RGT2_YEAST
ID RGT2_YEAST Reviewed; 763 AA.
AC Q12300; D6VRL0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=High glucose sensor RGT2 {ECO:0000303|PubMed:8901598};
DE AltName: Full=Low-affinity glucose receptor RGT2 {ECO:0000303|PubMed:9564039};
DE AltName: Full=Low-affinity transporter-like sensor RGT2 {ECO:0000305};
DE AltName: Full=Restores glucose transport protein 2 {ECO:0000303|PubMed:1874412};
GN Name=RGT2 {ECO:0000303|PubMed:1874412};
GN OrderedLocusNames=YDL138W {ECO:0000312|SGD:S000002297}; ORFNames=D2160;
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 96604 / S288c / FY1679;
RX PubMed=8972577;
RX DOI=10.1002/(sici)1097-0061(199612)12:15<1549::aid-yea42>3.0.co;2-s;
RA Woelfl S., Haneman V., Saluz H.P.;
RT "Analysis of a 26,756 bp segment from the left arm of yeast chromosome
RT IV.";
RL Yeast 12:1549-1554(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
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 GENE NAME.
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, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-231.
RX PubMed=8901598; DOI=10.1073/pnas.93.22.12428;
RA Oezcan S., Dover J., Rosenwald A.G., Woelfl S., Johnston M.;
RT "Two glucose transporters in Saccharomyces cerevisiae are glucose sensors
RT that generate a signal for induction of gene expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:12428-12432(1996).
RN [6]
RP FUNCTION.
RX PubMed=9564039; DOI=10.1093/emboj/17.9.2566;
RA Ozcan S., Dover J., Johnston M.;
RT "Glucose sensing and signaling by two glucose receptors in the yeast
RT Saccharomyces cerevisiae.";
RL EMBO J. 17:2566-2573(1998).
RN [7]
RP FUNCTION, AND INTERACTION WITH YCK1; MTH1 AND STD1.
RX PubMed=14755054; DOI=10.1073/pnas.0305901101;
RA Moriya H., Johnston M.;
RT "Glucose sensing and signaling in Saccharomyces cerevisiae through the Rgt2
RT glucose sensor and casein kinase I.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:1572-1577(2004).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [9]
RP FUNCTION, INTERACTION WITH MTH1 AND STD1, AND MUTAGENESIS OF
RP 684-SER--THR-690.
RX PubMed=27630263; DOI=10.1091/mbc.e16-05-0342;
RA Snowdon C., Johnston M.;
RT "A novel role for yeast casein kinases in glucose sensing and signaling.";
RL Mol. Biol. Cell 27:3369-3375(2016).
CC -!- FUNCTION: Low-affinity high glucose sensor that is part of the
CC sensor/receptor-repressor (SSR) glucose-signaling pathway, which
CC detects extracellular glucose and induces expression of glucose
CC transporters that bring glucose into the cell (PubMed:9564039,
CC PubMed:14755054, PubMed:27630263). The transporter-like sensor
CC generates an intracellular signal in the presence of high levels of
CC glucose to promote high glucose-induced expression of HXT1
CC (PubMed:9564039). Binding of glucose to the RGT2 transmembrane domain
CC activates a downstream signaling cascade, leading to phosphorylation of
CC the RGT1 corepressors MTH1 and STD1, targeting them for SCF(Grr1)-
CC dependent ubiquitination and degradation. Depletion of the corepressors
CC robs RGT1 of its ability to repress expression of HXT genes, leading to
CC accumulation of glucose transporters in the plasma membrane
CC (PubMed:8901598, PubMed:27630263). Even though RGT2 is similar to
CC glucose transporters, it appears to be unable to transport glucose
CC (PubMed:9564039). {ECO:0000269|PubMed:14755054,
CC ECO:0000269|PubMed:27630263, ECO:0000269|PubMed:8901598,
CC ECO:0000269|PubMed:9564039}.
CC -!- SUBUNIT: Interacts with YCK1 (PubMed:14755054). Interacts with MTH1 and
CC STD1 (PubMed:27630263). {ECO:0000269|PubMed:14755054,
CC ECO:0000269|PubMed:27630263}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8901598};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- PTM: Phosphorylated in the C-terminal tail on Yck consensus sites in a
CC yeast casein kinases YCK1 and YCK2 (Yck)-dependent manner. This
CC phosphorylation is required for interaction with HXT corepressors MTH1
CC and STD1 and ultimately HXT expression. {ECO:0000269|PubMed:27630263}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR EMBL; X96876; CAA65621.1; -; Genomic_DNA.
