ID   GEX2_YEAST              Reviewed;         615 AA.
AC   P36173; D6VXG7;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=Glutathione exchanger 2;
GN   Name=GEX2; OrderedLocusNames=YKR106W;
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=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
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   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   [4]
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. Expressed at a very low level.
CC       {ECO:0000269|PubMed:21490148}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000305}.
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DR   EMBL; Z28202; CAA82047.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09257.1; -; Genomic_DNA.
DR   PIR; S40624; S40624.
DR   RefSeq; NP_013032.1; NM_001179896.1.
DR   AlphaFoldDB; P36173; -.
DR   SMR; P36173; -.
DR   BioGRID; 34237; 35.
DR   DIP; DIP-4917N; -.
DR   IntAct; P36173; 1.
DR   STRING; 4932.YKR106W; -.
DR   PaxDb; 4932-YKR106W; -.
DR   EnsemblFungi; YKR106W_mRNA; YKR106W; YKR106W.
DR   GeneID; 853981; -.
DR   KEGG; sce:YKR106W; -.
DR   AGR; SGD:S000001814; -.
DR   SGD; S000001814; GEX2.
DR   VEuPathDB; FungiDB:YKR106W; -.
DR   eggNOG; KOG0254; Eukaryota.
DR   GeneTree; ENSGT00940000176305; -.
DR   HOGENOM; CLU_012970_2_1_1; -.
DR   InParanoid; P36173; -.
DR   OMA; NIAYIVC; -.
DR   OrthoDB; 2020805at2759; -.
DR   BioCyc; YEAST:G3O-32068-MONOMER; -.
DR   BioGRID-ORCS; 853981; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P36173; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P36173; Protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0005774; C:vacuolar membrane; IDA:SGD.
DR   GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; ISA:SGD.
DR   GO; GO:0015343; F:siderophore-iron transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0034775; P:glutathione transmembrane transport; ISA:SGD.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; IBA:GO_Central.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   CDD; cd17322; MFS_ARN_like; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 2.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   PANTHER; PTHR23501:SF92; GLUTATHIONE EXCHANGER 1-RELATED; 1.
DR   PANTHER; PTHR23501; MAJOR FACILITATOR SUPERFAMILY; 1.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 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 2"
FT                   /id="PRO_0000203231"
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..216
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        238..275
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        297..307
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        329..343
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        365..383
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        384..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        405..407
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        408..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        429..440
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        441..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        462..471
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        472..492
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        493..548
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        549..569
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        570..615
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   615 AA;  68954 MW;  B548FBC6E49326AD CRC64;
     MSSSVVGASS NKKSGIRQSC EIIERERHSN DDTYSMTSTF FKLKENEIMS AQFDSLKYKI
     LLISTAFVCG FGISLDYTLR STYTGYATNS YSEHSLLSTV QVINAVVSVG SQVVYSRLSD
     HFGRLRLFLV ATIFYIMGTI IQSQATRLTM YAAGSVFYNC GYVGTNLLLT LILSDFSSLK
     WRMFYQYASY WPYIIIPWIS GNIITAANPQ KNWSWNIAMW AFIYPLSTLP 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 FFTFTMFMRN PELIDKATHE EFTEDGLVVL PDEENIFSQI
     KALFRHNRSN KKSGC
//