RGT1_YEAST
ID RGT1_YEAST Reviewed; 1170 AA.
AC P32862; D6VXP8;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Glucose transport transcription regulator RGT1;
DE AltName: Full=Restores glucose transport protein 1;
GN Name=RGT1; OrderedLocusNames=YKL038W; ORFNames=YKL251;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1481573; DOI=10.1002/yea.320081108;
RA Purnelle B., Skala J., van Dyck L., Goffeau A.;
RT "The sequence of a 12 kb fragment on the left arm of yeast chromosome XI
RT reveals five new open reading frames, including a zinc finger protein and a
RT homolog of the UDP-glucose pyrophosphorylase from potato.";
RL Yeast 8:977-986(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION.
RX PubMed=1874412; DOI=10.1093/genetics/128.3.505;
RA Marshall-Carlson L., Neigeborn L., Coons D., Bisson L., Carlson M.;
RT "Dominant and recessive suppressors that restore glucose transport in a
RT yeast snf3 mutant.";
RL Genetics 128:505-512(1991).
RN [5]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=8887670; DOI=10.1128/mcb.16.11.6419;
RA Ozcan S., Leong T., Johnston M.;
RT "Rgt1p of Saccharomyces cerevisiae, a key regulator of glucose-induced
RT genes, is both an activator and a repressor of transcription.";
RL Mol. Cell. Biol. 16:6419-6426(1996).
RN [6]
RP FUNCTION, DNA-BINDING, AND PHOSPHORYLATION.
RX PubMed=12861007; DOI=10.1128/mcb.23.15.5208-5216.2003;
RA Kim J.H., Polish J., Johnston M.;
RT "Specificity and regulation of DNA binding by the yeast glucose transporter
RT gene repressor Rgt1.";
RL Mol. Cell. Biol. 23:5208-5216(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-229, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-229 AND SER-410, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-205; SER-208;
RP SER-229; SER-283; SER-284; SER-410; SER-414 AND SER-1130, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(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. Binds the consensus binding site sequence 5'-CGGANNA-3',
CC of which multiple copies are present in all HXT promoters regulated by
CC RGT1. {ECO:0000269|PubMed:12861007, ECO:0000269|PubMed:1874412,
CC ECO:0000269|PubMed:8887670}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227,
CC ECO:0000269|PubMed:14562095}. Cytoplasm {ECO:0000269|PubMed:14562095}.
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. {ECO:0000269|PubMed:12861007}.
CC -!- MISCELLANEOUS: Present with 195 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the EDS1/RGT1 family. {ECO:0000305}.
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DR EMBL; X69584; CAA49301.1; -; Genomic_DNA.
DR EMBL; Z28038; CAA81873.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09118.1; -; Genomic_DNA.
DR PIR; S30010; S30010.
DR RefSeq; NP_012886.3; NM_001179604.3.
DR AlphaFoldDB; P32862; -.
DR BioGRID; 34094; 126.
DR DIP; DIP-4177N; -.
DR IntAct; P32862; 6.
DR STRING; 4932.YKL038W; -.
DR iPTMnet; P32862; -.
DR MaxQB; P32862; -.
DR PaxDb; P32862; -.
DR PRIDE; P32862; -.
DR EnsemblFungi; YKL038W_mRNA; YKL038W; YKL038W.
DR GeneID; 853828; -.
DR KEGG; sce:YKL038W; -.
DR SGD; S000001521; RGT1.
DR VEuPathDB; FungiDB:YKL038W; -.
DR eggNOG; ENOG502QRVJ; Eukaryota.
DR GeneTree; ENSGT00940000176717; -.
DR HOGENOM; CLU_006525_0_0_1; -.
DR InParanoid; P32862; -.
DR OMA; WFRNSLE; -.
DR BioCyc; YEAST:G3O-31839-MON; -.
DR PRO; PR:P32862; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P32862; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IDA:SGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:CACAO.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IGI:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
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 1: Evidence at protein level;
KW Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Zinc.
FT CHAIN 1..1170
FT /note="Glucose transport transcription regulator RGT1"
FT /id="PRO_0000115001"
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:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
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