DR EMBL; Z74186; CAA98711.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11720.1; -; Genomic_DNA.
DR PIR; S67684; S67684.
DR RefSeq; NP_010143.1; NM_001180198.1.
DR AlphaFoldDB; Q12300; -.
DR SMR; Q12300; -.
DR BioGRID; 31923; 182.
DR DIP; DIP-2865N; -.
DR IntAct; Q12300; 20.
DR MINT; Q12300; -.
DR STRING; 4932.YDL138W; -.
DR TCDB; 2.A.1.1.19; the major facilitator superfamily (mfs).
DR PaxDb; Q12300; -.
DR EnsemblFungi; YDL138W_mRNA; YDL138W; YDL138W.
DR GeneID; 851417; -.
DR KEGG; sce:YDL138W; -.
DR SGD; S000002297; RGT2.
DR VEuPathDB; FungiDB:YDL138W; -.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000176821; -.
DR HOGENOM; CLU_001265_42_0_1; -.
DR InParanoid; Q12300; -.
DR OMA; ANYDYEM; -.
DR BioCyc; YEAST:G3O-29537-MON; -.
DR PRO; PR:Q12300; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12300; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IMP:SGD.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; IBA:GO_Central.
DR GO; GO:0008643; P:carbohydrate transport; IBA:GO_Central.
DR GO; GO:0051594; P:detection of glucose; IMP:SGD.
DR GO; GO:0010255; P:glucose mediated signaling pathway; IMP:SGD.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR037792; Rgt2/Snf3.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR PANTHER; PTHR48022:SF16; PTHR48022:SF16; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00879; SP; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..763
FT /note="High glucose sensor RGT2"
FT /id="PRO_0000050389"
FT TOPO_DOM 1..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 100..120
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..144
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 145..165
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 176..196
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 198..218
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 232..252
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..266
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 267..287
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 358..378
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..393
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 394..414
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 422..442
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..452
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 453..473
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 492..512
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 513..524
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 525..545
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 546..763
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 231
FT /note="R->K: In RGT2-1; constitutively signaling glucose
FT receptor."
FT /evidence="ECO:0000269|PubMed:8901598"
FT MUTAGEN 684..690
FT /note="SIISDST->AIIADAA: In Rgt2(4SA); Abolishes Yck-
FT dependent phosphorylation, interaction with MTH1 and STD1,
FT and glucose signaling, but does not affect protein
FT stability."
FT /evidence="ECO:0000269|PubMed:27630263"
SQ SEQUENCE 763 AA; 83159 MW; DF6E2F1C337F106E CRC64;
MNDSQNCLRQ REENSHLNPG NDFGHHQGAE CTINHNNMPH RNAYTESTND TEAKSIVMCD
DPNAYQISYT NNEPAGDGAI ETTSILLSQP LPLRSNVMSV LVGIFVAVGG FLFGYDTGLI
NSITDMPYVK TYIAPNHSYF TTSQIAILVS FLSLGTFFGA LIAPYISDSY GRKPTIMFST
AVIFSIGNSL QVASGGLVLL IVGRVISGIG IGIISAVVPL YQAEAAQKNL RGAIISSYQW
AITIGLLVSS AVSQGTHSKN GPSSYRIPIG LQYVWSSILA VGMIFLPESP RYYVLKDELN
KAAKSLSFLR GLPIEDPRLL EELVEIKATY DYEASFGPST LLDCFKTSEN RPKQILRIFT
GIAIQAFQQA SGINFIFYYG VNFFNNTGVD NSYLVSFISY AVNVAFSIPG MYLVDRIGRR
PVLLAGGVIM AIANLVIAIV GVSEGKTVVA SKIMIAFICL FIAAFSATWG GVVWVVSAEL
YPLGVRSKCT AICAAANWLV NFTCALITPY IVDVGSHTSS MGPKIFFIWG GLNVVAVIVV
YFAVYETRGL TLEEIDELFR KAPNSVISSK WNKKIRKRCL AFPISQQIEM KTNIKNAGKL
DNNNSPIVQD DSHNIIDVDG FLENQIQSND HMIAADKGSG SLVNIIDTAP LTSTEFKPVE
HPPVNYVDLG NGLGLNTYNR GPPSIISDST DEFYEENDSS YYNNNTERNG ANSVNTYMAQ
LINSSSTTSN DTSFSPSHNS NARTSSNWTS DLASKHSQYT SPQ
