KHA1_YEAST
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 03-AUG-2022, entry version 160.
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}.
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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; 73.
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; P40309; -.
DR PRIDE; P40309; -.
DR EnsemblFungi; YJL094C_mRNA; YJL094C; YJL094C.
DR GeneID; 853351; -.
DR KEGG; sce:YJL094C; -.
DR SGD; S000003630; KHA1.
DR VEuPathDB; FungiDB:YJL094C; -.
DR eggNOG; KOG1650; Eukaryota.
DR HOGENOM; CLU_005126_10_1_1; -.
DR InParanoid; P40309; -.
DR OMA; MEDIPNI; -.
DR BioCyc; YEAST:G3O-31549-MON; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Pfam; PF00999; Na_H_Exchanger; 1.
DR TIGRFAMs; TIGR00932; 2a37; 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
