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Potassium channel subfamily K member 1 (Inward rectifying potassium channel protein TWIK-1)

 KCNK1_MOUSE             Reviewed;         336 AA.
O08581; Q99L99;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
25-OCT-2017, entry version 149.
RecName: Full=Potassium channel subfamily K member 1;
AltName: Full=Inward rectifying potassium channel protein TWIK-1 {ECO:0000303|PubMed:9013852};
Name=Kcnk1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, SUBUNIT,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=9013852; DOI=10.1016/S0014-5793(96)01491-3;
Lesage F., Lauritzen I., Duprat F., Reyes R., Fink M., Heurteaux C.,
Lazdunski M.;
"The structure, function and distribution of the mouse TWIK-1 K+
channel.";
FEBS Lett. 402:28-32(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
STRAIN=129/SvJ; TISSUE=Liver;
PubMed=9559671; DOI=10.1016/S0014-5793(98)00260-9;
Arrighi I., Lesage F., Scimeca J.-C., Carle G.F., Barhanin J.;
"Structure, chromosome localization, and tissue distribution of the
mouse twik K+ channel gene.";
FEBS Lett. 425:310-316(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=12855359; DOI=10.1016/S0378-5955(03)00162-X;
Nicolas M.T., Barhanin J., Reyes R., Dememes D.;
"Cellular localization of TWIK-1, a two-pore-domain potassium channel
in the rodent inner ear.";
Hear. Res. 181:20-26(2003).
[6]
IDENTIFICATION IN A COMPLEX WITH PSD AND ARF6, TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
PubMed=15540117; DOI=10.1038/sj.embor.7400292;
Decressac S., Franco M., Bendahhou S., Warth R., Knauer S.,
Barhanin J., Lazdunski M., Lesage F.;
"ARF6-dependent interaction of the TWIK1 K+ channel with EFA6, a
GDP/GTP exchange factor for ARF6.";
EMBO Rep. 5:1171-1175(2004).
[7]
FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
SPECIFICITY.
PubMed=16025300; DOI=10.1007/s00424-005-1480-9;
Nie X., Arrighi I., Kaissling B., Pfaff I., Mann J., Barhanin J.,
Vallon V.;
"Expression and insights on function of potassium channel TWIK-1 in
mouse kidney.";
Pflugers Arch. 451:479-488(2005).
[8]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=16847696; DOI=10.1007/s00424-006-0107-0;
Millar I.D., Taylor H.C., Cooper G.J., Kibble J.D., Barhanin J.,
Robson L.;
"Adaptive downregulation of a quinidine-sensitive cation conductance
in renal principal cells of TWIK-1 knockout mice.";
Pflugers Arch. 453:107-116(2006).
[9]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=17079103; DOI=10.1016/j.heares.2006.09.002;
Chen W.C., Davis R.L.;
"Voltage-gated and two-pore-domain potassium channels in murine spiral
ganglion neurons.";
Hear. Res. 222:89-99(2006).
[10]
DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
PubMed=18222039; DOI=10.1016/j.neuroscience.2007.12.011;
Aller M.I., Wisden W.;
"Changes in expression of some two-pore domain potassium channel genes
(KCNK) in selected brain regions of developing mice.";
Neuroscience 151:1154-1172(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 293-ILE-MET-294.
PubMed=19959478; DOI=10.1074/jbc.M109.078535;
Feliciangeli S., Tardy M.P., Sandoz G., Chatelain F.C., Warth R.,
Barhanin J., Bendahhou S., Lesage F.;
"Potassium channel silencing by constitutive endocytosis and
intracellular sequestration.";
J. Biol. Chem. 285:4798-4805(2010).
[13]
FUNCTION, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=22431633; DOI=10.1073/pnas.1201132109;
Chatelain F.C., Bichet D., Douguet D., Feliciangeli S., Bendahhou S.,
Reichold M., Warth R., Barhanin J., Lesage F.;
"TWIK1, a unique background channel with variable ion selectivity.";
Proc. Natl. Acad. Sci. U.S.A. 109:5499-5504(2012).
