ID DGAT1_ARATH Reviewed; 520 AA. AC Q9SLD2; Q9S7F2; DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 2. DT 02-SEP-2026, entry version 152. DE RecName: Full=Diacylglycerol O-acyltransferase 1 {ECO:0000305}; DE Short=AtDGAT1 {ECO:0000303|PubMed:23770095}; DE EC=2.3.1.20 {ECO:0000269|PubMed:11171171}; DE AltName: Full=Protein TRIACYLGLYCEROL 1 {ECO:0000303|PubMed:10580283}; GN Name=DGAT1 {ECO:0000303|PubMed:12177474}; GN Synonyms=ABX45 {ECO:0000303|PubMed:10580283}, DAGAT GN {ECO:0000312|EMBL:AAF19262.1}, TAG1 {ECO:0000303|PubMed:10571850, GN ECO:0000303|PubMed:10580283}; OrderedLocusNames=At2g19450; GN ORFNames=F3P11.5; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY. RC STRAIN=cv. Columbia; RX PubMed=10386579; DOI=10.1016/s0014-5793(99)00646-8; RA Hobbs D.H., Lu C., Hills M.J.; RT "Cloning of a cDNA encoding diacylglycerol acyltransferase from Arabidopsis RT thaliana and its functional expression."; RL FEBS Lett. 452:145-149(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF GLN-130, AND TISSUE RP SPECIFICITY. RX PubMed=10571850; DOI=10.1046/j.1365-313x.1999.00555.x; RA Zou J., Wei Y., Jako C., Kumar A., Selvaraj G., Taylor D.C.; RT "The Arabidopsis thaliana TAG1 mutant has a mutation in a diacylglycerol RT acyltransferase gene."; RL Plant J. 19:645-653(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RX PubMed=10580283; DOI=10.1016/s0981-9428(99)00115-1; RA Routaboul J.M., Benning C., Bechtold N., Caboche M., Lepiniec L.; RT "The TAG1 locus of Arabidopsis encodes for a diacylglycerol RT acyltransferase."; RL Plant Physiol. Biochem. 37:831-840(1999). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RC STRAIN=cv. Columbia; RX PubMed=10601854; DOI=10.1046/j.1432-1327.2000.00961.x; RA Bouvier-Nave P., Benveniste P., Oelkers P., Sturley S.L., Schaller H.; RT "Expression in yeast and tobacco of plant cDNAs encoding acyl RT CoA:diacylglycerol acyltransferase."; RL Eur. J. Biochem. 267:85-96(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617197; DOI=10.1038/45471; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."; RL Nature 402:761-768(1999). RN [6] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [7] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RT "Community-consensus reference genome of Arabidopsis thaliana Col-0."; RL Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [9] RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION. RX PubMed=11171171; DOI=10.1042/bst0280687; RA Hobbs D.H., Hills M.J.; RT "Expression and characterization of diacylglycerol acyltransferase from RT Arabidopsis thaliana in insect cell cultures."; RL Biochem. Soc. Trans. 28:687-689(2000). RN [10] RP FUNCTION. RX PubMed=11402213; DOI=10.1104/pp.126.2.861; RA Jako C., Kumar A., Wei Y., Zou J., Barton D.L., Giblin E.M., Covello P.S., RA Taylor D.C.; RT "Seed-specific over-expression of an Arabidopsis cDNA encoding a RT diacylglycerol acyltransferase enhances seed oil content and seed weight."; RL Plant Physiol. 126:861-874(2001). RN [11] RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION. RX PubMed=12177474; DOI=10.1104/pp.003087; RA Kaup M.T., Froese C.D., Thompson J.E.; RT "A role for diacylglycerol acyltransferase during leaf senescence."; RL Plant Physiol. 129:1616-1626(2002). RN [12] RP FUNCTION. RX PubMed=12114588; DOI=10.1104/pp.006122; RA Lu C., Hills M.J.; RT "Arabidopsis mutants deficient in diacylglycerol acyltransferase display RT increased sensitivity to abscisic acid, sugars, and osmotic stress during RT germination and seedling development."; RL Plant Physiol. 