HXT2_YEAST
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 03-AUG-2022, entry version 191.
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; 122.
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 iPTMnet; P23585; -.
DR MaxQB; P23585; -.
DR PaxDb; P23585; -.
DR PRIDE; P23585; -.
DR TopDownProteomics; P23585; -.
DR EnsemblFungi; YMR011W_mRNA; YMR011W; YMR011W.
DR GeneID; 855023; -.
DR KEGG; sce:YMR011W; -.
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; YQIAVGR; -.
DR BioCyc; YEAST:G3O-32719-MON; -.
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: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; 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 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 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
