SUT1_SCHPO
ID SUT1_SCHPO Reviewed; 553 AA.
AC O14091; Q9UU60;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=General alpha-glucoside permease;
GN Name=sut1; ORFNames=SPAC2F3.08;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 35-166.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=11136464; DOI=10.1046/j.1365-2958.2001.02237.x;
RA Reinders A., Ward J.M.;
RT "Functional characterization of the alpha-glucoside transporter Sut1p from
RT Schizosaccharomyces pombe, the first fungal homologue of plant sucrose
RT transporters.";
RL Mol. Microbiol. 39:445-454(2001).
CC -!- FUNCTION: Responsible for the transport of maltose and sucrose into the
CC cell, with the concomitant uptake of protons (symport system).
CC {ECO:0000269|PubMed:11136464}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycoside-pentoside-hexuronide (GPH) cation
CC symporter transporter (TC 2.A.2.4) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAB16264.1; -; Genomic_DNA.
DR EMBL; AB027797; BAA87101.1; -; Genomic_DNA.
DR PIR; T38541; T38541.
DR RefSeq; NP_594387.1; NM_001019808.2.
DR AlphaFoldDB; O14091; -.
DR BioGRID; 278450; 16.
DR STRING; 4896.SPAC2F3.08.1; -.
DR TCDB; 2.A.2.6.1; the glycoside-pentoside-hexuronide (gph):cation symporter family.
DR iPTMnet; O14091; -.
DR MaxQB; O14091; -.
DR PaxDb; O14091; -.
DR PRIDE; O14091; -.
DR EnsemblFungi; SPAC2F3.08.1; SPAC2F3.08.1:pep; SPAC2F3.08.
DR PomBase; SPAC2F3.08; sut1.
DR VEuPathDB; FungiDB:SPAC2F3.08; -.
DR eggNOG; KOG0637; Eukaryota.
DR HOGENOM; CLU_018303_1_1_1; -.
DR InParanoid; O14091; -.
DR OMA; GMIVQFA; -.
DR PhylomeDB; O14091; -.
DR Reactome; R-SPO-189200; Cellular hexose transport.
DR PRO; PR:O14091; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0005887; C:integral component of plasma membrane; EXP:PomBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005364; F:maltose:proton symporter activity; IDA:PomBase.
DR GO; GO:0008506; F:sucrose:proton symporter activity; IDA:PomBase.
DR GO; GO:0106081; P:maltose import across plasma membrane; IDA:PomBase.
DR GO; GO:0106082; P:sucrose import across plasma membrane; IDA:PomBase.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR036259; MFS_trans_sf.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 3: Inferred from homology;
KW Membrane; Reference proteome; Sugar transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..553
FT /note="General alpha-glucoside permease"
FT /id="PRO_0000122532"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..72
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..140
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..280
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..322
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..452
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..494
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..521
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 543..553
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 553 AA; 61745 MW; 2C31DFC2D88A7C7A CRC64;
MSVDENQLEN GQLLSSENEA SSPFKESIPS RSSLYLIALT VSLLGVQLTW SVELGYGTPY
LFSLGLRKEW TSIIWIAGPL TGILIQPIAG ILSDRVNSRI GRRRPFMLCA SLLGTFSLFL
MGWAPDICLF IFSNEVLMKR VTIVLATISI YLLDVAVNVV MASTRSLIVD SVRSDQQHEA
NSWAGRMIGV GNVLGYLLGY LPLYRIFSFL NFTQLQVFCV LASISLVLTV TITTIFVSER
RFPPVEHEKS VAGEIFEFFT TMRQSITALP FTLKRICFVQ FFAYFGWFPF LFYITTYVGI
LYLRHAPKGH EEDWDMATRQ GSFALLLFAI ISLAANTALP LLLEDTEDDE EDESSDASNN
EYNIQERNDL GNIRTGTNTP RLGNLSETTS FRSENEPSRR RLLPSSRSIM TTISSKVQIK
GLTLPILWLS SHVLFGVCML STIFLQTSWQ AQAMVAICGL SWACTLWIPY SLFSSEIGKL
GLRESSGKMI GVHNVFISAP QVLSTIIATI VFIQSEGSHR DIADNSIAWV LRIGGISAFL
AAYQCRHLLP INF