[14]
FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
SPECIFICITY.
PubMed=24368895; DOI=10.3389/fncel.2013.00246;
Wang W., Putra A., Schools G.P., Ma B., Chen H., Kaczmarek L.K.,
Barhanin J., Lesage F., Zhou M.;
"The contribution of TWIK-1 channels to astrocyte K(+) current is
limited by retention in intracellular compartments.";
Front. Cell. Neurosci. 7:246-246(2013).
[15]
REVIEW.
PubMed=25530075; DOI=10.1113/jphysiol.2014.287268;
Feliciangeli S., Chatelain F.C., Bichet D., Lesage F.;
"The family of K2P channels: salient structural and functional
properties.";
J. Physiol. (Lond.) 593:2587-2603(2015).
[16]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=25406588; DOI=10.1186/s13041-014-0080-z;
Yarishkin O., Lee D.Y., Kim E., Cho C.H., Choi J.H., Lee C.J.,
Hwang E.M., Park J.Y.;
"TWIK-1 contributes to the intrinsic excitability of dentate granule
cells in mouse hippocampus.";
Mol. Brain 7:80-80(2014).
[17]
FUNCTION, SUBUNIT, INTERACTION WITH KCNK2 AND GNG4, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-69 AND GLY-119, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=24496152; DOI=10.1038/ncomms4227;
Hwang E.M., Kim E., Yarishkin O., Woo D.H., Han K.S., Park N., Bae Y.,
Woo J., Kim D., Park M., Lee C.J., Park J.Y.;
"A disulphide-linked heterodimer of TWIK-1 and TREK-1 mediates passive
conductance in astrocytes.";
Nat. Commun. 5:3227-3227(2014).
[18]
REVIEW.
PubMed=25339226; DOI=10.1007/s00424-014-1631-y;
Bichet D., Blin S., Feliciangeli S., Chatelain F.C., Bobak N.,
Lesage F.;
"Silent but not dumb: how cellular trafficking and pore gating
modulate expression of TWIK1 and THIK2.";
Pflugers Arch. 467:1121-1131(2015).
-!- FUNCTION: Ion channel that contributes to passive transmembrane
potassium transport and to the regulation of the resting membrane
potential in brain astrocytes, but also in kidney and in other
tissues (PubMed:16847696, PubMed:22431633, PubMed:24368895). Forms
dimeric channels through which potassium ions pass in accordance
with their electrochemical gradient. The channel is selective for
K(+) ions at physiological potassium concentrations and at neutral
pH, but becomes permeable to Na(+) at subphysiological K(+) levels
and upon acidification of the extracellular medium. The homodimer
has very low potassium channel activity, when expressed in
heterologous systems, and can function as weakly inward rectifying
potassium channel (PubMed:9013852, PubMed:24496152). Channel
activity is modulated by activation of serotonin receptors
(PubMed:24368895). Heterodimeric channels containing KCNK1 and
KCNK2 have much higher activity, and may represent the predominant
form in astrocytes (PubMed:24496152). Heterodimeric channels
containing KCNK1 and KCNK3 or KCNK9 have much higher activity.
Heterodimeric channels formed by KCNK1 and KCNK9 may contribute to
halothane-sensitive currents (By similarity). Mediates outward
rectifying potassium currents in dentate gyrus granule cells and
contributes to the regulation of their resting membrane potential
(PubMed:25406588). Contributes to the regulation of action
potential firing in dentate gyrus granule cells and down-regulates
their intrinsic excitability (PubMed:25406588). In astrocytes, the
heterodimer formed by KCNK1 and KCNK2 is required for rapid
glutamate release in response to activation of G-protein coupled
receptors, such as F2R and CNR1 (PubMed:24496152). Required for
normal ion and water transport in the kidney (PubMed:16025300).
