U88A1_ARATH
ID U88A1_ARATH Reviewed; 462 AA.
AC Q9LK73; B9DFF7; Q3EB57; Q3EB58; Q8L9U9;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=UDP-glycosyltransferase 88A1;
DE EC=2.4.1.-;
GN Name=UGT88A1; OrderedLocusNames=At3g16520; ORFNames=MDC8.15;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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] (ISOFORM 1).
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] (ISOFORM 3).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
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 [6]
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 [7]
RP FUNCTION.
RX PubMed=15352060; DOI=10.1002/bit.20154;
RA Lim E.K., Ashford D.A., Hou B., Jackson R.G., Bowles D.J.;
RT "Arabidopsis glycosyltransferases as biocatalysts in fermentation for
RT regioselective synthesis of diverse quercetin glucosides.";
RL Biotechnol. Bioeng. 87:623-631(2004).
CC -!- FUNCTION: Possesses low quercetin 3-O-glucosyltransferase, 7-O-
CC glucosyltransferase, 3'-O-glucosyltransferase and 4'-O-
CC glucosyltransferase activities in vitro. {ECO:0000269|PubMed:15352060}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9LK73-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LK73-2; Sequence=VSP_041233, VSP_041236;
CC Name=3;
CC IsoId=Q9LK73-3; Sequence=VSP_041234, VSP_041235;
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AP000373; BAB01151.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75829.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75830.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75831.1; -; Genomic_DNA.
DR EMBL; AY037255; AAK59856.1; -; mRNA.
DR EMBL; AY143902; AAN28841.1; -; mRNA.
DR EMBL; AK316752; BAH19474.1; -; mRNA.
DR EMBL; AY088211; AAM65752.1; -; mRNA.
DR RefSeq; NP_566549.1; NM_112523.1. [Q9LK73-2]
DR RefSeq; NP_566550.1; NM_112524.4. [Q9LK73-1]
DR RefSeq; NP_850597.1; NM_180266.3. [Q9LK73-3]
DR AlphaFoldDB; Q9LK73; -.
DR SMR; Q9LK73; -.
DR STRING; 3702.AT3G16520.3; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; Q9LK73; -.
DR PRIDE; Q9LK73; -.
DR ProteomicsDB; 228652; -. [Q9LK73-1]
DR EnsemblPlants; AT3G16520.1; AT3G16520.1; AT3G16520. [Q9LK73-2]
DR EnsemblPlants; AT3G16520.2; AT3G16520.2; AT3G16520. [Q9LK73-3]
DR EnsemblPlants; AT3G16520.3; AT3G16520.3; AT3G16520. [Q9LK73-1]
DR GeneID; 820900; -.
DR Gramene; AT3G16520.1; AT3G16520.1; AT3G16520. [Q9LK73-2]
DR Gramene; AT3G16520.2; AT3G16520.2; AT3G16520. [Q9LK73-3]
DR Gramene; AT3G16520.3; AT3G16520.3; AT3G16520. [Q9LK73-1]
DR KEGG; ath:AT3G16520; -.
DR Araport; AT3G16520; -.
DR TAIR; locus:2088339; AT3G16520.
DR eggNOG; KOG1192; Eukaryota.
DR InParanoid; Q9LK73; -.
DR OMA; QCFLENS; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q9LK73; -.
DR PRO; PR:Q9LK73; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LK73; baseline and differential.
DR Genevisible; Q9LK73; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0080045; F:quercetin 3'-O-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0080043; F:quercetin 3-O-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0080046; F:quercetin 4'-O-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0080044; F:quercetin 7-O-glucosyltransferase activity; IDA:TAIR.
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 2: Evidence at transcript level;
KW Alternative splicing; Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..462
FT /note="UDP-glycosyltransferase 88A1"
FT /id="PRO_0000409135"
FT BINDING 279
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 342..344
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 359..367
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 381..384
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT VAR_SEQ 446..451
FT /note="GSSHTA -> DCNSDG (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041233"
FT VAR_SEQ 446
FT /note="G -> E (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_041234"
FT VAR_SEQ 447..462
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_041235"
FT VAR_SEQ 452..462
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041236"
FT CONFLICT 79
FT /note="S -> F (in Ref. 5; AAM65752)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="F -> Y (in Ref. 5; AAM65752)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="Y -> F (in Ref. 5; AAM65752)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="D -> H (in Ref. 5; AAM65752)"
FT /evidence="ECO:0000305"
FT CONFLICT 171..172
FT /note="VH -> LN (in Ref. 5; AAM65752)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="S -> P (in Ref. 5; AAM65752)"
FT /evidence="ECO:0000305"
FT CONFLICT 249..250
FT /note="IE -> TD (in Ref. 5; AAM65752)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="R -> K (in Ref. 5; AAM65752)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="A -> T (in Ref. 5; AAM65752)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="N -> D (in Ref. 5; AAM65752)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="V -> L (in Ref. 5; AAM65752)"
FT /evidence="ECO:0000305"
FT CONFLICT 333..334
FT /note="DK -> NR (in Ref. 5; AAM65752)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="K -> E (in Ref. 5; AAM65752)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 51205 MW; 0C92D8A2CCBE4460 CRC64;
MGEEAIVLYP APPIGHLVSM VELGKTILSK NPSLSIHIIL VPPPYQPEST ATYISSVSSS
FPSITFHHLP AVTPYSSSST SRHHHESLLL EILCFSNPSV HRTLFSLSRN FNVRAMIIDF
FCTAVLDITA DFTFPVYFFY TSGAACLAFS FYLPTIDETT PGKNLKDIPT VHIPGVPPMK
GSDMPKAVLE RDDEVYDVFI MFGKQLSKSS GIIINTFDAL ENRAIKAITE ELCFRNIYPI
GPLIVNGRIE DRNDNKAVSC LNWLDSQPEK SVVFLCFGSL GLFSKEQVIE IAVGLEKSGQ
RFLWVVRNPP ELEKTELDLK SLLPEGFLSR TEDKGMVVKS WAPQVPVLNH KAVGGFVTHC
GWNSILEAVC AGVPMVAWPL YAEQRFNRVM IVDEIKIAIS MNESETGFVS STEVEKRVQE
IIGECPVRER TMAMKNAAEL ALTETGSSHT ALTTLLQSWS PK
