ID   FEX1_NEUCR              Reviewed;         526 AA.
AC   Q7SB51;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 2.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Fluoride export protein 1 {ECO:0000303|PubMed:24173035};
GN   Name=fex-1 {ECO:0000303|PubMed:24173035}; ORFNames=NCU06262;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24173035; DOI=10.1073/pnas.1310439110;
RA   Li S., Smith K.D., Davis J.H., Gordon P.B., Breaker R.R., Strobel S.A.;
RT   "Eukaryotic resistance to fluoride toxicity mediated by a widespread family
RT   of fluoride export proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:19018-19023(2013).
CC   -!- FUNCTION: Fluoride channel required for the rapid expulsion of
CC       cytoplasmic fluoride. {ECO:0000269|PubMed:24173035}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q08913};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Highly sensible to fluoride. Growth is inhibited
CC       at a 200-fold lower fluoride concentration than in the wild-type.
CC       {ECO:0000269|PubMed:24173035}.
CC   -!- SIMILARITY: Belongs to the fluoride exporter Fluc/FEX family.
CC       {ECO:0000305}.
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DR   EMBL; CM002238; EAA33630.2; -; Genomic_DNA.
DR   RefSeq; XP_962866.2; XM_957773.3.
DR   AlphaFoldDB; Q7SB51; -.
DR   STRING; 5141.EFNCRP00000006039; -.
DR   TCDB; 1.A.43.2.6; the camphor resistance or fluoride exporter (fluc) family.
DR   EnsemblFungi; EAA33630; EAA33630; NCU06262.
DR   GeneID; 3879005; -.
DR   KEGG; ncr:NCU06262; -.
DR   VEuPathDB; FungiDB:NCU06262; -.
DR   HOGENOM; CLU_030507_0_0_1; -.
DR   InParanoid; Q7SB51; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:1903425; F:fluoride transmembrane transporter activity; IBA:GO_Central.
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; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..526
FT                   /note="Fluoride export protein 1"
FT                   /id="PRO_0000437222"
FT   TOPO_DOM        1..159
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q08913"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        181..194
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q08913"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        216..260
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q08913"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        282..310
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q08913"
FT   TRANSMEM        311..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        332..361
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q08913"
FT   TRANSMEM        362..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        383..398
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q08913"
FT   TRANSMEM        399..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        420..424
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q08913"
FT   TRANSMEM        425..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        446..452
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q08913"
FT   TRANSMEM        453..473
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        474..492
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q08913"
FT   TRANSMEM        493..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        514..526
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q08913"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          90..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          223..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..130
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   526 AA;  57329 MW;  7C2B4CC285B1DF09 CRC64;
     MMTAPSDTEG YTGGQGDSPD SPDRNRQRNL VDDHNHNQGQ DDGYSQGHVT GTGLHPLHQS
     QGRYPRASSR RASAAPLNYD VPDDYAHLEA SNISPVQNPD EDPITRLDTL ERVRTRDRDY
     LREQRRKPLP PPQEPESSAE DYEREKQAGV VAKRQKVSRL ATELYTISYL IFFSLLGTLA
     RLGLQALTSA YPQSPIIFPS IWPNFAGCVV MGFLAEDRML FRPDWGQQQP NPKKDDDDDE
     EAKDIDPAAA KKAHMALKKT IPLYVGLATG FCGSFTSFSS FIRDIYLALS NDLAAHGSSA
     APVSRNGGYS FMALLAVTIT TISLSLSGLF AGAHLAIAIA TLFTRFDLGL PYTFVSRILD
     RLIVLLGFGC WLGAVLLSIW PPDRHSAQPE KERWRGTATF ALVFAPLGCL TRFYASAHLN
     GRLPSFPLGT FVVNMLGTAV LGMAWDLNHV PSLGGVVGCQ VLQGVADGFC GCLTTVSTWV
     SELAALRRRH AYVYGGASVG GGLALMVVVM GSLRWTEGFG EVKCIS