Q9SLD2 (DGAT1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Diacylglycerol O-acyltransferase 1
EC=2.3.1.20

Gene names

Name:	DGAT1
Synonyms:	DAGAT, TAG1
Ordered Locus Names:	At2g19450
ORF Names:	F3P11.5

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	520 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Major enzyme for oil accumulation in seeds. Catalyzes the acylation of the sn-3 hydroxy group of sn-1,2-diacylglycerol using acyl-CoA. Can use palmitoyl-CoA and oleoyl-CoA as substrates. Has complementary functions with PDAT1 that are essential for triacylglycerol synthesis and normal development of both seeds and pollen. Ref.3 Ref.4 Ref.10 Ref.12 Ref.13
Catalytic activity	Acyl-CoA + 1,2-diacylglycerol = CoA + triacylglycerol. Ref.8
Enzyme regulation	Partially inhibited by niacin. Ref.8
Pathway	Glycerolipid metabolism; triacylglycerol biosynthesis.
Subcellular location	Plastid › chloroplast membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.9.
Tissue specificity	Ubiquitous. Highest expression in young developing seeds. Ref.2 Ref.11 Ref.12 Ref.13
Developmental stage	Peak of expression in seeds 15 days after flowering. Highly expressed in senescing leaves. Ref.9 Ref.13
Induction	Up-regulated by glucose. Ref.8 Ref.11
Disruption phenotype	Decreased oil content and modified size and shape of oil bodies. Ref.12
Miscellaneous	The AS11 mutant has a complete duplication of exon 2. DGAT1 deficiency alters carbohydrate metabolism.
Sequence similarities	Belongs to the membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily.
Biophysicochemical properties	pH dependence: Optimum pH is between 6.75-7.25. Ref.8

