GHT5_SCHPO
ID GHT5_SCHPO Reviewed; 546 AA.
AC P78831;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=High-affinity glucose transporter ght5;
DE AltName: Full=Hexose transporter 5;
GN Name=ght5; ORFNames=SPCC1235.14;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=10735857; DOI=10.1128/jb.182.8.2153-2162.2000;
RA Heiland S., Radovanovic N., Hoefer M., Winderickx J., Lichtenberg H.;
RT "Multiple hexose transporters of Schizosaccharomyces pombe.";
RL J. Bacteriol. 182:2153-2162(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 176-546.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-537, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: High-affinity glucose transporter.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
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; AF051141; AAC63977.1; -; mRNA.
DR EMBL; CU329672; CAA21118.1; -; Genomic_DNA.
DR EMBL; D89179; BAA13841.1; -; mRNA.
DR PIR; T40888; T40888.
DR PIR; T42623; T42623.
DR RefSeq; NP_587740.1; NM_001022735.2.
DR AlphaFoldDB; P78831; -.
DR SMR; P78831; -.
DR BioGRID; 275810; 2.
DR STRING; 4896.SPCC1235.14.1; -.
DR iPTMnet; P78831; -.
DR SwissPalm; P78831; -.
DR MaxQB; P78831; -.
DR PaxDb; P78831; -.
DR PRIDE; P78831; -.
DR EnsemblFungi; SPCC1235.14.1; SPCC1235.14.1:pep; SPCC1235.14.
DR GeneID; 2539240; -.
DR KEGG; spo:SPCC1235.14; -.
DR PomBase; SPCC1235.14; ght5.
DR VEuPathDB; FungiDB:SPCC1235.14; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_001265_30_1_1; -.
DR InParanoid; P78831; -.
DR OMA; MYQSEST; -.
DR PhylomeDB; P78831; -.
DR PRO; PR:P78831; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000328; C:fungal-type vacuole lumen; IDA:PomBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IC:PomBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0031520; C:plasma membrane of cell tip; IDA:PomBase.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; IBA:GO_Central.
DR GO; GO:0140108; F:high-affinity glucose transmembrane transporter activity; IMP:PomBase.
DR GO; GO:0008643; P:carbohydrate transport; IBA:GO_Central.
DR GO; GO:0098708; P:glucose import across plasma membrane; IMP:PomBase.
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.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..546
FT /note="High-affinity glucose transporter ght5"
FT /id="PRO_0000050413"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..58
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..112
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..179
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..285
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..301
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..328
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..363
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 385..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..432
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..546
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 486..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 546 AA; 60320 MW; D9B4947CFE2889D7 CRC64;
MGKNLTIVML VFVSMAGWMF GADTGSIGGI TNMRDFQSRF ADRYNPVTDS YSYSSARQGL
ITGMVNVGSF FGCFLSSPLM DRIGKRTSIM FWTIVYLIGI ILQVTAVPSW VQIMVAKIWT
GLSIGALSVL APGFQSEVAP ADLRGTIVTT YQLAVTGGIF IAACINMGTH KLHKTAQWRV
SMGINLLWGI ITFIGISFLP ESPRYLISVG RDEEALQIMA KNNDLPIEHE VIQTEYHVIK
SDCEAELAGG PATWPEIFGP DIRYRTFLGL GVMSLQQLTG DNYYFYYGFE VFEGTGMNSP
YLSALILDAV NFGCTFGGLF VLEFFGRRMP LIIGALWQSI TFFIYAAVGN RALTRKNGTS
NHRAGAVMIV FSCLFIFSFA QTWGPAAYVI VGESYPIRYR SKCAAVATTG NWLWGFLISF
FTPFITNSIG FKYGYIFAAC NLCAACIIFL FAHETKGLTL EEINELYISG AKPWMPRPKN
LGNFTKQQEE VREKSRGVQG ESAAHLENVD GEEGIEDSSN DISSTTSSDG RAKPESSYHD
QEEQFA
