RGT1_KLULA
ID RGT1_KLULA Reviewed; 1007 AA.
AC Q6CIL8;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Glucose transport transcription regulator RGT1;
DE AltName: Full=Restores glucose transport protein 1;
GN Name=RGT1; OrderedLocusNames=KLLA0F25630g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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}.
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DR EMBL; CR382126; CAG98929.1; -; Genomic_DNA.
DR RefSeq; XP_456221.1; XM_456221.1.
DR AlphaFoldDB; Q6CIL8; -.
DR STRING; 28985.XP_456221.1; -.
DR PRIDE; Q6CIL8; -.
DR EnsemblFungi; CAG98929; CAG98929; KLLA0_F25630g.
DR GeneID; 2895143; -.
DR KEGG; kla:KLLA0_F25630g; -.
DR eggNOG; ENOG502QRVJ; Eukaryota.
DR HOGENOM; CLU_006525_0_0_1; -.
DR InParanoid; Q6CIL8; -.
DR OMA; WFRNSLE; -.
DR Proteomes; UP000000598; Chromosome F.
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; 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..1007
FT /note="Glucose transport transcription regulator RGT1"
FT /id="PRO_0000408014"
FT DNA_BIND 117..151
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1007 AA; 112261 MW; 37D96CDB8652A74B CRC64;
MLSALIQNGM SKSGDPTDVE NNTTNGSSST TDNANDVGRG VNTENNSKLE NDSSNAATIT
TSKQDPSAVD EATTPRSINT GASTVPEPDN TRRDSVSSNV STATTESRRR SKVSRACDQC
RKKKIKCDFI EGHDINPDQS CTGCRKIGEK CSFERIPLKR GPSKGYTRSN SQSRERRGSQ
RRRSSSEVSQ KGKKPSVSNP VNAVNESKSE VDASLHPGQS ATSTTNVSLH PLLQYLPGMN
HSAVSASSPS ALQQPFWKVP YHEYQNQRRP SLDSLASDSS QKPGGKTNQQ QPLPSQSQPQ
SLQNIGNSRS NTGPLPTQDT FRNQRYYYQP SQDSVSEAGS DNRRGSSAIP PLLNPAIQLQ
QQQYSYSQFA IAQQQQQQQQ QQQQQQLQLQ QHLQQQHQLQ QQQSLHSPQA NTMNASTGIS
NGGFVPYSGN KGLPSGGHVL ERTDSVASDA MSLNASPNIY TAEVESAPAS PVQKKRKRSN
RSSTSKKGKS TQQNLPATTP TLINYGQIAD AQLIDTYYAY IHLRFPIIPI NKDTLTNDLL
LVNTQPISEL HELNNYILLW FRNSLELLIR ICLKDKESEE ILYQQSTFVS AINECFQKIV
DIHPRFRDLE TQIDEKIATI YLVTFIILNC TLALVSYNNS FVLGMSVIIF NELKLWKNFI
FGNWNTVTGH DKICLRLYFE LNTFDSLQSC SFGVPKLMNL KLDETTASKL FYDEVSNDGT
GQETDKWNVD EDPERIRIIV DNMELGYFLS RLCQARRSSF EKPLPLVGEH NENKTIPGLF
RAFLSIKRQF TDTLLDLPDA EGKLPEMTPE LVTRLSNMIC DLTTTIHDLL KLNVEVNPTN
CLELFPDNSM QTVDESSAHN SAAQSSDPSN IEVGTVSPYV IAIYKDLFNV VELIKNMPTS
LIGCVMGTQA PNFDSQPLVL QLSQCMNNML QITTFTSSLS PFKIFKHELN AQSKNKTIDA
VPLWKQKMKS SLAPLQTAIT PQEIMMAQFI DIAWCIADTE ELGWFNQ