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U84A2_ARATH
ID   U84A2_ARATH             Reviewed;         496 AA.
AC   Q9LVF0; Q8RX23;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=UDP-glycosyltransferase 84A2 {ECO:0000303|PubMed:11042215};
DE   AltName: Full=Protein BRIGHT TRICHOMES 1 {ECO:0000303|PubMed:17217457};
DE   AltName: Full=Sinapate 1-glucosyltransferase 1 {ECO:0000303|PubMed:11187886};
DE            Short=AtSGT1 {ECO:0000303|PubMed:11187886};
DE            EC=2.4.1.120 {ECO:0000269|PubMed:11187886};
GN   Name=UGT84A2 {ECO:0000303|PubMed:11042215};
GN   Synonyms=BRT1 {ECO:0000303|PubMed:17217457}, SGT,
GN   SGT1 {ECO:0000303|PubMed:11187886};
GN   OrderedLocusNames=At3g21560 {ECO:0000312|Araport:AT3G21560};
GN   ORFNames=MIL23.13 {ECO:0000312|EMBL:BAB02351.1};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(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   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=11187886; DOI=10.1016/s0014-5793(00)02270-5;
RA   Milkowski C., Baumert A., Strack D.;
RT   "Identification of four Arabidopsis genes encoding hydroxycinnamate
RT   glucosyltransferases.";
RL   FEBS Lett. 486:183-184(2000).
RN   [5]
RP   GENE FAMILY.
RX   PubMed=11042215; DOI=10.1074/jbc.m007447200;
RA   Li Y., Baldauf S., Lim E.K., Bowles D.J.;
RT   "Phylogenetic analysis of the UDP-glycosyltransferase multigene family of
RT   Arabidopsis thaliana.";
RL   J. Biol. Chem. 276:4338-4343(2001).
RN   [6]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=11042211; DOI=10.1074/jbc.m007263200;
RA   Lim E.K., Li Y., Parr A., Jackson R., Ashford D.A., Bowles D.J.;
RT   "Identification of glucosyltransferase genes involved in sinapate
RT   metabolism and lignin synthesis in Arabidopsis.";
RL   J. Biol. Chem. 276:4344-4349(2001).
RN   [7]
RP   FUNCTION.
RX   PubMed=12721858; DOI=10.1007/s00425-002-0969-0;
RA   Messner B., Thulke O., Schaeffner A.R.;
RT   "Arabidopsis glucosyltransferases with activities toward both endogenous
RT   and xenobiotic substrates.";
RL   Planta 217:138-146(2003).
RN   [8]
RP   FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   GLY-344; GLY-369; ALA-396 AND ARG-463.
RX   PubMed=17217457; DOI=10.1111/j.1365-313x.2006.02984.x;
RA   Sinlapadech T., Stout J., Ruegger M.O., Deak M., Chapple C.;
RT   "The hyper-fluorescent trichome phenotype of the brt1 mutant of Arabidopsis
RT   is the result of a defect in a sinapic acid: UDPG glucosyltransferase.";
RL   Plant J. 49:655-668(2007).
RN   [9]
RP   FUNCTION.
RX   PubMed=21899608; DOI=10.1111/j.1365-313x.2011.04779.x;
RA   Yonekura-Sakakibara K., Fukushima A., Nakabayashi R., Hanada K.,
RA   Matsuda F., Sugawara S., Inoue E., Kuromori T., Ito T., Shinozaki K.,
RA   Wangwattana B., Yamazaki M., Saito K.;
RT   "Two glycosyltransferases involved in anthocyanin modification delineated
RT   by transcriptome independent component analysis in Arabidopsis thaliana.";
RL   Plant J. 69:154-167(2012).
RN   [10]
RP   FUNCTION, AND INDUCTION BY AUXIN.
RX   PubMed=29027578; DOI=10.1007/s00299-017-2225-x;
RA   Zhang G.Z., Jin S.H., Li P., Jiang X.Y., Li Y.J., Hou B.K.;
RT   "Ectopic expression of UGT84A2 delayed flowering by indole-3-butyric acid-
RT   mediated transcriptional repression of ARF6 and ARF8 genes in
RT   Arabidopsis.";
RL   Plant Cell Rep. 36:1995-2006(2017).
CC   -!- FUNCTION: Sinapate glucosyltransferase (SGT) required for the
CC       biosynthesis of the glucose ester sinapoylglucose and subsequently
CC       sinapoylmalate and sinapoylcholine. Is the major SGT activity in plant
CC       (PubMed:11187886, PubMed:11042211, PubMed:17217457, PubMed:21899608).
CC       Plays an important role in sinapoylation of anthocyanins.
CC       Sinapoylglucose produced by UGT84A2 is a significant source of sinapoyl
CC       moieties for anthocyanins (PubMed:21899608). Indole-3-butyric acid
CC       (IBA)-specific glucosyltransferase that catalyzes the glucosylation of
CC       the auxin IBA, but not indole-3-acetic acid (IAA). May be involved in
CC       flowering regulation through IBA-mediated transcriptional repression of
CC       the auxin-response factors ARF6 and ARF8 and downstream flowering
CC       pathway genes (PubMed:29027578). Can glucosylate the phytotoxic
CC       xenobiotic compound 2,4,5-trichlorophenol (TCP) (PubMed:12721858).
