DGAT2_ARATH
ID DGAT2_ARATH Reviewed; 314 AA.
AC Q9ASU1; Q9SCZ7;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Diacylglycerol O-acyltransferase 2 {ECO:0000305};
DE Short=AtDGAT2 {ECO:0000303|PubMed:23770095};
DE EC=2.3.1.20 {ECO:0000269|PubMed:23770095};
GN Name=DGAT2 {ECO:0000303|PubMed:20040537}; OrderedLocusNames=At3g51520;
GN ORFNames=F26O13.160;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP 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 [6]
RP TISSUE SPECIFICITY.
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 [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23042274; DOI=10.5603/19752;
RA Kwiatkowska M., Stepinski D., Poplonska K., Wojtczak A., Polit J.T.;
RT "DGAT2 revealed by the immunogold technique in Arabidopsis thaliana lipid
RT bodies associated with microtubules.";
RL Folia Histochem. Cytobiol. 50:427-431(2012).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 [9]
RP FUNCTION.
RX PubMed=24663078; DOI=10.1371/journal.pone.0092237;
RA Ayme L., Baud S., Dubreucq B., Joffre F., Chardot T.;
RT "Function and localization of the Arabidopsis thaliana diacylglycerol
RT acyltransferase DGAT2 expressed in yeast.";
RL PLoS ONE 9:E92237-E92237(2014).
CC -!- FUNCTION: Involved in triacylglycerol (TAG) synthesis. Catalyzes the
CC acylation of the sn-3 hydroxy group of sn-1,2-diacylglycerol using
CC acyl-CoA (PubMed:23770095, PubMed:24663078). Can use oleoyl-CoA,
CC linoleoyl-CoA and linolenoyl-CoA as substrates. Has substrate
CC preference for linolenoyl-CoA or oleoyl-CoA compared to linoleoyl-CoA
CC (PubMed:23770095). {ECO:0000269|PubMed:23770095,
CC ECO:0000269|PubMed:24663078}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = 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:23770095};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1,2-dihexanoyl-sn-glycerol = 1,2-
CC dihexanoyl-3-(9Z-octadecenoyl)-sn-glycerol + CoA;
CC Xref=Rhea:RHEA:56540, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:140526, ChEBI:CHEBI:140527;
CC Evidence={ECO:0000269|PubMed:23770095};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56541;
CC Evidence={ECO:0000269|PubMed:23770095};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23042274}; Multi-pass membrane protein
CC {ECO:0000255}. Lipid droplet {ECO:0000269|PubMed:23042274}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Lower levels in seeds than in other
CC tissues. Expressed in embryo and root meristematic cells
CC (PubMed:23042274). {ECO:0000269|PubMed:20101470,
CC ECO:0000269|PubMed:23042274}.
CC -!- DISRUPTION PHENOTYPE: No decrease in oil content.
CC {ECO:0000269|PubMed:20040537}.
CC -!- SIMILARITY: Belongs to the diacylglycerol acyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB63016.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL133452; CAB63016.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78802.1; -; Genomic_DNA.
DR EMBL; AF361832; AAK32844.1; -; mRNA.
DR EMBL; AY078045; AAL77746.1; -; mRNA.
DR EMBL; AY087571; AAM65113.1; -; mRNA.
DR PIR; T45783; T45783.
DR RefSeq; NP_566952.1; NM_115011.3.
DR AlphaFoldDB; Q9ASU1; -.
DR STRING; 3702.AT3G51520.1; -.
DR SwissLipids; SLP:000001912; -.
DR PaxDb; Q9ASU1; -.
DR PRIDE; Q9ASU1; -.
DR ProteomicsDB; 224034; -.
DR EnsemblPlants; AT3G51520.1; AT3G51520.1; AT3G51520.
DR GeneID; 824315; -.
DR Gramene; AT3G51520.1; AT3G51520.1; AT3G51520.
DR KEGG; ath:AT3G51520; -.
DR Araport; AT3G51520; -.
DR TAIR; locus:2081865; AT3G51520.
DR eggNOG; KOG0831; Eukaryota.
DR HOGENOM; CLU_023995_2_0_1; -.
DR InParanoid; Q9ASU1; -.
DR OMA; PFYRDYI; -.
DR OrthoDB; 1347007at2759; -.
DR PhylomeDB; Q9ASU1; -.
DR BioCyc; ARA:AT3G51520-MON; -.
DR BRENDA; 2.3.1.20; 399.
DR UniPathway; UPA00282; -.
DR PRO; PR:Q9ASU1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9ASU1; baseline and differential.
DR Genevisible; Q9ASU1; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IDA:TAIR.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IDA:TAIR.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0034389; P:lipid droplet organization; IDA:TAIR.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0046460; P:neutral lipid biosynthetic process; IDA:TAIR.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IDA:TAIR.
DR InterPro; IPR007130; DAGAT.
DR Pfam; PF03982; DAGAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Glycerol metabolism;
KW Lipid biosynthesis; Lipid droplet; Lipid metabolism; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..314
FT /note="Diacylglycerol O-acyltransferase 2"
FT /id="PRO_0000398614"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 314 AA; 35854 MW; 28DC9E0B50FF5949 CRC64;
MGGSREFRAE EHSNQFHSII AMAIWLGAIH FNVALVLCSL IFLPPSLSLM VLGLLSLFIF
IPIDHRSKYG RKLARYICKH ACNYFPVSLY VEDYEAFQPN RAYVFGYEPH SVLPIGVVAL
CDLTGFMPIP NIKVLASSAI FYTPFLRHIW TWLGLTAASR KNFTSLLDSG YSCVLVPGGV
QETFHMQHDA ENVFLSRRRG FVRIAMEQGS PLVPVFCFGQ ARVYKWWKPD CDLYLKLSRA
IRFTPICFWG VFGSPLPCRQ PMHVVVGKPI EVTKTLKPTD EEIAKFHGQY VEALRDLFER
HKSRVGYDLE LKIL
