GHT3_SCHPO
ID GHT3_SCHPO Reviewed; 555 AA.
AC Q92339;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 145.
DE RecName: Full=High-affinity gluconate transporter ght3;
DE AltName: Full=Hexose transporter 3;
GN Name=ght3; ORFNames=SPAC1F8.01;
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 [GENOMIC DNA].
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).
CC -!- FUNCTION: High-affinity gluconate 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; AF051139; AAC63975.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB03595.1; -; Genomic_DNA.
DR PIR; T38108; T38108.
DR RefSeq; NP_592790.1; NM_001018190.2.
DR AlphaFoldDB; Q92339; -.
DR SMR; Q92339; -.
DR STRING; 4896.SPAC1F8.01.1; -.
DR TCDB; 2.A.1.1.23; the major facilitator superfamily (mfs).
DR iPTMnet; Q92339; -.
DR PaxDb; Q92339; -.
DR EnsemblFungi; SPAC1F8.01.1; SPAC1F8.01.1:pep; SPAC1F8.01.
DR GeneID; 2541758; -.
DR KEGG; spo:SPAC1F8.01; -.
DR PomBase; SPAC1F8.01; ght3.
DR VEuPathDB; FungiDB:SPAC1F8.01; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_001265_30_1_1; -.
DR InParanoid; Q92339; -.
DR OMA; YCISIGA; -.
DR PhylomeDB; Q92339; -.
DR PRO; PR:Q92339; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS: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:0015128; F:gluconate transmembrane transporter activity; IMP:PomBase.
DR GO; GO:0008643; P:carbohydrate transport; IBA:GO_Central.
DR GO; GO:0035429; P:gluconate transmembrane transport; 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.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Reference proteome; Repeat; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..555
FT /note="High-affinity gluconate transporter ght3"
FT /id="PRO_0000050411"
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..555
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 492..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 555 AA; 62095 MW; 30DFF04294D318DB CRC64;
MNRFITSILV VFISMSGWLQ GADTGSISGI LGMRDFQSRF ADRYNPISNS YSYSAWRQAL
LTGTINAGCL FGAMLSSPFT ERIGKKYSIC FFSGVYIIAE LLLVTAVPSW IQVLVGKILA
GVGIGALSVL SPGYQSEVAP PQIRGAVVAT YQIFSTGAAL VAACINMGTH KLRKTASWRT
SFGINMLWGI LLMVGVLFLP ESPRYLIYKG RDEEALRIMC NMAELSPESE IIQTNFNTIK
SDIEIEMAGG KARWIEIFGK DIRYRTCLGF LVMLFRELIG NNYYFYYATQ VFKGTGMTDI
FLPAVILGAI NFGTTFGALY TIDNLGRRNP LIFGAAFQSI CFFIYAAVGD RKLIYKNGTS
DHRAGSVMIV FSCLFLFSYC CSWGPMGWVI VGETFPIRYR SKCASVATSG NWLGNFMISF
FTPFINNAIG FKLGYIYACI NLFSSFMIFF LAKETKGLTL EEVNDLYMSN IKPWESYKYV
REIESHRIHF SKEEEKRERE KSKGIRGQEE EFIENADEDN NDSSSSSGSV VSAVKPRRSA
VSNDRFSEDS HPTYI
