PRM6_YEAST
ID PRM6_YEAST Reviewed; 352 AA.
AC Q04705; D6VZC8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Pheromone-regulated membrane protein 6 {ECO:0000303|PubMed:11062271};
DE AltName: Full=Low affinity K(+) transporter 2 {ECO:0000303|PubMed:23204190};
GN Name=PRM6 {ECO:0000303|PubMed:11062271};
GN Synonyms=KCH2 {ECO:0000303|PubMed:23204190}; OrderedLocusNames=YML047C;
GN ORFNames=YM9827.05C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP NOMENCLATURE, AND INDUCTION.
RX PubMed=11062271; DOI=10.1083/jcb.151.3.719;
RA Heiman M.G., Walter P.;
RT "Prm1p, a pheromone-regulated multispanning membrane protein, facilitates
RT plasma membrane fusion during yeast mating.";
RL J. Cell Biol. 151:719-730(2000).
RN [5]
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 [6]
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 KCH1,
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 PRM6/KCH2 act at the apex of the calcium signaling pathway that is
CC used 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: Cell membrane {ECO:0000269|PubMed:23204190};
CC Multi-pass membrane protein {ECO:0000255}. Bud tip
CC {ECO:0000269|PubMed:23204190}. Vacuole lumen
CC {ECO:0000269|PubMed:23204190}. Note=Localizes to the distal tip of
CC growing buds. {ECO:0000269|PubMed:23204190}.
CC -!- INDUCTION: Expression is strongly induced during the response to alpha-
CC factor. {ECO:0000269|PubMed:11062271, 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 KCH1 is
CC also deleted (PubMed:23204190). {ECO:0000269|PubMed:21252230,
CC ECO:0000269|PubMed:23204190}.
CC -!- SIMILARITY: Belongs to the KCH1 low affinity K(+) transporter family.
CC {ECO:0000305}.
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DR EMBL; Z47816; CAA87827.1; -; Genomic_DNA.
DR EMBL; AY692915; AAT92934.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09852.1; -; Genomic_DNA.
DR PIR; S50945; S50945.
DR RefSeq; NP_013666.1; NM_001182404.1.
DR AlphaFoldDB; Q04705; -.
DR BioGRID; 35121; 93.
DR STRING; 4932.YML047C; -.
DR TCDB; 1.A.88.1.2; the fungal potassium channel (f-kch) family.
DR iPTMnet; Q04705; -.
DR PaxDb; Q04705; -.
DR PRIDE; Q04705; -.
DR EnsemblFungi; YML047C_mRNA; YML047C; YML047C.
DR GeneID; 854959; -.
DR KEGG; sce:YML047C; -.
DR SGD; S000004510; PRM6.
DR VEuPathDB; FungiDB:YML047C; -.
DR eggNOG; ENOG502QVFG; Eukaryota.
DR GeneTree; ENSGT00940000176676; -.
DR HOGENOM; CLU_036942_0_0_1; -.
DR InParanoid; Q04705; -.
DR OMA; PFLEFRI; -.
DR BioCyc; YEAST:G3O-32644-MON; -.
DR PRO; PR:Q04705; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04705; protein.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
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:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0005775; C:vacuolar lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; IGI:SGD.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IGI:SGD.
DR InterPro; IPR031606; Kch1/2.
DR PANTHER; PTHR36424; PTHR36424; 1.
DR Pfam; PF16944; KCH; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..352
FT /note="Pheromone-regulated membrane protein 6"
FT /id="PRO_0000203256"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P47114"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P47114"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..227
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P47114"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P47114"
SQ SEQUENCE 352 AA; 41372 MW; 7B9CCDB3F34BE722 CRC64;
MESSLQKLKF QDIDINLIPT AKWTTKLQYI LYTWCQSILH VAMFFSDIYT CIKLLAFNTW
SNNIIQPFLE FRISKWLFSG CILCSSLILI WELVIGLRVY RKKEITSNYM NGISRLINCL
FNFKKYQIFE LIVLTDEKKF SKWLFFSYFE ISGCLRLLFG DSPRQIINGL TLWSVLLTVS
NETSSGTHST QSLGNLDDLN GIINKIKHIA KTNYEESVIL SFMLFSFIIW VILISKLILS
IIIFIIFIRP RFLSSKRKVK GYELKLRKYV SKVIDENLSR TVYELGILID DEEEGTICGD
NKTQKKFDYD SPDYGDESTI PSYYCYSDVE TYERVYTPIK AYFPQKYKHK YI
