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 24-JAN-2024, entry version 182. 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 CC (TC 1.A.1.8) family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; O08581; 1 site, No reported glycans. DR GlyGen; O08581; 1 site. DR iPTMnet; O08581; -. DR PhosphoSitePlus; O08581; -. DR SwissPalm; O08581; -. DR MaxQB; O08581; -. DR PaxDb; 10090-ENSMUSP00000046103; -. DR PeptideAtlas; O08581; -. DR ProteomicsDB; 263403; -. DR Antibodypedia; 20802; 335 antibodies from 32 providers. DR DNASU; 16525; -. DR Ensembl; ENSMUST00000046765.10; ENSMUSP00000046103.9; ENSMUSG00000033998.10. DR GeneID; 16525; -. DR KEGG; mmu:16525; -. DR UCSC; uc009nyr.3; mouse. DR AGR; MGI:109322; -. 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; SAWCFGL; -. DR OrthoDB; 600333at2759; -. 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 77 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 245 other cell types or tissues. DR ExpressionAtlas; O08581; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI. DR GO; GO:0031526; C:brush border membrane; ISO:MGI. DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell. DR GO; GO:0005768; C:endosome; IDA:MGI. 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:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IMP:UniProtKB. 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:0015271; F:outward rectifier potassium channel activity; IBA:GO_Central. 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 Gene3D; 1.10.287.70; -; 1. 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:SF59; POTASSIUM CHANNEL SUBFAMILY K MEMBER 1; 1. DR PANTHER; PTHR11003; POTASSIUM CHANNEL, SUBFAMILY K; 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. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 2. DR Genevisible; O08581; MM. 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 //