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Reviewed, UniProtKB/Swiss-Prot Q08650 (DGA1_YEAST)

Last modified February 9, 2010. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Diacylglycerol O-acyltransferase 1
    EC=2.3.1.20
Gene names
Name: DGA1
Ordered Locus Names: YOR245C
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length418 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. Required for storage lipid synthesis. May be involved in lipid particle synthesis from the endoplasmic reticulum and ergosterol biosynthesis. Ref.2 Ref.3 Ref.4 Ref.7 Ref.8

Catalytic activity

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

Pathway

Glycerolipid metabolism; triacylglycerol biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein Potential. Lipid droplet Ref.2 Ref.5.

Miscellaneous

Present with 907 molecules/cell in log phase SD medium. Ref.6

Sequence similarities

Belongs to the diacylglycerol acyltransferase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PDC1P061691EBI-33586,EBI-5687

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 418418Diacylglycerol O-acyltransferase 1
PRO_0000233001

Regions

Transmembrane72 – 9221 Potential

Amino acid modifications

Modified residue171Phosphoserine Ref.9 Ref.10

Sequences

Sequence LengthMass (Da)Tools
Q08650-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E6ECAA95219583BD

FASTA41847,711
        10         20         30         40         50         60 
MSGTFNDIRR RKKEEGSPTA GITERHENKS LSSIDKREQT LKPQLESCCP LATPFERRLQ 

        70         80         90        100        110        120 
TLAVAWHTSS FVLFSIFTLF AISTPALWVL AIPYMIYFFF DRSPATGEVV NRYSLRFRSL 

       130        140        150        160        170        180 
PIWKWYCDYF PISLIKTVNL KPTFTLSKNK RVNEKNYKIR LWPTKYSINL KSNSTIDYRN 

       190        200        210        220        230        240 
QECTGPTYLF GYHPHGIGAL GAFGAFATEG CNYSKIFPGI PISLMTLVTQ FHIPLYRDYL 

       250        260        270        280        290        300 
LALGISSVSR KNALRTLSKN QSICIVVGGA RESLLSSTNG TQLILNKRKG FIKLAIQTGN 

       310        320        330        340        350        360 
INLVPVFAFG EVDCYNVLST KKDSVLGKMQ LWFKENFGFT IPIFYARGLF NYDFGLLPFR 

       370        380        390        400        410 
APINVVVGRP IYVEKKITNP PDDVVNHFHD LYIAELKRLY YENREKYGVP DAELKIVG 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed: 9169874] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[2]"Synthesis of triacylglycerols by the acyl-coenzyme A:diacyl-glycerol acyltransferase Dga1p in lipid particles of the yeast Saccharomyces cerevisiae."
Sorger D., Daum G.
J. Bacteriol. 184:519-524(2002) [PubMed: 11751830] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[3]"Storage lipid synthesis is non-essential in yeast."
Sandager L., Gustavsson M.H., Staahl U., Dahlqvist A., Wiberg E., Banas A., Lenman M., Ronne H., Stymne S.
J. Biol. Chem. 277:6478-6482(2002) [PubMed: 11741946] [Abstract]
Cited for: FUNCTION.
[4]"The DGA1 gene determines a second triglyceride synthetic pathway in yeast."
Oelkers P., Cromley D., Padamsee M., Billheimer J.T., Sturley S.L.
J. Biol. Chem. 277:8877-8881(2002) [PubMed: 11751875] [Abstract]
Cited for: FUNCTION.
[5]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"Lipid dynamics in yeast under haem-induced unsaturated fatty acid and/or sterol depletion."
Ferreira T., Regnacq M., Alimardani P., Moreau-Vauzelle C., Berges T.
Biochem. J. 378:899-908(2004) [PubMed: 14640980] [Abstract]
Cited for: FUNCTION.
[8]"A yeast strain lacking lipid particles bears a defect in ergosterol formation."
Sorger D., Athenstaedt K., Hrastnik C., Daum G.
J. Biol. Chem. 279:31190-31196(2004) [PubMed: 15155725] [Abstract]
Cited for: FUNCTION.
[9]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, MASS SPECTROMETRY.
[10]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z75153 Genomic DNA. Translation: CAA99466.1.
PIRS67138.
RefSeqNP_014888.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2923N.
IntActQ08650. 5 interactions.
STRINGQ08650.

Genome annotation databases

EnsemblYOR245C; YOR245C; YOR245C; Saccharomyces cerevisiae. [Genome view]
GeneID854419.
KEGGsce:YOR245C.
NMPDRfig|4932.3.peg.6000.

Organism-specific databases

CYGDYOR245c.
SGDS000005771. DGA1.

Phylogenomic databases

eggNOGfuNOG04748.
HOGENOMHBG561030.
OMAENDIFNQ.
OrthoDBEOG92JQ84.
PhylomeDBQ08650.

Enzyme and pathway databases

BRENDA2.3.1.20. 250.

Gene expression databases

ArrayExpressQ08650.
GenevestigatorQ08650.
GermOnlineYOR245C. Saccharomyces cerevisiae.

Family and domain databases

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

Other Resources

NextBio976625.

Entry information

Entry nameDGA1_YEAST
AccessionPrimary (citable) accession number: Q08650
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: November 1, 1996
Last modified: February 9, 2010
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents