DGAT3_ARATH
ID DGAT3_ARATH Reviewed; 360 AA.
AC Q9C5W0; A0A2H1ZED4; Q0WTD3; Q84MB9; Q9SX63;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Diacylglycerol O-acyltransferase 3 {ECO:0000305};
DE Short=AtDGAT3 {ECO:0000303|PubMed:22760209};
DE EC=2.3.1.20 {ECO:0000269|PubMed:30467384, ECO:0000305|PubMed:22760209};
GN Name=DGAT3 {ECO:0000303|PubMed:22760209};
GN OrderedLocusNames=At1g48300 {ECO:0000312|Araport:AT1G48300};
GN ORFNames=F11A17.15 {ECO:0000312|EMBL:AAD49767.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] OF 76-360 AND 157-360.
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] OF 115-360.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22760209; DOI=10.1104/pp.112.201541;
RA Hernandez M.L., Whitehead L., He Z., Gazda V., Gilday A., Kozhevnikova E.,
RA Vaistij F.E., Larson T.R., Graham I.A.;
RT "A cytosolic acyltransferase contributes to triacylglycerol synthesis in
RT sucrose-rescued Arabidopsis seed oil catabolism mutants.";
RL Plant Physiol. 160:215-225(2012).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND DEVELOPMENTAL STAGE.
RX PubMed=30467384; DOI=10.1038/s41598-018-35545-7;
RA Ayme L., Arragain S., Canonge M., Baud S., Touati N., Bimai O., Jagic F.,
RA Louis-Mondesir C., Briozzo P., Fontecave M., Chardot T.;
RT "Arabidopsis thaliana DGAT3 is a [2Fe-2S] protein involved in TAG
RT biosynthesis.";
RL Sci. Rep. 8:17254-17254(2018).
CC -!- FUNCTION: Involved in triacylglycerol (TAG) biosynthesis
CC (PubMed:22760209, PubMed:30467384). Catalyzes the acylation of the sn-3
CC hydroxy group of sn-1,2-diacylglycerol using acyl-CoA (PubMed:22760209,
CC PubMed:30467384). May preferentially use linolenoyl-CoA as substrate
CC and to a lesser extent linoleoyl-CoA (PubMed:22760209). May contribute
CC to the active recycling of linoleate and linolenate into TAG when seed
CC oil breakdown is blocked (PubMed:22760209).
CC {ECO:0000269|PubMed:22760209, ECO:0000269|PubMed:30467384}.
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:30467384, ECO:0000305|PubMed:22760209};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:30467384};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed in germinating seeds 48 hours after
CC exposure to the light, just after the emergence of the radicle.
CC {ECO:0000269|PubMed:30467384}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:22760209}.
CC -!- SIMILARITY: Belongs to the diacylglycerol acyltransferase family.
CC {ECO:0000305}.
CC -!- CAUTION: The subcellular localization of a truncated sequence of DGAT3,
CC lacking AA 1-75, has been shown to be cytosolic (PubMed:22760209).
CC However, the N-terminus of the full-length protein is predicted to
CC contain a transit peptide for chloroplast targeting. Therefore, the
CC localization of DGAT3 is unsure. {ECO:0000269|PubMed:22760209,
CC ECO:0000305}.
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DR EMBL; AC007932; AAD49767.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32272.2; -; Genomic_DNA.
DR EMBL; AF344322; AAK06873.1; -; mRNA.
DR EMBL; BT006415; AAP21223.1; -; mRNA.
DR EMBL; AK227624; BAE99615.1; -; mRNA.
DR PIR; H96522; H96522.
DR RefSeq; NP_175264.3; NM_103727.5.
DR AlphaFoldDB; Q9C5W0; -.
DR SMR; Q9C5W0; -.
DR STRING; 3702.AT1G48300.1; -.
DR PaxDb; Q9C5W0; -.
DR PRIDE; Q9C5W0; -.
DR ProteomicsDB; 201587; -.
DR ProteomicsDB; 224656; -.
DR EnsemblPlants; AT1G48300.1; AT1G48300.1; AT1G48300.
DR GeneID; 841250; -.
DR Gramene; AT1G48300.1; AT1G48300.1; AT1G48300.
DR KEGG; ath:AT1G48300; -.
DR Araport; AT1G48300; -.
DR TAIR; locus:2007750; AT1G48300.
DR eggNOG; ENOG502RS12; Eukaryota.
DR HOGENOM; CLU_065888_0_0_1; -.
DR InParanoid; Q9C5W0; -.
DR OMA; TVVGCKC; -.
DR OrthoDB; 1019509at2759; -.
DR BRENDA; 2.3.1.20; 399.
DR UniPathway; UPA00282; -.
DR PRO; PR:Q9C5W0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C5W0; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IMP:TAIR.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Acyltransferase; Glycerol metabolism; Iron; Iron-sulfur;
KW Lipid biosynthesis; Lipid metabolism; Metal-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..360
FT /note="Diacylglycerol O-acyltransferase 3"
FT /id="PRO_0000438912"
FT REGION 153..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 265
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305|PubMed:30467384"
FT BINDING 270
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305|PubMed:30467384"
FT BINDING 298
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305|PubMed:30467384"
FT BINDING 302
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305|PubMed:30467384"
SQ SEQUENCE 360 AA; 39146 MW; A62D0A3E7B0EBB04 CRC64;
MEVSGVVLRQ IPCVSSGSVA GLRLVSEFSG NTRTVGFRTR RFRGIVCNNE FADKGHVNYY
IEPTRCGEEK EKVKVMEKEK KALKKKAKVL KSLSKNLDMF SSIGFGLDPE AGLVGEIQTK
TISEATEILV KQLEQLKAEE KILKKQRKEE KAKAKAMKKM TEMDSESSSS SESSDSDCDK
GKVVDMSSLR NKAKPVLEPL QPEATVATLP RIQEDAISCK NTSEALQIAL QTSTIFPSMA
NPGQTLKTVE AVSVVGLPLN RVEVCMGGKC KRSGGALLLD EFQRAMTGFE GSAVACKCMG
KCRDGPNVRV VKETDAVMTD SVRTPSKTLC VGVGLQDVET IVTSFFDEEC SREGLGSVSY
