GHT6_SCHPO
ID GHT6_SCHPO Reviewed; 535 AA.
AC O74849; Q96TK9;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=High-affinity fructose transporter ght6;
DE AltName: Full=Hexose transporter 6;
DE AltName: Full=Meiotic expression up-regulated protein 12;
GN Name=ght6; Synonyms=meu12; ORFNames=SPCC1235.13;
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], 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 [MRNA] OF 478-535.
RC STRAIN=CD16-1;
RX PubMed=11376151; DOI=10.1093/nar/29.11.2327;
RA Watanabe T., Miyashita K., Saito T.T., Yoneki T., Kakihara Y.,
RA Nabeshima K., Kishi Y.A., Shimoda C., Nojima H.;
RT "Comprehensive isolation of meiosis-specific genes identifies novel
RT proteins and unusual non-coding transcripts in Schizosaccharomyces pombe.";
RL Nucleic Acids Res. 29:2327-2337(2001).
CC -!- FUNCTION: High-affinity fructose 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; AF098076; AAC64976.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA21117.1; -; Genomic_DNA.
DR EMBL; AB054532; BAB60886.1; -; mRNA.
DR PIR; T40887; T40887.
DR RefSeq; NP_587739.1; NM_001022734.2.
DR AlphaFoldDB; O74849; -.
DR SMR; O74849; -.
DR BioGRID; 275426; 14.
DR STRING; 4896.SPCC1235.13.1; -.
DR TCDB; 2.A.1.1.22; the major facilitator superfamily (mfs).
DR PaxDb; O74849; -.
DR EnsemblFungi; SPCC1235.13.1; SPCC1235.13.1:pep; SPCC1235.13.
DR GeneID; 2538845; -.
DR KEGG; spo:SPCC1235.13; -.
DR PomBase; SPCC1235.13; ght6.
DR VEuPathDB; FungiDB:SPCC1235.13; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_001265_30_1_1; -.
DR InParanoid; O74849; -.
DR OMA; VMVVFAC; -.
DR PhylomeDB; O74849; -.
DR PRO; PR:O74849; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0000324; C:fungal-type vacuole; 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:0005351; F:carbohydrate:proton symporter activity; IBA:GO_Central.
DR GO; GO:0008643; P:carbohydrate transport; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
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; Meiosis; Membrane; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..535
FT /note="High-affinity fructose transporter ght6"
FT /id="PRO_0000050414"
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..181
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..287
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..303
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..365
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..434
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 456..535
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 483..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 535 AA; 59404 MW; FECBDB9A4E51E844 CRC64;
MAKILTIVML VFVSMAGWMF GADTGSIGGI TNMRDFQSRY ADRYDPVTDT YSYSSARQGL
LVGMVNTGTT VGCLLSSPLG DRFGKRKCIM GWTLVYITGV IVQLTTIPSW VQMMVAKIWT
GLGIGALSVI APGYQSESSP PHIRGAIVTT YQLFITLGIF IAACINMGTH KYTTHPEAQW
RVPIGINLLW GILMFFGMLF LPESPRYLAV KGRNEECMKI LTRNAGLPAD HPIMQKEYNA
IQADVEAELA GGPCSWPQIF SNEIRYRTLL GMGVMAFQQL TGNNYFFYYG TQVFRGTGLN
SPFLAALILD AVNFGCTFGA IFVLEYFGRR GPLIVGGVWQ SICFFIYASV GDRALTRPNG
TSNHRAGAVM IVFSCLFIFS FAQTWAPAAY VIVGESYPIR YRSKCAAVAT ASNWFWNFMI
SFFTPFISNS IGFKYGYVFA ACNLCAAIII FLFAKETKGL TLEEINQLYL SNIKPWNTGA
YQRDREDIKQ SDSEKERGPT SKLHEYVEHA PNSYASTHST ESENYPQQVT NPVGL
