RGT1_ZYGRC
ID RGT1_ZYGRC Reviewed; 1066 AA.
AC C5E4G1;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Glucose transport transcription regulator RGT1;
DE AltName: Full=Restores glucose transport protein 1;
GN Name=RGT1; OrderedLocusNames=ZYRO0E05676g;
OS Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS / NRRL Y-229) (Candida mogii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX NCBI_TaxID=559307;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC Y-229;
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EDS1/RGT1 family. {ECO:0000305}.
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DR EMBL; CU928181; CAR30922.1; -; Genomic_DNA.
DR RefSeq; XP_002499177.1; XM_002499132.1.
DR AlphaFoldDB; C5E4G1; -.
DR STRING; 559307.C5E4G1; -.
DR EnsemblFungi; CAR30922; CAR30922; ZYRO0E05676g.
DR GeneID; 8204730; -.
DR KEGG; zro:ZYRO0E05676g; -.
DR HOGENOM; CLU_006525_0_0_1; -.
DR InParanoid; C5E4G1; -.
DR Proteomes; UP000008536; Chromosome E.
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;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Zinc.
FT CHAIN 1..1066
FT /note="Glucose transport transcription regulator RGT1"
FT /id="PRO_0000408020"
FT DNA_BIND 68..97
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1066 AA; 118463 MW; A7D074185906329E CRC64;
MTPMSENNGS ENTRDVSAAM MKSRSNSSEY AGGDGSFHAS EVESQSSQGA SGGNTSASKR
RTKASRACDQ CRKRKIRCDY DDDKGVCTSC RKNGESCAFE RIQLKRGPSK GAVRGHSVSR
SISGENNNTA ATAVGSGGEF SSPSSRQGSV LLPPLGQYLP QPAPVPSNLN ATQQQQFWKV
PYHDFQGQRR GSIDSLSSDM SAKSVNIPQE HLLYASPSAG HPPLHSPVTF GPNNSSTDSG
YWPFRNSGGE ESDELRRKSG SNPPSLKNVS QPPPPPLQQQ QQQQYSYSKF NNSFAQYGAN
GFPSRHGSIA SEGMSPSASV PYQSVPMNQS NSNGLSQQQQ QPIQWPKVQP KNLPPPQVQV
QAADKEETLG NSFQKTIKKR RTVSASSGEN KAEPGEYPLA RFSSSGNDSL LGGNLVSPAG
FVYGQIPEIQ LIDIYYEFIH MVFPIIPLNK ETVTNEILLV NTQPISPIHE INNYVILWFR
NSLELLIRIT LKRRSGHFYD SLTHSKEREL SNEIRGNSNG GGSNDSKDDN LEMQGVFVTA
LNECLQKIVD IHPSFRENKD KISPKVKIIY LSTFVLLNYI LAVVGYDNSF VLGMSTTIFK
DFKVYELLLY DDEDDDATKS GSNDNDNTNN DNNSNNANND NNDSRFYDEN NAMNWDQAGY
SITFKRLYVL LIIFDSLQCC SYGGPKLLNV PIEGASERFF QTKPHSNSKW VVDQSPTRMK
FILQSVKFGE LLAECSMKRR SICDLSRTQL TWEIPPYFLK GVTDEDDELF SLAQLLAAFI
LIRKEFVDCL LNLQDLETGE LPTVDMELCG ELIKLLCQLT SIILQALTVM MRTNPKNHID
YNYRPMKPME HDDSGNSASR KFTTSQAESG KNSGNDFYHK LLGLQDNAEA CLTNLLRGSI
SPYCISMLRE IRNVMELVKK MPASLIGVVM ACAGTHHNTA NNNNNDPLAI TFQSQELVVK
LSNCMNDMMQ ITSLLNMIKP VNLSDQDSDN TSATATITTT ETISKSLNRD HSIMRRLYYS
KAAKRDKKHI YPSSSSSPQL QETITTLKSF VLIGWKLLDD FELGWS