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Q96PD7 (DGAT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Diacylglycerol O-acyltransferase 2

EC=2.3.1.20
Alternative name(s):
Acyl-CoA retinol O-fatty-acyltransferase
Short name=ARAT
Short name=Retinol O-fatty-acyltransferase
EC=2.3.1.76
Diglyceride acyltransferase 2
Gene names
Name:DGAT2
ORF Names:HMFN1045, UNQ738/PRO1433
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity. Functions also as an acyl-CoA retinol acyltransferase (ARAT).

Catalytic activity

Acyl-CoA + 1,2-diacylglycerol = CoA + triacylglycerol. Ref.9

Acyl-CoA + retinol = CoA + retinyl ester. Ref.9

Enzyme regulation

Inhibited by niacin By similarity.

Pathway

Glycerolipid metabolism; triacylglycerol biosynthesis.

Subunit structure

Forms multimeric complexes consisting of several DGAT2 subunits By similarity.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Lipid droplet By similarity Ref.2.

Tissue specificity

Predominantly expressed in liver and white adipose tissue. Expressed at lower level in mammary gland, testis and peripheral blood leukocytes. Expressed in sebaceous glands of normal skin but decreased psoriatic skin. Ref.1 Ref.2

Sequence similarities

Belongs to the diacylglycerol acyltransferase family.

Sequence caution

The sequence BAD38635.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAD38961.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processGlycerol metabolism
Lipid biosynthesis
Lipid metabolism
   Cellular componentEndoplasmic reticulum
Lipid droplet
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   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

cellular response to oleic acid

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

cellular triglyceride homeostasis

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

cholesterol homeostasis

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

diacylglycerol metabolic process

Inferred from direct assay Ref.1. Source: BHF-UCL

fat pad development

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

fatty acid homeostasis

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

glycerol metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

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 direct assay Ref.1. Source: BHF-UCL

low-density lipoprotein particle clearance

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

phospholipid metabolic process

Traceable author statement. Source: Reactome

regulation of plasma lipoprotein particle levels

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

small molecule metabolic process

Traceable author statement. Source: Reactome

triglyceride biosynthetic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentendoplasmic reticulum

Inferred from direct assay Ref.2. Source: BHF-UCL

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of endoplasmic reticulum membrane

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

integral component of membrane

Inferred from direct assay Ref.1. Source: BHF-UCL

lipid particle

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

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 direct assay Ref.1. Source: UniProtKB

protein homodimerization activity

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

retinol O-fatty-acyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96PD7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q96PD7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     41-83: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 388388Diacylglycerol O-acyltransferase 2
PRO_0000249045

Regions

Topological domain1 – 6969Cytoplasmic Potential
Transmembrane70 – 8819Helical; Potential
Topological domain89 – 924Lumenal Potential
Transmembrane93 – 11220Helical; Potential
Topological domain113 – 388276Cytoplasmic Potential

Natural variations

Alternative sequence41 – 8343Missing in isoform 2.
VSP_020356
Natural variant3171R → G.
Corresponds to variant rs34421064 [ dbSNP | Ensembl ].
VAR_033864
Natural variant3611M → I.
Corresponds to variant rs34113941 [ dbSNP | Ensembl ].
VAR_033865

Experimental info

Sequence conflict2951W → C in AAV35727. Ref.7
Sequence conflict3041Q → H in AAV35727. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2002. Version 2.
Checksum: 39EE7783A3F06593

FASTA38843,831
        10         20         30         40         50         60 
MKTLIAAYSG VLRGERQAEA DRSQRSHGGP ALSREGSGRW GTGSSILSAL QDLFSVTWLN 

        70         80         90        100        110        120 
RSKVEKQLQV ISVLQWVLSF LVLGVACSAI LMYIFCTDCW LIAVLYFTWL VFDWNTPKKG 

       130        140        150        160        170        180 
GRRSQWVRNW AVWRYFRDYF PIQLVKTHNL LTTRNYIFGY HPHGIMGLGA FCNFSTEATE 

       190        200        210        220        230        240 
VSKKFPGIRP YLATLAGNFR MPVLREYLMS GGICPVSRDT IDYLLSKNGS GNAIIIVVGG 

       250        260        270        280        290        300 
AAESLSSMPG KNAVTLRNRK GFVKLALRHG ADLVPIYSFG ENEVYKQVIF EEGSWGRWVQ 

       310        320        330        340        350        360 
KKFQKYIGFA PCIFHGRGLF SSDTWGLVPY SKPITTVVGE PITIPKLEHP TQQDIDLYHT 

       370        380 
MYMEALVKLF DKHKTKFGLP ETEVLEVN 

« Hide

Isoform 2 [UniParc].

