RGT1_VANPO
ID RGT1_VANPO Reviewed; 958 AA.
AC A7TE38;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Glucose transport transcription regulator RGT1;
DE AltName: Full=Restores glucose transport protein 1;
GN Name=RGT1; ORFNames=Kpol_1002p5;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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 (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; DS480379; EDO19360.1; -; Genomic_DNA.
DR RefSeq; XP_001647218.1; XM_001647168.1.
DR AlphaFoldDB; A7TE38; -.
DR SMR; A7TE38; -.
DR STRING; 436907.A7TE38; -.
DR EnsemblFungi; EDO19360; EDO19360; Kpol_1002p5.
DR GeneID; 5547708; -.
DR KEGG; vpo:Kpol_1002p5; -.
DR eggNOG; ENOG502QRVJ; Eukaryota.
DR HOGENOM; CLU_006525_0_0_1; -.
DR InParanoid; A7TE38; -.
DR OMA; WFRNSLE; -.
DR OrthoDB; 754354at2759; -.
DR PhylomeDB; A7TE38; -.
DR Proteomes; UP000000267; 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;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Zinc.
FT CHAIN 1..958
FT /note="Glucose transport transcription regulator RGT1"
FT /id="PRO_0000408016"
FT DNA_BIND 75..104
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 958 AA; 104960 MW; 2DF7F270FB1F183E CRC64;
MTDIAESTAH PRDGVPPSQQ TTASVASAAL ATATASASPT TGSATSTAAP GKRSRSSSTG
SAKGSIGGKK ATRACDQCRK RKIKCDYDND KNVCSSCNRN GDRCQFNRVQ LKRGPSKGFN
RNNSTSSAAG ASTTSSTHQT FNANASGNTN SSNNNNHNNN NNNSVLLPPI TQYFQGNEQN
HDQQFWKVPV DLAGHLSPHH SQSHLHRDSV DSATSNNSNL NINGINIVDN STTNSQSGGY
FPVSACRSRA SSVPSFPRKP PMQIQPPMTS MYASSLGGGT PATGAIGASN TAVSGATVPG
TSSKRRKSVV SSNESPRTSR ASLLPRPDFA VVNLVPVPQN VVTPASSLPA VPSGPLPSTG
VGVGGSTGQV RLTDLDLINT YYEFVHLNFP VIPINKKALT SDILVINTSI EELNDLVIVW
FRNSLELLVT VSLEQPQTQS THAYTESLNS CFQNVVNLYP RLKQNNGIDP KVKIVYLCTF
LILIYVLFFL GQHNSFIISV SVTIFNNFGL YGKLLSLNTS SPDSSSPYDI IFVRLYLLLV
TFDSSYSMAL GTPKLLNLEI NGLVDKFFNL KSQNEHLFID ENLIKVNCIL KNLELGEYIC
NASHMKDSSD AMKVIKSTYM SKKHQSKKAD HSSSVSPMFI SEWFQKFLVD KKNLISLLLD
YQLRINDITP LQLSKLYVDL TNSLCALITV ILEILKLMMK LNPTNSIDYN YRPLQHFDID
KPPSGGGGSS STNTSSNPYS NPNSNEFYQK LLGLSSDRNT NLADMTRGCI TPFAIITINE
LFNVTELIKN IPSSLISVVM ESTKEEKENT INPQDLVLKL SNSMNEIVQI TSLLTMVKPY
KGIDSSYPRW QKFSKRSGPI PSMAPSNTAT STIQDFSEYN MTRSPSLGSS AYSNNPHSQH
SDHNFNETND YNDNISIFKK IYYENNNIQN NTTPQNEVLQ SYIDTAWRLL DDSELGWL
