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Potassium channel subfamily K member 1 (Inward rectifying potassium channel protein TWIK-1) (Potassium channel K2P1) (Potassium channel KCNO1)

 KCNK1_HUMAN             Reviewed;         336 AA.
O00180; Q13307; Q5T5E8;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
25-APR-2018, entry version 165.
RecName: Full=Potassium channel subfamily K member 1;
AltName: Full=Inward rectifying potassium channel protein TWIK-1 {ECO:0000303|PubMed:8605869};
AltName: Full=Potassium channel K2P1 {ECO:0000303|PubMed:15820677};
AltName: Full=Potassium channel KCNO1;
Name=KCNK1; Synonyms=HOHO1 {ECO:0000303|PubMed:9462864}, KCNO1, TWIK1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION,
MUTAGENESIS OF THR-161, ENZYME REGULATION, BIOPHYSICOCHEMICAL
PROPERTIES, AND TISSUE SPECIFICITY.
TISSUE=Kidney;
PubMed=8605869;
Lesage F., Guillemare E., Fink M., Duprat F., Lazdunski M., Romey G.,
Barhanin J.;
"TWIK-1, a ubiquitous human weakly inward rectifying K+ channel with a
novel structure.";
EMBO J. 15:1004-1011(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND REVIEW.
TISSUE=Brain;
PubMed=9462864; DOI=10.1007/s109-1998-8100-0;
Goldstein S.A.N., Wang K.-W., Ilan N., Pausch M.H.;
"Sequence and function of the two P domain potassium channels:
implications of an emerging superfamily.";
J. Mol. Med. 76:13-20(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=9362344;
Orias M., Velazquez H., Tung F., Lee G., Desir G.V.;
"Cloning and localization of a double-pore K channel, KCNK1: exclusive
expression in distal nephron segments.";
Am. J. Physiol. 273:F663-F666(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[7]
FUNCTION, SUBUNIT, DISULFIDE BOND, GLYCOSYLATION AT ASN-95,
MUTAGENESIS OF CYS-69 AND ASN-95, SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=8978667;
Lesage F., Reyes R., Fink M., Duprat F., Guillemare E., Lazdunski M.;
"Dimerization of TWIK-1 K+ channel subunits via a disulfide bridge.";
EMBO J. 15:6400-6407(1996).
[8]
TISSUE SPECIFICITY.
PubMed=11165377; DOI=10.1016/S0169-328X(00)00263-1;
Medhurst A.D., Rennie G., Chapman C.G., Meadows H., Duckworth M.D.,
Kelsell R.E., Gloger I.I., Pangalos M.N.;
"Distribution analysis of human two pore domain potassium channels in
tissues of the central nervous system and periphery.";
Brain Res. Mol. Brain Res. 86:101-114(2001).
[9]
FUNCTION, SUBCELLULAR LOCATION, SUMOYLATION AT LYS-274, MUTAGENESIS OF
HIS-122 AND LYS-274, AND INTERACTION WITH UBE2I.
PubMed=15820677; DOI=10.1016/j.cell.2005.01.019;
Rajan S., Plant L.D., Rabin M.L., Butler M.H., Goldstein S.A.;
"Sumoylation silences the plasma membrane leak K+ channel K2P1.";
Cell 121:37-47(2005).
[10]
LACK OF SUMOYLATION AT LYS-274, MUTAGENESIS OF LYS-274, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=17693262; DOI=10.1016/j.cell.2007.06.012;
Feliciangeli S., Bendahhou S., Sandoz G., Gounon P., Reichold M.,
Warth R., Lazdunski M., Barhanin J., Lesage F.;
"Does sumoylation control K2P1/TWIK1 background K+ channels?";
Cell 130:563-569(2007).
[11]
TISSUE SPECIFICITY.
PubMed=17478540; DOI=10.1113/jphysiol.2006.126714;
Gaborit N., Le Bouter S., Szuts V., Varro A., Escande D., Nattel S.,
Demolombe S.;
"Regional and tissue specific transcript signatures of ion channel
genes in the non-diseased human heart.";
J. Physiol. (Lond.) 582:675-693(2007).
[12]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF LYS-274; 293-ILE-ILE-294 AND 299-LEU--HIS-336.
