FEX2_YEAST
ID FEX2_YEAST Reviewed; 375 AA.
AC Q08991; D6W393;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Fluoride export protein 2 {ECO:0000303|PubMed:24173035};
GN Name=FEX2 {ECO:0000303|PubMed:24173035};
GN OrderedLocusNames=YPL279C {ECO:0000312|SGD:S000006200};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
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).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND LEVEL OF PROTEIN EXPRESSION.
RX PubMed=26055717; DOI=10.1074/jbc.m115.651976;
RA Smith K.D., Gordon P.B., Rivetta A., Allen K.E., Berbasova T., Slayman C.,
RA Strobel S.A.;
RT "Yeast Fex1p is a constitutively expressed fluoride channel with functional
RT asymmetry of its two homologous domains.";
RL J. Biol. Chem. 290:19874-19887(2015).
CC -!- FUNCTION: Fluoride channel required for the rapid expulsion of
CC cytoplasmic fluoride. {ECO:0000269|PubMed:24173035}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26055717};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Highly sensible to fluoride, but not to other
CC halide salts. The growth of a double deletion of both FEX1 and FEX2 is
CC inhibited at almost a 1000-fold lower fluoride concentration than in
CC the wild-type. Has increased intracellular fluoride concentrations.
CC {ECO:0000269|PubMed:24173035}.
CC -!- MISCELLANEOUS: Present with 220 molecules/cell in the plasma membrane.
CC {ECO:0000269|PubMed:26055717}.
CC -!- SIMILARITY: Belongs to the fluoride exporter Fluc/FEX family.
CC {ECO:0000305}.
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DR EMBL; Z73635; CAA98016.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11159.1; -; Genomic_DNA.
DR PIR; S65312; S65312.
DR RefSeq; NP_015044.1; NM_001184093.1.
DR AlphaFoldDB; Q08991; -.
DR SMR; Q08991; -.
DR BioGRID; 35936; 60.
DR STRING; 4932.YPL279C; -.
DR TCDB; 1.A.43.2.5; the camphor resistance or fluoride exporter (fluc) family.
DR iPTMnet; Q08991; -.
DR MaxQB; Q08991; -.
DR PaxDb; Q08991; -.
DR EnsemblFungi; YPL279C_mRNA; YPL279C; YPL279C.
DR GeneID; 855850; -.
DR KEGG; sce:YPL279C; -.
DR SGD; S000006200; FEX2.
DR VEuPathDB; FungiDB:YPL279C; -.
DR eggNOG; ENOG502QT5F; Eukaryota.
DR GeneTree; ENSGT00940000176800; -.
DR HOGENOM; CLU_030507_1_2_1; -.
DR InParanoid; Q08991; -.
DR OMA; CYDLQHV; -.
DR BioCyc; YEAST:G3O-34160-MON; -.
DR PRO; PR:Q08991; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08991; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:1903425; F:fluoride transmembrane transporter activity; IGI:SGD.
DR GO; GO:1903424; P:fluoride transmembrane transport; IMP:SGD.
DR InterPro; IPR003691; CrcB.
DR PANTHER; PTHR28259; PTHR28259; 1.
DR Pfam; PF02537; CRCB; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..375
FT /note="Fluoride export protein 2"
FT /id="PRO_0000255979"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q08913"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..34
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q08913"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q08913, ECO:0000305"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..127
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q08913"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q08913"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..241
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q08913"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q08913"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..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..338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q08913"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..375
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q08913"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 375 AA; 41971 MW; D4408B910F7794CE CRC64;
MIFNPVISNH KLSHYIHVFC TFTTFCILGT ETRQAITALS TYTPAFVTAP TVLWSNCSSC
MLMGIMQSLN AYTWMKDHQV LFLGVTTGYC GALSSFSSML LEMFEHSTNL TNGNIANHTK
LPNRAYGIME FLSVLLVHLM VSMGSLIFGR QLGKEVIVAY GSSSFSKPYT PPSDTVKENA
GDVDTQEMEK NILEFKFKTP APFFKKFFDV VDKLAYALAF PLIILFVVLC AYYENYSRGK
WTLPCLFGIF AGFLRYWLAE MFNKTNKKFP LGTFLANVFA TLLIGIFTMV QRGKKHFSTD
IPIVNSLNSC HIVSALISGF CGTLSTISTF INEGYKLSFI NMLIYYTVSI GISYCLLVIT
LGSYAWTRGL TNPIC