129:1352-1358(2002). RN [13] RP TISSUE SPECIFICITY, AND INDUCTION BY GLUCOSE. RX PubMed=12825687; DOI=10.1023/a:1023935605864; RA Lu C.L., de Noyer S.B., Hobbs D.H., Kang J., Wen Y., Krachtus D., RA Hills M.J.; RT "Expression pattern of diacylglycerol acyltransferase-1, an enzyme involved RT in triacylglycerol biosynthesis, in Arabidopsis thaliana."; RL Plant Mol. Biol. 52:31-41(2003). RN [14] RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE. RX PubMed=20040537; DOI=10.1105/tpc.109.071795; RA Zhang M., Fan J., Taylor D.C., Ohlrogge J.B.; RT "DGAT1 and PDAT1 acyltransferases have overlapping functions in Arabidopsis RT triacylglycerol biosynthesis and are essential for normal pollen and seed RT development."; RL Plant Cell 21:3885-3901(2009). RN [15] RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=20101470; DOI=10.1007/s11745-010-3385-4; RA Li R., Yu K., Hildebrand D.F.; RT "DGAT1, DGAT2 and PDAT expression in seeds and other tissues of epoxy and RT hydroxy fatty acid accumulating plants."; RL Lipids 45:145-157(2010). RN [16] RP INDUCTION. RX PubMed=23942253; DOI=10.1016/j.febslet.2013.07.045; RA Kong Y., Chen S., Yang Y., An C.; RT "ABA-insensitive (ABI) 4 and ABI5 synergistically regulate DGAT1 expression RT in Arabidopsis seedlings under stress."; RL FEBS Lett. 587:3076-3082(2013). RN [17] RP FUNCTION. RX PubMed=23770095; DOI=10.1016/j.febslet.2013.06.003; RA Zhou X.R., Shrestha P., Yin F., Petrie J.R., Singh S.P.; RT "AtDGAT2 is a functional acyl-CoA:diacylglycerol acyltransferase and RT displays different acyl-CoA substrate preferences than AtDGAT1."; RL FEBS Lett. 587:2371-2376(2013). RN [18] RP INTERACTION WITH LPCAT2 AND LPAT2. RC STRAIN=cv. Columbia; RX PubMed=26586834; DOI=10.1104/pp.15.01563; RA Shockey J., Regmi A., Cotton K., Adhikari N., Browse J., Bates P.D.; RT "Identification of Arabidopsis GPAT9 (At5g60620) as an essential gene RT involved in triacylglycerol biosynthesis."; RL Plant Physiol. 170:163-179(2016). CC -!- FUNCTION: Major contributor to triacylglycerol (TAG) synthesis and oil CC accumulation in seeds. Catalyzes the acylation of the sn-3 hydroxy CC group of sn-1,2-diacylglycerol using acyl-CoA (PubMed:10571850, CC PubMed:10580283, PubMed:10601854, PubMed:11402213, PubMed:12114588, CC PubMed:20040537, PubMed:20101470). Can use palmitoyl-CoA and oleoyl-CoA CC as substrates (PubMed:20101470). Can use oleoyl-CoA and linoleoyl-CoA CC as substrates. Has substrate preference for oleoyl-CoA compared to CC linoleoyl-CoA (PubMed:23770095). Has complementary functions with PDAT1 CC that are essential for triacylglycerol synthesis and normal development CC of both seeds and pollen (PubMed:20040537). CC {ECO:0000269|PubMed:10571850, ECO:0000269|PubMed:10580283, CC ECO:0000269|PubMed:10601854, ECO:0000269|PubMed:11402213, CC ECO:0000269|PubMed:12114588, ECO:0000269|PubMed:20040537, CC ECO:0000269|PubMed:20101470, ECO:0000269|PubMed:23770095}. CC -!- CATALYTIC ACTIVITY: CC Reaction=an acyl-CoA + a 1,2-diacyl-sn-glycerol = a triacyl-sn-glycerol CC + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20; CC Evidence={ECO:0000269|PubMed:11171171}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10869; CC Evidence={ECO:0000269|PubMed:11171171}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + (9Z)-octadecenoyl-CoA = CC 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38219, CC ChEBI:CHEBI:52333, ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57387; Evidence={ECO:0000269|PubMed:10386579}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38220; CC Evidence={ECO:0000269|PubMed:10386579}; CC -!