KCNK1_MOUSE
ID KCNK1_MOUSE Reviewed; 336 AA.
AC O08581; Q99L99;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Potassium channel subfamily K member 1;
DE AltName: Full=Inward rectifying potassium channel protein TWIK-1 {ECO:0000303|PubMed:9013852};
GN Name=Kcnk1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9013852; DOI=10.1016/s0014-5793(96)01491-3;
RA Lesage F., Lauritzen I., Duprat F., Reyes R., Fink M., Heurteaux C.,
RA Lazdunski M.;
RT "The structure, function and distribution of the mouse TWIK-1 K+ channel.";
RL FEBS Lett. 402:28-32(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=129/SvJ; TISSUE=Liver;
RX PubMed=9559671; DOI=10.1016/s0014-5793(98)00260-9;
RA Arrighi I., Lesage F., Scimeca J.-C., Carle G.F., Barhanin J.;
RT "Structure, chromosome localization, and tissue distribution of the mouse
RT twik K+ channel gene.";
RL FEBS Lett. 425:310-316(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12855359; DOI=10.1016/s0378-5955(03)00162-x;
RA Nicolas M.T., Barhanin J., Reyes R., Dememes D.;
RT "Cellular localization of TWIK-1, a two-pore-domain potassium channel in
RT the rodent inner ear.";
RL Hear. Res. 181:20-26(2003).
RN [6]
RP IDENTIFICATION IN A COMPLEX WITH PSD AND ARF6, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15540117; DOI=10.1038/sj.embor.7400292;
RA Decressac S., Franco M., Bendahhou S., Warth R., Knauer S., Barhanin J.,
RA Lazdunski M., Lesage F.;
RT "ARF6-dependent interaction of the TWIK1 K+ channel with EFA6, a GDP/GTP
RT exchange factor for ARF6.";
RL EMBO Rep. 5:1171-1175(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=16025300; DOI=10.1007/s00424-005-1480-9;
RA Nie X., Arrighi I., Kaissling B., Pfaff I., Mann J., Barhanin J.,
RA Vallon V.;
RT "Expression and insights on function of potassium channel TWIK-1 in mouse
RT kidney.";
RL Pflugers Arch. 451:479-488(2005).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=16847696; DOI=10.1007/s00424-006-0107-0;
RA Millar I.D., Taylor H.C., Cooper G.J., Kibble J.D., Barhanin J., Robson L.;
RT "Adaptive downregulation of a quinidine-sensitive cation conductance in
RT renal principal cells of TWIK-1 knockout mice.";
RL Pflugers Arch. 453:107-116(2006).
RN [9]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=17079103; DOI=10.1016/j.heares.2006.09.002;
RA Chen W.C., Davis R.L.;
RT "Voltage-gated and two-pore-domain potassium channels in murine spiral
RT ganglion neurons.";
RL Hear. Res. 222:89-99(2006).
RN [10]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=18222039; DOI=10.1016/j.neuroscience.2007.12.011;
RA Aller M.I., Wisden W.;
RT "Changes in expression of some two-pore domain potassium channel genes
RT (KCNK) in selected brain regions of developing mice.";
RL Neuroscience 151:1154-1172(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 293-ILE-MET-294.
RX PubMed=19959478; DOI=10.1074/jbc.m109.078535;
RA Feliciangeli S., Tardy M.P., Sandoz G., Chatelain F.C., Warth R.,
RA Barhanin J., Bendahhou S., Lesage F.;
RT "Potassium channel silencing by constitutive endocytosis and intracellular
RT sequestration.";
RL J. Biol. Chem. 285:4798-4805(2010).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22431633; DOI=10.1073/pnas.1201132109;
RA Chatelain F.C., Bichet D., Douguet D., Feliciangeli S., Bendahhou S.,
RA Reichold M., Warth R., Barhanin J., Lesage F.;
RT "TWIK1, a unique background channel with variable ion selectivity.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5499-5504(2012).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=24368895; DOI=10.3389/fncel.2013.00246;
RA Wang W., Putra A., Schools G.P., Ma B., Chen H., Kaczmarek L.K.,
RA Barhanin J., Lesage F., Zhou M.;
RT "The contribution of TWIK-1 channels to astrocyte K(+) current is limited
RT by retention in intracellular compartments.";
RL Front. Cell. Neurosci. 7:246-246(2013).
