GEX1_YEAST
ID GEX1_YEAST Reviewed; 615 AA.
AC P25596; D6VQU9; P25597; P25599; P87002; Q8NIN5;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2003, sequence version 4.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Glutathione exchanger 1;
GN Name=GEX1; OrderedLocusNames=YCL073C; ORFNames=YCL70C/YCL71C/YCL73C;
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=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=8771713;
RX DOI=10.1002/(sici)1097-0061(199605)12:6<583::aid-yea936>3.0.co;2-y;
RA Gromadka R., Gora M., Zielenkiewicz U., Slonimski P.P., Rytka J.;
RT "Subtelomeric duplications in Saccharomyces cerevisiae chromosomes III and
RT XI: topology, arrangements, corrections of sequence and strain-specific
RT polymorphism.";
RL Yeast 12:583-591(1996).
RN [3]
RP SEQUENCE REVISION TO 605; 610 AND 612-613.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP INDUCTION.
RX PubMed=14561723; DOI=10.1093/jb/mvg155;
RA Sakaki K., Tashiro K., Kuhara S., Mihara K.;
RT "Response of genes associated with mitochondrial function to mild heat
RT stress in yeast Saccharomyces cerevisiae.";
RL J. Biochem. 134:373-384(2003).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [7]
RP INDUCTION, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21490148; DOI=10.1091/mbc.e10-11-0906;
RA Dhaoui M., Auchere F., Blaiseau P.L., Lesuisse E., Landoulsi A.,
RA Camadro J.M., Haguenauer-Tsapis R., Belgareh-Touze N.;
RT "Gex1 is a yeast glutathione exchanger that interferes with pH and redox
RT homeostasis.";
RL Mol. Biol. Cell 22:2054-2067(2011).
CC -!- FUNCTION: Proton/glutathione antiporter that imports glutathione from
CC the vacuole and exports it through the plasma membrane. Involved in
CC resistance to oxidative stress and modulation of the PKA pathway.
CC {ECO:0000269|PubMed:21490148}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21490148};
CC Multi-pass membrane protein {ECO:0000269|PubMed:21490148}. Vacuole
CC membrane {ECO:0000269|PubMed:21490148}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21490148}.
CC -!- INDUCTION: By iron depletion and by heat. {ECO:0000269|PubMed:14561723,
CC ECO:0000269|PubMed:21490148}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; X59720; CAC42950.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07418.1; -; Genomic_DNA.
DR PIR; S74277; S74277.
DR RefSeq; NP_009863.2; NM_001178711.1.
DR AlphaFoldDB; P25596; -.
DR BioGRID; 30919; 5.
DR DIP; DIP-8068N; -.
DR IntAct; P25596; 2.
DR MINT; P25596; -.
DR STRING; 4932.YCL073C; -.
DR iPTMnet; P25596; -.
DR PaxDb; P25596; -.
DR PRIDE; P25596; -.
DR EnsemblFungi; YCL073C_mRNA; YCL073C; YCL073C.
DR GeneID; 850289; -.
DR KEGG; sce:YCL073C; -.
DR SGD; S000000575; GEX1.
DR VEuPathDB; FungiDB:YCL073C; -.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000176305; -.
DR HOGENOM; CLU_012970_2_1_1; -.
DR InParanoid; P25596; -.
DR OMA; CAYPTQA; -.
DR BioCyc; YEAST:G3O-29317-MON; -.
DR PRO; PR:P25596; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25596; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
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:0005774; C:vacuolar membrane; IDA:SGD.
DR GO; GO:0015343; F:siderophore transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015299; F:solute:proton antiporter activity; IMP:SGD.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0034775; P:glutathione transmembrane transport; IMP:SGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Antiport; Cell membrane; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..615
FT /note="Glutathione exchanger 1"
FT /id="PRO_0000202557"
FT TOPO_DOM 1..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..120
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..186
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..275
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..343
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..407
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 429..440
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..547
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..615
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 615 AA; 68921 MW; DB62B9A0DFD27F12 CRC64;
MSSSVVGASS NKKSGIRQSC EIIERERHSN DDTYSMTSTF FKLKENEIMS AQFDSLKYKI
LLISTAFVCG FGISLDYTLR STYTGYATNS YSEHSLLSTV QVINAVVSVG SQVVYSRLSD
HFGRLRLFLV ATIFYIMGTI IQSQATRLTM YAAGSVFYNC GYVGTNLLLT LILSDFSSLK
WRMFYQYASY WPYIIIPWIS GNIITAANPQ KNWSWNIAMW AFIYPLSALP IIFLILYMKY
KSSKTAEWRS LKEQARKERT GGLFENLVFL FWKLDIVGIL LITVSLGCIL VPLTLANETS
QKWHNSKIIA TLVSGGCLFF IFLYWEAKFA KSPLLPFKLL SDRGIWAPLG VTFFNFFTFF
ISCDYLYPVL LVSMKESSTS AARIVNLPDF VAATASPFYS LLVAKTRKLK LSVIGGCAAW
MVCMGLFYKY RGGSGSHEGV IAASVIMGLS GLLCSNSVIV ILQAMTTHSR MAVITGIQYT
FSKLGAAIGA SVSGAIWTQT MPNQLYKNLG NDTLAEIAYA SPYTFISDYP WGSPERDAVV
ESYRYVQRII MTVGLACTVP FFAFTMFMRD PELIDKATHE EFTEDGLVVL PDEENIFSQI
KALFRHNRSN KKLGC
