NHX1_YEAST
ID NHX1_YEAST Reviewed; 633 AA.
AC Q04121; D6VT80;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Endosomal/prevacuolar sodium/hydrogen exchanger;
DE AltName: Full=Endosomal/prevacuolar Na(+)/H(+) exchanger;
DE AltName: Full=Vacuolar protein sorting-associated protein 44;
DE Flags: Precursor;
GN Name=NHX1; Synonyms=NHA2, VPL27, VPS44; OrderedLocusNames=YDR456W;
GN ORFNames=D9461.40;
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 [GENOMIC DNA].
RX PubMed=9507001; DOI=10.1074/jbc.273.12.6951;
RA Numata M., Petrecca K., Lake N., Orlowski J.;
RT "Identification of a mitochondrial Na+/H+ exchanger.";
RL J. Biol. Chem. 273:6951-6959(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
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 [4]
RP FUNCTION.
RX PubMed=1493335; DOI=10.1091/mbc.3.12.1389;
RA Raymond C.K., Howald-Stevenson I., Vater C.A., Stevens T.H.;
RT "Morphological classification of the yeast vacuolar protein sorting
RT mutants: evidence for a prevacuolar compartment in class E vps mutants.";
RL Mol. Biol. Cell 3:1389-1402(1992).
RN [5]
RP FUNCTION.
RX PubMed=9334180; DOI=10.1074/jbc.272.42.26145;
RA Nass R., Cunningham K.W., Rao R.;
RT "Intracellular sequestration of sodium by a novel Na+/H+ exchanger in yeast
RT is enhanced by mutations in the plasma membrane H+-ATPase. Insights into
RT mechanisms of sodium tolerance.";
RL J. Biol. Chem. 272:26145-26152(1997).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9694857; DOI=10.1074/jbc.273.33.21054;
RA Nass R., Rao R.;
RT "Novel localization of a Na+/H+ exchanger in a late endosomal compartment
RT of yeast. Implications for vacuole biogenesis.";
RL J. Biol. Chem. 273:21054-21060(1998).
RN [7]
RP FUNCTION.
RX PubMed=10589731; DOI=10.1099/00221287-145-11-3221;
RA Nass R., Rao R.;
RT "The yeast endosomal Na+/H+ exchanger, Nhx1, confers osmotolerance
RT following acute hypertonic shock.";
RL Microbiology 145:3221-3228(1999).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=10998367; DOI=10.1042/0264-6021:3510241;
RA Darley C.P., van Wuytswinkel O.C.M., van der Woude K., Mager W.H.,
RA de Boer A.H.;
RT "Arabidopsis thaliana and Saccharomyces cerevisiae NHX1 genes encode
RT amiloride sensitive electroneutral Na(+)/H(+) exchangers.";
RL Biochem. J. 351:241-249(2000).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-201; GLU-225 AND
RP ASP-230.
RX PubMed=11102523; DOI=10.1091/mbc.11.12.4277;
RA Bowers K., Levi B.P., Patel F.I., Stevens T.H.;
RT "The sodium/proton exchanger Nhx1p is required for endosomal protein
RT trafficking in the yeast Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 11:4277-4294(2000).
RN [10]
RP GLYCOSYLATION, AND TOPOLOGY.
RX PubMed=11036065; DOI=10.1074/jbc.m001688200;
RA Wells K.M., Rao R.;
RT "The yeast Na+/H+ exchanger Nhx1 is an N-linked glycoprotein. Topological
RT implications.";
RL J. Biol. Chem. 276:3401-3407(2001).
RN [11]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CYP6.
RX PubMed=14610088; DOI=10.1074/jbc.m307446200;
RA Ali R., Brett C.L., Mukherjee S., Rao R.;
RT "Inhibition of sodium/proton exchange by a Rab-GTPase-activating protein
RT regulates endosomal traffic in yeast.";
RL J. Biol. Chem. 279:4498-4506(2004).
RN [13]
RP FUNCTION.
RX PubMed=15635088; DOI=10.1091/mbc.e04-11-0999;
RA Brett C.L., Tukaye D.N., Mukherjee S., Rao R.;
RT "The yeast endosomal Na+K+/H+ exchanger Nhx1 regulates cellular pH to
RT control vesicle trafficking.";
RL Mol. Biol. Cell 16:1396-1405(2005).
RN [14]
RP FUNCTION.
RX PubMed=15659172; DOI=10.1111/j.1365-2958.2004.04410.x;
RA Maresova L., Sychrova H.;
RT "Physiological characterization of Saccharomyces cerevisiae kha1 deletion
RT mutants.";
RL Mol. Microbiol. 55:588-600(2005).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF GLU-355;
RP PHE-357; TYR-361; GLU-365; GLU-369 AND PRO-376.
RX PubMed=16671892; DOI=10.1042/bj20060388;
RA Mukherjee S., Kallay L., Brett C.L., Rao R.;
RT "Mutational analysis of the intramembranous H10 loop of yeast Nhx1 reveals
RT a critical role in ion homoeostasis and vesicle trafficking.";
RL Biochem. J. 398:97-105(2006).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=17543551; DOI=10.1016/j.cellbi.2007.04.008;
RA Hedman J.M., Eggleston M.D., Attryde A.L., Marshall P.A.;
RT "Prevacuolar compartment morphology in vps mutants of Saccharomyces
RT cerevisiae.";
RL Cell Biol. Int. 31:1237-1244(2007).