RN [15]
RP REVIEW.
RX PubMed=25530075; DOI=10.1113/jphysiol.2014.287268;
RA Feliciangeli S., Chatelain F.C., Bichet D., Lesage F.;
RT "The family of K2P channels: salient structural and functional
RT properties.";
RL J. Physiol. (Lond.) 593:2587-2603(2015).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25406588; DOI=10.1186/s13041-014-0080-z;
RA Yarishkin O., Lee D.Y., Kim E., Cho C.H., Choi J.H., Lee C.J., Hwang E.M.,
RA Park J.Y.;
RT "TWIK-1 contributes to the intrinsic excitability of dentate granule cells
RT in mouse hippocampus.";
RL Mol. Brain 7:80-80(2014).
RN [17]
RP FUNCTION, SUBUNIT, INTERACTION WITH KCNK2 AND GNG4, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, MUTAGENESIS OF CYS-69 AND GLY-119, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24496152; DOI=10.1038/ncomms4227;
RA Hwang E.M., Kim E., Yarishkin O., Woo D.H., Han K.S., Park N., Bae Y.,
RA Woo J., Kim D., Park M., Lee C.J., Park J.Y.;
RT "A disulphide-linked heterodimer of TWIK-1 and TREK-1 mediates passive
RT conductance in astrocytes.";
RL Nat. Commun. 5:3227-3227(2014).
RN [18]
RP REVIEW.
RX PubMed=25339226; DOI=10.1007/s00424-014-1631-y;
RA Bichet D., Blin S., Feliciangeli S., Chatelain F.C., Bobak N., Lesage F.;
RT "Silent but not dumb: how cellular trafficking and pore gating modulate
RT expression of TWIK1 and THIK2.";
RL Pflugers Arch. 467:1121-1131(2015).
CC -!- FUNCTION: Ion channel that contributes to passive transmembrane
CC potassium transport and to the regulation of the resting membrane
CC potential in brain astrocytes, but also in kidney and in other tissues
CC (PubMed:16847696, PubMed:22431633, PubMed:24368895). Forms dimeric
CC channels through which potassium ions pass in accordance with their
CC electrochemical gradient. The channel is selective for K(+) ions at
CC physiological potassium concentrations and at neutral pH, but becomes
CC permeable to Na(+) at subphysiological K(+) levels and upon
CC acidification of the extracellular medium. The homodimer has very low
CC potassium channel activity, when expressed in heterologous systems, and
CC can function as weakly inward rectifying potassium channel
CC (PubMed:9013852, PubMed:24496152). Channel activity is modulated by
CC activation of serotonin receptors (PubMed:24368895). Heterodimeric
CC channels containing KCNK1 and KCNK2 have much higher activity, and may
CC represent the predominant form in astrocytes (PubMed:24496152).
