ID   HXT2_YEAST              Reviewed;         541 AA.
AC   P23585; D6VZI5;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   27-MAR-2024, entry version 198.
DE   RecName: Full=High-affinity glucose transporter HXT2;
GN   Name=HXT2; OrderedLocusNames=YMR011W; ORFNames=YM8270.15;
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=2233722; DOI=10.1128/mcb.10.11.5903-5913.1990;
RA   Kruckeberg A.L., Bisson L.F.;
RT   "The HXT2 gene of Saccharomyces cerevisiae is required for high-affinity
RT   glucose transport.";
RL   Mol. Cell. Biol. 10:5903-5913(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(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   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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-13; SER-17; SER-20;
RP   THR-29 AND SER-32, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-29, 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-20; THR-29 AND
RP   SER-32, AND 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).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: High-affinity glucose transporter. Is only indispensable for
CC       growth on low glucose-containing media, because S.cerevisiae possesses
CC       other sugar transporters.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
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   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC       transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR   EMBL; M33270; AAA34701.1; -; Genomic_DNA.
DR   EMBL; Z48613; CAA88528.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09909.1; -; Genomic_DNA.
DR   PIR; A36380; MMBYH2.
DR   RefSeq; NP_013724.1; NM_001182507.1.
DR   AlphaFoldDB; P23585; -.
DR   SMR; P23585; -.
DR   BioGRID; 35180; 136.
DR   DIP; DIP-7912N; -.
DR   IntAct; P23585; 6.
DR   MINT; P23585; -.
DR   STRING; 4932.YMR011W; -.
DR   TCDB; 2.A.1.1.111; the major facilitator superfamily (mfs).
DR   GlyCosmos; P23585; 1 site, No reported glycans.
DR   GlyGen; P23585; 1 site.
DR   iPTMnet; P23585; -.
DR   MaxQB; P23585; -.
DR   PaxDb; 4932-YMR011W; -.
DR   PeptideAtlas; P23585; -.
DR   TopDownProteomics; P23585; -.
DR   EnsemblFungi; YMR011W_mRNA; YMR011W; YMR011W.
DR   GeneID; 855023; -.
DR   KEGG; sce:YMR011W; -.
DR   AGR; SGD:S000004613; -.
DR   SGD; S000004613; HXT2.
DR   VEuPathDB; FungiDB:YMR011W; -.
DR   eggNOG; KOG0254; Eukaryota.
DR   GeneTree; ENSGT00940000176280; -.
DR   HOGENOM; CLU_001265_30_1_1; -.
DR   InParanoid; P23585; -.
DR   OMA; YTLGTKH; -.
DR   OrthoDB; 1058279at2759; -.
DR   BioCyc; YEAST:G3O-32719-MONOMER; -.
DR   BioGRID-ORCS; 855023; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P23585; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P23585; Protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0000324; C:fungal-type vacuole; 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:0005353; F:fructose transmembrane transporter activity; TAS:SGD.
DR   GO; GO:0005355; F:glucose transmembrane transporter activity; IDA: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   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: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   Acetylation; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW   Repeat; Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..541
FT                   /note="High-affinity glucose transporter HXT2"
FT                   /id="PRO_0000050392"
FT   TOPO_DOM        2..49
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        71..107
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        129..134
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        135..155
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        156..162
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        184..192
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        214..227
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        249..327
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        328..347
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        348..350
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        351..371
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        372..379
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        401..418
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        419..439
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        440..456
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        457..477
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        478..484
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        485..505
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        506..541
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         20
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         29
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         32
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         266
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         539
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   541 AA;  59841 MW;  6AEFEC0A87391CA7 CRC64;
     MSEFATSRVE SGSQQTSIHS TPIVQKLETD ESPIQTKSEY TNAELPAKPI AAYWTVICLC
     LMIAFGGFVF GWDTGTISGF VNQTDFKRRF GQMKSDGTYY LSDVRTGLIV GIFNIGCAFG
     GLTLGRLGDM YGRRIGLMCV VLVYIVGIVI QIASSDKWYQ YFIGRIISGM GVGGIAVLSP
     TLISETAPKH IRGTCVSFYQ LMITLGIFLG YCTNYGTKDY SNSVQWRVPL GLNFAFAIFM
     IAGMLMVPES PRFLVEKGRY EDAKRSLAKS NKVTIEDPSI VAEMDTIMAN VETERLAGNA
     SWGELFSNKG AILPRVIMGI MIQSLQQLTG NNYFFYYGTT IFNAVGMKDS FQTSIVLGIV
     NFASTFVALY TVDKFGRRKC LLGGSASMAI CFVIFSTVGV TSLYPNGKDQ PSSKAAGNVM
     IVFTCLFIFF FAISWAPIAY VIVAESYPLR VKNRAMAIAV GANWIWGFLI GFFTPFITSA
     IGFSYGYVFM GCLVFSFFYV FFFVCETKGL TLEEVNEMYV EGVKPWKSGS WISKEKRVSE
     E
//