RGT1_YEAS1
ID RGT1_YEAS1 Reviewed; 1170 AA.
AC B3LR49;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Glucose transport transcription regulator RGT1;
DE AltName: Full=Restores glucose transport protein 1;
GN Name=RGT1; ORFNames=SCRG_03981;
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; CH408051; EDV13052.1; -; Genomic_DNA.
DR AlphaFoldDB; B3LR49; -.
DR EnsemblFungi; EDV13052; EDV13052; SCRG_03981.
DR HOGENOM; CLU_006525_0_0_1; -.
DR Proteomes; UP000008335; 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_0000408017"
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..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..323
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 944..977
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..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..323
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 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; 128240 MW; 2063178C29F8128C CRC64;
MNELNTVSTN SSDSTKNGGT SNSPDDMDSA AAASHAIKKR TKASRACDQC RKKKIKCDYK
DEKGVCSNCQ RNGDRCSFDR VPLKRGPSKG YTRSTSHPRT NEIQDHNNSR SYNTFDNSNN
TLNNNTGNSG DNGINSNTVP STPSRSNSVL LPPLTQYIPQ AGGIPPSFQN PAIQSTMPAG
NIGQQQFWKV PYHEFQHQRK GSIDSLQSDI SVRTLNPNEQ LSYNTVQQSP ITNKHTNDSG
NANGSVTGSG SASGSGGYWS FIRTSGLLAP TDDHNGEQTR RSSSIPSLLR NTSNSLLLGG
QPQLPPPQQQ SQPQAHQQKL QQGQNLYSYS 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 LFPEPDINDV
KPPVDEEVST GNGNTKTSEF EIGSESAGHM NPSNSPNSMD ENISHYSVLF KRLYVLLSVF
DSLQSCAFGG PKLLNISIQG STERFFSNDL GSKWCLEQSQ LRLKSVLQSL KLGELMSELT
RNRISMNGNR KPGFDITNSS SLLSEYVETQ PLSVAQLFCK LLIGKHNFIN CLLSLYDSEA
GVYSDLTLDL SSKIADSLCS LISIILQVLT LILRLNPTNS IDFNYRPPNP PANNPTVQEG
PSAMGSSPVA GNLSAAPPSE GNPDFYKKLL GLKQDTGTIL SDLCRGIISP FAIAILHEVY
NITELVKQMP TSLISIMMTA TTTQNTQDTK KSQDLVMKLS NSMNEVVQIT SVLTMIKPFK
IFEHELNKPI MSLTGGLSST TRNDVMWPKS GQGLRESSVM KTLLDERRTS GTQPTTAPVA
AEEPRLENVA LENFVSIGWK LLDDSELGWY
