GGGPAAAEEE VRDAAAGPDV GAAGDAPAPA PNKDGDAGVG 

        70         80         90        100        110        120 
SGHWELRCHR LQDSLFSSDS GFSNYRGILN WCVVMLILSN ARLFLENLIK YGILVDPIQV 

       130        140        150        160        170        180 
VSLFLKDPYS WPAPCLVIAA NVFAVAAFQV EKRLAVGALT EQAGLLLHVA NLATILCFPA 

       190        200        210        220        230        240 
AVVLLVESIT PVGSLLALMA HTILFLKLFS YRDVNSWCRR ARAKAASAGK KASSAAAPHT 

       250        260        270        280        290        300 
VSYPDNLTYR DLYYFLFAPT LCYELNFPRS PRIRKRFLLR RILEMLFFTQ LQVGLIQQWM 

       310        320        330        340        350        360 
VPTIQNSMKP FKDMDYSRII ERLLKLAVPN HLIWLIFFYW LFHSCLNAVA ELMQFGDREF 

       370        380        390        400        410        420 
YRDWWNSESV TYFWQNWNIP VHKWCIRHFY KPMLRRGSSK WMARTGVFLA SAFFHEYLVS 

       430        440        450        460        470        480 
VPLRMFRLWA FTGMMAQIPL AWFVGRFFQG NYGNAAVWLS LIIGQPIAVL MYVHDYYVLN 


YEAPAAEA 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes."
Oelkers P., Behari A., Cromley D., Billheimer J.T., Sturley S.L.
J. Biol. Chem. 273:26765-26771(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Yamasaki Y., Watanabe T.K., Tanigami A.
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Skin.
[5]"Acyl coenzyme A dependent retinol esterification by acyl coenzyme A: diacylglycerol acyltransferase 1."
Orland M.D., Anwar K., Cromley D., Chu C.H., Chen L., Billheimer J.T., Hussain M.M., Cheng D.
Biochim. Biophys. Acta 1737:76-82(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF059202 mRNA. Translation: AAC63997.1.
AB057815 mRNA. Translation: BAC66170.1.
CH471162 Genomic DNA. Translation: EAW82127.1.
CH471162 Genomic DNA. Translation: EAW82129.1.
BC015762 mRNA. Translation: AAH15762.1.
BC023565 mRNA. Translation: AAH23565.1.
BC150649 mRNA. Translation: AAI50650.1.
RefSeqNP_036211.2. NM_012079.5.
UniGeneHs.521954.

3D structure databases

ProteinModelPortalO75907.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114241. 5 interactions.
IntActO75907. 3 interactions.
STRING9606.ENSP00000332258.

Chemistry

BindingDBO75907.
ChEMBLCHEMBL6009.

PTM databases

PhosphoSiteO75907.

Proteomic databases

PaxDbO75907.
PRIDEO75907.

Protocols and materials databases

DNASU8694.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000332324; ENSP00000332258; ENSG00000185000.
ENST00000565657; ENSP00000454624; ENSG00000261698.
GeneID8694.
KEGGhsa:8694.
UCSCuc003zbv.3. human.

Organism-specific databases

CTD8694.
GeneCardsGC08M145510.
HGNCHGNC:2843. DGAT1.
HPACAB032853.
MIM604900. gene.
neXtProtNX_O75907.
Orphanet329242. Congenital chronic diarrhea with protein-losing enteropathy.
PharmGKBPA27303.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5056.
HOGENOMHOG000213917.
HOVERGENHBG051341.
InParanoidO75907.
KOK11155.
OMALWAFTAM.
PhylomeDBO75907.
TreeFamTF314921.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
UniPathwayUPA00230.

Gene expression databases

ArrayExpressO75907.
BgeeO75907.
CleanExHS_DGAT1.
GenevestigatorO75907.

Family and domain databases

InterProIPR027251. Diacylglycerol_acylTrfase1.
IPR004299. MBOAT_fam.
IPR014371. Oat_ACAT_DAG_ARE.
[Graphical view]
PANTHERPTHR10408. PTHR10408. 1 hit.
PfamPF03062. MBOAT. 1 hit.
[Graphical view]
PIRSFPIRSF000439. Oat_ACAT_DAG_ARE. 1 hit.
PIRSF500231. Oat_dag. 1 hit.
ProtoNetSearch...

Other

ChiTaRSDGAT1. human.
GenomeRNAi8694.
NextBio32607.
PROO75907.
SOURCESearch...

Entry information

Entry nameDGAT1_HUMAN
AccessionPrimary (citable) accession number: O75907
Secondary accession number(s): B2RWQ2, D3DWL6, Q96BB8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: July 25, 2003
Last modified: April 16, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM