KCNK1_RAT
ID KCNK1_RAT Reviewed; 336 AA.
AC Q9Z2T2;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Potassium channel subfamily K member 1;
DE AltName: Full=Inward rectifying potassium channel protein TWIK-1;
DE Short=rTWIK;
DE AltName: Full=Potassium channel K2P1 {ECO:0000303|PubMed:25305496};
GN Name=Kcnk1 {ECO:0000312|RGD:621447};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAD09336.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Gan L., Joiner W.J., Quinn A.M., Wang L.-Y., Hughes T., Kaczmarek L.K.;
RT "Cloning and localization of rTWIK, a putative potassium channel with two P
RT domains.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAH61807.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate {ECO:0000312|EMBL:AAH61807.1};
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 [3]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=9843722; DOI=10.1152/ajpcell.1998.275.6.c1602;
RA Cluzeaud F., Reyes R., Escoubet B., Fay M., Lazdunski M., Bonvalet J.P.,
RA Lesage F., Farman N.;
RT "Expression of TWIK-1, a novel weakly inward rectifying potassium channel
RT in rat kidney.";
RL Am. J. Physiol. 275:C1602-C1609(1998).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=11567039; DOI=10.1523/jneurosci.21-19-07491.2001;
RA Talley E.M., Solorzano G., Lei Q., Kim D., Bayliss D.A.;
RT "Cns distribution of members of the two-pore-domain (KCNK) potassium
RT channel family.";
RL J. Neurosci. 21:7491-7505(2001).
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 FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RX PubMed=17452494; DOI=10.1124/mol.107.034389;
RA Deng P.Y., Poudel S.K., Rojanathammanee L., Porter J.E., Lei S.;
RT "Serotonin inhibits neuronal excitability by activating two-pore domain K+
RT channels in the entorhinal cortex.";
RL Mol. Pharmacol. 72:208-218(2007).
RN [7]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=18838117; DOI=10.1016/j.heares.2008.09.004;
RA Popper P., Winkler J., Erbe C.B., Lerch-Gaggl A., Siebeneich W.,
RA Wackym P.A.;
RT "Distribution of two-pore-domain potassium channels in the adult rat
RT vestibular periphery.";
RL Hear. Res. 246:1-8(2008).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-274,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19571146; DOI=10.1523/jneurosci.5784-08.2009;
RA Zhou M., Xu G., Xie M., Zhang X., Schools G.P., Ma L., Kimelberg H.K.,
RA Chen H.;
RT "TWIK-1 and TREK-1 are potassium channels contributing significantly to
RT astrocyte passive conductance in rat hippocampal slices.";
RL J. Neurosci. 29:8551-8564(2009).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-274.
RX PubMed=22948150; DOI=10.1074/jbc.m112.398164;
RA Ma L., Zhang X., Zhou M., Chen H.;
RT "Acid-sensitive TWIK and TASK two-pore domain potassium channels change ion
RT selectivity and become permeable to sodium in extracellular
RT acidification.";
RL J. Biol. Chem. 287:37145-37153(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=23169818; DOI=10.1126/scisignal.2003431;
RA Plant L.D., Zuniga L., Araki D., Marks J.D., Goldstein S.A.;
RT "SUMOylation silences heterodimeric TASK potassium channels containing K2P1
RT subunits in cerebellar granule neurons.";
RL Sci. Signal. 5:RA84-RA84(2012).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=25305496; DOI=10.1016/j.bbrc.2014.10.012;
RA Burgos P., Zuniga R., Dominguez P., Delgado-Lopez F., Plant L.D.,
RA Zuniga L.;
RT "Differential expression of two-pore domain potassium channels in rat
RT cerebellar granule neurons.";
RL Biochem. Biophys. Res. Commun. 453:754-760(2014).