Contributes to the regulation of the resting membrane potential of
pancreatic beta cells (PubMed:22431633). The low channel activity
of homodimeric KCNK1 may be due to sumoylation. The low channel
activity may be due to rapid internalization from the cell
membrane and retention in recycling endosomes (PubMed:15540117).
{ECO:0000250|UniProtKB:O00180, ECO:0000250|UniProtKB:Q9Z2T2,
ECO:0000269|PubMed:15540117, ECO:0000269|PubMed:16025300,
ECO:0000269|PubMed:16847696, ECO:0000269|PubMed:22431633,
ECO:0000269|PubMed:24368895, ECO:0000269|PubMed:24496152,
ECO:0000269|PubMed:9013852}.
-!- ENZYME REGULATION: Inhibited by quinine, quinidine, barium, and
internal acidification. {ECO:0000269|PubMed:9013852,
ECO:0000305|PubMed:16847696}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Note=Both activation and channel closure are very rapid. Is not
voltage-gated (PubMed:22431633, PubMed:24496152). The
relationship between voltage and current is nearly linear
(PubMed:22431633, PubMed:24496152).
{ECO:0000269|PubMed:22431633, ECO:0000269|PubMed:24496152,
ECO:0000305};
-!- SUBUNIT: Homodimer; disulfide-linked (PubMed:9013852). Heterodimer
with KCNK2; disulfide-linked (PubMed:24496152). In astrocytes,
forms mostly heterodimeric potassium channels with KCNK2, with
only a minor proportion of functional channels containing
homodimeric KCNK1 (By similarity). Interacts with KCNK3 and KCNK9,
forming functional heterodimeric channels (By similarity).
Interacts with GNG4 (PubMed:24496152). Identified in a complex
with PSD and ARF6; interacts only with PSD that is bound to ARF6
(PubMed:15540117). Interacts with UBE2I (By similarity).
{ECO:0000250|UniProtKB:O00180, ECO:0000269|PubMed:15540117,
ECO:0000269|PubMed:24496152, ECO:0000269|PubMed:9013852}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15540117,
ECO:0000269|PubMed:19959478, ECO:0000269|PubMed:24368895,
ECO:0000269|PubMed:24496152, ECO:0000269|PubMed:9013852}; Multi-
pass membrane protein {ECO:0000305}. Recycling endosome
{ECO:0000269|PubMed:15540117}. Apical cell membrane
{ECO:0000269|PubMed:12855359, ECO:0000305|PubMed:16025300}.
Cytoplasmic vesicle {ECO:0000269|PubMed:16025300,
ECO:0000269|PubMed:24368895}. Perikaryon
{ECO:0000269|PubMed:12855359, ECO:0000269|PubMed:17079103,
ECO:0000269|PubMed:25406588}. Cell projection, dendrite
{ECO:0000269|PubMed:25406588}. Cell projection
{ECO:0000269|PubMed:17079103}. Cell junction, synapse
{ECO:0000250|UniProtKB:Q9Z2T2}. Note=The heterodimer with KCNK2 is
detected at the astrocyte cell membrane (PubMed:24496152). Not
detected at the astrocyte cell membrane when KCNK2 is absent
(PubMed:24496152). Detected on neuronal cell bodies, and to a
lesser degree on neuronal cell projections (PubMed:12855359,
PubMed:17079103). Detected on hippocampus dentate gyrus granule
cell bodies and to a lesser degree on proximal dendrites
(PubMed:25406588). Detected in synaptic membranes. Detected at the
apical cell membrane in stria vascularis in the cochlea (By
similarity). Detected at the apical cell membrane of vestibular
dark cells situated between the crista and the utricle in the
inner ear (PubMed:12855359). Detected at the apical cell membrane
in stria vascularis in the cochlea (PubMed:12855359). Detected at
the apical cell membrane in kidney proximal tubule segment S1 and
in subapical compartments in segments S1, S2 and S3
(PubMed:16025300). Predominantly in cytoplasmic structures in
kidney distal convoluted tubules and collecting ducts
(PubMed:16025300). Predominantly in cytoplasmic structures in
hippocampus astrocytes; only a minor proportion of the protein is
present at the cell membrane (PubMed:24368895).