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]
SUMOYLATION AT LYS-274, MUTAGENESIS OF HIS-122 AND LYS-274, FUNCTION,
AND SUBCELLULAR LOCATION.
PubMed=20498050; DOI=10.1073/pnas.1004712107;
Plant L.D., Dementieva I.S., Kollewe A., Olikara S., Marks J.D.,
Goldstein S.A.;
"One SUMO is sufficient to silence the dimeric potassium channel
K2P1.";
Proc. Natl. Acad. Sci. U.S.A. 107:10743-10748(2010).
[14]
FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-118 AND LYS-274,
TISSUE SPECIFICITY, AND ENZYME REGULATION.
PubMed=21653227; DOI=10.1126/scisignal.2001726;
Ma L., Zhang X., Chen H.;
"TWIK-1 two-pore domain potassium channels change ion selectivity and
conduct inward leak sodium currents in hypokalemia.";
Sci. Signal. 4:RA37-RA37(2011).
[15]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=21964404; DOI=10.1152/ajplung.00102.2011;
Zhao K.Q., Xiong G., Wilber M., Cohen N.A., Kreindler J.L.;
"A role for two-pore K? channels in modulating Na? absorption and Cl?
secretion in normal human bronchial epithelial cells.";
Am. J. Physiol. 302:L4-L12(2012).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[17]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 108-LEU-PHE-109;
THR-118; HIS-122; LEU-146; LEU-228; THR-250 AND LYS-274.
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).
[18]
SUBCELLULAR LOCATION, FUNCTION, SUMOYLATION, INTERACTION WITH KCNK3
AND KCNK9, AND MUTAGENESIS OF TYR-231.
PubMed=23169818; DOI=10.1126/scisignal.2003431;
Plant L.D., Zuniga L., Araki D., Marks J.D., Goldstein S.A.;
"SUMOylation silences heterodimeric TASK potassium channels containing
K2P1 subunits in cerebellar granule neurons.";
Sci. Signal. 5:RA84-RA84(2012).
[19]
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).
[20]
FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-146 AND LEU-261,
AND SITE.
PubMed=25001086; DOI=10.1038/ncomms5377;
Aryal P., Abd-Wahab F., Bucci G., Sansom M.S., Tucker S.J.;
"A hydrophobic barrier deep within the inner pore of the TWIK-1 K2P
potassium channel.";
Nat. Commun. 5:4377-4377(2014).
[21]
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).
[22]
X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 23-288 IN COMPLEX WITH
POTASSIUM IONS, FUNCTION, SUBUNIT, DISULFIDE BOND, TOPOLOGY, AND
SUBCELLULAR LOCATION.
PubMed=22282804; DOI=10.1126/science.1213274;
Miller A.N., Long S.B.;
"Crystal structure of the human two-pore domain potassium channel
K2P1.";
Science 335:432-436(2012).
-!- 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:15820677, PubMed:21653227). 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 (PubMed:21653227,
PubMed:22431633). The homodimer has very low potassium channel
activity, when expressed in heterologous systems, and can function
as weakly inward rectifying potassium channel (PubMed:8605869,
PubMed:8978667, PubMed:15820677, PubMed:21653227, PubMed:22431633,
PubMed:23169818, PubMed:25001086). Channel activity is modulated
by activation of serotonin receptors (By similarity).
Heterodimeric channels containing KCNK1 and KCNK2 have much higher
activity, and may represent the predominant form in astrocytes (By
similarity). Heterodimeric channels containing KCNK1 and KCNK3 or
KCNK9 have much higher activity (PubMed:23169818). Heterodimeric
channels formed by KCNK1 and KCNK9 may contribute to halothane-
sensitive currents (PubMed:23169818). Mediates outward rectifying
potassium currents in dentate gyrus granule cells and contributes
to the regulation of their resting membrane potential (By
similarity). Contributes to the regulation of action potential
firing in dentate gyrus granule cells and down-regulates their
intrinsic excitability (By similarity). 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 (By similarity). Required for
normal ion and water transport in the kidney (By similarity).