CC Heterodimeric channels containing KCNK1 and KCNK3 or KCNK9 have much
CC higher activity. Heterodimeric channels formed by KCNK1 and KCNK9 may
CC contribute to halothane-sensitive currents (By similarity). Mediates
CC outward rectifying potassium currents in dentate gyrus granule cells
CC and contributes to the regulation of their resting membrane potential
CC (PubMed:25406588). Contributes to the regulation of action potential
CC firing in dentate gyrus granule cells and down-regulates their
CC intrinsic excitability (PubMed:25406588). In astrocytes, the
CC heterodimer formed by KCNK1 and KCNK2 is required for rapid glutamate
CC release in response to activation of G-protein coupled receptors, such
CC as F2R and CNR1 (PubMed:24496152). Required for normal ion and water
CC transport in the kidney (PubMed:16025300). Contributes to the
CC regulation of the resting membrane potential of pancreatic beta cells
CC (PubMed:22431633). The low channel activity of homodimeric KCNK1 may be
CC due to sumoylation. The low channel activity may be due to rapid
CC internalization from the cell membrane and retention in recycling
CC endosomes (PubMed:15540117). {ECO:0000250|UniProtKB:O00180,
CC ECO:0000250|UniProtKB:Q9Z2T2, ECO:0000269|PubMed:15540117,
CC ECO:0000269|PubMed:16025300, ECO:0000269|PubMed:16847696,
CC ECO:0000269|PubMed:22431633, ECO:0000269|PubMed:24368895,
CC ECO:0000269|PubMed:24496152, ECO:0000269|PubMed:9013852}.
CC -!- ACTIVITY REGULATION: Inhibited by quinine, quinidine, barium, and
CC internal acidification. {ECO:0000269|PubMed:9013852,
CC ECO:0000305|PubMed:16847696}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=Both activation and channel closure are very rapid. Is not
CC voltage-gated (PubMed:22431633, PubMed:24496152). The relationship
CC between voltage and current is nearly linear (PubMed:22431633,
CC PubMed:24496152). {ECO:0000269|PubMed:22431633,
CC ECO:0000269|PubMed:24496152, ECO:0000305};
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:9013852). Heterodimer with
CC KCNK2; disulfide-linked (PubMed:24496152). In astrocytes, forms mostly
CC heterodimeric potassium channels with KCNK2, with only a minor
CC proportion of functional channels containing homodimeric KCNK1 (By
CC similarity). Interacts with KCNK3 and KCNK9, forming functional
CC heterodimeric channels (By similarity). Interacts with GNG4
CC (PubMed:24496152). Identified in a complex with PSD and ARF6; interacts
CC only with PSD that is bound to ARF6 (PubMed:15540117). Interacts with
CC UBE2I (By similarity). {ECO:0000250|UniProtKB:O00180,
CC ECO:0000269|PubMed:15540117, ECO:0000269|PubMed:24496152,
CC ECO:0000269|PubMed:9013852}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15540117,
CC ECO:0000269|PubMed:19959478, ECO:0000269|PubMed:24368895,
CC ECO:0000269|PubMed:24496152, ECO:0000269|PubMed:9013852}; Multi-pass
CC membrane protein {ECO:0000305}. Recycling endosome
CC {ECO:0000269|PubMed:15540117}. Apical cell membrane
CC {ECO:0000269|PubMed:12855359, ECO:0000305|PubMed:16025300}. Cytoplasmic
CC vesicle {ECO:0000269|PubMed:16025300, ECO:0000269|PubMed:24368895}.
CC Perikaryon {ECO:0000269|PubMed:12855359, ECO:0000269|PubMed:17079103,
CC ECO:0000269|PubMed:25406588}. Cell projection, dendrite
CC {ECO:0000269|PubMed:25406588}. Cell projection
CC {ECO:0000269|PubMed:17079103}. Synaptic cell membrane
CC {ECO:0000250|UniProtKB:Q9Z2T2}. Note=The heterodimer with KCNK2 is
CC detected at the astrocyte cell membrane (PubMed:24496152). Not detected
CC at the astrocyte cell membrane when KCNK2 is absent (PubMed:24496152).
