RGT1_CANGA
ID RGT1_CANGA Reviewed; 1287 AA.
AC Q6FLP2;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Glucose transport transcription regulator RGT1;
DE AltName: Full=Restores glucose transport protein 1;
GN Name=RGT1; OrderedLocusNames=CAGL0L01903g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR380958; CAG61822.1; -; Genomic_DNA.
DR RefSeq; XP_448852.1; XM_448852.1.
DR AlphaFoldDB; Q6FLP2; -.
DR SMR; Q6FLP2; -.
DR STRING; 5478.XP_448852.1; -.
DR EnsemblFungi; CAG61822; CAG61822; CAGL0L01903g.
DR GeneID; 2890674; -.
DR KEGG; cgr:CAGL0L01903g; -.
DR CGD; CAL0135076; RGT1.
DR VEuPathDB; FungiDB:CAGL0L01903g; -.
DR eggNOG; ENOG502QRVJ; Eukaryota.
DR HOGENOM; CLU_006525_0_0_1; -.
DR InParanoid; Q6FLP2; -.
DR OMA; WFRNSLE; -.
DR Proteomes; UP000002428; Chromosome L.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:EnsemblFungi.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:EnsemblFungi.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:EnsemblFungi.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:EnsemblFungi.
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..1287
FT /note="Glucose transport transcription regulator RGT1"
FT /id="PRO_0000408013"
FT DNA_BIND 16..45
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 49..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..521
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1287 AA; 143425 MW; AA6CDBD5E6AFDA3A CRC64;
MPHNNDKKRT NVSRACDQCR RKKIKCDRNQ ERNICTSCQR NGERCKFERV PLKRGPSKGA
HKASDPELKL SSNKPSKSSL FEDSNSIIRP KSVGEDSNMD PLSRHGSNTP ILDNNSNSGI
NDRNMGGIDD RLGGSTDPGT PSRSGSILLP PLGQYPQQQN YTNNSTSASN NMLNSTSLNS
TILQQQQPFW KVPYHEFQNQ RRGSIESLQS DLSVRTFNPQ DQLVYNTFQQ SPIAMKHSSD
PTNSIPPNTK SQHLTTTSNI GSVVGANDLL SGNPNYWGSV RAGSFIPNGD ENDDQIPQNL
QRRSSSIPSI LRNTSTSILL SQPQLPHPTN GAGSTSNNFN NTNDNSNLIN NKGTGSTAGL
GNNIDNAVGS ASPQAQRQSQ QLYSYSQFLN QSKPYNNQNF SSFGQFSTNG FQSRHGSITS
EAMSPSTALG YNQNNSNNLP GANNPNISDI SLLPNKESDP RVNDSQKVVK TEVSNDIFQF
GEQNLANTIE SNADKSEDKV KSGGKKGGKV PRKRKTKQVK ESNKKLKVNK KSNFDSDSIN
SPKVPTPVQQ IKTGFQYGQI LDVELIDLYY EFIHVGFPVI PLNKQTLTND ILLVNTHPYS
NIHEVNSYVI LWFRNSLELL VRVALKRKND SPFFDSHNTP GPLRSASGDE NMAFNDTPKK
KDITSSHADS ISSGDDNGMA EVQSAFISAL NECFQRVVDI HPKVRENKDR ISPKIKIIYL
TTFILLNYIL ALVGYDNSFV LGMSVTIFNE FKLYKLLVLP YKAICQDSEF SFNAKQSISL
DDDFIENKNI GNGNGNRTNG STPGEPNNDE GENALTNFNP SKEQQNSQKG GSGEGNENQG
NQIRSKIGKA VNIEEETETN ENYTIMFKRL YILLTMFDSL QSCLFGGPKL LNVCITNTTE
KFFSGTTNSK WNIEDSLVRE KGALISLKLG ETLSEIASNR IIMNHFDIIT LTNNNQANAT
DIVFNLKKLS NNRDYDNFLQ ENKGLELFDQ QPLCISQLFH KMLIMKSSFT YQLLSLMDAN
NGNFVNMDLK RLEQIVESLC SLISVILQLL TLIMRLNPTN SIDLNYRPVT PTQRMEDMLS
NKNTDSTDSI SNSNKTNSGN DFYRRLLGLE HSNDIVYSDI SRGVISPFAM AILHESHNIH
ELIKMTPTIL IRVVMTLNVQ DDTGNSVNNN ATPGDHEEDM KLKRANTSQD LVYKLSNSMN
DVVQIASLLS MIKPLKLFDH GFKTFESEDV LQGNDEDAKK RQRPVLKRLF YDTTNVPKPE
AVDPLVVSLV NTGWNLLDDM ELGFLPQ