Contributes to the regulation of the resting membrane potential of
pancreatic beta cells (By similarity). The low channel activity of
homodimeric KCNK1 may be due to sumoylation (PubMed:15820677,
PubMed:20498050, PubMed:23169818). The low channel activity may be
due to rapid internalization from the cell membrane and retention
in recycling endosomes (PubMed:19959478).
{ECO:0000250|UniProtKB:O08581, ECO:0000250|UniProtKB:Q9Z2T2,
ECO:0000269|PubMed:15820677, ECO:0000269|PubMed:17693262,
ECO:0000269|PubMed:19959478, ECO:0000269|PubMed:20498050,
ECO:0000269|PubMed:21653227, ECO:0000269|PubMed:22282804,
ECO:0000269|PubMed:22431633, ECO:0000269|PubMed:23169818,
ECO:0000269|PubMed:25001086, ECO:0000269|PubMed:8605869,
ECO:0000269|PubMed:8978667}.
-!- ENZYME REGULATION: Inhibited by Ba(2+) ions and quinidine
(PubMed:8605869). Inhibited by quinine (PubMed:8605869,
PubMed:21653227). Is slightly inhibited by 10 mM
tetraethylammonium (TEA), and only marginally inhibited by 4-
aminopyridine, charybdotoxin and dendrotoxin (PubMed:8605869).
Lowering the extracellular pH to below 6.5 transiently activates
the channel, and then inhibits channel activity (PubMed:15820677,
PubMed:22431633). Inhibited when the intracellular pH is decreased
down to pH 6.0, but this may be due to indirect effects
(PubMed:8605869). {ECO:0000269|PubMed:15820677,
ECO:0000269|PubMed:21653227, ECO:0000269|PubMed:22431633,
ECO:0000269|PubMed:8605869}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Note=Has a unit conductance of 34 pS. Both activation and
channel closure are very rapid. Is not voltage-gated. The
relationship between voltage and current is nearly linear. Has a
mean open time of 0.3 msec at a membrane potential of -80 mV,
and 1.9 msec at +80 mV (PubMed:8605869).
{ECO:0000269|PubMed:19959478, ECO:0000269|PubMed:8605869};
-!- SUBUNIT: Homodimer; disulfide-linked (PubMed:8978667,
PubMed:22282804). Heterodimer with KCNK2; disulfide-linked (By
similarity). 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
(PubMed:23169818). Interacts with GNG4 (By similarity). Identified
in a complex with PSD and ARF6; interacts only with PSD that is
bound to ARF6 (By similarity). Interacts with UBE2I
(PubMed:15820677). {ECO:0000250|UniProtKB:O08581,
ECO:0000269|PubMed:15820677, ECO:0000269|PubMed:22282804,
ECO:0000269|PubMed:23169818, ECO:0000269|PubMed:8978667}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-3914675, EBI-3914675;
A8MQ03:CYSRT1; NbExp=4; IntAct=EBI-3914675, EBI-3867333;
P63165:SUMO1; NbExp=3; IntAct=EBI-3914675, EBI-80140;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15820677,
ECO:0000269|PubMed:17693262, ECO:0000269|PubMed:20498050,
ECO:0000269|PubMed:21653227, ECO:0000269|PubMed:22282804,
ECO:0000269|PubMed:22431633, ECO:0000269|PubMed:23169818,
ECO:0000269|PubMed:25001086, ECO:0000269|PubMed:8605869,
ECO:0000269|PubMed:8978667}; Multi-pass membrane protein
{ECO:0000269|PubMed:22282804, ECO:0000269|PubMed:8978667,
ECO:0000305}. Recycling endosome {ECO:0000269|PubMed:19959478}.
