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

 KCNK1_RAT               Reviewed;         336 AA.
Q9Z2T2;
21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
12-SEP-2018, entry version 119.
RecName: Full=Potassium channel subfamily K member 1;
AltName: Full=Inward rectifying potassium channel protein TWIK-1;
Short=rTWIK;
AltName: Full=Potassium channel K2P1 {ECO:0000303|PubMed:25305496};
Name=Kcnk1 {ECO:0000312|RGD:621447};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1] {ECO:0000312|EMBL:AAD09336.1}
NUCLEOTIDE SEQUENCE [MRNA].
Gan L., Joiner W.J., Quinn A.M., Wang L.-Y., Hughes T.,
Kaczmarek L.K.;
"Cloning and localization of rTWIK, a putative potassium channel with
two P domains.";
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000312|EMBL:AAH61807.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate {ECO:0000312|EMBL:AAH61807.1};
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).
[3]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=9843722;
Cluzeaud F., Reyes R., Escoubet B., Fay M., Lazdunski M.,
Bonvalet J.P., Lesage F., Farman N.;
"Expression of TWIK-1, a novel weakly inward rectifying potassium
channel in rat kidney.";
Am. J. Physiol. 275:C1602-C1609(1998).
[4]
TISSUE SPECIFICITY.
PubMed=11567039;
Talley E.M., Solorzano G., Lei Q., Kim D., Bayliss D.A.;
"Cns distribution of members of the two-pore-domain (KCNK) potassium
channel family.";
J. Neurosci. 21:7491-7505(2001).
[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]
FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
PubMed=17452494; DOI=10.1124/mol.107.034389;
Deng P.Y., Poudel S.K., Rojanathammanee L., Porter J.E., Lei S.;
"Serotonin inhibits neuronal excitability by activating two-pore
domain K+ channels in the entorhinal cortex.";
Mol. Pharmacol. 72:208-218(2007).
[7]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=18838117; DOI=10.1016/j.heares.2008.09.004;
Popper P., Winkler J., Erbe C.B., Lerch-Gaggl A., Siebeneich W.,
Wackym P.A.;
"Distribution of two-pore-domain potassium channels in the adult rat
vestibular periphery.";
Hear. Res. 246:1-8(2008).
[8]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF
LYS-274, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=19571146; DOI=10.1523/JNEUROSCI.5784-08.2009;
Zhou M., Xu G., Xie M., Zhang X., Schools G.P., Ma L., Kimelberg H.K.,
Chen H.;
"TWIK-1 and TREK-1 are potassium channels contributing significantly
to astrocyte passive conductance in rat hippocampal slices.";
J. Neurosci. 29:8551-8564(2009).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-274.
PubMed=22948150; DOI=10.1074/jbc.M112.398164;
Ma L., Zhang X., Zhou M., Chen H.;
"Acid-sensitive TWIK and TASK two-pore domain potassium channels
change ion selectivity and become permeable to sodium in extracellular
acidification.";
J. Biol. Chem. 287:37145-37153(2012).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[11]
TISSUE SPECIFICITY.
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).
[12]
TISSUE SPECIFICITY.
PubMed=25305496; DOI=10.1016/j.bbrc.2014.10.012;
Burgos P., Zuniga R., Dominguez P., Delgado-Lopez F., Plant L.D.,
Zuniga L.;
"Differential expression of two-pore domain potassium channels in rat
cerebellar granule neurons.";
Biochem. Biophys. Res. Commun. 453:754-760(2014).
[13]
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).
[14]
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:17452494, PubMed:19571146). 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:22948150).
The homodimer has very low potassium channel activity, when
expressed in heterologous systems, and can function as weakly
inward rectifying potassium channel. Channel activity is modulated
by activation of serotonin receptors (PubMed:17452494).
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. 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 (By similarity). Contributes to
the regulation of action potential firing in dentate gyrus granule
cells and down-regulates their intrinsic excitability (By
similarity). Contributes to the regulation of the resting membrane
potential of pancreatic beta cells (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). 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 (By similarity). {ECO:0000250|UniProtKB:O00180,
ECO:0000250|UniProtKB:O08581, ECO:0000269|PubMed:17452494,
ECO:0000269|PubMed:19571146, ECO:0000269|PubMed:22948150}.
-!- ACTIVITY REGULATION: Inhibited by 100 uM quinine. Slightly
inhibited by Ba(+) (PubMed:17452494). Activity is first increased
and then decreased when the extracellular pH is lowered to 6.0
(PubMed:17452494, PubMed:22948150). {ECO:0000269|PubMed:17452494,
ECO:0000269|PubMed:22948150}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Note=Both activation and channel closure are very rapid. Is not
voltage-gated (PubMed:19571146). The relationship between
voltage and current is nearly linear (PubMed:19571146).
{ECO:0000269|PubMed:19571146, ECO:0000305};
-!- SUBUNIT: Homodimer; disulfide-linked (PubMed:9843722). 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 (By similarity). 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 (By similarity).
{ECO:0000250|UniProtKB:O00180, ECO:0000250|UniProtKB:O08581,
ECO:0000305|PubMed:9843722}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17452494,
ECO:0000269|PubMed:19571146, ECO:0000269|PubMed:22948150}; Multi-
pass membrane protein {ECO:0000250|UniProtKB:O00180}. Recycling
endosome {ECO:0000250|UniProtKB:O00180}. Apical cell membrane
{ECO:0000269|PubMed:12855359, ECO:0000269|PubMed:9843722}; Multi-
pass membrane protein {ECO:0000250|UniProtKB:O00180}. Cytoplasmic
vesicle {ECO:0000269|PubMed:9843722}. Perikaryon
{ECO:0000269|PubMed:18838117, ECO:0000269|PubMed:19571146}. Cell
projection, dendrite {ECO:0000250|UniProtKB:O08581}. Cell
projection {ECO:0000250|UniProtKB:O08581}. Cell junction, synapse
{ECO:0000269|PubMed:9843722}. 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
(By similarity). Detected in synaptic membranes (PubMed:9843722).
