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   27-MAR-2024, entry version 185.
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};
GN   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   GlyCosmos; Q12300; 2 sites, No reported glycans.
DR   GlyGen; Q12300; 2 sites.
DR   PaxDb; 4932-YDL138W; -.
DR   PeptideAtlas; Q12300; -.
DR   EnsemblFungi; YDL138W_mRNA; YDL138W; YDL138W.
DR   GeneID; 851417; -.
DR   KEGG; sce:YDL138W; -.
DR   AGR; SGD:S000002297; -.
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; AVCQGTR; -.
DR   OrthoDB; 1058279at2759; -.
DR   BioCyc; YEAST:G3O-29537-MONOMER; -.
DR   BioGRID-ORCS; 851417; 0 hits in 10 CRISPR screens.
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: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:0010255; P:glucose mediated signaling pathway; IMP:SGD.
DR   CDD; cd17356; MFS_HXT; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR005828; MFS_sugar_transport-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR003663; Sugar/inositol_transpt.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   NCBIfam; TIGR00879; SP; 1.
DR   PANTHER; PTHR48022:SF17; HIGH GLUCOSE SENSOR RGT2-RELATED; 1.
DR   PANTHER; PTHR48022; PLASTIDIC GLUCOSE TRANSPORTER 4; 1.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   PRINTS; PR00171; SUGRTRNSPORT.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 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
FT                   Yck-dependent phosphorylation, interaction with MTH1 and
FT                   STD1, 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
//