Cell junction, synapse {ECO:0000250|UniProtKB:Q9Z2T2}. Cytoplasmic
vesicle {ECO:0000250|UniProtKB:O08581}. Perikaryon
{ECO:0000250|UniProtKB:O08581}. Cell projection, dendrite
{ECO:0000250|UniProtKB:O08581}. Cell projection
{ECO:0000250|UniProtKB:O08581}. Apical cell membrane
{ECO:0000269|PubMed:21964404}; Multi-pass membrane protein
{ECO:0000305}. Note=The heterodimer with KCNK2 is detected at the
astrocyte cell membrane. Not detected at the astrocyte cell
membrane when KCNK2 is absent. Detected on neuronal cell bodies,
and to a lesser degree on neuronal cell projections. Detected on
hippocampus dentate gyrus granule cell bodies and to a lesser
degree on proximal dendrites. Detected in synaptic membranes.
Detected at the apical cell membrane in stria vascularis in the
cochlea. Detected at the apical cell membrane of vestibular dark
cells situated between the crista and the utricle in the inner
ear. Detected at the apical cell membrane in kidney proximal
tubule segment S1 and in subapical compartments in segments S1, S2
and S3. Predominantly in cytoplasmic structures in kidney distal
convoluted tubules and collecting ducts (By similarity). Detected
at the apical cell membrane of bronchial epithelial cells
(PubMed:21964404). {ECO:0000250|UniProtKB:O08581,
ECO:0000250|UniProtKB:Q9Z2T2, ECO:0000269|PubMed:21964404}.
-!- TISSUE SPECIFICITY: Detected in bronchial epithelial cells
(PubMed:21964404). Detected in heart left atrium and left
ventricle (PubMed:17478540). Detected in cardiac myocytes (at
protein level) (PubMed:21653227). Widely expressed with high
levels in heart, brain and kidney, and lower levels in colon,
ovary, placenta, lung and liver (PubMed:8605869, PubMed:9362344).
Highly expressed in cerebellum, and detected at lower levels in
amygdala, caudate nucleus, brain cortex, hippocampus, putamen,
substantia nigra, thalamus, dorsal root ganglion, spinal cord,
pituitary, heart, kidney, lung, placenta, pancreas, stomach, small
intestine, uterus and prostate (PubMed:11165377). Detected in
right and left heart ventricle and atrium, and in heart Purkinje
fibers (PubMed:17478540). Detected in bronchial epithelial cells
(PubMed:21964404). {ECO:0000269|PubMed:11165377,
ECO:0000269|PubMed:17478540, ECO:0000269|PubMed:21653227,
ECO:0000269|PubMed:21964404, ECO:0000269|PubMed:8605869,
ECO:0000269|PubMed:9362344}.
-!- PTM: Sumoylation is controversial. Sumoylated by UBE2I
(PubMed:15820677). Not sumoylated when expressed in xenopus
oocytes or mammalian cells (PubMed:17693262). Sumoylation
inactivates the channel, but does not interfere with expression at
the cell membrane (PubMed:15820677). Sumoylation of a single
subunit is sufficient to silence the dimeric channel
(PubMed:20498050, PubMed:23169818). Sumoylation of KCNK1 is
sufficient to silence heterodimeric channels formed by KCNK1 and
KCNK3 or KCNK9 (PubMed:23169818). Desumoylated by SENP1; this
activates the channel (PubMed:15820677, PubMed:20498050,
PubMed:23169818). Desumoylated by SENP1; this strongly increases
halothane-mediated activation of heterodimeric channels formed
with KCNK9 (PubMed:23169818). SENP1 treatment has no effect
(PubMed:17693262). {ECO:0000269|PubMed:15820677,
ECO:0000269|PubMed:17693262, ECO:0000269|PubMed:20498050,
ECO:0000269|PubMed:23169818}.
-!- MISCELLANEOUS: When the external K(+) concentration is lowered to
subphysiological levels, it takes several minutes till the channel
has reached a new, stable state characterized by increased Na(+)
permeability (PubMed:21653227). Likewise, when the external pH is
lowered to values below 6.5, it takes several minutes till the
channel has reached a new, stable state characterized by increased
Na(+) permeability (PubMed:22431633). When raising the K(+)
concentration back to 5 mM, it takes 40 to 70 minutes for the
channel to regain its original selectivity for K(+)
(PubMed:21653227). Likewise, it takes more that 25 minutes for the
channel to regain its original K(+) selectivity when the pH is
raised back to 7.4 (PubMed:22431633).