{ECO:0000250|UniProtKB:Q9Z2T2, ECO:0000269|PubMed:16025300,
ECO:0000269|PubMed:17079103, ECO:0000269|PubMed:24368895,
ECO:0000269|PubMed:24496152, ECO:0000269|PubMed:25406588}.
-!- TISSUE SPECIFICITY: Detected in spiral ganglion neurons
(PubMed:17079103). Detected in hippocampus CA1 and CA1 regions and
in the molecular layer of the dentate gyrus (PubMed:24368895,
PubMed:25406588). Detected on hippocampus astrocytes
(PubMed:24368895, PubMed:24496152). Highly expressed in the stria
vascularis in the cochlea (PubMed:12855359). Detected in pancreas
islet beta cells (PubMed:22431633). Detected in kidney, at brush
border membranes in proximal tubules and in cytoplasmic structures
in distal convoluted tubules, thick ascending limbs and collecting
ducts (at protein level) (PubMed:15540117, PubMed:16025300).
Widely expressed. Detected in spiral ganglion cells
(PubMed:17079103). Highest expression in brain, kidney, thyroid,
salivary gland, adrenal gland, prostate, epididymis, uterus,
placenta, colon and jejunum. Moderate expression in eyes,
pituitary, pancreas, smooth muscle, testis and ovary. Very low
levels in lung, aorta, liver, heart, skeletal muscle, thymus and
spleen. In the brain, highest expression in cerebellar granule
cells, brainstem, hippocampus and cerebral cortex
(PubMed:18222039). {ECO:0000269|PubMed:15540117,
ECO:0000269|PubMed:16025300, ECO:0000269|PubMed:18222039,
ECO:0000269|PubMed:22431633, ECO:0000269|PubMed:24368895,
ECO:0000269|PubMed:25406588, ECO:0000269|PubMed:9013852,
ECO:0000269|PubMed:9559671}.
-!- DEVELOPMENTAL STAGE: Detected at very low levels in the embyonic
central nervous system (PubMed:9559671, PubMed:18222039). Detected
as early as 7 days post conception (PubMed:9559671). Detected in
dorsal root ganglia, hippocampus, olfactory epithelia and
intestine at 19 dpc (PubMed:18222039). Expression in the brain
increases strongly 3-8 days after birth, a period of intense
postnatal brain development (PubMed:9559671, PubMed:18222039).
Detected in dentate granule cells; expression levels show no
significant variability during postnatal development
(PubMed:18222039). Expression is higher in adults than in neonates
(PubMed:9559671, PubMed:18222039). {ECO:0000269|PubMed:18222039,
ECO:0000269|PubMed:9559671}.
-!- PTM: Sumoylation is controversial. Sumoylated by UBE2I. Not
sumoylated when expressed in xenopus oocytes or mammalian cells.
Sumoylation inactivates the channel, but does not interfere with
expression at the cell membrane. Sumoylation of a single subunit
is sufficient to silence the dimeric channel. Sumoylation of KCNK1
is sufficient to silence heterodimeric channels formed by KCNK1
and KCNK3 or KCNK9. Desumoylated by SENP1; this activates the
channel. Desumoylated by SENP1; this strongly increases halothane-
mediated activation of heterodimeric channels formed with KCNK9.
SENP1 treatment has no effect. {ECO:0000250|UniProtKB:O00180}.