- ACTIVITY REGULATION: Partially inhibited by niacin. CC {ECO:0000269|PubMed:11171171}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is between 6.75-7.25. {ECO:0000269|PubMed:11171171}; CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis. CC -!- SUBUNIT: Interacts with LPCAT2 and LPAT2. CC {ECO:0000269|PubMed:26586834}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane CC {ECO:0000269|PubMed:12177474}; Multi-pass membrane protein CC {ECO:0000269|PubMed:12177474}. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:12177474}; Multi-pass membrane protein CC {ECO:0000269|PubMed:12177474}. CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in young developing CC seeds. {ECO:0000269|PubMed:10571850, ECO:0000269|PubMed:12825687, CC ECO:0000269|PubMed:20040537, ECO:0000269|PubMed:20101470}. CC -!- DEVELOPMENTAL STAGE: Peak of expression in seeds 15 days after CC flowering. Highly expressed in senescing leaves. CC {ECO:0000269|PubMed:12177474, ECO:0000269|PubMed:20101470}. CC -!- INDUCTION: Up-regulated by glucose (PubMed:12825687). Induced by CC abscisic acid (ABA), jasmonate, salicylate, salt and osmotic stress CC (PubMed:23942253). {ECO:0000269|PubMed:12825687, CC ECO:0000269|PubMed:23942253}. CC -!- DISRUPTION PHENOTYPE: Decreased oil content and modified size and shape CC of oil bodies. {ECO:0000269|PubMed:20040537}. CC -!- MISCELLANEOUS: The AS11 mutant has a complete duplication of exon 2. CC -!- MISCELLANEOUS: DGAT1 deficiency alters carbohydrate metabolism. CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family. CC Sterol o-acyltransferase subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ131831; CAB44774.1; -; mRNA. DR EMBL; AJ238008; CAB45373.1; -; mRNA. DR EMBL; AF051849; AAF19262.1; -; mRNA. DR EMBL; AC003058; AAM14875.1; -; Genomic_DNA. DR EMBL; AC005917; AAD10144.2; -; Genomic_DNA. DR EMBL; CP002685; AEC06882.1; -; Genomic_DNA. DR EMBL; OZ408684; CAO7035547.1; -; Genomic_DNA. DR EMBL; AY054480; AAK96671.1; -; mRNA. DR EMBL; BT008883; AAP68322.1; -; mRNA. DR PIR; H84576; H84576. DR PIR; T01293; T01293. DR PIR; T01294; T01294. DR PIR; T52584; T52584. DR RefSeq; NP_179535.1; NM_127503.3. DR PDB; 9VJM; EM; 3.28 A; A/B=1-520. DR PDB; 9VJX; EM; 2.60 A; A/B=1-520. DR PDB; 9VK0; EM; 3.01 A; A/B=1-520. DR PDB; 9VK1; EM; 3.54 A; A/B=1-520. DR AlphaFoldDB; Q9SLD2; -. DR EMDB; EMD-65115; -. DR EMDB; EMD-65126; -. DR EMDB; EMD-65127; -. DR EMDB; EMD-65128; -. DR SMR; Q9SLD2; -. DR BioGRID; 1819; 1. DR FunCoup; Q9SLD2; 1623. DR IntAct; Q9SLD2; 1. DR STRING; 3702.Q9SLD2; -. DR SwissLipids; SLP:000001794; -. DR iPTMnet; Q9SLD2; -. DR PaxDb; 3702-Q9SLD2; -. DR ProteomicsDB; 224212; -. DR GeneID; 816464; -. DR KEGG; ath:AT2G19450; -. DR Araport; AT2G19450; -. DR TAIR; AT2G19450; TAG1. DR eggNOG; KOG0380; Eukaryota. DR HOGENOM; CLU_018190_0_1_1; -. DR InParanoid; Q9SLD2; -. DR OMA; RCHDYRR; -. DR OrthoDB; 10039049at2759; -. DR PhylomeDB; Q9SLD2; -. DR BioCyc; MetaCyc:MONOMER-2081; -. DR BRENDA; 2.3.1.20; 399. DR UniPathway; UPA00282; -. DR PRO; PR:Q9SLD2; -. DR Proteomes; UP000006548; Chromosome 2. DR ExpressionAtlas; Q9SLD2; baseline and differential. DR GO; GO:0009941; C:chloroplast