{ECO:0000269|PubMed:21653227, ECO:0000269|PubMed:22431633}.
-!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
1.A.1.8) family. {ECO:0000305}.
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EMBL; U33632; AAB01688.1; -; mRNA.
EMBL; U76996; AAB97878.1; -; mRNA.
EMBL; U90065; AAB51147.1; -; mRNA.
EMBL; AL356357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471098; EAW69989.1; -; Genomic_DNA.
EMBL; BC018051; AAH18051.1; -; mRNA.
CCDS; CCDS1599.1; -.
PIR; S65566; S65566.
RefSeq; NP_002236.1; NM_002245.3.
UniGene; Hs.208544; -.
PDB; 3UKM; X-ray; 3.40 A; A/B/C/D=19-288.
PDBsum; 3UKM; -.
ProteinModelPortal; O00180; -.
SMR; O00180; -.
BioGrid; 109976; 6.
DIP; DIP-59532N; -.
IntAct; O00180; 5.
STRING; 9606.ENSP00000355580; -.
DrugBank; DB00308; Ibutilide.
DrugBank; DB00908; Quinidine.
DrugBank; DB01346; Quinidine barbiturate.
iPTMnet; O00180; -.
PhosphoSitePlus; O00180; -.
BioMuta; KCNK1; -.
EPD; O00180; -.
MaxQB; O00180; -.
PaxDb; O00180; -.
PeptideAtlas; O00180; -.
PRIDE; O00180; -.
DNASU; 3775; -.
Ensembl; ENST00000366621; ENSP00000355580; ENSG00000135750.
GeneID; 3775; -.
KEGG; hsa:3775; -.
UCSC; uc010pxo.1; human.
CTD; 3775; -.
DisGeNET; 3775; -.
EuPathDB; HostDB:ENSG00000135750.14; -.
GeneCards; KCNK1; -.
HGNC; HGNC:6272; KCNK1.
HPA; CAB022588; -.
HPA; HPA016049; -.
MIM; 601745; gene.
neXtProt; NX_O00180; -.
OpenTargets; ENSG00000135750; -.
PharmGKB; PA219; -.
eggNOG; KOG1418; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00760000118858; -.
HOGENOM; HOG000286014; -.
HOVERGEN; HBG052237; -.
InParanoid; O00180; -.
KO; K04912; -.
OMA; VQRVTIH; -.
OrthoDB; EOG091G0DIX; -.
PhylomeDB; O00180; -.
TreeFam; TF313947; -.
Reactome; R-HSA-1299308; Tandem of pore domain in a weak inwardly rectifying K+ channels (TWIK).
Reactome; R-HSA-5576886; Phase 4 - resting membrane potential.
ChiTaRS; KCNK1; human.
GeneWiki; KCNK1; -.
GenomeRNAi; 3775; -.
PRO; PR:O00180; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000135750; -.
CleanEx; HS_KCNK1; -.
ExpressionAtlas; O00180; baseline and differential.
Genevisible; O00180; HS.
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:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:1902937; C:inward rectifier potassium channel complex; IEA:Ensembl.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0034705; C:potassium channel complex; IDA:UniProtKB.
GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
GO; GO:0008076; C:voltage-gated potassium channel complex; TAS:ProtInc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005242; F:inward rectifier potassium channel activity; TAS:ProtInc.
GO; GO:0005267; F:potassium channel activity; IDA:UniProtKB.
GO; GO:0022841; F:potassium ion leak channel activity; IDA:UniProtKB.
GO; GO:0005272; F:sodium channel activity; IDA:UniProtKB.
GO; GO:0061337; P:cardiac conduction; TAS:Reactome.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0006813; P:potassium ion transport; TAS:ProtInc.
GO; GO:0060075; P:regulation of resting membrane potential; IMP:UniProtKB.
GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
GO; GO:0035725; P:sodium ion transmembrane transport; IDA: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;
3D-structure; 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_0000101740.