-!- DISRUPTION PHENOTYPE: No visible phenotype on standard chow,
excepting a lower urinary flow rate (PubMed:16025300). Mice appear
normal and are fertile (PubMed:24368895). When kept on a low
phosphate diet, both wild-type and mutant mice show strongly
reduced urinary phosphate secretion. Still, mutant mice display
higher fractional urinary phosphate secretion relative to wild-
type, leading to reduced inorganic phosphate levels in blood
plasma. The impaired phosphate homeostasis seems to be due to
indirect effects on the expression of other transporters, such as
SLC34A1 and AQP2 (PubMed:16025300). Principal cells from kidney
collecting duct are hyperpolarized, display reduced potassium
conductance and strongly reduced quinidine-sensitive potassium
channel activity (PubMed:16847696). Besides, collecting ducts from
mutant mouse kidney display a larger diameter relative to wild-
type (PubMed:16847696). {ECO:0000269|PubMed:16025300,
ECO:0000269|PubMed:16847696, ECO:0000269|PubMed:24368895}.
-!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
1.A.1.8) family. {ECO:0000305}.
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EMBL; AF033017; AAC16973.1; -; mRNA.
EMBL; CH466525; EDL11808.1; -; Genomic_DNA.
EMBL; BC003729; AAH03729.1; -; mRNA.
CCDS; CCDS22783.1; -.
RefSeq; NP_032456.2; NM_008430.2.
UniGene; Mm.10800; -.
ProteinModelPortal; O08581; -.
BioGrid; 200907; 46.
IntAct; O08581; 45.
STRING; 10090.ENSMUSP00000046103; -.
TCDB; 1.A.1.8.1; the voltage-gated ion channel (vic) superfamily.
iPTMnet; O08581; -.
PhosphoSitePlus; O08581; -.
MaxQB; O08581; -.
PaxDb; O08581; -.
PeptideAtlas; O08581; -.
PRIDE; O08581; -.
Ensembl; ENSMUST00000046765; ENSMUSP00000046103; ENSMUSG00000033998.
GeneID; 16525; -.
KEGG; mmu:16525; -.
UCSC; uc009nyr.3; mouse.
CTD; 3775; -.
MGI; MGI:109322; Kcnk1.
eggNOG; KOG1418; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00760000118858; -.
HOGENOM; HOG000286014; -.
HOVERGEN; HBG052237; -.
InParanoid; O08581; -.
KO; K04912; -.
OMA; VQRVTIH; -.
OrthoDB; EOG091G0DIX; -.
TreeFam; TF313947; -.
Reactome; R-MMU-1299308; Tandem of pore domain in a weak inwardly rectifying K+ channels (TWIK).
Reactome; R-MMU-5576886; Phase 4 - resting membrane potential.
ChiTaRS; Kcnk1; mouse.
PRO; PR:O08581; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000033998; -.
CleanEx; MM_KCNK1; -.
ExpressionAtlas; O08581; baseline and differential.
Genevisible; O08581; MM.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:1902937; C:inward rectifier potassium channel complex; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0034705; C:potassium channel complex; ISS:UniProtKB.
GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0005242; F:inward rectifier potassium channel activity; IDA:UniProtKB.
GO; GO:0005267; F:potassium channel activity; IDA:MGI.
GO; GO:0022841; F:potassium ion leak channel activity; ISS:UniProtKB.
GO; GO:0005272; F:sodium channel activity; ISS:UniProtKB.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0006813; P:potassium ion transport; IC:MGI.
GO; GO:0060075; P:regulation of resting membrane potential; ISS:UniProtKB.
GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
GO; GO:0035725; P:sodium ion transmembrane transport; ISS:UniProtKB.
GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
InterPro; IPR003280; 2pore_dom_K_chnl.
InterPro; IPR003092; 2pore_dom_K_chnl_TASK.
InterPro; IPR005408; 2pore_dom_K_chnl_TWIK.
InterPro; IPR001779; 2pore_dom_K_chnl_TWIK1.
InterPro; IPR013099; K_chnl_dom.
Pfam; PF07885; Ion_trans_2; 2.
PIRSF; PIRSF038061; K_channel_subfamily_K_type; 1.
PRINTS; PR01333; 2POREKCHANEL.
PRINTS; PR01096; TWIK1CHANNEL.
PRINTS; PR01586; TWIKCHANNEL.
