ID   HXT1_YEAST              Reviewed;         570 AA.
AC   P32465; D3DL45;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   10-JUN-2026, entry version 211.
DE   RecName: Full=Low-affinity glucose transporter HXT1;
GN   Name=HXT1; Synonyms=HOR4; OrderedLocusNames=YHR094C;
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].
RX   PubMed=2046678; DOI=10.1128/mcb.11.7.3804-3813.1991;
RA   Lewis D.A., Bisson L.F.;
RT   "The HXT1 gene product of Saccharomyces cerevisiae is a new member of the
RT   family of hexose transporters.";
RL   Mol. Cell. Biol. 11:3804-3813(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8417358; DOI=10.1128/mcb.13.1.638-648.1993;
RA   Ko C.H., Liang H., Gaber R.F.;
RT   "Roles of multiple glucose transporters in Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 13:638-648(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [4]
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   [5]
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   [6]
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND SER-44, AND
RP   IDENTIFICATION BY 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   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY
RP   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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND SER-44, 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: Low-affinity glucose transporter. HXT1 is as well involved in
CC       the transport of mannose.
CC   -!- INTERACTION:
CC       P32465; P33302: PDR5; NbExp=3; IntAct=EBI-8759, EBI-13038;
CC       P32465; P32568: SNQ2; NbExp=3; IntAct=EBI-8759, EBI-17590;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- DEVELOPMENTAL STAGE: Expression is maximal during lag and early
CC       exponential phases of growth, decreasing upon further entry into
CC       exponential growth.
CC   -!- INDUCTION: Repressed at high glucose concentrations.
CC   -!- MISCELLANEOUS: Glucose transport is thought to be mediated by two
CC       kinetically distinct systems, a glucose-repressible high-affinity
CC       system and a constitutive low-affinity system.
CC   -!- MISCELLANEOUS: Present with 23300 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
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; L07079; AAB59311.1; -; Genomic_DNA.
DR   EMBL; M82963; AAA34700.1; -; Genomic_DNA.
DR   EMBL; U00060; AAB68933.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06789.1; -; Genomic_DNA.
DR   PIR; S38798; S38798.
DR   RefSeq; NP_011962.1; NM_001179224.1.
DR   AlphaFoldDB; P32465; -.
DR   SMR; P32465; -.
DR   BioGRID; 36528; 137.
DR   DIP; DIP-5593N; -.
DR   FunCoup; P32465; 1541.
DR   IntAct; P32465; 43.
DR   MINT; P32465; -.
DR   STRING; 4932.YHR094C; -.
DR   TCDB; 2.A.1.1.108; the major facilitator superfamily (mfs).
DR   GlyCosmos; P32465; 1 site, No reported glycans.
DR   GlyGen; P32465; 2 sites.
DR   iPTMnet; P32465; -.
DR   PaxDb; 4932-YHR094C; -.
DR   PeptideAtlas; P32465; -.
DR   EnsemblFungi; YHR094C_mRNA; YHR094C; YHR094C.
DR   GeneID; 856494; -.
DR   KEGG; sce:YHR094C; -.
DR   AGR; SGD:S000001136; -.
DR   SGD; S000001136; HXT1.
DR   VEuPathDB; FungiDB:YHR094C; -.
DR   eggNOG; KOG0254; Eukaryota.
DR   HOGENOM; CLU_001265_30_1_1; -.
DR   InParanoid; P32465; -.
DR   OMA; INNMACP; -.
DR   OrthoDB; 5141738at2759; -.
DR   BioCyc; MetaCyc:G3O-31140-MONOMER; -.
DR   BioCyc; YEAST:G3O-31140-MONOMER; -.
DR   BioGRID-ORCS; 856494; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P32465; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P32465; protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0005351; F:carbohydrate:proton symporter activity; IBA:GO_Central.
DR   GO; GO:0055056; F:D-glucose transmembrane transporter activity; TAS:SGD.
DR   GO; GO:0005353; F:fructose transmembrane transporter activity; IMP:SGD.
DR   GO; GO:0005354; F:galactose transmembrane transporter activity; TAS:SGD.
DR   GO; GO:0015578; F:mannose transmembrane transporter activity; TAS:SGD.
DR   GO; GO:0015146; F:pentose transmembrane transporter activity; IMP:SGD.
DR   GO; GO:0008643; P:carbohydrate transport; IBA:GO_Central.
DR   GO; GO:1904659; P:D-glucose transmembrane transport; IMP:SGD.
DR   GO; GO:0015761; P:mannose transmembrane transport; IMP:SGD.
DR   CDD; cd17356; MFS_HXT; 1.
DR   FunFam; 1.20.1250.20:FF:000044; Hexose transporter Hxt3p; 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; IPR050360; MFS_Sugar_Transporters.
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:SF75; GALACTOSE TRANSPORTER-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   Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW   Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..570
FT                   /note="Low-affinity glucose transporter HXT1"
FT                   /id="PRO_0000050391"
FT   TOPO_DOM        1..60
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        82..116
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..143
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        165..174
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        196..201
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        223..236
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        237..257
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        258..340
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        341..357
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        358..363
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        364..381
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        382..388
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        389..409
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        410..431
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        432..452
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        453..469
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        470..490
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        491
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        492..512
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        513..570
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         38
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         44
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        70
FT                   /note="Missing (in Ref. 1; AAA34700)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        469
FT                   /note="S -> T (in Ref. 1; AAA34700)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   570 AA;  63261 MW;  311CBB35AE80D19E CRC64;
     MNSTPDLISP QKSNSSNSYE LESGRSKAMN TPEGKNESFH DNLSESQVQP AVAPPNTGKG
     VYVTVSICCV MVAFGGFIFG WDTGTISGFV AQTDFLRRFG MKHHDGSHYL SKVRTGLIVS
     IFNIGCAIGG IVLAKLGDMY GRRIGLIVVV VIYTIGIIIQ IASINKWYQY FIGRIISGLG
     VGGITVLSPM LISEVAPSEM RGTLVSCYQV MITLGIFLGY CTNFGTKNYS NSVQWRVPLG
     LCFAWALFMI GGMMFVPESP RYLVEAGRID EARASLAKVN KCPPDHPYIQ YELETIEASV
     EEMRAAGTAS WGELFTGKPA MFQRTMMGIM IQSLQQLTGD NYFFYYGTIV FQAVGLSDSF
     ETSIVFGVVN FFSTCCSLYT VDRFGRRNCL MWGAVGMVCC YVVYASVGVT RLWPNGQDQP
     SSKGAGNCMI VFACFYIFCF ATTWAPIAYV VISECFPLRV KSKCMSIASA ANWIWGFLIS
     FFTPFITGAI NFYYGYVFMG CMVFAYFYVF FFVPETKGLS LEEVNDMYAE GVLPWKSASW
     VPVSKRGADY NADDLMHDDQ PFYKSLFSRK
//