TOPO_DOM 1 20 Cytoplasmic.
{ECO:0000269|PubMed:22282804}.
TRANSMEM 21 41 Helical. {ECO:0000269|PubMed:22282804}.
TOPO_DOM 42 103 Extracellular.
{ECO:0000269|PubMed:22282804,
ECO:0000305|PubMed:8978667}.
INTRAMEM 104 116 Helical; Name=Pore helix 1.
{ECO:0000269|PubMed:22282804}.
INTRAMEM 117 122 {ECO:0000269|PubMed:22282804}.
TOPO_DOM 123 132 Extracellular.
{ECO:0000269|PubMed:22282804}.
TRANSMEM 133 156 Helical. {ECO:0000269|PubMed:22282804}.
TOPO_DOM 157 181 Cytoplasmic.
{ECO:0000269|PubMed:22282804}.
TRANSMEM 182 202 Helical. {ECO:0000269|PubMed:22282804}.
TOPO_DOM 203 211 Extracellular.
{ECO:0000269|PubMed:22282804}.
INTRAMEM 212 224 Helical; Name=Pore helix 2.
{ECO:0000269|PubMed:22282804}.
INTRAMEM 225 231 {ECO:0000269|PubMed:22282804}.
TOPO_DOM 232 243 Extracellular.
{ECO:0000269|PubMed:22282804}.
TRANSMEM 244 267 Helical. {ECO:0000269|PubMed:22282804}.
TOPO_DOM 268 336 Cytoplasmic.
{ECO:0000269|PubMed:22282804}.
REGION 117 122 Selectivity filter 1.
{ECO:0000269|PubMed:22282804,
ECO:0000305|PubMed:21653227}.
REGION 225 230 Selectivity filter 2.
{ECO:0000269|PubMed:22282804}.
REGION 293 299 Important for intracellular retention in
recycling endosomes.
{ECO:0000269|PubMed:19959478}.
SITE 118 118 Important for increased permeability to
Na(+) when K(+) levels are
subphysiological.
{ECO:0000269|PubMed:21653227}.
SITE 146 146 Part of a hydrophobic barrier that is
stochastically dewetted and limits ion
permeability.
{ECO:0000269|PubMed:22431633,
ECO:0000269|PubMed:25001086}.
SITE 261 261 Part of a hydrophobic barrier that is
stochastically dewetted and limits ion
permeability.
{ECO:0000269|PubMed:25001086}.
MOD_RES 326 326 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z2T2}.
CARBOHYD 95 95 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8978667}.
DISULFID 69 69 Interchain. {ECO:0000269|PubMed:22282804,
ECO:0000269|PubMed:8978667}.
CROSSLNK 274 274 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:15820677,
ECO:0000269|PubMed:20498050}.
MUTAGEN 69 69 C->A: Abolishes channel activity and
formation of disulfide-linked homodimers.
{ECO:0000269|PubMed:8978667}.
MUTAGEN 95 95 N->A: Abolishes N-glycosylation.
{ECO:0000269|PubMed:8978667}.
MUTAGEN 108 109 LF->FY: Impairs selectivity for K(+) ions
and increases permeability to Na(+) ions,
both at pH 7.4 and at pH 6.
{ECO:0000269|PubMed:22431633}.
MUTAGEN 118 118 T->I: Abolishes change in ion selectivity
in the presence of subphysiological K(+)
levels. {ECO:0000269|PubMed:21653227}.
MUTAGEN 122 122 H->K: Increases channel activity, and has
only a minor effect on the inhibition by
acidification of the extracellular
medium. {ECO:0000269|PubMed:22431633}.
MUTAGEN 122 122 H->N: Decreases channel activity and
abolishes inhibition by acidification of
the extracellular medium.
{ECO:0000269|PubMed:15820677,
ECO:0000269|PubMed:20498050,
ECO:0000269|PubMed:22431633}.
MUTAGEN 146 146 L->A,V: Does not increase the low
intrinsic channel activity.
{ECO:0000269|PubMed:25001086}.
MUTAGEN 146 146 L->D: Increases channel activity.
