U80A2_ARATH
ID U80A2_ARATH Reviewed; 637 AA.
AC Q9M8Z7; B9DFL3; O23649; Q93ZJ2;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Sterol 3-beta-glucosyltransferase UGT80A2;
DE EC=2.4.1.173;
DE AltName: Full=UDP-glucose:sterol glucosyltransferase 80A2;
GN Name=UGT80A2; OrderedLocusNames=At3g07020; ORFNames=F17A9.17;
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=9349281; DOI=10.1023/a:1005806119807;
RA Warnecke D.C., Baltrusch M., Buck F., Wolter F.P., Heinz E.;
RT "UDP-glucose:sterol glucosyltransferase: cloning and functional expression
RT in Escherichia coli.";
RL Plant Mol. Biol. 35:597-603(1997).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 27-637 AND 83-637 (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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP TISSUE SPECIFICITY.
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19641030; DOI=10.1104/pp.109.140582;
RA DeBolt S., Scheible W.R., Schrick K., Auer M., Beisson F., Bischoff V.,
RA Bouvier-Nave P., Carroll A., Hematy K., Li Y., Milne J., Nair M.,
RA Schaller H., Zemla M., Somerville C.;
RT "Mutations in UDP-Glucose:sterol glucosyltransferase in Arabidopsis cause
RT transparent testa phenotype and suberization defect in seeds.";
RL Plant Physiol. 151:78-87(2009).
RN [9]
RP FUNCTION.
RX PubMed=21830156; DOI=10.1007/s11745-011-3602-9;
RA Schrick K., Shiva S., Arpin J.C., Delimont N., Isaac G., Tamura P.,
RA Welti R.;
RT "Steryl glucoside and acyl steryl glucoside analysis of Arabidopsis seeds
RT by electrospray ionization tandem mass spectrometry.";
RL Lipids 47:185-193(2012).
CC -!- FUNCTION: Involved in the biosynthesis of sterol glucosides. Catalyzes
CC the synthesis of steryl glycosides (SGs) and acyl steryl glycosides
CC (ASGs) which are the most abundant sterol derivatives in higher plants.
CC Can act on several sterols like sitosterol, campesterol and
CC stigmasterol. Both UGT80A2 and UGT80B1 are required for the normal
CC production of SGs and ASGs in seeds. {ECO:0000269|PubMed:19641030,
CC ECO:0000269|PubMed:21830156}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sterol + UDP-alpha-D-glucose = a sterol 3-beta-D-glucoside +
CC H(+) + UDP; Xref=Rhea:RHEA:22724, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15889, ChEBI:CHEBI:37424, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885; EC=2.4.1.173;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9M8Z7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M8Z7-2; Sequence=VSP_046337;
CC -!- TISSUE SPECIFICITY: Expressed in roots, cauline leaf epidermal cells,
CC stomata, stamen, pollen and around the base of siliques.
CC {ECO:0000269|PubMed:12721858, ECO:0000269|PubMed:19641030}.
CC -!- DISRUPTION PHENOTYPE: Reduced growth rates.
CC {ECO:0000269|PubMed:19641030}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL09737.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z83833; CAB06082.1; -; mRNA.
DR EMBL; AC016827; AAF27006.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74489.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74490.1; -; Genomic_DNA.
DR EMBL; AY057496; AAL09737.1; ALT_INIT; mRNA.
DR EMBL; AY079032; AAL79582.1; -; mRNA.
DR EMBL; AK316817; BAH19530.1; -; mRNA.
DR RefSeq; NP_001326118.1; NM_001337686.1.
DR RefSeq; NP_566297.2; NM_111582.3. [Q9M8Z7-1]
DR RefSeq; NP_850529.1; NM_180198.3. [Q9M8Z7-2]
DR AlphaFoldDB; Q9M8Z7; -.
DR SMR; Q9M8Z7; -.
DR BioGRID; 5222; 1.
DR STRING; 3702.AT3G07020.2; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR iPTMnet; Q9M8Z7; -.
