GHT2_SCHPO
ID GHT2_SCHPO Reviewed; 531 AA.
AC O74969; O13346;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=High-affinity glucose transporter ght2;
DE AltName: Full=Hexose transporter 2;
GN Name=ght2; ORFNames=SPBC4B4.08;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507; SER-515; SER-519;
RP SER-520 AND TYR-523, AND 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; AF017180; AAB70519.1; -; mRNA.
DR EMBL; CU329671; CAA19288.1; -; Genomic_DNA.
DR PIR; T40480; T40480.
DR PIR; T43533; T43533.
DR RefSeq; NP_596425.1; NM_001022344.2.
DR AlphaFoldDB; O74969; -.
DR SMR; O74969; -.
DR BioGRID; 276521; 4.
DR STRING; 4896.SPBC4B4.08.1; -.
DR TCDB; 2.A.1.1.21; the major facilitator superfamily (mfs).
DR iPTMnet; O74969; -.
DR MaxQB; O74969; -.
DR PaxDb; O74969; -.
DR PRIDE; O74969; -.
DR EnsemblFungi; SPBC4B4.08.1; SPBC4B4.08.1:pep; SPBC4B4.08.
DR GeneID; 2539977; -.
DR KEGG; spo:SPBC4B4.08; -.
DR PomBase; SPBC4B4.08; ght2.
DR VEuPathDB; FungiDB:SPBC4B4.08; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_001265_30_1_1; -.
DR InParanoid; O74969; -.
DR OMA; FWNIIFC; -.
DR PhylomeDB; O74969; -.
DR PRO; PR:O74969; -.
DR Proteomes; UP000002485; Chromosome II.
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:0005354; F:galactose transmembrane transporter activity; EXP:PomBase.
DR GO; GO:0008643; P:carbohydrate transport; IBA:GO_Central.
DR GO; GO:0140425; P:galactose import across plasma membrane; EXP: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..531
FT /note="High-affinity glucose transporter ght2"
FT /id="PRO_0000050410"
FT TOPO_DOM 5..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..62
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..183
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..289
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..305
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 354..367
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..408
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..436
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..531
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 491..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 523
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 1..12
FT /note="Missing (in Ref. 1; AAB70519)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="G -> R (in Ref. 1; AAB70519)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 531 AA; 58846 MW; 6446BAAAC7FF698E CRC64;
MGFKRGKNFT LVMLIFVSMA GWMFGADTGS IGGVTSMRDF RERYADRYDP ITDQYSLSSA
RQGLLTGMVN VGSLFGCIIS SPIADRFGKR LSIIGFCAVY IIGIIVQVTA VPSWVQIMVA
KIWTGIGIGA LSVLAPGYQS ETAPPSIRGT VVVTYQLFVT GGIFIAACIN MGTHKLHKTA
QWRVSIGINL LWGIITMIGI LFLPESPRYL IQVGKDEEAV RVLSESAELF PDSEEVQNEY
HRLKSSIDEE FAGGPCSWAS IFGKDIRYRT FLGMFVMSLQ QLTGNNYFFY YGFSVMQGAG
INSPYLSAMI LDAVNFGCTF GGMYVLERFG RRNPLIIGGI WQSICFFIYS AVGSRALYHK
NGTSNTRAGA VMIVMACLFI FGFAQTWAPA AYVIVGESYP VRYRSKCAAV ATASNWLWNF
LISFFTPFIQ ASIGFKYGYV FASCNLTGAI VIFLFAKETK GLTLEEINEL YMSVIKPWES
GNFKLNYSEQ KKVEKEKSRK GGARGESVEY VERASNTDSS PQYSSHEEDY A
