NAH1_YEAST
ID NAH1_YEAST Reviewed; 985 AA.
AC Q99271; D6VYD3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Na(+)/H(+) antiporter;
GN Name=NHA1; OrderedLocusNames=YLR138W; ORFNames=L3149, L9606.4;
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=8654575; DOI=10.1016/0014-5793(96)00470-x;
RA Prior C., Potier S., Souciet J.-L., Sychrova H.;
RT "Characterization of the NHA1 gene encoding a Na+/H+-antiporter of the
RT yeast Saccharomyces cerevisiae.";
RL FEBS Lett. 387:89-93(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; THR-765; SER-768 AND
RP SER-774, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; THR-765 AND SER-768, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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: Sodium export from cell, takes up external protons in
CC exchange for internal sodium ions. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 1480 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the fungal Na(+)/H(+) exchanger family.
CC {ECO:0000305}.
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DR EMBL; U53881; AAB82392.1; -; Genomic_DNA.
DR EMBL; X91258; CAA62653.1; -; Genomic_DNA.
DR EMBL; Z73310; CAA97709.1; -; Genomic_DNA.
DR EMBL; Z73311; CAA97711.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09449.1; -; Genomic_DNA.
DR PIR; S59330; S59330.
DR RefSeq; NP_013239.1; NM_001182025.1.
DR PDB; 6QK8; X-ray; 2.92 A; E/F/G/H=478-485.
DR PDBsum; 6QK8; -.
DR AlphaFoldDB; Q99271; -.
DR SMR; Q99271; -.
DR BioGRID; 31407; 107.
DR DIP; DIP-6364N; -.
DR IntAct; Q99271; 4.
DR MINT; Q99271; -.
DR STRING; 4932.YLR138W; -.
DR TCDB; 2.A.36.4.1; the monovalent cation:proton antiporter-1 (cpa1) family.
DR iPTMnet; Q99271; -.
DR MaxQB; Q99271; -.
DR PaxDb; Q99271; -.
DR PRIDE; Q99271; -.
DR EnsemblFungi; YLR138W_mRNA; YLR138W; YLR138W.
DR GeneID; 850829; -.
DR KEGG; sce:YLR138W; -.
DR SGD; S000004128; NHA1.
DR VEuPathDB; FungiDB:YLR138W; -.
DR eggNOG; KOG4505; Eukaryota.
DR HOGENOM; CLU_008635_0_1_1; -.
DR InParanoid; Q99271; -.
DR OMA; WPITCFF; -.
DR BioCyc; YEAST:G3O-32278-MON; -.
DR PRO; PR:Q99271; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q99271; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0015491; F:cation:cation antiporter activity; IMP:SGD.
DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015385; F:sodium:proton antiporter activity; IDA:SGD.
DR GO; GO:0030004; P:cellular monovalent inorganic cation homeostasis; IMP:SGD.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IMP:SGD.
DR GO; GO:0097623; P:potassium ion export across plasma membrane; IMP:SGD.
DR GO; GO:0006970; P:response to osmotic stress; IMP:SGD.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IMP:SGD.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1530.20; -; 1.
DR InterPro; IPR013928; Cation/H_antiporter_C.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR004712; Na+/H+_antiporter_fungi.
DR InterPro; IPR038770; Na+/solute_symporter_sf.
DR InterPro; IPR032516; Nha1.
DR PANTHER; PTHR31382:SF4; PTHR31382:SF4; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
DR Pfam; PF08619; Nha1_C; 2.
DR TIGRFAMs; TIGR00844; c_cpa1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiport; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Sodium; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..985
FT /note="Na(+)/H(+) antiporter"
FT /id="PRO_0000052407"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..36
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..105
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..176
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..244
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..319
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..410
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 432..985
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 489..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..556
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..828
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..917
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 765
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 768
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
SQ SEQUENCE 985 AA; 109369 MW; AD0B86D483DCDD89 CRC64;
MAIWEQLEVS KAHVAYACVG VFSSIFSLVS LYVKEKLYIG ESTVAGIFGL IVGPVCLNWF
NPLKWGNSDS ITLEITRIVL CLQIFAVAVE LPRKYMLKHW VSVTMLLLPV MTAGWLIIGL
FVWILIPGLN FSASLLISAC ITATDPILAQ SVVSGKFAQR VPGHLRNLLS AESGCNDGMA
FPFLFLSMNL ILHPGNGREI VKDWICVTIL YECLFGCLLG CFIGYVGRIT IRFAEKKNII
DRESFLAFYV VLAFMCAGFG SILGVDDLLV SFAAGATFAW DGWFSQKTQE SNVSTVIDLL
LNYAYFIYFG AIIPWSQFNN GEIGTNVWRL IILSIVVIFL RRIPAVMILR PLIPDIKSWR
EALFVGHFGP IGVGAIFAAI LARGELESTF SDEPTPLNVV PSKEESKHWQ LIACIWPITC
FFIVTSIIVH GSSVAIITLG RHLNTITLTK TFTTHTTNGD NGKSSWMQRL PSLDKAGRSF
SLHRMDTQMT LSGDEGEAEE GGGRKGLAGG EDEEGLNNDQ IGSVATSGIP ARPAGGMPRR
RKLSRKEKRL NRRQKLRNKG REIFSSRSKN EMYDDDELND LGRERLQKEK EARAATFALS
TAVNTQRNEE IGMGGDEEED EYTPEKEYSD NYNNTPSFES SERSSSLRGR TYVPRNRYDG
EETESEIESE DEMENESERS MASSEERRIR KMKEEEMKPG TAYLDGNRMI IENKQGEILN
QVDIEDRNEA RDDEVSVDST AHSSLTTTMT NLSSSSGGRL KRILTPTSLG KIHSLVDKGK
DKNKNSKYHA FKIDNLLIIE NEDGDVIKRY KINPHKSDDD KSKNRPRNDS VVSRALTAVG
LKSKANSGVP PPVDEEKAIE GPSRKGPGML KKRTLTPAPP RGVQDSLDLE DEPSSEEDLG
DSYNMDDSED YDDNAYESET EFERQRRLNA LGEMTAPADQ DDEELPPLPV EAQTGNDGPG
TAEGKKKQKS AAVKSALSKT LGLNK