CC       {ECO:0000269|PubMed:11042211, ECO:0000269|PubMed:11187886,
CC       ECO:0000269|PubMed:12721858, ECO:0000269|PubMed:17217457,
CC       ECO:0000269|PubMed:21899608, ECO:0000269|PubMed:29027578}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=E-sinapate + UDP-alpha-D-glucose = 1-O-(trans-sinapoyl)-beta-
CC         D-glucose + UDP; Xref=Rhea:RHEA:13305, ChEBI:CHEBI:16546,
CC         ChEBI:CHEBI:30023, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC         EC=2.4.1.120; Evidence={ECO:0000269|PubMed:11187886};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=250 uM for sinapate {ECO:0000269|PubMed:11042211};
CC   -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons, leaf veins and
CC       trichomes. {ECO:0000269|PubMed:17217457}.
CC   -!- INDUCTION: Induced by the auxin indole-3-butyric acid (IBA).
CC       {ECO:0000269|PubMed:29027578}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       condition, but reduced epidermal fluorescence due to reduced content of
CC       sinapoylmalate and hyper-fluorescence of trichomes due to accumulation
CC       of sinapic acid-derived polyketide. {ECO:0000269|PubMed:17217457}.
CC   -!- MISCELLANEOUS: Ectopic expression of UGT84A2 causes delay in flowering
CC       increase of indole-3-butyric acid (IBA) level, down-regulation of the
CC       auxin-response factors ARF6 and ARF8, and down-regulation of the
CC       flowering-related genes FT, SOC1, AP1, and LFY.
CC       {ECO:0000269|PubMed:29027578}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AB019232; BAB02351.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76523.1; -; Genomic_DNA.
DR   EMBL; AY090952; AAM13998.1; -; mRNA.
DR   EMBL; AY150475; AAN13000.1; -; mRNA.
DR   RefSeq; NP_188793.1; NM_113051.3.
DR   AlphaFoldDB; Q9LVF0; -.
DR   SMR; Q9LVF0; -.
DR   STRING; 3702.AT3G21560.1; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   PaxDb; Q9LVF0; -.
DR   PRIDE; Q9LVF0; -.
DR   ProteomicsDB; 228733; -.
DR   EnsemblPlants; AT3G21560.1; AT3G21560.1; AT3G21560.
DR   GeneID; 821710; -.
DR   Gramene; AT3G21560.1; AT3G21560.1; AT3G21560.
DR   KEGG; ath:AT3G21560; -.
DR   Araport; AT3G21560; -.
DR   TAIR; locus:2089880; AT3G21560.
DR   eggNOG; KOG1192; Eukaryota.
DR   HOGENOM; CLU_001724_0_1_1; -.
DR   InParanoid; Q9LVF0; -.
DR   OMA; SDDCIEW; -.
DR   OrthoDB; 508327at2759; -.
DR   PhylomeDB; Q9LVF0; -.
DR   BRENDA; 2.4.1.120; 399.
DR   SABIO-RK; Q9LVF0; -.
DR   PRO; PR:Q9LVF0; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LVF0; baseline and differential.
DR   Genevisible; Q9LVF0; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0080043; F:quercetin 3-O-glucosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0080044; F:quercetin 7-O-glucosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0050284; F:sinapate 1-glucosyltransferase activity; IDA:TAIR.
DR   GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; IMP:TAIR.
DR   GO; GO:0009801; P:cinnamic acid ester metabolic process; IMP:TAIR.
DR   GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   InterPro; IPR035595; UDP_glycos_trans_CS.
DR   Pfam; PF00201; UDPGT; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Detoxification; Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..496
FT                   /note="UDP-glycosyltransferase 84A2"
FT                   /id="PRO_0000409121"
FT   BINDING         295
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         350..352
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         367..375
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         389..392
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         344
FT                   /note="G->R: In brt1-6; reduces sinapoylmalate content in
FT                   leaves."
FT                   /evidence="ECO:0000269|PubMed:17217457"
FT   MUTAGEN         369
FT                   /note="G->E: In brt1-7; reduces sinapoylmalate content in
FT                   leaves."
FT                   /evidence="ECO:0000269|PubMed:17217457"
FT   MUTAGEN         396
FT                   /note="A->T: In brt1-5; reduces sinapoylmalate content in
FT                   leaves."
FT                   /evidence="ECO:0000269|PubMed:17217457"
FT   MUTAGEN         463
FT                   /note="R->K: In brt1-2; reduces sinapoylmalate content in
FT                   leaves."
FT                   /evidence="ECO:0000269|PubMed:17217457"
FT   CONFLICT        168
FT                   /note="D -> G (in Ref. 3; AAM13998)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   496 AA;  55799 MW;  11EDB18C8381477A CRC64;
     MELESSPPLP PHVMLVSFPG QGHVNPLLRL GKLLASKGLL ITFVTTESWG KKMRISNKIQ
     DRVLKPVGKG YLRYDFFDDG LPEDDEASRT NLTILRPHLE LVGKREIKNL VKRYKEVTKQ
     PVTCLINNPF VSWVCDVAED LQIPCAVLWV QSCACLAAYY YYHHNLVDFP TKTEPEIDVQ
     ISGMPLLKHD EIPSFIHPSS PHSALREVII DQIKRLHKTF SIFIDTFNSL EKDIIDHMST
     LSLPGVIRPL GPLYKMAKTV AYDVVKVNIS EPTDPCMEWL DSQPVSSVVY ISFGTVAYLK
     QEQIDEIAYG VLNADVTFLW VIRQQELGFN KEKHVLPEEV KGKGKIVEWC SQEKVLSHPS
     VACFVTHCGW NSTMEAVSSG VPTVCFPQWG DQVTDAVYMI DVWKTGVRLS RGEAEERLVP
     REEVAERLRE VTKGEKAIEL KKNALKWKEE AEAAVARGGS SDRNLEKFVE KLGAKPVGKV
     QNGSHNHVLA GSIKSF
 
 
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