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Protein

Diacylglycerol O-acyltransferase 2

Gene

DGAT2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 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. Required for storage lipid synthesis (By similarity).By similarity

Catalytic activityi

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

Pathwayi: triacylglycerol biosynthesis

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

GO - Molecular functioni

  • diacylglycerol O-acyltransferase activity Source: TAIR

GO - Biological processi

  • glycerol metabolic process Source: UniProtKB-KW
  • lipid particle organization Source: TAIR
  • neutral lipid biosynthetic process Source: TAIR
  • triglyceride biosynthetic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Glycerol metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BioCyciARA:AT3G51520-MONOMER.
ReactomeiR-ATH-1482883. Acyl chain remodeling of DAG and TAG.
R-ATH-2142753. Arachidonic acid metabolism.
R-ATH-535734. Fatty acid, triacylglycerol, and ketone body metabolism.
R-ATH-75109. Triglyceride Biosynthesis.
R-ATH-8848584. Wax biosynthesis.
UniPathwayiUPA00282.

Names & Taxonomyi

Protein namesi
Recommended name:
Diacylglycerol O-acyltransferase 2 (EC:2.3.1.20)
Gene namesi
Name:DGAT2
Ordered Locus Names:At3g51520
ORF Names:F26O13.160
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G51520.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei18 – 3821HelicalSequence analysisAdd
BLAST
Transmembranei41 – 6121HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • lipid particle Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

No decrease in oil content.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 314314Diacylglycerol O-acyltransferase 2PRO_0000398614Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi162 – 1621N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9ASU1.
PRIDEiQ9ASU1.

Expressioni

Tissue specificityi

Ubiquitous. Lower levels in seeds than in other tissues.1 Publication

Gene expression databases

GenevisibleiQ9ASU1. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT3G51520.1.

Structurei

3D structure databases

ProteinModelPortaliQ9ASU1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0831. Eukaryota.
ENOG410XTG3. LUCA.
HOGENOMiHOG000239410.
InParanoidiQ9ASU1.
KOiK14457.
OMAiKPDCDLY.
PhylomeDBiQ9ASU1.

Family and domain databases

InterProiIPR007130. DAGAT.
[Graphical view]
PfamiPF03982. DAGAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ASU1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGSREFRAE EHSNQFHSII AMAIWLGAIH FNVALVLCSL IFLPPSLSLM
60 70 80 90 100
VLGLLSLFIF IPIDHRSKYG RKLARYICKH ACNYFPVSLY VEDYEAFQPN
110 120 130 140 150
RAYVFGYEPH SVLPIGVVAL CDLTGFMPIP NIKVLASSAI FYTPFLRHIW
160 170 180 190 200
TWLGLTAASR KNFTSLLDSG YSCVLVPGGV QETFHMQHDA ENVFLSRRRG
210 220 230 240 250
FVRIAMEQGS PLVPVFCFGQ ARVYKWWKPD CDLYLKLSRA IRFTPICFWG
260 270 280 290 300
VFGSPLPCRQ PMHVVVGKPI EVTKTLKPTD EEIAKFHGQY VEALRDLFER
310
HKSRVGYDLE LKIL
Length:314
Mass (Da):35,854
Last modified:June 1, 2001 - v1
Checksum:i28DC9E0B50FF5949
GO

Sequence cautioni

The sequence CAB63016.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL133452 Genomic DNA. Translation: CAB63016.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE78802.1.
AF361832 mRNA. Translation: AAK32844.1.
AY078045 mRNA. Translation: AAL77746.1.
AY087571 mRNA. Translation: AAM65113.1.
PIRiT45783.
RefSeqiNP_566952.1. NM_115011.3.
UniGeneiAt.28717.

Genome annotation databases

EnsemblPlantsiAT3G51520.1; AT3G51520.1; AT3G51520.
GeneIDi824315.
GrameneiAT3G51520.1; AT3G51520.1; AT3G51520.
KEGGiath:AT3G51520.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL133452 Genomic DNA. Translation: CAB63016.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE78802.1.
AF361832 mRNA. Translation: AAK32844.1.
AY078045 mRNA. Translation: AAL77746.1.
AY087571 mRNA. Translation: AAM65113.1.
PIRiT45783.
RefSeqiNP_566952.1. NM_115011.3.
UniGeneiAt.28717.

3D structure databases

ProteinModelPortaliQ9ASU1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT3G51520.1.

Proteomic databases

PaxDbiQ9ASU1.
PRIDEiQ9ASU1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G51520.1; AT3G51520.1; AT3G51520.
GeneIDi824315.
GrameneiAT3G51520.1; AT3G51520.1; AT3G51520.
KEGGiath:AT3G51520.

Organism-specific databases

TAIRiAT3G51520.

Phylogenomic databases

eggNOGiKOG0831. Eukaryota.
ENOG410XTG3. LUCA.
HOGENOMiHOG000239410.
InParanoidiQ9ASU1.
KOiK14457.
OMAiKPDCDLY.
PhylomeDBiQ9ASU1.

Enzyme and pathway databases

UniPathwayiUPA00282.
BioCyciARA:AT3G51520-MONOMER.
ReactomeiR-ATH-1482883. Acyl chain remodeling of DAG and TAG.
R-ATH-2142753. Arachidonic acid metabolism.
R-ATH-535734. Fatty acid, triacylglycerol, and ketone body metabolism.
R-ATH-75109. Triglyceride Biosynthesis.
R-ATH-8848584. Wax biosynthesis.

Miscellaneous databases

PROiQ9ASU1.

Gene expression databases

GenevisibleiQ9ASU1. AT.

Family and domain databases

InterProiIPR007130. DAGAT.
[Graphical view]
PfamiPF03982. DAGAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "DGAT1 and PDAT1 acyltransferases have overlapping functions in Arabidopsis triacylglycerol biosynthesis and are essential for normal pollen and seed development."
    Zhang M., Fan J., Taylor D.C., Ohlrogge J.B.
    Plant Cell 21:3885-3901(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  6. "DGAT1, DGAT2 and PDAT expression in seeds and other tissues of epoxy and hydroxy fatty acid accumulating plants."
    Li R., Yu K., Hildebrand D.F.
    Lipids 45:145-157(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiDGAT2_ARATH
AccessioniPrimary (citable) accession number: Q9ASU1
Secondary accession number(s): Q9SCZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  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.