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
//