CC Detected on neuronal cell bodies, and to a lesser degree on neuronal
CC cell projections (PubMed:12855359, PubMed:17079103). Detected on
CC hippocampus dentate gyrus granule cell bodies and to a lesser degree on
CC proximal dendrites (PubMed:25406588). Detected at the apical cell
CC membrane in stria vascularis in the cochlea (By similarity). Detected
CC at the apical cell membrane of vestibular dark cells situated between
CC the crista and the utricle in the inner ear (PubMed:12855359). Detected
CC at the apical cell membrane in stria vascularis in the cochlea
CC (PubMed:12855359). Detected at the apical cell membrane in kidney
CC proximal tubule segment S1 and in subapical compartments in segments
CC S1, S2 and S3 (PubMed:16025300). Predominantly in cytoplasmic
CC structures in kidney distal convoluted tubules and collecting ducts
CC (PubMed:16025300). Predominantly in cytoplasmic structures in
CC hippocampus astrocytes; only a minor proportion of the protein is
CC present at the cell membrane (PubMed:24368895).
CC {ECO:0000250|UniProtKB:Q9Z2T2, ECO:0000269|PubMed:16025300,
CC ECO:0000269|PubMed:17079103, ECO:0000269|PubMed:24368895,
CC ECO:0000269|PubMed:24496152, ECO:0000269|PubMed:25406588}.
CC -!- TISSUE SPECIFICITY: Detected in spiral ganglion neurons
CC (PubMed:17079103). Detected in hippocampus CA1 and CA1 regions and in
CC the molecular layer of the dentate gyrus (PubMed:24368895,
CC PubMed:25406588). Detected on hippocampus astrocytes (PubMed:24368895,
CC PubMed:24496152). Highly expressed in the stria vascularis in the
CC cochlea (PubMed:12855359). Detected in pancreas islet beta cells
CC (PubMed:22431633). Detected in kidney, at brush border membranes in
CC proximal tubules and in cytoplasmic structures in distal convoluted
CC tubules, thick ascending limbs and collecting ducts (at protein level)
CC (PubMed:15540117, PubMed:16025300). Widely expressed. Detected in
CC spiral ganglion cells (PubMed:17079103). Highest expression in brain,
CC kidney, thyroid, salivary gland, adrenal gland, prostate, epididymis,
CC uterus, placenta, colon and jejunum. Moderate expression in eyes,
CC pituitary, pancreas, smooth muscle, testis and ovary. Very low levels
CC in lung, aorta, liver, heart, skeletal muscle, thymus and spleen. In
CC the brain, highest expression in cerebellar granule cells, brainstem,
CC hippocampus and cerebral cortex (PubMed:18222039).
CC {ECO:0000269|PubMed:15540117, ECO:0000269|PubMed:16025300,
CC ECO:0000269|PubMed:18222039, ECO:0000269|PubMed:22431633,
CC ECO:0000269|PubMed:24368895, ECO:0000269|PubMed:25406588,
CC ECO:0000269|PubMed:9013852, ECO:0000269|PubMed:9559671}.
CC -!- DEVELOPMENTAL STAGE: Detected at very low levels in the embryonic
CC central nervous system (PubMed:9559671, PubMed:18222039). Detected as
CC early as 7 days post conception (PubMed:9559671). Detected in dorsal
CC root ganglia, hippocampus, olfactory epithelia and intestine at 19 dpc
CC (PubMed:18222039). Expression in the brain increases strongly 3-8 days
CC after birth, a period of intense postnatal brain development
CC (PubMed:9559671, PubMed:18222039). Detected in dentate granule cells;
CC expression levels show no significant variability during postnatal
CC development (PubMed:18222039). Expression is higher in adults than in
CC neonates (PubMed:9559671, PubMed:18222039).
CC {ECO:0000269|PubMed:18222039, ECO:0000269|PubMed:9559671}.
CC -!- PTM: Sumoylation is controversial. Sumoylated by UBE2I. Not sumoylated
CC when expressed in xenopus oocytes or mammalian cells. Sumoylation
CC inactivates the channel, but does not interfere with expression at the
CC cell membrane. Sumoylation of a single subunit is sufficient to silence
CC the dimeric channel. Sumoylation of KCNK1 is sufficient to silence
CC heterodimeric channels formed by KCNK1 and KCNK3 or KCNK9. Desumoylated
CC by SENP1; this activates the channel. Desumoylated by SENP1; this
CC strongly increases halothane-mediated activation of heterodimeric
CC channels formed with KCNK9. SENP1 treatment has no effect.
