KCH1_YEAST
ID KCH1_YEAST Reviewed; 497 AA.
AC P47114; D6VWM5;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Low affinity K(+) transporter 1 {ECO:0000303|PubMed:23204190};
GN Name=KCH1 {ECO:0000303|PubMed:23204190}; OrderedLocusNames=YJR054W;
GN ORFNames=J1669;
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=8840504;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<869::aid-yea964>3.0.co;2-1;
RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading
RT frames and a gene cluster with a counterpart on chromosome XI.";
RL Yeast 12:869-875(1996).
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291 AND SER-319, 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).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21252230; DOI=10.1074/jbc.m110.177451;
RA Martin D.C., Kim H., Mackin N.A., Maldonado-Baez L., Evangelista C.C. Jr.,
RA Beaudry V.G., Dudgeon D.D., Naiman D.Q., Erdman S.E., Cunningham K.W.;
RT "New regulators of a high affinity Ca2+ influx system revealed through a
RT genome-wide screen in yeast.";
RL J. Biol. Chem. 286:10744-10754(2011).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, SUBCELLULAR LOCATION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=23204190; DOI=10.1128/ec.00299-12;
RA Stefan C.P., Zhang N., Sokabe T., Rivetta A., Slayman C.L., Montell C.,
RA Cunningham K.W.;
RT "Activation of an essential calcium signaling pathway in Saccharomyces
RT cerevisiae by Kch1 and Kch2, putative low-affinity potassium
RT transporters.";
RL Eukaryot. Cell 12:204-214(2013).
CC -!- FUNCTION: Low affinity potassium transporter that, with PRM6/KCH2,
CC participates in high-affinity Ca(2+) influx system (HACS) activation
CC during the response to mating pheromone (PubMed:21252230,
CC PubMed:23204190). Directly promotes K(+) influx and HACS may
CC electrochemically respond to this K(+) influx (PubMed:23204190). KCH1
CC and KCH2 act at the apex of the calcium signaling pathway that is used
CC for survival during prolonged exposures to mating pheromones
CC (PubMed:23204190). {ECO:0000269|PubMed:21252230,
CC ECO:0000269|PubMed:23204190}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103;
CC Evidence={ECO:0000269|PubMed:23204190};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29465;
CC Evidence={ECO:0000269|PubMed:23204190};
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095};
CC Multi-pass membrane protein {ECO:0000269|PubMed:14562095}. Cell
CC membrane {ECO:0000269|PubMed:23204190}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Expression is strongly induced during the response to alpha-
CC factor. {ECO:0000269|PubMed:23204190}.
CC -!- DISRUPTION PHENOTYPE: Leads to high-affinity Ca(2+) influx system
CC (HACS) deficiency (PubMed:21252230, PubMed:23204190). Causes a large
CC increase of cell death in response to mating pheromone, when PRM6/KCH2
CC is also deleted (PubMed:23204190). {ECO:0000269|PubMed:21252230,
CC ECO:0000269|PubMed:23204190}.
CC -!- MISCELLANEOUS: Present with 538 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the KCH1 low affinity K(+) transporter family.
CC {ECO:0000305}.
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DR EMBL; Z49554; CAA89582.1; -; Genomic_DNA.
DR EMBL; L47993; AAB39280.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08841.1; -; Genomic_DNA.
DR PIR; S57073; S57073.
DR RefSeq; NP_012588.1; NM_001181712.1.
DR AlphaFoldDB; P47114; -.
DR SMR; P47114; -.
DR BioGRID; 33808; 415.
DR DIP; DIP-7378N; -.
DR MINT; P47114; -.
DR STRING; 4932.YJR054W; -.
DR TCDB; 1.A.88.1.1; the fungal potassium channel (f-kch) family.
DR iPTMnet; P47114; -.
DR MaxQB; P47114; -.
DR PaxDb; P47114; -.
DR PRIDE; P47114; -.
DR EnsemblFungi; YJR054W_mRNA; YJR054W; YJR054W.
DR GeneID; 853514; -.
DR KEGG; sce:YJR054W; -.
DR SGD; S000003815; KCH1.
DR VEuPathDB; FungiDB:YJR054W; -.
DR eggNOG; ENOG502QVFG; Eukaryota.
DR GeneTree; ENSGT00940000176676; -.
DR HOGENOM; CLU_036942_1_0_1; -.
DR InParanoid; P47114; -.
DR OMA; IELFRNH; -.
DR BioCyc; YEAST:G3O-31688-MON; -.
DR PRO; PR:P47114; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47114; protein.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:SGD.
DR GO; GO:0005937; C:mating projection; IDA:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; IDA:SGD.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:SGD.
DR InterPro; IPR031606; Kch1/2.
DR PANTHER; PTHR36424; PTHR36424; 2.
DR Pfam; PF16944; KCH; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..497
FT /note="Low affinity K(+) transporter 1"
FT /id="PRO_0000203096"
FT TOPO_DOM 1..29
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..216
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..497
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT REGION 420..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 497 AA; 57517 MW; D16DD33BCC5F8EDA CRC64;
MFNHDWKYSI NSKTFADLNI ELFRNHKFKT VLNYIIGVVG WNGLKLALFV SDIYTCIKLL
AFNSWSNNII KPYLPFKISK WLFSGCILAS IVLLIWEAIA GMRIYKTGNI SLTYVNNFSR
NLNSVLNYSK FCVYNMIERK GFRQKMTFFT FFQLKDCIRL IFTDTPRQVI NGLTLWSVLV
TVNKNEDLGD LESFTGLINK IKNIGQTNHE EAVILSLMLF SFIIWALFVF KFLLAVICSI
FVYYKIINDQ EYSGLREYIC VTVSENVDEL VERQRKKEND DTIYKTGLLE SQTFDDFKEV
ENKIETSFND TSYASNNDSM IELIERRPEY KSQDVCGPIP TMKKTETMES FVDNGNPQYT
TRFSAILDSP YINSYESNDI KKAKIQSRSV NTPKYEDLSS SDIFNKIHSA GQLKSTTSME
FHGPLDSMPN TTNNIRNFNS NSSRPRPPPL QTKSSINSKA DSNDNGRIYT PMKAYFREPD
LPRKGLLEDE DRTYNYT
