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FEX1_SCHPO
ID   FEX1_SCHPO              Reviewed;         311 AA.
AC   P0CU19; Q9UTS8;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   07-SEP-2016, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Fluoride export protein 1 {ECO:0000250|UniProtKB:Q08913};
GN   Name=fex1; ORFNames=SPAC977.11;
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].
RX   PubMed=10712506; DOI=10.1091/mbc.11.3.873;
RA   Albrecht E.B., Hunyady A.B., Stark G.R., Patterson T.E.;
RT   "Mechanisms of sod2 gene amplification in Schizosaccharomyces pombe.";
RL   Mol. Biol. Cell 11:873-886(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: Fluoride channel required for the rapid expulsion of
CC       cytoplasmic fluoride. {ECO:0000250|UniProtKB:Q08913}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q08913};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the fluoride exporter Fluc/FEX family.
CC       {ECO:0000305}.
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DR   EMBL; AF192974; AAF13925.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB69633.1; -; Genomic_DNA.
DR   PIR; T50283; T50283.
DR   RefSeq; NP_001018767.1; NM_001020942.2.
DR   RefSeq; NP_592783.1; NM_001018183.2.
DR   AlphaFoldDB; P0CU19; -.
DR   SMR; P0CU19; -.
DR   STRING; 4896.SPAC977.11.1; -.
DR   EnsemblFungi; SPAC977.11.1; SPAC977.11.1:pep; SPAC977.11.
DR   EnsemblFungi; SPBPB8B6.06c.1; SPBPB8B6.06c.1:pep; SPBPB8B6.06c.
DR   GeneID; 2543234; -.
DR   GeneID; 3361186; -.
DR   KEGG; spo:SPAC977.11; -.
DR   KEGG; spo:SPBPB8B6.06c; -.
DR   PomBase; SPAC977.11; fex1.
DR   VEuPathDB; FungiDB:SPAC977.11; -.
DR   VEuPathDB; FungiDB:SPBPB8B6.06c; -.
DR   eggNOG; ENOG502QT5F; Eukaryota.
DR   OMA; RSWTFSM; -.
DR   PhylomeDB; P0CU19; -.
DR   PRO; PR:P0CU19; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:1903425; F:fluoride transmembrane transporter activity; IMP:PomBase.
DR   GO; GO:0140114; P:cellular detoxification of fluoride; IMP:PomBase.
DR   GO; GO:0140116; P:fluoride export across plasma membrane; IMP:PomBase.
DR   GO; GO:1903424; P:fluoride transmembrane transport; IBA:GO_Central.
DR   InterPro; IPR003691; CrcB.
DR   PANTHER; PTHR28259; PTHR28259; 1.
DR   Pfam; PF02537; CRCB; 2.
PE   3: Inferred from homology;
KW   Cell membrane; Glycoprotein; Ion channel; Ion transport; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..311
FT                   /note="Fluoride export protein 1"
FT                   /id="PRO_0000317096"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q08913"
FT   TRANSMEM        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        26..29
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q08913"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        51..65
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q08913"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        87..106
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q08913"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        128..154
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q08913"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        176..186
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q08913"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        208..212
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q08913"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        234..250
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q08913"
FT   TRANSMEM        251..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        269..278
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q08913"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        300..311
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q08913"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   311 AA;  34557 MW;  D86BBC7F953C1338 CRC64;
     MLLTQSYFCI MSMLGTLARL GLTALNTYPG APFSGLLWVQ FVGCVIMGFC QTESVFFPRP
     KHNATFLLAI TTGFCGSLTT FSSWMLQMFT GMANLDPFER RGRGYSFLSV VSDFMVTMCI
     AMSSLIWGKQ IGKTTGQWRI GKVAFAWPIP AHTHIVVRVL LLLLSICFFV GAAFYTAYTT
     NVTHRGIGFS LIFSPFAALT RLYLARFLNS PQYFIPYGTL CANVFATLLL SIMYMIPQIT
     HCTPVSRSVM YGIQNGFCAV LSTLSTFSNE LHTMPIKRAY IYCIISVAIS FSICVIVDGA
     TAWGHGYTEK Y
 
 
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