CC {ECO:0000250|UniProtKB:O00180}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype on standard chow, excepting
CC a lower urinary flow rate (PubMed:16025300). Mice appear normal and are
CC fertile (PubMed:24368895). When kept on a low phosphate diet, both
CC wild-type and mutant mice show strongly reduced urinary phosphate
CC secretion. Still, mutant mice display higher fractional urinary
CC phosphate secretion relative to wild-type, leading to reduced inorganic
CC phosphate levels in blood plasma. The impaired phosphate homeostasis
CC seems to be due to indirect effects on the expression of other
CC transporters, such as SLC34A1 and AQP2 (PubMed:16025300). Principal
CC cells from kidney collecting duct are hyperpolarized, display reduced
CC potassium conductance and strongly reduced quinidine-sensitive
CC potassium channel activity (PubMed:16847696). Besides, collecting ducts
CC from mutant mouse kidney display a larger diameter relative to wild-
CC type (PubMed:16847696). {ECO:0000269|PubMed:16025300,
CC ECO:0000269|PubMed:16847696, ECO:0000269|PubMed:24368895}.
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; AF033017; AAC16973.1; -; mRNA.
DR EMBL; CH466525; EDL11808.1; -; Genomic_DNA.
DR EMBL; BC003729; AAH03729.1; -; mRNA.
DR CCDS; CCDS22783.1; -.
DR RefSeq; NP_032456.2; NM_008430.2.
DR AlphaFoldDB; O08581; -.
DR SMR; O08581; -.
DR BioGRID; 200907; 46.
DR IntAct; O08581; 45.
DR STRING; 10090.ENSMUSP00000046103; -.
DR TCDB; 1.A.1.8.1; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; O08581; 1 site.
DR iPTMnet; O08581; -.
DR PhosphoSitePlus; O08581; -.
DR SwissPalm; O08581; -.
DR MaxQB; O08581; -.
DR PaxDb; O08581; -.
DR PeptideAtlas; O08581; -.
DR PRIDE; O08581; -.
DR ProteomicsDB; 263403; -.
DR Antibodypedia; 20802; 311 antibodies from 32 providers.
DR DNASU; 16525; -.
DR Ensembl; ENSMUST00000046765; ENSMUSP00000046103; ENSMUSG00000033998.
DR GeneID; 16525; -.
DR KEGG; mmu:16525; -.
DR UCSC; uc009nyr.3; mouse.
DR CTD; 3775; -.
DR MGI; MGI:109322; Kcnk1.
DR VEuPathDB; HostDB:ENSMUSG00000033998; -.
DR eggNOG; KOG1418; Eukaryota.
DR GeneTree; ENSGT00940000155293; -.
DR HOGENOM; CLU_022504_6_0_1; -.
DR InParanoid; O08581; -.
DR OMA; MVAIVHA; -.
DR OrthoDB; 1211599at2759; -.
DR PhylomeDB; O08581; -.
DR TreeFam; TF313947; -.
DR Reactome; R-MMU-1299308; Tandem of pore domain in a weak inwardly rectifying K+ channels (TWIK).
DR Reactome; R-MMU-5576886; Phase 4 - resting membrane potential.
DR BioGRID-ORCS; 16525; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Kcnk1; mouse.
DR PRO; PR:O08581; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; O08581; protein.
DR Bgee; ENSMUSG00000033998; Expressed in seminal vesicle and 243 other tissues.
DR ExpressionAtlas; O08581; baseline and differential.
DR Genevisible; O08581; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:1902937; C:inward rectifier potassium channel complex; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0034705; C:potassium channel complex; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0097060; C:synaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IDA:UniProtKB.
DR GO; GO:0005267; F:potassium channel activity; IDA:MGI.
DR GO; GO:0022841; F:potassium ion leak channel activity; ISS:UniProtKB.