Ontologies

Keywords
Biological process	Glycerol metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Chloroplast Endoplasmic reticulum Membrane Plastid
Domain	Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aging Inferred from expression pattern Ref.9. Source: TAIR carbohydrate metabolic process Inferred from mutant phenotype Ref.10. Source: TAIR embryo development ending in seed dormancy Traceable author statement Ref.10. Source: TAIR glycerol metabolic process Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of seed germination Inferred from mutant phenotype Ref.3. Source: TAIR regulation of embryonic development Inferred from mutant phenotype PubMed 11402213. Source: TAIR response to abscisic acid stimulus Inferred from mutant phenotype Ref.10. Source: TAIR response to cold Inferred from mutant phenotype Ref.10. Source: TAIR response to glucose stimulus Inferred from mutant phenotype Ref.10. Source: TAIR response to salt stress Inferred from mutant phenotype Ref.10. Source: TAIR triglyceride biosynthetic process Inferred from mutant phenotype PubMed 11402213. Source: TAIR
Cellular_component	chloroplast envelope Inferred from direct assay Ref.9. Source: TAIR chloroplast membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	diacylglycerol O-acyltransferase activity Inferred from direct assay Ref.2PubMed 12502715. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 520	520	Diacylglycerol O-acyltransferase 1		PRO_0000398613
Regions
	Transmembrane	126 – 146	21	Helical; Potential
	Transmembrane	176 – 196	21	Helical; Potential
	Transmembrane	207 – 227	21	Helical; Potential
	Transmembrane	233 – 253	21	Helical; Potential
	Transmembrane	276 – 296	21	Helical; Potential
	Transmembrane	317 – 337	21	Helical; Potential
	Transmembrane	365 – 385	21	Helical; Potential
	Transmembrane	434 – 454	21	Helical; Potential
	Transmembrane	457 – 477	21	Helical; Potential
	Transmembrane	487 – 507	21	Helical; Potential
	Compositional bias	79 – 99	21	Gly-rich
Sites
	Active site	447	1	Potential
Experimental info
	Mutagenesis	130	1	Q → QSHAGLFNLCVVVLIAVNSR LIIENLMK in AS11; strong reduction of enzymatic activity and delayed seed development. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9SLD2 [UniParc]. Last modified June 1, 2002. Version 2. Checksum: 9CD0E3E8956CEFF4	FASTA	520	58,986
	10 20 30 40 50 60 MAILDSAGVT TVTENGGGEF VDLDRLRRRK SRSDSSNGLL LSGSDNNSPS DDVGAPADVR 70 80 90 100 110 120 DRIDSVVNDD AQGTANLAGD NNGGGDNNGG GRGGGEGRGN ADATFTYRPS VPAHRRARES 130 140 150 160 170 180 PLSSDAIFKQ SHAGLFNLCV VVLIAVNSRL IIENLMKYGW LIRTDFWFSS RSLRDWPLFM 190 200 210 220 230 240 CCISLSIFPL AAFTVEKLVL QKYISEPVVI FLHIIITMTE VLYPVYVTLR CDSAFLSGVT 250 260 270 280 290 300 LMLLTCIVWL KLVSYAHTSY DIRSLANAAD KANPEVSYYV SLKSLAYFMV APTLCYQPSY 310 320 330 340 350 360 PRSACIRKGW VARQFAKLVI FTGFMGFIIE QYINPIVRNS KHPLKGDLLY AIERVLKLSV 370 380 390 400 410 420 PNLYVWLCMF YCFFHLWLNI LAELLCFGDR EFYKDWWNAK SVGDYWRMWN MPVHKWMVRH 430 440 450 460 470 480 IYFPCLRSKI PKTLAIIIAF LVSAVFHELC IAVPCRLFKL WAFLGIMFQV PLVFITNYLQ 490 500 510 520 ERFGSTVGNM IFWFIFCIFG QPMCVLLYYH DLMNRKGSMS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a cDNA encoding diacylglycerol acyltransferase from Arabidopsis thaliana and its functional expression." Hobbs D.H., Lu C., Hills M.J. FEBS Lett. 452:145-149(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"The Arabidopsis thaliana TAG1 mutant has a mutation in a diacylglycerol acyltransferase gene." Zou J., Wei Y., Jako C., Kumar A., Selvaraj G., Taylor D.C. Plant J. 19:645-653(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF GLN-130, TISSUE SPECIFICITY.
[3]	"The TAG1 locus of Arabidopsis encodes for a diacylglycerol acyltransferase." Routaboul J.M., Benning C., Bechtold N., Caboche M., Lepiniec L. Plant Physiol. Biochem. 37:831-840(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[4]	"Expression in yeast and tobacco of plant cDNAs encoding acyl CoA:diacylglycerol acyltransferase." Bouvier-Nave P., Benveniste P., Oelkers P., Sturley S.L., Schaller H. Eur. J. Biochem. 267:85-96(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. Strain: cv. Columbia.
[5]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[6]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[7]	"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.
[8]	"Expression and characterization of diacylglycerol acyltransferase from Arabidopsis thaliana in insect cell cultures." Hobbs D.H., Hills M.J. Biochem. Soc. Trans. 28:687-689(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[9]	"A role for diacylglycerol acyltransferase during leaf senescence." Kaup M.T., Froese C.D., Thompson J.E. Plant Physiol. 129:1616-1626(2002) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.
[10]	"Arabidopsis mutants deficient in diacylglycerol acyltransferase display increased sensitivity to abscisic acid, sugars, and osmotic stress during germination and seedling development." Lu C., Hills M.J. Plant Physiol. 129:1352-1358(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Expression pattern of diacylglycerol acyltransferase-1, an enzyme involved in triacylglycerol biosynthesis, in Arabidopsis thaliana." Lu C.L., de Noyer S.B., Hobbs D.H., Kang J., Wen Y., Krachtus D., Hills M.J. Plant Mol. Biol. 52:31-41(2003) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION BY GLUCOSE.
[12]	"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: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[13]	"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: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ131831 mRNA. Translation: CAB44774.1. AJ238008 mRNA. Translation: CAB45373.1. AF051849 mRNA. Translation: AAF19262.1. AC003058 Genomic DNA. Translation: AAM14875.1. AC005917 Genomic DNA. Translation: AAD10144.2. CP002685 Genomic DNA. Translation: AEC06882.1. AY054480 mRNA. Translation: AAK96671.1. BT008883 mRNA. Translation: AAP68322.1.
IPI	IPI00516527.
PIR	H84576. T01293. T01294. T52584.
RefSeq	NP_179535.1. NM_127503.2.
UniGene	At.20259.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9SLD2. 1 interaction.
Proteomic databases
PaxDb	Q9SLD2.
PRIDE	Q9SLD2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G19450.1; AT2G19450.1; AT2G19450.
GeneID	816464.
KEGG	ath:AT2G19450.
Organism-specific databases
TAIR	At2g19450.
Phylogenomic databases
eggNOG	COG5056.
HOGENOM	HOG000213917.
InParanoid	Q9SLD2.
KO	K11155.
OMA	LTQQWMV.
PhylomeDB	Q9SLD2.
ProtClustDB	PLN02401.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-2081.
BRENDA	2.3.1.20. 399.
UniPathway	UPA00282.
Gene expression databases
Genevestigator	Q9SLD2.
Family and domain databases
InterPro	IPR027251. Diacylglycerol_acylTrfase1. IPR004299. MBOAT_fam. IPR014371. Oat_ACAT_DAG_ARE. [Graphical view]
PANTHER	PTHR10408. PTHR10408. 1 hit.
Pfam	PF03062. MBOAT. 1 hit. [Graphical view]
PIRSF	PIRSF000439. Oat_ACAT_DAG_ARE. 1 hit. PIRSF500231. Oat_dag. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DGAT1_ARATH

Accession

Primary (citable) accession number: Q9SLD2
Secondary accession number(s): Q9S7F2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	June 1, 2002
Last modified:	May 1, 2013
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program