1: Evidence at protein level;
Cell junction; Cell membrane; Cell projection; Complete proteome;
Cytoplasmic vesicle; Disulfide bond; Endosome; Glycoprotein;
Ion channel; Ion transport; Isopeptide bond; Membrane; Phosphoprotein;
Potassium; Potassium channel; Potassium transport; Reference proteome;
Synapse; Transmembrane; Transmembrane helix; Transport;
Ubl conjugation.
CHAIN 1 336 Potassium channel subfamily K member 1.
/FTId=PRO_0000101741.
TOPO_DOM 1 20 Cytoplasmic.
{ECO:0000250|UniProtKB:O00180}.
TRANSMEM 21 41 Helical. {ECO:0000250|UniProtKB:O00180}.
TOPO_DOM 42 103 Extracellular.
{ECO:0000250|UniProtKB:O00180}.
INTRAMEM 104 116 Helical; Name=Pore helix 1.
{ECO:0000250|UniProtKB:O00180}.
INTRAMEM 117 122 {ECO:0000250|UniProtKB:O00180}.
TOPO_DOM 123 132 Extracellular.
{ECO:0000250|UniProtKB:O00180}.
TRANSMEM 133 156 Helical. {ECO:0000250|UniProtKB:O00180}.
TOPO_DOM 157 181 Cytoplasmic.
{ECO:0000250|UniProtKB:O00180}.
TRANSMEM 182 202 Helical. {ECO:0000250|UniProtKB:O00180}.
TOPO_DOM 203 211 Extracellular.
{ECO:0000250|UniProtKB:O00180}.
INTRAMEM 212 224 Helical; Name=Pore helix 2.
{ECO:0000250|UniProtKB:O00180}.
INTRAMEM 225 231 {ECO:0000250|UniProtKB:O00180}.
TOPO_DOM 232 243 Extracellular.
{ECO:0000250|UniProtKB:O00180}.
TRANSMEM 244 267 Helical. {ECO:0000250|UniProtKB:O00180}.
TOPO_DOM 268 336 Cytoplasmic.
{ECO:0000250|UniProtKB:O00180}.
REGION 117 122 Selectivity filter 1.
{ECO:0000250|UniProtKB:O00180}.
REGION 225 230 Selectivity filter 2.
{ECO:0000250|UniProtKB:O00180}.
REGION 293 299 Important for intracellular retention in
recycling endosomes.
{ECO:0000250|UniProtKB:O00180}.
SITE 118 118 Important for increased permeability to
Na(+) when K(+) levels are
subphysiological.
{ECO:0000250|UniProtKB:O00180}.
SITE 146 146 Part of a hydrophobic barrier that is
stochastically dewetted and limits ion
permeability.
{ECO:0000250|UniProtKB:O00180}.
SITE 261 261 Part of a hydrophobic barrier that is
stochastically dewetted and limits ion
permeability.
{ECO:0000250|UniProtKB:O00180}.
MOD_RES 326 326 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z2T2}.
CARBOHYD 95 95 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 69 69 Interchain.
{ECO:0000250|UniProtKB:O00180,
ECO:0000269|PubMed:24496152}.
CROSSLNK 274 274 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250|UniProtKB:O00180}.
MUTAGEN 69 69 C->S: Abolishes formation of a disulfide-
linked heterodimer with KCNK2.
{ECO:0000269|PubMed:24496152}.
MUTAGEN 119 119 G->E: Abolishes potassium channel
activity. {ECO:0000269|PubMed:24496152}.
MUTAGEN 293 294 IM->AA: Increases channel expression at
the cell membrane, resulting in higher
channel activity.
{ECO:0000269|PubMed:19959478}.
CONFLICT 44 44 V -> E (in Ref. 1; AAC16973).
{ECO:0000305}.
CONFLICT 152 152 V -> L (in Ref. 1; AAC16973).
{ECO:0000305}.
CONFLICT 259 259 A -> T (in Ref. 1; AAC16973).
{ECO:0000305}.
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


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