RN [17]
RP FUNCTION.
RX PubMed=17588950; DOI=10.1074/jbc.m703116200;
RA Cagnac O., Leterrier M., Yeager M., Blumwald E.;
RT "Identification and characterization of Vnx1p, a novel type of vacuolar
RT monovalent cation/H+ antiporter of Saccharomyces cerevisiae.";
RL J. Biol. Chem. 282:24284-24293(2007).
RN [18]
RP FUNCTION.
RX PubMed=18378800; DOI=10.1085/jgp.200709905;
RA Jennings M.L., Cui J.;
RT "Chloride homeostasis in Saccharomyces cerevisiae: high affinity influx, V-
RT ATPase-dependent sequestration, and identification of a candidate Cl-
RT sensor.";
RL J. Gen. Physiol. 131:379-391(2008).
RN [19]
RP FUNCTION.
RX PubMed=18799619; DOI=10.1091/mbc.e08-05-0486;
RA Chen S., Tarsio M., Kane P.M., Greenberg M.L.;
RT "Cardiolipin mediates cross-talk between mitochondria and the vacuole.";
RL Mol. Biol. Cell 19:5047-5058(2008).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-490; SER-494; THR-498;
RP SER-499 AND SER-569, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Endosomal/prevacuolar electroneutral Na(+)/H(+) exchanger
CC which mediates intracellular sequestration of Na(+) cations, regulates
CC vacuolar pH and contributes to osmotolerance following sudden exposure
CC to hyperosmotic media. Contributes also to the postdiauxic/stationary
CC phase resistance to osmotic stress and allows for the continued growth
CC of cells until the acquired osmotolerance response can occur. Involved
CC in hygromycin resistance probably through its influence on the
CC electrochemical proton gradient affecting secondarily the entrance of
CC hygromycin. Mediates pH-dependent vesicle trafficking out of the
CC endosome. Contributes to K(+) sequestration and homeostasis.
CC {ECO:0000269|PubMed:10589731, ECO:0000269|PubMed:10998367,
CC ECO:0000269|PubMed:11102523, ECO:0000269|PubMed:14610088,
CC ECO:0000269|PubMed:1493335, ECO:0000269|PubMed:15635088,
CC ECO:0000269|PubMed:15659172, ECO:0000269|PubMed:16671892,
CC ECO:0000269|PubMed:17588950, ECO:0000269|PubMed:18378800,
CC ECO:0000269|PubMed:18799619, ECO:0000269|PubMed:9334180,
CC ECO:0000269|PubMed:9694857}.
CC -!- SUBUNIT: Interacts with CYP6. {ECO:0000269|PubMed:14610088}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane protein.
CC Prevacuolar compartment membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: Present with 521 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1)
CC transporter (TC 2.A.36) family. {ECO:0000305}.
CC -!- CAUTION: Numerous studies suggest that the C-terminal tail of the
CC Na(+)/H(+) exchangers assumes a cytosolic orientation and constitutes a
CC regulatory region. This cytosolic localization is confirmed by
CC phosphorylation analysis (PubMed:15665377 and PubMed:18407956).
CC However, residues Asn-515, Asn-550 and Asn-563 have been shown to be
CC glycosylated and localized at the lumenal side (PubMed:11036065). These
CC contradictory results suggest an unusual topology of the C-terminal
CC tail which may contain membrane spans formed by beta-sheets or even may
CC switch from one side to the other of the membrane.
CC {ECO:0000305|PubMed:11036065}.
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DR EMBL; U33007; AAB64861.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12290.1; -; Genomic_DNA.
DR PIR; S69734; S69734.
DR RefSeq; NP_010744.3; NM_001180764.3.
DR AlphaFoldDB; Q04121; -.
DR SMR; Q04121; -.
DR BioGRID; 32510; 287.
DR DIP; DIP-4145N; -.
DR IntAct; Q04121; 17.
DR MINT; Q04121; -.
DR STRING; 4932.YDR456W; -.
DR TCDB; 2.A.36.1.12; the monovalent cation:proton antiporter-1 (cpa1) family.
DR iPTMnet; Q04121; -.
DR MaxQB; Q04121; -.
DR PaxDb; Q04121; -.
DR PRIDE; Q04121; -.
DR TopDownProteomics; Q04121; -.
DR EnsemblFungi; YDR456W_mRNA; YDR456W; YDR456W.
DR GeneID; 852066; -.
DR KEGG; sce:YDR456W; -.
DR SGD; S000002864; NHX1.
DR VEuPathDB; FungiDB:YDR456W; -.
DR eggNOG; KOG1965; Eukaryota.
DR GeneTree; ENSGT00940000170200; -.
DR HOGENOM; CLU_005912_5_1_1; -.
DR InParanoid; Q04121; -.
DR OMA; IHETVIS; -.
DR BioCyc; YEAST:G3O-29984-MON; -.