Detected at the apical cell membrane in stria vascularis in the
cochlea (PubMed:12855359). Detected on hippocampus dentate gyrus
granule cell bodies and to a lesser degree on proximal dendrites.
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
(PubMed:9843722). Predominantly in cytoplasmic structures in
kidney distal convoluted tubules and collecting ducts (By
similarity). Detected at the apical cell membrane of bronchial
epithelial cells (By similarity). {ECO:0000250|UniProtKB:O00180,
ECO:0000250|UniProtKB:O08581, ECO:0000269|PubMed:12855359,
ECO:0000269|PubMed:9843722}.
-!- TISSUE SPECIFICITY: Detected in brain and in kidney cortex and
medulla, especially at the renal brush border membranes of the
proximal convoluted tubules, in distal tubules and on intercalated
cells of the collecting duct (PubMed:9843722). Detected cerebellum
granule neurons (PubMed:25305496). Detected in astrocytes in
hippocampus stratum radiatum (PubMed:19571146). Highly expressed
in the stria vascularis in the cochlea (PubMed:12855359). Detected
in neurons in Scarpa's ganglion in the inner ear, at nerve
terminals in the crista ampullaris, in supporting cells and dark
cells, but not in hair cells (PubMed:18838117) (at protein level).
Detected in the brain cerebellar granule cell layer, amygdala,
thalamus reticular nucleus, habenula, mesencephalic trigeminal
neurons, neocortex and piriform cortex, and at lower levels in the
olfactory bulb (PubMed:11567039). Detected cerebellum granule
neurons (PubMed:23169818, PubMed:25305496). Detected in Scarpa's
ganglia and crista ampullaris in the inner ear (PubMed:18838117).
{ECO:0000269|PubMed:11567039, ECO:0000269|PubMed:12855359,
ECO:0000269|PubMed:18838117, ECO:0000269|PubMed:19571146,
ECO:0000269|PubMed:23169818, ECO:0000269|PubMed:25305496,
ECO:0000269|PubMed:9843722}.
-!- 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}.
-!- MISCELLANEOUS: When the external pH is lowered, it takes about 8
minutes till the channel has reached a new, stable state
characterized by increased Na(+) permeability. Likewise, when
raising the pH back to 7.4, it takes about 12 minutes for the
channel to regain its original selectivity for K(+).
{ECO:0000269|PubMed:22948150}.
-!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
1.A.1.8) family. {ECO:0000255}.
-----------------------------------------------------------------------
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EMBL; AF022819; AAD09336.1; -; mRNA.
EMBL; BC061807; AAH61807.1; -; mRNA.
RefSeq; NP_067720.1; NM_021688.3.
UniGene; Rn.15693; -.
ProteinModelPortal; Q9Z2T2; -.
STRING; 10116.ENSRNOP00000027058; -.
iPTMnet; Q9Z2T2; -.
PhosphoSitePlus; Q9Z2T2; -.
PaxDb; Q9Z2T2; -.
Ensembl; ENSRNOT00000027058; ENSRNOP00000027058; ENSRNOG00000019937.
Ensembl; ENSRNOT00000088626; ENSRNOP00000070146; ENSRNOG00000019937.
GeneID; 59324; -.
KEGG; rno:59324; -.
UCSC; RGD:621447; rat.
CTD; 3775; -.
RGD; 621447; Kcnk1.
eggNOG; KOG1418; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00760000118858; -.
HOGENOM; HOG000286014; -.
HOVERGEN; HBG052237; -.
InParanoid; Q9Z2T2; -.
KO; K04912; -.
OMA; VQRVTIH; -.
PhylomeDB; Q9Z2T2; -.
TreeFam; TF313947; -.
Reactome; R-RNO-1299308; Tandem of pore domain in a weak inwardly rectifying K+ channels (TWIK).
Reactome; R-RNO-5576886; Phase 4 - resting membrane potential.
PRO; PR:Q9Z2T2; -.
Proteomes; UP000002494; Chromosome 19.
Bgee; ENSRNOG00000019937; Expressed in 10 organ(s), highest expression level in brain.
Genevisible; Q9Z2T2; RN.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0031526; C:brush border membrane; IDA:RGD.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
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; IEA:Ensembl.
GO; GO:1902937; C:inward rectifier potassium channel complex; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0005267; F:potassium channel activity; ISS:UniProtKB.
GO; GO:0022841; F:potassium ion leak channel activity; IDA:UniProtKB.
GO; GO:0005272; F:sodium channel activity; ISS:UniProtKB.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0060075; P:regulation of resting membrane potential; ISS:UniProtKB.
GO; GO:0035094; P:response to nicotine; IEP:RGD.
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_0000299071.
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:0000244|PubMed:22673903}.
CARBOHYD 95 95 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 69 69 Interchain.
{ECO:0000250|UniProtKB:O00180}.
CROSSLNK 274 274 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250|UniProtKB:O00180}.
MUTAGEN 274 274 K->E: Strongly increases channel
activity. {ECO:0000269|PubMed:19571146,
ECO:0000269|PubMed:22948150}.
SEQUENCE 336 AA; 38228 MW; 5E78031947D75DE6 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 YVKKDKDEDQ VHIMEHDQLS
FSSITEQAAG LKEEQKQNEP FVASQSPPYE DGSANH


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