{ECO:0000269|PubMed:22431633,
ECO:0000269|PubMed:25001086}.
MUTAGEN 146 146 L->N,T: Increases channel activity.
{ECO:0000269|PubMed:25001086}.
MUTAGEN 146 146 L->S: Increases channel activity.
Strongly increases channel activity; when
associated with S-261.
{ECO:0000269|PubMed:25001086}.
MUTAGEN 161 161 T->A: No effect on channel activity.
{ECO:0000269|PubMed:8605869}.
MUTAGEN 228 228 L->F: No effect on selectivity for K(+)
ions. {ECO:0000269|PubMed:22431633}.
MUTAGEN 231 231 Y->F: Strongly decreases activity of
homodimeric channels and of heterodimeric
channels formed with KCNK3 and with
KCNK9. No effect on location at the cell
membrane. {ECO:0000269|PubMed:23169818}.
MUTAGEN 250 250 T->L: Slighly decreases the increased
permeability to Na(+) ions at pH 6.
{ECO:0000269|PubMed:22431633}.
MUTAGEN 261 261 L->D,N: Increases channel activity.
{ECO:0000269|PubMed:25001086}.
MUTAGEN 261 261 L->S: Increases channel activity.
Strongly increases channel activity; when
associated with S-146.
{ECO:0000269|PubMed:25001086}.
MUTAGEN 274 274 K->A,C,D,Q,R: Converts the electrically
silent channel that is present at the
cell membrane to an active channel.
{ECO:0000269|PubMed:20498050}.
MUTAGEN 274 274 K->E: Converts the electrically silent
channel that is present at the cell
membrane to an active channel. No effect
on retention in recycling endosomes.
{ECO:0000269|PubMed:15820677,
ECO:0000269|PubMed:17693262,
ECO:0000269|PubMed:19959478,
ECO:0000269|PubMed:20498050,
ECO:0000269|PubMed:21653227,
ECO:0000269|PubMed:22431633}.
MUTAGEN 293 294 II->AA: Strongly increases location at
the cell membrane.
{ECO:0000269|PubMed:19959478}.
MUTAGEN 299 336 Missing: No effect on intracellular
retention in recycling endosomes.
{ECO:0000269|PubMed:19959478}.
HELIX 19 66 {ECO:0000244|PDB:3UKM}.
HELIX 72 86 {ECO:0000244|PDB:3UKM}.
TURN 87 89 {ECO:0000244|PDB:3UKM}.
HELIX 104 115 {ECO:0000244|PDB:3UKM}.
HELIX 128 160 {ECO:0000244|PDB:3UKM}.
TURN 163 167 {ECO:0000244|PDB:3UKM}.
HELIX 177 195 {ECO:0000244|PDB:3UKM}.
HELIX 197 206 {ECO:0000244|PDB:3UKM}.
STRAND 207 209 {ECO:0000244|PDB:3UKM}.
HELIX 212 223 {ECO:0000244|PDB:3UKM}.
STRAND 236 238 {ECO:0000244|PDB:3UKM}.
HELIX 242 268 {ECO:0000244|PDB:3UKM}.
HELIX 271 278 {ECO:0000244|PDB:3UKM}.
SEQUENCE 336 AA; 38143 MW; 2A41D9501323215D CRC64;
MLQSLAGSSC VRLVERHRSA WCFGFLVLGY LLYLVFGAVV FSSVELPYED LLRQELRKLK
RRFLEEHECL SEQQLEQFLG RVLEASNYGV SVLSNASGNW NWDFTSALFF ASTVLSTTGY
GHTVPLSDGG KAFCIIYSVI GIPFTLLFLT AVVQRITVHV TRRPVLYFHI RWGFSKQVVA
IVHAVLLGFV TVSCFFFIPA AVFSVLEDDW NFLESFYFCF ISLSTIGLGD YVPGEGYNQK
FRELYKIGIT CYLLLGLIAM LVVLETFCEL HELKKFRKMF YVKKDKDEDQ VHIIEHDQLS
FSSITDQAAG MKEDQKQNEP FVATQSSACV DGPANH


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