DR GO; GO:0005272; F:sodium channel activity; ISS:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; IC:MGI.
DR GO; GO:0060075; P:regulation of resting membrane potential; ISS:UniProtKB.
DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR003092; 2pore_dom_K_chnl_TASK.
DR InterPro; IPR005408; 2pore_dom_K_chnl_TWIK.
DR InterPro; IPR001779; 2pore_dom_K_chnl_TWIK1.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR11003; PTHR11003; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PIRSF; PIRSF038061; K_channel_subfamily_K_type; 1.
DR PRINTS; PR01333; 2POREKCHANEL.
DR PRINTS; PR01096; TWIK1CHANNEL.
DR PRINTS; PR01586; TWIKCHANNEL.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cytoplasmic vesicle; Disulfide bond;
KW Endosome; Glycoprotein; Ion channel; Ion transport; Isopeptide bond;
KW Membrane; Phosphoprotein; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Synapse; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..336
FT /note="Potassium channel subfamily K member 1"
FT /id="PRO_0000101741"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT TOPO_DOM 42..103
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT INTRAMEM 104..116
FT /note="Helical; Name=Pore helix 1"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT INTRAMEM 117..122
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT TOPO_DOM 123..132
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT TRANSMEM 133..156
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT TOPO_DOM 157..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT TOPO_DOM 203..211
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT INTRAMEM 212..224
FT /note="Helical; Name=Pore helix 2"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT INTRAMEM 225..231
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT TOPO_DOM 232..243
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT TRANSMEM 244..267
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT TOPO_DOM 268..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT REGION 117..122
FT /note="Selectivity filter 1"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT REGION 225..230
FT /note="Selectivity filter 2"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT REGION 293..299
FT /note="Important for intracellular retention in recycling
FT endosomes"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT REGION 310..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 118
FT /note="Important for increased permeability to Na(+) when
FT K(+) levels are subphysiological"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT SITE 146
FT /note="Part of a hydrophobic barrier that is stochastically
FT dewetted and limits ion permeability"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT SITE 261
FT /note="Part of a hydrophobic barrier that is stochastically
FT dewetted and limits ion permeability"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2T2"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 69
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:O00180,
FT ECO:0000269|PubMed:24496152"
FT CROSSLNK 274
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT MUTAGEN 69
FT /note="C->S: Abolishes formation of a disulfide-linked
FT heterodimer with KCNK2."
FT /evidence="ECO:0000269|PubMed:24496152"
FT MUTAGEN 119
FT /note="G->E: Abolishes potassium channel activity."
FT /evidence="ECO:0000269|PubMed:24496152"
FT MUTAGEN 293..294
FT /note="IM->AA: Increases channel expression at the cell
FT membrane, resulting in higher channel activity."
FT /evidence="ECO:0000269|PubMed:19959478"
FT CONFLICT 44
FT /note="V -> E (in Ref. 1; AAC16973)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="V -> L (in Ref. 1; AAC16973)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="A -> T (in Ref. 1; AAC16973)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 336 AA; 38201 MW; 76B7FD5361A6216C CRC64;
MLQSLAGSSC VRLVERHRSA WCFGFLVLGY LLYLVFGAVV FSSVELPYED LLRQELRKLK
RRFLEEHECL SEPQLEQFLG RVLEASNYGV SVLSNASGNW NWDFTSALFF ASTVLSTTGY
GHTVPLSDGG KAFCIIYSVI GIPFTLLFLT AVVQRVTVHV TRRPVLYFHI RWGFSKQVVA
IVHAVLLGFV TVSCFFFIPA AVFSVLEDDW NFLESFYFCF ISLSTIGLGD YVPGEGYNQK
FRELYKIGIT CYLLLGLIAM LVVLETFCEL HELKKFRKMF YVKKDKDEDL VHIMEHDQLS
FSSVTEQVAG LKEEQKQSEP FVASQSPPYE DGSADH
