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U75C1_SOLLC
ID   U75C1_SOLLC             Reviewed;         470 AA.
AC   K4CWS6;
DT   07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=UDP-glycosyltransferase 75C1 {ECO:0000303|PubMed:28482127};
DE            Short=Abscisic acid beta-glucosyltransferase {ECO:0000305};
DE            Short=Indole-3-acetate beta-glucosyltransferase {ECO:0000305};
DE            Short=SlUGT75C1 {ECO:0000303|PubMed:28482127};
DE            EC=2.4.1.121 {ECO:0000269|PubMed:28482127};
DE            EC=2.4.1.263 {ECO:0000269|PubMed:28482127};
GN   Name=UGT75C1 {ECO:0000303|PubMed:28482127};
GN   OrderedLocusNames=Solyc09g092500.1.1 {ECO:0000305};
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Heinz 1706;
RX   PubMed=22660326; DOI=10.1038/nature11119;
RG   Tomato Genome Consortium;
RT   "The tomato genome sequence provides insights into fleshy fruit
RT   evolution.";
RL   Nature 485:635-641(2012).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP   AND INDUCTION BY ABSCISIC ACID.
RC   STRAIN=cv. MicroTom;
RX   PubMed=28482127; DOI=10.1111/tpj.13588;
RA   Sun Y., Ji K., Liang B., Du Y., Jiang L., Wang J., Kai W., Zhang Y.,
RA   Zhai X., Chen P., Wang H., Leng P.;
RT   "Suppressing ABA uridine diphosphate glucosyltransferase (SlUGT75C1) alters
RT   fruit ripening and the stress response in tomato.";
RL   Plant J. 91:574-589(2017).
CC   -!- FUNCTION: Glucosyltransferase acting on both abscisic acid (ABA) and
CC       auxin (IAA). Required for ABA-mediated fruit ripening, seed
CC       germination, and negative responses to drought.
CC       {ECO:0000269|PubMed:28482127}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-cis-(+)-abscisate + UDP-alpha-D-glucose = beta-D-
CC         glucopyranosyl cis-(+)-abscisate + UDP; Xref=Rhea:RHEA:31031,
CC         ChEBI:CHEBI:22151, ChEBI:CHEBI:37569, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885; EC=2.4.1.263;
CC         Evidence={ECO:0000269|PubMed:28482127};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(indol-3-yl)acetate + UDP-alpha-D-glucose = 1-O-(indol-3-
CC         ylacetyl)-beta-D-glucose + UDP; Xref=Rhea:RHEA:14921,
CC         ChEBI:CHEBI:17990, ChEBI:CHEBI:30854, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885; EC=2.4.1.121;
CC         Evidence={ECO:0000269|PubMed:28482127};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.27 mM for abscisic acid {ECO:0000269|PubMed:28482127};
CC         Vmax=0.026 umol/min/ug enzyme with abscisic acid as substrate (in the
CC         presence of UDP-glucose) {ECO:0000269|PubMed:28482127};
CC       pH dependence:
CC         Optimum pH is 3.67-8. {ECO:0000269|PubMed:28482127};
CC       Temperature dependence:
CC         Optimum temperature is 37 degrees Celsius.
CC         {ECO:0000269|PubMed:28482127};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28482127}. Nucleus
CC       {ECO:0000269|PubMed:28482127}.
CC   -!- TISSUE SPECIFICITY: Expressed in flowers and fruits, especially in
CC       pulp, and, at lower levels, in seeds. {ECO:0000269|PubMed:28482127}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed during fruit ripening and flower
CC       development. In flowers, present at low levels during early
CC       developmental stages and later accumulates rapidly to reach a peak at
CC       the pre-blooming stage. Highly expressed in the sporogenous cells in
CC       the anther, pistil stigma and ovule and in basal vascular bundles. In
CC       fruits, accumulates progressively in the pulp with a maximum level at
CC       the pink stage. Highly expressed in the seeds, fruit peel and vascular
CC       tissues. {ECO:0000269|PubMed:28482127}.
CC   -!- INDUCTION: Induced by abscisic acid (ABA).
CC       {ECO:0000269|PubMed:28482127}.
CC   -!- DISRUPTION PHENOTYPE: Increased sensitivity to exogenous abscisic acid
CC       (ABA) and increased resistance to drought stress due to smaller
CC       stomatal apertures. Acceleration of fruit ripening with abnormally long
CC       shape by enhancing ABA levels and promoting the early release of
CC       ethylene (IAA) in immature fruit, and associated with altered
CC       expression of fruit ripening genes (e.g. ethylene biosynthesis and cell
CC       wall catabolism). Up-regulation of the expression of CYP707A2, which
CC       encodes an ABA 8'-hydroxylase, thus preventing excessive ABA
CC       accumulation. Seeds exhibit delayed germination and root growth.
CC       {ECO:0000269|PubMed:28482127}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; CM001072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004247894.1; XM_004247846.3.
DR   AlphaFoldDB; K4CWS6; -.
DR   SMR; K4CWS6; -.
DR   STRING; 4081.Solyc09g092500.1.1; -.
DR   PaxDb; K4CWS6; -.
DR   PRIDE; K4CWS6; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   HOGENOM; CLU_001724_0_1_1; -.
DR   InParanoid; K4CWS6; -.
DR   OrthoDB; 508327at2759; -.
DR   PhylomeDB; K4CWS6; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; K4CWS6; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0010294; F:abscisic acid glucosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0047215; F:indole-3-acetate beta-glucosyltransferase activity; IDA:UniProtKB.
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:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0009835; P:fruit ripening; IMP:UniProtKB.
DR   GO; GO:0080148; P:negative regulation of response to water deprivation; IMP:UniProtKB.
DR   GO; GO:0009787; P:regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR   GO; GO:0009845; P:seed germination; IMP:UniProtKB.
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   Abscisic acid signaling pathway; Cytoplasm; Developmental protein;
KW   Glycosyltransferase; Nucleus; Reference proteome; Transferase.
FT   CHAIN           1..470
FT                   /note="UDP-glycosyltransferase 75C1"
FT                   /id="PRO_0000445697"
FT   BINDING         290
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         344..345
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         362..370
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         384..387
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ   SEQUENCE   470 AA;  52739 MW;  74B74E60B55B9896 CRC64;
     MVQPHVLLVT FPAQGHINPS LQFAKRLIEM GIEVTFTTSV FAHRRMAKIA ASTAPKGLNL
     AAFSDGFDDG FKSNVDDSKR YMSEIRSRGS QTLRDVILKS SDEGRPVTSL VYTLLLPWAA
     EVARELHIPS ALLWIQPATV LDIYYYYFNG YEDEMKCSSS NDPNWSIQLP RLPLLKSQDL
     PSFLVSSSSK DDKYSFALPT FKEQLDTLDG EENPKVLVNT FDALELEPLK AIEKYNLIGI
     GPLIPSSFLG GKDSLESSFG GDLFQKSNDD YMEWLNTKPK SSIVYISFGS LLNLSRNQKE
     EIAKGLIEIQ RPFLWVIRDQ EEEKEEEKLS CMMELEKQGK IVPWCSQLEV LTHPSLGCFV
     SHCGWNSTLE SLSSGVPVVA FPHWTDQGTN AKLIEDVWKT GVRMRVNEDG VVESDEIKRC
     IEIVMDGGEK GEEMRKNAQK WKELARAAVK EGGSSEVNLK AFVLQVSKSC
 
 
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