HXT3_YEAST
ID HXT3_YEAST Reviewed; 567 AA.
AC P32466; D6VSX5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Low-affinity glucose transporter HXT3;
GN Name=HXT3; OrderedLocusNames=YDR345C; ORFNames=D9651.14;
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=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 [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 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Low-affinity glucose transporter.
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 -!- MISCELLANEOUS: Present with 37200 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; L07080; AAA34672.1; -; Genomic_DNA.
DR EMBL; U51032; AAB64781.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12185.1; -; Genomic_DNA.
DR PIR; S31294; S31294.
DR RefSeq; NP_010632.1; NM_001180653.1.
DR AlphaFoldDB; P32466; -.
DR SMR; P32466; -.
DR BioGRID; 32401; 85.
DR DIP; DIP-4178N; -.
DR IntAct; P32466; 6.
DR MINT; P32466; -.
DR STRING; 4932.YDR345C; -.
DR iPTMnet; P32466; -.
DR MaxQB; P32466; -.
DR PaxDb; P32466; -.
DR PRIDE; P32466; -.
DR EnsemblFungi; YDR345C_mRNA; YDR345C; YDR345C.
DR GeneID; 851946; -.
DR KEGG; sce:YDR345C; -.
DR SGD; S000002753; HXT3.
DR VEuPathDB; FungiDB:YDR345C; -.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000176280; -.
DR HOGENOM; CLU_001265_30_1_1; -.
DR InParanoid; P32466; -.
DR OMA; MWGCSAV; -.
DR BioCyc; YEAST:G3O-29899-MON; -.
DR PRO; PR:P32466; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P32466; 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; 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: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; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..567
FT /note="Low-affinity glucose transporter HXT3"
FT /id="PRO_0000050393"
FT TOPO_DOM 1..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..113
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..171
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..233
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..354
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..360
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..378
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..428
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..466
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 489..509
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..567
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 567 AA; 62558 MW; F6CA1F7B70204526 CRC64;
MNSTPDLISP QKSSENSNAD LPSNSSQVMN MPEEKGVQDD FQAEADQVLT NPNTGKGAYV
TVSICCVMVA FGGFVFGWDT GTISGFVAQT DFLRRFGMKH KDGSYYLSKV RTGLIVSIFN
IGCAIGGIIL AKLGDMYGRK MGLIVVVVIY IIGIIIQIAS INKWYQYFIG RIISGLGVGG
IAVLSPMLIS EVAPKEMRGT LVSCYQLMIT LGIFLGYCTN FGTKNYSNSV QWRVPLGLCF
AWALFMIGGM TFVPESPRYL VEAGQIDEAR ASLSKVNKVA PDHPFIQQEL EVIEASVEEA
RAAGSASWGE LFTGKPAMFK RTMMGIMIQS LQQLTGDNYF FYYGTTVFNA VGMSDSFETS
IVFGVVNFFS TCCSLYTVDR FGRRNCLLYG AIGMVCCYVV YASVGVTRLW PNGEGNGSSK
GAGNCMIVFA CFYIFCFATT WAPIAYVVIS ETFPLRVKSK AMSIATAANW LWGFLIGFFT
PFITGAINFY YGYVFMGCMV FAYFYVFFFV PETKGLTLEE VNDMYAEGVL PWKSASWVPT
SQRGANYDAD ALMHDDQPFY KKMFGKK