envelope; IDA:TAIR. DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0005811; C:lipid droplet; IDA:TAIR. DR GO; GO:0016020; C:membrane; IDA:TAIR. DR GO; GO:0005634; C:nucleus; ISM:TAIR. DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IDA:TIGR. DR GO; GO:0005975; P:carbohydrate metabolic process; IMP:TAIR. DR GO; GO:0009793; P:embryo development ending in seed dormancy; TAS:TAIR. DR GO; GO:0010030; P:positive regulation of seed germination; IMP:TAIR. DR GO; GO:0045995; P:regulation of embryonic development; IMP:TAIR. DR GO; GO:0010029; P:regulation of seed germination; IMP:TAIR. DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR. DR GO; GO:0009409; P:response to cold; IMP:TAIR. DR GO; GO:0009749; P:response to glucose; IMP:TAIR. DR GO; GO:0009651; P:response to salt stress; IMP:TAIR. DR GO; GO:0019432; P:triglyceride biosynthetic process; IDA:TAIR. DR InterPro; IPR027251; Diacylglycerol_acylTrfase1. DR InterPro; IPR004299; MBOAT_fam. DR InterPro; IPR014371; Oat_ACAT_DAG_ARE. DR PANTHER; PTHR10408:SF7; DIACYLGLYCEROL O-ACYLTRANSFERASE 1; 1. DR PANTHER; PTHR10408; STEROL O-ACYLTRANSFERASE; 1. DR Pfam; PF03062; MBOAT; 1. DR PIRSF; PIRSF000439; Oat_ACAT_DAG_ARE; 1. DR PIRSF; PIRSF500231; Oat_dag; 1. DR PDBsum; 9VJM; -. DR PDBsum; 9VJX; -. DR PDBsum; 9VK0; -. DR PDBsum; 9VK1; -. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Chloroplast; Endoplasmic reticulum; KW Glycerol metabolism; Lipid biosynthesis; Lipid metabolism; Membrane; KW Plastid; Reference proteome; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1..520 FT /note="Diacylglycerol O-acyltransferase 1" FT /id="PRO_0000398613" FT TRANSMEM 126..146 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 176..196 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 207..227 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 233..253 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 276..296 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 317..337 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 365..385 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 434..454 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 457..477 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 487..507 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 28..57 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 72..116 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 392..398 FT /note="FYXDWWN motif" FT /evidence="ECO:0000250|UniProtKB:O75907" FT COMPBIAS 34..54 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 81..98 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 447 FT /evidence="ECO:0000250|UniProtKB:O75907" FT MUTAGEN 130 FT /note="Q->QSHAGLFNLCVVVLIAVNSRLIIENLMK: In AS11; strong FT reduction of enzymatic activity and delayed seed FT development." FT /evidence="ECO:0000269|PubMed:10571850" SQ SEQUENCE 520 AA; 58986 MW; 9CD0E3E8956CEFF4 CRC64; MAILDSAGVT TVTENGGGEF VDLDRLRRRK SRSDSSNGLL LSGSDNNSPS DDVGAPADVR DRIDSVVNDD AQGTANLAGD NNGGGDNNGG GRGGGEGRGN ADATFTYRPS VPAHRRARES PLSSDAIFKQ SHAGLFNLCV VVLIAVNSRL IIENLMKYGW LIRTDFWFSS RSLRDWPLFM CCISLSIFPL AAFTVEKLVL QKYISEPVVI FLHIIITMTE VLYPVYVTLR CDSAFLSGVT LMLLTCIVWL KLVSYAHTSY DIRSLANAAD KANPEVSYYV SLKSLAYFMV APTLCYQPSY PRSACIRKGW VARQFAKLVI FTGFMGFIIE QYINPIVRNS KHPLKGDLLY AIERVLKLSV PNLYVWLCMF YCFFHLWLNI LAELLCFGDR EFYKDWWNAK SVGDYWRMWN MPVHKWMVRH IYFPCLRSKI PKTLAIIIAF LVSAVFHELC IAVPCRLFKL WAFLGIMFQV PLVFITNYLQ ERFGSTVGNM IFWFIFCIFG QPMCVLLYYH DLMNRKGSMS //