DR SwissPalm; Q9M8Z7; -.
DR PaxDb; Q9M8Z7; -.
DR PRIDE; Q9M8Z7; -.
DR ProteomicsDB; 242610; -. [Q9M8Z7-1]
DR EnsemblPlants; AT3G07020.1; AT3G07020.1; AT3G07020. [Q9M8Z7-2]
DR EnsemblPlants; AT3G07020.2; AT3G07020.2; AT3G07020. [Q9M8Z7-1]
DR GeneID; 819887; -.
DR Gramene; AT3G07020.1; AT3G07020.1; AT3G07020. [Q9M8Z7-2]
DR Gramene; AT3G07020.2; AT3G07020.2; AT3G07020. [Q9M8Z7-1]
DR KEGG; ath:AT3G07020; -.
DR Araport; AT3G07020; -.
DR TAIR; locus:2077627; AT3G07020.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_000537_8_3_1; -.
DR InParanoid; Q9M8Z7; -.
DR PhylomeDB; Q9M8Z7; -.
DR BioCyc; ARA:AT3G07020-MON; -.
DR BioCyc; MetaCyc:AT3G07020-MON; -.
DR BRENDA; 2.4.1.173; 399.
DR PRO; PR:Q9M8Z7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M8Z7; baseline and differential.
DR Genevisible; Q9M8Z7; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0051507; F:beta-sitosterol UDP-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0102203; F:brassicasterol glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102205; F:cholesterol alpha-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102202; F:soladodine glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016906; F:sterol 3-beta-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030259; P:lipid glycosylation; IEA:InterPro.
DR GO; GO:0048316; P:seed development; IMP:TAIR.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016125; P:sterol metabolic process; IMP:TAIR.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR004276; GlycoTrans_28_N.
DR InterPro; IPR002213; UDP_glucos_trans.
DR Pfam; PF03033; Glyco_transf_28; 1.
DR Pfam; PF00201; UDPGT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycosyltransferase; Lipid biosynthesis;
KW Lipid metabolism; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transferase.
FT CHAIN 1..637
FT /note="Sterol 3-beta-glucosyltransferase UGT80A2"
FT /id="PRO_0000422074"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 636
FT /note="C -> F (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_046337"
FT CONFLICT 93
FT /note="K -> R (in Ref. 1; CAB06082)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 637 AA; 69277 MW; 11FF5572F5FA4094 CRC64;
MPEISPAELA KVSSSSSSSS SSSSGRASVK IEEIEGGAAA SGVVIVSEEL ETNPKTVVAS
IADETVAESS GTGNKSFSRV WTMPLEGSSS SDKAESSSTN QPRLDKSKTE RQQKVTHILA
EDAAKIFDDK ISAGKKLKLL NRIATVKHDG TVEFEVPADA IPQPIVVDRG ESKNGVCADE
SIDGVDLQYI PPMQIVMLIV GTRGDVQPFV AIAKRLQDYG HRVRLATHAN FKEFVLTAGL
EFYPLGGDPK VLAGYMVKNK GFLPSGPSEI PIQRNQMKDI IYSLLPACKE PDPDSGISFK
ADAIIANPPA YGHTHVAEAL KIPIHVFFTM PWTPTSEFPH PLSRVKQPAG YRLSYQIVDS
LIWLGIRDMV NDLRKKKLKL RPVTYLSGTQ GSGSNIPHGY MWSPHLVPKP KDWGPQIDVV
GFCYLDLASN YEPPAELVEW LEAGDKPIYI GFGSLPVQEP EKMTEIIVEA LQRTKQRGII
NKGWGGLGNL KEPKDFVYLL DNVPHDWLFP RCKAVVHHGG AGTTAAGLKA SCPTTIVPFF
GDQPFWGERV HARGVGPSPI PVDEFSLHKL EDAINFMLDD KVKSSAETLA KAMKDEDGVA
GAVKAFFKHL PSAKQNISDP IPEPSGFLSF RKCFGCS
