HXT1_YEAST
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 03-AUG-2022, entry version 196.
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 -!- 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; 128.
DR DIP; DIP-5593N; -.
DR IntAct; P32465; 38.
DR MINT; P32465; -.
DR STRING; 4932.YHR094C; -.
DR TCDB; 2.A.1.1.108; the major facilitator superfamily (mfs).
DR iPTMnet; P32465; -.
DR MaxQB; P32465; -.
DR PaxDb; P32465; -.
DR PRIDE; P32465; -.
DR EnsemblFungi; YHR094C_mRNA; YHR094C; YHR094C.
DR GeneID; 856494; -.
DR KEGG; sce:YHR094C; -.
DR SGD; S000001136; HXT1.
DR VEuPathDB; FungiDB:YHR094C; -.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000176280; -.
DR HOGENOM; CLU_001265_30_1_1; -.
DR InParanoid; P32465; -.
DR OMA; FWNIIFC; -.
DR BioCyc; MetaCyc:G3O-31140-MON; -.
DR BioCyc; YEAST:G3O-31140-MON; -.
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: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; IDA:SGD.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; IBA:GO_Central.
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:0005355; F:glucose 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:glucose transmembrane transport; IMP:SGD.
DR GO; GO:0015761; P:mannose transmembrane transport; 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; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
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 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 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
