HXT5_YEAST
ID HXT5_YEAST Reviewed; 592 AA.
AC P38695; D3DL46;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Probable glucose transporter HXT5;
GN Name=HXT5; OrderedLocusNames=YHR096C;
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=MC996;
RA Reifenberger E., Koetter P., Ciriacy M.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-61, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [5]
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 [6]
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 [7]
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: Probable glucose transporter.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
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; X77961; CAA54923.1; -; Genomic_DNA.
DR EMBL; U00060; AAB68934.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06790.1; -; Genomic_DNA.
DR PIR; S43742; S43742.
DR RefSeq; NP_011964.1; NM_001179226.1.
DR AlphaFoldDB; P38695; -.
DR SMR; P38695; -.
DR BioGRID; 36529; 84.
DR DIP; DIP-5594N; -.
DR IntAct; P38695; 23.
DR MINT; P38695; -.
DR STRING; 4932.YHR096C; -.
DR iPTMnet; P38695; -.
DR MaxQB; P38695; -.
DR PaxDb; P38695; -.
DR PRIDE; P38695; -.
DR EnsemblFungi; YHR096C_mRNA; YHR096C; YHR096C.
DR GeneID; 856496; -.
DR KEGG; sce:YHR096C; -.
DR SGD; S000001138; HXT5.
DR VEuPathDB; FungiDB:YHR096C; -.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000176280; -.
DR HOGENOM; CLU_001265_30_1_1; -.
DR InParanoid; P38695; -.
DR OMA; VMVVFAC; -.
DR BioCyc; YEAST:G3O-31141-MON; -.
DR SABIO-RK; P38695; -.
DR PRO; PR:P38695; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38695; 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; HDA: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:0005355; F:glucose transmembrane transporter activity; IDA:SGD.
DR GO; GO:0015578; F:mannose 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:0008645; P:hexose 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; Isopeptide bond; Membrane; Reference proteome; Repeat;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..592
FT /note="Probable glucose transporter HXT5"
FT /id="PRO_0000050395"
FT TOPO_DOM 1..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..137
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..195
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..378
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..384
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..402
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..452
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..490
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..511
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 512
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 513..533
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 534..592
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 61
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:12872131"
SQ SEQUENCE 592 AA; 66251 MW; 6906721BAC1A5F87 CRC64;
MSELENAHQG PLEGSATVST NSNSYNEKSG NSTAPGTAGY NDNLAQAKPV SSYISHEGPP
KDELEELQKE VDKQLEKKSK SDLLFVSVCC LMVAFGGFVF GWDTGTISGF VRQTDFIRRF
GSTRANGTTY LSDVRTGLMV SIFNIGCAIG GIVLSKLGDM YGRKIGLMTV VVIYSIGIII
QIASIDKWYQ YFIGRIISGL GVGGITVLAP MLISEVSPKQ LRGTLVSCYQ LMITFGIFLG
YCTNFGTKNY SNSVQWRVPL GLCFAWSIFM IVGMTFVPES PRYLVEVGKI EEAKRSLARA
NKTTEDSPLV TLEMENYQSS IEAERLAGSA SWGELVTGKP QMFRRTLMGM MIQSLQQLTG
DNYFFYYGTT IFQAVGLEDS FETAIVLGVV NFVSTFFSLY TVDRFGRRNC LLWGCVGMIC
CYVVYASVGV TRLWPNGQDQ PSSKGAGNCM IVFACFYIFC FATTWAPVAY VLISESYPLR
VRGKAMSIAS ACNWIWGFLI SFFTPFITSA INFYYGYVFM GCMVFAYFYV FFFVPETKGL
TLEEVNEMYE ENVLPWKSTK WIPPSRRTTD YDLDATRNDP RPFYKRMFTK EK