Checksum: CDDCB976A9D4E539
Show »

FASTA34539,044

References

« Hide 'large scale' references
[1]"Cloning of DGAT2, a second mammalian diacylglycerol acyltransferase, and related family members."
Cases S., Stone S.J., Zhou P., Yen C.-L.E., Tow B., Lardizabal K.D., Voelker T., Farese R.V. Jr.
J. Biol. Chem. 276:38870-38876(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Testis.
[2]"A novel diacylglycerol acyltransferase (DGAT2) is decreased in human psoriatic skin and increased in diabetic mice."
Wakimoto K., Chiba H., Michibata H., Seishima M., Kawasaki S., Okubo K., Mitsui H., Torii H., Imai Y.
Biochem. Biophys. Res. Commun. 310:296-302(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lymph node and Uterus.
[5]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: Pancreas.
[7]"Evaluation of gene structure of human DGAT2 gene."
Reichwald K., Petz U., Platzer M.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-341 (ISOFORM 2).
Tissue: Adipocyte.
[8]"Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas."
Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S., Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S., Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.
Oncogene 23:5901-5911(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 66-388.
Tissue: Hepatoblastoma.
[9]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF384161 mRNA. Translation: AAK84176.2.
AB048286 mRNA. Translation: BAB40641.2.
AY358532 mRNA. Translation: AAQ88896.1.
AL834287 mRNA. Translation: CAD38961.1. Different initiation.
CR749377 mRNA. Translation: CAH18230.1.
AP001922 Genomic DNA. No translation available.
BC015234 mRNA. Translation: AAH15234.1.
AY780647 mRNA. Translation: AAV35727.1.
AB073384 mRNA. Translation: BAD38635.1. Different initiation.
RefSeqNP_001240820.1. NM_001253891.1.
NP_115953.2. NM_032564.4.
UniGeneHs.129798.

3D structure databases

ProteinModelPortalQ96PD7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000228027.

Chemistry

BindingDBQ96PD7.
ChEMBLCHEMBL5853.

PTM databases

PhosphoSiteQ96PD7.

Polymorphism databases

DMDM74732654.

Proteomic databases

PaxDbQ96PD7.
PRIDEQ96PD7.

Protocols and materials databases

DNASU84649.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000228027; ENSP00000228027; ENSG00000062282. [Q96PD7-1]
ENST00000376262; ENSP00000365438; ENSG00000062282. [Q96PD7-2]
GeneID84649.
KEGGhsa:84649.
UCSCuc001oxa.3. human. [Q96PD7-1]
uc001oxb.3. human. [Q96PD7-2]

Organism-specific databases

CTD84649.
GeneCardsGC11P075479.
HGNCHGNC:16940. DGAT2.
HPAHPA013351.
MIM606983. gene.
neXtProtNX_Q96PD7.
PharmGKBPA27304.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG258143.
HOVERGENHBG065791.
InParanoidQ96PD7.
KOK11160.
OMALMYTFCT.
OrthoDBEOG7KH9KB.
PhylomeDBQ96PD7.
TreeFamTF314707.

Enzyme and pathway databases

BRENDA2.3.1.20. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKQ96PD7.
UniPathwayUPA00282.

Gene expression databases

BgeeQ96PD7.
CleanExHS_DGAT2.
GenevestigatorQ96PD7.

Family and domain databases

InterProIPR007130. DAGAT.
[Graphical view]
PANTHERPTHR12317. PTHR12317. 1 hit.
PfamPF03982. DAGAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDGAT2. human.
GenomeRNAi84649.
NextBio74602.
PROQ96PD7.
SOURCESearch...

Entry information

Entry nameDGAT2_HUMAN
AccessionPrimary (citable) accession number: Q96PD7
Secondary accession number(s): A6ND76 expand/collapse secondary AC list , Q5U810, Q68CL3, Q68DJ0, Q8NDB7, Q96BS0, Q9BYE5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 98 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM