HXT7_YEAST
ID HXT7_YEAST Reviewed; 570 AA.
AC P39004; D6VSX3;
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=High-affinity hexose transporter HXT7;
GN Name=HXT7; OrderedLocusNames=YDR342C; ORFNames=D9651.11;
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;
RX PubMed=7651133; DOI=10.1111/j.1365-2958.1995.tb02400.x;
RA Reifenberger E., Ciriacy M.;
RT "Identification of novel HXT genes in Saccharomyces cerevisiae reveals the
RT impact of individual hexose transporters on glycolytic flux.";
RL Mol. Microbiol. 16:157-167(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 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 [5]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-560, AND IDENTIFICATION BY
RP MASS 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 [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 THR-556, AND IDENTIFICATION BY
RP 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: High-affinity glucose transporter.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: Present with 7350 molecules/cell in log phase SD medium.
CC {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; Z31692; CAA83497.1; -; Genomic_DNA.
DR EMBL; U51032; AAB64778.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12183.1; -; Genomic_DNA.
DR PIR; S43186; S43186.
DR RefSeq; NP_010629.3; NM_001180650.3.
DR AlphaFoldDB; P39004; -.
DR SMR; P39004; -.
DR BioGRID; 32399; 63.
DR DIP; DIP-5182N; -.
DR IntAct; P39004; 31.
DR MINT; P39004; -.
DR STRING; 4932.YDR342C; -.
DR TCDB; 2.A.1.1.31; the major facilitator superfamily (mfs).
DR iPTMnet; P39004; -.
DR MaxQB; P39004; -.
DR PaxDb; P39004; -.
DR PRIDE; P39004; -.
DR EnsemblFungi; YDR342C_mRNA; YDR342C; YDR342C.
DR GeneID; 851943; -.
DR KEGG; sce:YDR342C; -.
DR SGD; S000002750; HXT7.
DR VEuPathDB; FungiDB:YDR342C; -.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000176280; -.
DR HOGENOM; CLU_001265_30_1_1; -.
DR InParanoid; P39004; -.
DR OMA; MYQSEST; -.
DR BioCyc; YEAST:G3O-29897-MON; -.
DR PRO; PR:P39004; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P39004; 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:0005739; C:mitochondrion; 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; IDA:SGD.
DR GO; GO:0008645; P:hexose transmembrane transport; TAS:SGD.
DR GO; GO:0055085; P:transmembrane transport; TAS: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; Phosphoprotein;
KW Reference proteome; Repeat; Sugar transport; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..570
FT /note="High-affinity hexose transporter HXT7"
FT /id="PRO_0000050397"
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 MOD_RES 556
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 560
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:12872131"
SQ SEQUENCE 570 AA; 62735 MW; 251A2CF0F0FEB75C CRC64;
MSQDAAIAEQ TPVEHLSAVD SASHSVLSTP SNKAERDEIK AYGEGEEHEP VVEIPKRPAS
AYVTVSIMCI MIAFGGFVFG WDTGTISGFI NQTDFIRRFG MKHKDGTNYL SKVRTGLIVS
IFNIGCAIGG IILSKLGDMY GRKVGLIVVV VIYIIGIIIQ IASINKWYQY FIGRIISGLG
VGGIAVLSPM LISEVSPKHL RGTLVSCYQL MITAGIFLGY CTNFGTKNYS NSVQWRVPLG
LCFAWALFMI GGMTFVPESP RYLAEVGKIE EAKRSIAVSN KVAVDDPSVL AEVEAVLAGV
EAEKLAGNAS WGELFSSKTK VLQRLIMGAM IQSLQQLTGD NYFFYYGTTI FKAVGLSDSF
ETSIVLGIVN FASTFVGIYV VERYGRRTCL LWGAASMTAC MVVYASVGVT RLWPNGQDQP
SSKGAGNCMI VFACFYIFCF ATTWAPIPYV VVSETFPLRV KSKAMSIATA ANWLWGFLIG
FFTPFITGAI NFYYGYVFMG CLVFMFFYVL LVVPETKGLT LEEVNTMWEE GVLPWKSASW
VPPSRRGANY DAEEMTHDDK PLYKRMFSTK
