ID   RGT1_YEAS7              Reviewed;        1170 AA.
AC   A6ZZS7;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Glucose transport transcription regulator RGT1;
DE   AltName: Full=Restores glucose transport protein 1;
GN   Name=RGT1; ORFNames=SCY_3337;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Glucose-responsive transcription factor that regulates
CC       expression of several glucose transporter (HXT) genes in response to
CC       glucose. In the absence of glucose, it functions as a transcriptional
CC       repressor, whereas high concentrations of glucose cause it to function
CC       as a transcriptional activator. In cells growing on low levels of
CC       glucose, has a neutral role, neither repressing nor activating
CC       transcription. Binds the consensus binding site sequence 5'-CGGANNA-3',
CC       of which multiple copies are present in all HXT promoters regulated by
CC       RGT1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC       Cytoplasm {ECO:0000250}.
CC   -!- PTM: Glucose-induced phosphorylation regulates the DNA-binding
CC       activity. Hyperphosphorylation in cells growing on high levels of
CC       glucose does prevents DNA-binding and dephosphorylation restores DNA-
CC       binding ability (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the EDS1/RGT1 family. {ECO:0000305}.
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DR   EMBL; AAFW02000152; EDN59870.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZZS7; -.
DR   EnsemblFungi; EDN59870; EDN59870; SCY_3337.
DR   HOGENOM; CLU_006525_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd00067; GAL4; 1.
DR   Gene3D; 4.10.240.10; -; 1.
DR   InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   Pfam; PF00172; Zn_clus; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF57701; SSF57701; 1.
DR   PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   3: Inferred from homology;
KW   Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Repressor; Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..1170
FT                   /note="Glucose transport transcription regulator RGT1"
FT                   /id="PRO_0000408019"
FT   DNA_BIND        47..76
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          77..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          217..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          384..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          725..757
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          946..974
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..343
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        384..471
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        728..757
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        956..973
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         202
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32862"
FT   MOD_RES         205
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32862"
FT   MOD_RES         208
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32862"
FT   MOD_RES         229
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32862"
FT   MOD_RES         283
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32862"
FT   MOD_RES         284
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32862"
FT   MOD_RES         410
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32862"
FT   MOD_RES         414
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32862"
FT   MOD_RES         1130
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32862"
SQ   SEQUENCE   1170 AA;  128228 MW;  53892AB766314AE9 CRC64;
     MNELNTVSTN SSDSTKNGGT SNSPDDMDSA AAASHAIKKR TKASRACDQC RKKKIKCDYK
     DEKGVCSNCQ RNGDRCSFDR VPLKRGPSKG YTRSTSHPRT NEIQDHNNSR SYNTFDNSNN
     TLNNNTGNSG DNGINSNTVP STPSRSNSVL LPPLTQYIPQ VGGIPPSFQN PAIQSTMPAG
     NIGQQQFWKV PYHEFQHQRK GSIDSLQSDI SVRTLNPNEQ LSYNTVQQSP ITNKHTNDSG
     NANGSVTGSG SASGSGGYWS FIRTSGLLAP TDDHNGEQTR RSSSIPSLLR NTSNSLLLGG
     QPQLPPPQQQ SQPQAHQQKL QQGQNPYSYS QFSQQQPYNP SISSFGQFAA NGFHSRQGSV
     ASEAMSPSAP AMFTSTSTNP VNVAQQTQRP QGQQVPQFSS ELDGNKRRQS APVSVTLSTD
     RLNGNENNNG EINNNNGSNN SGSSKDTSQH SQESVTTPAA LEASSPGSTP QRSTKKRRKS
     YVSKKTKPKR DSSISITSKD SAHPMTTSST IAYGQISDVD LIDTYYEFIH VGFPIIPLNK
     TTLTSDLLLV NTQPISNIHE VNSYVILWFR NSLELLVRVA LKQKPGGKFF DNIVGVALSP
     SNDNNKAGFT TATARDDAEK TRRDSHNEVQ DTLEVQSVFI AALNECFQKI VDIHPKFREN
     NDQISPKIKV IYLSTFILLN YILAFVGYDN SFVLGMSVTI FNEFKLYKLL LFPEPDVNDV
     KAPVDEEANT GNGNTKTSEF EIGSESAGHM NPSNSPNSMD ENISHYSVLF KRLYVLLSVF
     DSLQSCAFGG PKLLNISIQG STERFFSNDL GSKWCLEQSQ LRLKSVLQSL KLGELMSELT
     RNRISMNGNR KPGFDITNSS SLLSEYVETQ PLSVAQLFCK LLIGKHNFIN CLLSLYDSEA
     GVYSDLTLDL SSKIADSLCS LISIILQVLT LILRLNPTNS IDFNYRPPNP PANNPTVQEG
     PSAMGSSPVA GNLNAAPPSE GNPDFYKKLL GLKQDTGTIL SDLCRGIISP FAIAILHEVY
     NITELVKQMP TSLISIMMTA TTTQNTQDTK KSQDLVMKLS NSMNEVVQIT SVLTMIKPFK
     IFEHELNKPI MSLTGGLSST TRNDVMWPKS GQGLRESSVM KTLLDERRTS GTQPTTAPVA
     AEESRLENVA LENFVSIGWK LLDDSELGWY