DR Reactome; R-SCE-425986; Sodium/Proton exchangers.
DR PRO; PR:Q04121; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04121; protein.
DR GO; GO:0005769; C:early endosome; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IDA:SGD.
DR GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR GO; GO:0015386; F:potassium:proton antiporter activity; IMP:SGD.
DR GO; GO:0015385; F:sodium:proton antiporter activity; IMP:SGD.
DR GO; GO:0030004; P:cellular monovalent inorganic cation homeostasis; IMP:SGD.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IMP:SGD.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IMP:SGD.
DR GO; GO:0007035; P:vacuolar acidification; IMP:SGD.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR018422; Cation/H_exchanger_CPA1.
DR InterPro; IPR004709; NaH_exchanger.
DR PANTHER; PTHR10110; PTHR10110; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
DR PRINTS; PR01084; NAHEXCHNGR.
DR TIGRFAMs; TIGR00840; b_cpa1; 1.
PE 1: Evidence at protein level;
KW Antiport; Endosome; Glycoprotein; Ion transport; Membrane; Phosphoprotein;
KW Potassium; Potassium transport; Reference proteome; Signal; Sodium;
KW Sodium transport; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..633
FT /note="Endosomal/prevacuolar sodium/hydrogen exchanger"
FT /id="PRO_0000052380"
FT TOPO_DOM 22..61
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..117
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..189
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..258
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..313
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..431
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 25..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 124..133
FT /note="Amiloride-binding"
FT COMPBIAS 553..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 490
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 498
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11036065"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11036065"
FT CARBOHYD 563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11036065"
FT MUTAGEN 201
FT /note="D->N: Impairs protein-trafficking to the vacuole."
FT /evidence="ECO:0000269|PubMed:11102523"
FT MUTAGEN 225
FT /note="E->Q: Impairs protein-trafficking to the vacuole."
FT /evidence="ECO:0000269|PubMed:11102523"
FT MUTAGEN 230
FT /note="D->N: Impairs protein-trafficking to the vacuole."
FT /evidence="ECO:0000269|PubMed:11102523"
FT MUTAGEN 355
FT /note="E->Q: Impairs partially resistance to osmotic stress
FT and hygromycin."
FT /evidence="ECO:0000269|PubMed:16671892"
FT MUTAGEN 357
FT /note="F->A,L,I: Impairs resistance to osmotic stress and
FT hygromycin, and blocks protein-trafficking to the vacuole."
FT /evidence="ECO:0000269|PubMed:16671892"
FT MUTAGEN 357
FT /note="F->V: Impairs partially resistance to osmotic stress
FT and hygromycin."
FT /evidence="ECO:0000269|PubMed:16671892"
FT MUTAGEN 361
FT /note="Y->A: Impairs resistance to osmotic stress and
FT hygromycin, and blocks protein-trafficking to the vacuole."
FT /evidence="ECO:0000269|PubMed:16671892"
FT MUTAGEN 365
FT /note="E->A: Impairs resistance to osmotic stress and
FT hygromycin, and blocks protein-trafficking to the vacuole."
FT /evidence="ECO:0000269|PubMed:16671892"
FT MUTAGEN 369
FT /note="E->A: Impairs partially resistance to osmotic stress
FT and hygromycin."
FT /evidence="ECO:0000269|PubMed:16671892"
FT MUTAGEN 376
FT /note="P->N: Impairs resistance to osmotic stress and
FT hygromycin."
FT /evidence="ECO:0000269|PubMed:16671892"
SQ SEQUENCE 633 AA; 70148 MW; 9B771ABDE41CEB0A CRC64;
MLSKVLLNIA FKVLLTTAKR AVDPDDDDEL LPSPDLPGSD DPIAGDPDVD LNPVTEEMFS
SWALFIMLLL LISALWSSYY LTQKRIRAVH ETVLSIFYGM VIGLIIRMSP GHYIQDTVTF
NSSYFFNVLL PPIILNSGYE LNQVNFFNNM LSILIFAIPG TFISAVVIGI ILYIWTFLGL
ESIDISFADA MSVGATLSAT DPVTILSIFN AYKVDPKLYT IIFGESLLND AISIVMFETC
QKFHGQPATF SSVFEGAGLF LMTFSVSLLI GVLIGILVAL LLKHTHIRRY PQIESCLILL
IAYESYFFSN GCHMSGIVSL LFCGITLKHY AYYNMSRRSQ ITIKYIFQLL ARLSENFIFI
YLGLELFTEV ELVYKPLLII VAAISICVAR WCAVFPLSQF VNWIYRVKTI RSMSGITGEN
ISVPDEIPYN YQMMTFWAGL RGAVGVALAL GIQGEYKFTL LATVLVVVVL TVIIFGGTTA
GMLEVLNIKT GCISEEDTSD DEFDIEAPRA INLLNGSSIQ TDLGPYSDNN SPDISIDQFA
VSSNKNLPNN ISTTGGNTFG GLNETENTSP NPARSSMDKR NLRDKLGTIF NSDSQWFQNF
DEQVLKPVFL DNVSPSLQDS ATQSPADFSS QNH
