TOK1_YEAST
ID TOK1_YEAST Reviewed; 691 AA.
AC P40310; D6VW91; Q05721;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Outward-rectifier potassium channel TOK1;
DE AltName: Full=Two-domain outward rectifier K(+) channel YORK;
GN Name=TOK1; Synonyms=DUK1; OrderedLocusNames=YJL093C; ORFNames=J0911;
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], AND CHARACTERIZATION.
RC STRAIN=NY13;
RX PubMed=7651518; DOI=10.1038/376690a0;
RA Ketchum K.A., Joiner W.J., Sellers A.J., Kaczmarek L.K., Goldstein S.A.N.;
RT "A new family of outwardly rectifying potassium channel proteins with two
RT pore domains in tandem.";
RL Nature 376:690-695(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8723646;
RA Reid J.D., Lukas W., Shafaatian R., Bertl A., Scheurmann-Kettner C.,
RA Guy H.R., North R.A.;
RT "The S. cerevisiae outwardly-rectifying potassium channel (DUK1) identifies
RT a new family of channels with duplicated pore domains.";
RL Recept. Channels 4:51-62(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8626760; DOI=10.1074/jbc.271.8.4183;
RA Lesage F., Guillemare E., Fink M., Duprat F., Lazdunski M., Romey G.,
RA Barhanin J.;
RT "A pH-sensitive yeast outward rectifier K+ channel with two pore domains
RT and novel gating properties.";
RL J. Biol. Chem. 271:4183-4187(1996).
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Outwardly rectifying potassium channel.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000305}.
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DR EMBL; U28005; AAC49070.1; -; Genomic_DNA.
DR EMBL; X94403; CAA64176.1; -; Genomic_DNA.
DR EMBL; U37254; AAC49168.1; -; Genomic_DNA.
DR EMBL; X77087; CAA54360.1; -; Genomic_DNA.
DR EMBL; Z49368; CAA89386.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08707.1; -; Genomic_DNA.
DR PIR; S46585; S46585.
DR RefSeq; NP_012442.1; NM_001181526.1.
DR AlphaFoldDB; P40310; -.
DR BioGRID; 33664; 64.
DR DIP; DIP-8165N; -.
DR IntAct; P40310; 1.
DR MINT; P40310; -.
DR STRING; 4932.YJL093C; -.
DR TCDB; 1.A.1.7.1; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; P40310; -.
DR MaxQB; P40310; -.
DR PaxDb; P40310; -.
DR PRIDE; P40310; -.
DR DNASU; 853352; -.
DR EnsemblFungi; YJL093C_mRNA; YJL093C; YJL093C.
DR GeneID; 853352; -.
DR KEGG; sce:YJL093C; -.
DR SGD; S000003629; TOK1.
DR VEuPathDB; FungiDB:YJL093C; -.
DR eggNOG; KOG1418; Eukaryota.
DR GeneTree; ENSGT00940000174000; -.
DR HOGENOM; CLU_013394_2_0_1; -.
DR InParanoid; P40310; -.
DR OMA; RVFFVSW; -.
DR BioCyc; YEAST:G3O-31548-MON; -.
DR Reactome; R-SCE-1299287; Tandem pore domain halothane-inhibited K+ channel (THIK).
DR Reactome; R-SCE-1299308; Tandem of pore domain in a weak inwardly rectifying K+ channels (TWIK).
DR Reactome; R-SCE-1299316; TWIK-releated acid-sensitive K+ channel (TASK).
DR Reactome; R-SCE-1299344; TWIK-related spinal cord K+ channel (TRESK).
DR Reactome; R-SCE-1299361; TWIK-related alkaline pH activated K+ channel (TALK).
DR Reactome; R-SCE-1299503; TWIK related potassium channel (TREK).
DR Reactome; R-SCE-5576886; Phase 4 - resting membrane potential.
DR PRO; PR:P40310; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P40310; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0005267; F:potassium channel activity; IDA:SGD.
DR GO; GO:0022841; F:potassium ion leak channel activity; IBA:GO_Central.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IMP:SGD.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IDA:SGD.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR11003; PTHR11003; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PRINTS; PR01333; 2POREKCHANEL.
PE 1: Evidence at protein level;
KW Ion channel; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..691
FT /note="Outward-rectifier potassium channel TOK1"
FT /id="PRO_0000101774"
FT TOPO_DOM 1..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical; Name=S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..137
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical; Name=S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical; Name=S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..203
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical; Name=S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..266
FT /note="Helical; Name=S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..301
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical; Name=S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical; Name=S7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..435
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical; Name=S8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..691
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 504..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 442
FT /note="A -> T (in Ref. 2; CAA64176)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="E -> G (in Ref. 2; CAA64176)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 691 AA; 77408 MW; 507167E487B77AAF CRC64;
MTRFMNSFAK QTLGYGNMAT VEQESSAQAV DSHSNNTPKQ AKGVLAEELK DALRFRDERV
SIINAEPSST LFVFWFVVSC YFPVITACLG PVANTISIAC VVEKWRSLKN NSVVTNPRSN
DTDVLMNQVK TVFDPPGIFA VNIISLVLGF TSNIILMLHF SKKLTYLKSQ LINITGWTIA
GGMLLVDVIV CSLNDMPSIY SKTIGFWFAC ISSGLYLVCT IILTIHFIGY KLGKYPPTFN
LLPNERSIMA YTVLLSLWLI WGAGMFSGLL HITYGNALYF CTVSLLTVGL GDILPKSVGA
KIMVLIFSLS GVVLMGLIVF MTRSIIQKSS GPIFFFHRVE KGRSKSWKHY MDSSKNLSER
EAFDLMKCIR QTASRKQHWF SLSVTIAIFM AFWLLGALVF KFAENWSYFN CIYFCFLCLL
TIGYGDYAPR TGAGRAFFVI WALGAVPLMG AILSTVGDLL FDISTSLDIK IGESFNNKVK
SIVFNGRQRA LSFMVNTGEI FEESDTADGD LEENTTSSQS SQISEFNDNN SEENDSGVTS
PPASLQESFS SLSKASSPEG ILPLEYVSSA EYALQDSGTC NLRNLQELLK AVKKLHRICL
ADKDYTLSFS DWSYIHKLHL RNITDIEEYT RGPEFWISPD TPLKFPLNEP HFAFMMLFKN
IEELVGNLVE DEELYKVISK RKFLGEHRKT L
