ID   KHA1_YEAST              Reviewed;         873 AA.
AC   P40309; D6VW90;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=K(+)/H(+) antiporter 1;
GN   Name=KHA1; OrderedLocusNames=YJL094C; ORFNames=J0909;
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7985424; DOI=10.1002/yea.320100712;
RA   Miosga T., Witzel A., Zimmermann F.K.;
RT   "Sequence and function analysis of a 9.46 kb fragment of Saccharomyces
RT   cerevisiae chromosome X.";
RL   Yeast 10:965-973(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
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-557, AND IDENTIFICATION BY
RP   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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, AND IDENTIFICATION BY
RP   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).
RN   [8]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-562, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22106047; DOI=10.1002/pmic.201100166;
RA   Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT   "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL   Proteomics 12:236-240(2012).
CC   -!- FUNCTION: Potassium-proton antiport.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 172 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 (CPA2)
CC       transporter (TC 2.A.37) family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X77087; CAA54359.1; -; Genomic_DNA.
DR   EMBL; Z49369; CAA89387.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08706.1; -; Genomic_DNA.
DR   PIR; S46584; S46584.
DR   RefSeq; NP_012441.1; NM_001181527.1.
DR   AlphaFoldDB; P40309; -.
DR   SMR; P40309; -.
DR   BioGRID; 33663; 74.
DR   DIP; DIP-4799N; -.
DR   IntAct; P40309; 1.
DR   STRING; 4932.YJL094C; -.
DR   TCDB; 2.A.37.4.1; the monovalent cation:proton antiporter-2 (cpa2) family.
DR   CarbonylDB; P40309; -.
DR   iPTMnet; P40309; -.
DR   MaxQB; P40309; -.
DR   PaxDb; 4932-YJL094C; -.
DR   PeptideAtlas; P40309; -.
DR   EnsemblFungi; YJL094C_mRNA; YJL094C; YJL094C.
DR   GeneID; 853351; -.
DR   KEGG; sce:YJL094C; -.
DR   AGR; SGD:S000003630; -.
DR   SGD; S000003630; KHA1.
DR   VEuPathDB; FungiDB:YJL094C; -.
DR   eggNOG; KOG1650; Eukaryota.
DR   HOGENOM; CLU_005126_10_1_1; -.
DR   InParanoid; P40309; -.
DR   OMA; GMFILMA; -.
DR   OrthoDB; 6504at2759; -.
DR   BioCyc; YEAST:G3O-31549-MONOMER; -.
DR   BioGRID-ORCS; 853351; 9 hits in 10 CRISPR screens.
DR   PRO; PR:P40309; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P40309; Protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0015386; F:potassium:proton antiporter activity; IMP:SGD.
DR   GO; GO:0098662; P:inorganic cation transmembrane transport; IMP:SGD.
DR   Gene3D; 1.20.1530.20; -; 1.
DR   InterPro; IPR006153; Cation/H_exchanger.
DR   InterPro; IPR004771; K/H_exchanger.
DR   InterPro; IPR038770; Na+/solute_symporter_sf.
DR   NCBIfam; TIGR00932; 2a37; 1.
DR   PANTHER; PTHR32468; CATION/H + ANTIPORTER; 1.
DR   PANTHER; PTHR32468:SF0; K(+)_H(+) ANTIPORTER 1; 1.
DR   Pfam; PF00999; Na_H_Exchanger; 1.
PE   1: Evidence at protein level;
KW   Antiport; Ion transport; Isopeptide bond; Membrane; Phosphoprotein;
KW   Potassium; Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Ubl conjugation.
FT   CHAIN           1..873
FT                   /note="K(+)/H(+) antiporter 1"
FT                   /id="PRO_0000196618"
FT   TOPO_DOM        1..23
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        45..51
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        73..82
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        104..116
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..154
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        176..188
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..220
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        242..267
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        289..316
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        338..341
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        363..375
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        376..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        397..404
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        405..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        426..726
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        727..747
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        748..873
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         557
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   CROSSLNK        562
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
SQ   SEQUENCE   873 AA;  97111 MW;  881E55A1F59C8CE6 CRC64;
     MANTVGGILS GVNPFHYNSS SPLTLFLFQA CLILLVCNLI HIPFSMMRQP KVISEVISGV
     ILGPTIFGQI PNYTNTIFPT SSIPGLNLVA NLGIILFMFF LGLEVDIAFI KKHLKKALVI
     GIVTLAVPFG FGCLLAIPLF HTYANKTEGE RHIKFSVFMV FIAVSISVTA FPVLCRILNE
     LRLIKDRAGI VVLAAGIIND IMGWILLALS IILSSAEGSP VNTVYILLIT FAWFLIYFFP
     LKYLLRWVLI RTHELDRSKP SPLATMCILF IMFISAYFTD IIGVHPIFGA FIAGLVVPRD
     DHYVVKLTER MEDIPNIVFI PIYFAVAGLN VDLTLLNEGR DWGYVFATIG IAIFTKIISG
     TLTAKLTGLF WREATAAGVL MSCKGIVEIV VLTVGLNAGI ISRKIFGMFV LMALVSTFVT
     TPLTQLVYPD SYRDGVRKSL STPAEDDGAA DGLDSEGVDK TEINTQLNSL ADVSKYRIGE
     LTTVINTTEA ISPSLKLLNY LSLGVSPKPK NNKHKNETSL SRMTTATDST LKSNTFKIKK
     MVHIWSKSVD DVDTNLSVID EKLTPFEGVG ALRAIHLRLL TERTTDLLQS SSLYNDDPHF
     TANTDSLLQI FDIFSNLSKI PFSSEVIFST MREKAANIAT MKMDSTDLIL LPLKGASYEY
     RGSPVFIDEK YANFDHIYSH LLGLNELSST FFKSIFQSLK ANFAVQISNT YGRLNADRFK
     RKRFNLLLPK PYLTQSDYLG LYLLLLICYR DGYNNDNASC SIFINSKNID FAKDLSTAFA
     EHDWLNESTI KIVDIPFETK VPEEAIEKPS FIETVLDVGL SDTALADIEE TTFIIGEDLP
     DESEPFSEEV RTVIFEGSNR RFDTLIVHHF SSE
//