RN [13]
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 [14]
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:17452494, PubMed:19571146). Forms dimeric channels through
CC which potassium ions pass in accordance with their electrochemical
CC gradient. The channel is selective for K(+) ions at physiological
CC potassium concentrations and at neutral pH, but becomes permeable to
CC Na(+) at subphysiological K(+) levels and upon acidification of the
CC extracellular medium (PubMed:22948150). The homodimer has very low
CC potassium channel activity, when expressed in heterologous systems, and
CC can function as weakly inward rectifying potassium channel. Channel
CC activity is modulated by activation of serotonin receptors
CC (PubMed:17452494). Heterodimeric channels containing KCNK1 and KCNK2
CC have much higher activity, and may represent the predominant form in
CC astrocytes (By similarity). Heterodimeric channels containing KCNK1 and
CC KCNK3 or KCNK9 have much higher activity. Heterodimeric channels formed
CC by KCNK1 and KCNK9 may contribute to halothane-sensitive currents (By
CC similarity). Mediates outward rectifying potassium currents in dentate
CC gyrus granule cells and contributes to the regulation of their resting
CC membrane potential (By similarity). Contributes to the regulation of
CC action potential firing in dentate gyrus granule cells and down-
CC regulates their intrinsic excitability (By similarity). Contributes to
CC the regulation of the resting membrane potential of pancreatic beta
CC cells (By similarity). In astrocytes, the heterodimer formed by KCNK1
CC and KCNK2 is required for rapid glutamate release in response to
CC activation of G-protein coupled receptors, such as F2R and CNR1 (By
CC similarity). Required for normal ion and water transport in the kidney
CC (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:O00180,
CC ECO:0000250|UniProtKB:O08581, ECO:0000269|PubMed:17452494,
CC ECO:0000269|PubMed:19571146, ECO:0000269|PubMed:22948150}.
CC -!- ACTIVITY REGULATION: Inhibited by 100 uM quinine. Slightly inhibited by
CC Ba(+) (PubMed:17452494). Activity is first increased and then decreased
CC when the extracellular pH is lowered to 6.0 (PubMed:17452494,
CC PubMed:22948150). {ECO:0000269|PubMed:17452494,
CC ECO:0000269|PubMed:22948150}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=Both activation and channel closure are very rapid. Is not
CC voltage-gated (PubMed:19571146). The relationship between voltage and
CC current is nearly linear (PubMed:19571146).
CC {ECO:0000269|PubMed:19571146, ECO:0000305};
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:9843722). Heterodimer with
CC KCNK2; disulfide-linked (By similarity). 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 (By
CC similarity). Identified in a complex with PSD and ARF6; interacts only
CC with PSD that is bound to ARF6 (By similarity). Interacts with UBE2I
CC (By similarity). {ECO:0000250|UniProtKB:O00180,
CC ECO:0000250|UniProtKB:O08581, ECO:0000305|PubMed:9843722}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17452494,
CC ECO:0000269|PubMed:19571146, ECO:0000269|PubMed:22948150}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:O00180}. Recycling endosome
CC {ECO:0000250|UniProtKB:O00180}. Apical cell membrane
CC {ECO:0000269|PubMed:12855359, ECO:0000269|PubMed:9843722}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:O00180}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:9843722}. Perikaryon {ECO:0000269|PubMed:18838117,
CC ECO:0000269|PubMed:19571146}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:O08581}. Cell projection
CC {ECO:0000250|UniProtKB:O08581}. Synaptic cell membrane
CC {ECO:0000269|PubMed:9843722}. Note=The heterodimer with KCNK2 is
CC detected at the astrocyte cell membrane. Not detected at the astrocyte
CC cell membrane when KCNK2 is absent. Detected on neuronal cell bodies,
CC and to a lesser degree on neuronal cell projections (By similarity).
CC Detected in synaptic membranes (PubMed:9843722). Detected at the apical
CC cell membrane in stria vascularis in the cochlea (PubMed:12855359).
CC Detected on hippocampus dentate gyrus granule cell bodies and to a
CC lesser degree on proximal dendrites. Detected at the apical cell
CC membrane of vestibular dark cells situated between the crista and the
CC utricle in the inner ear. Detected at the apical cell membrane in
CC kidney proximal tubule segment S1 and in subapical compartments in
CC segments S1, S2 and S3 (PubMed:9843722). Predominantly in cytoplasmic
CC structures in kidney distal convoluted tubules and collecting ducts (By
CC similarity). Detected at the apical cell membrane of bronchial
CC epithelial cells (By similarity). {ECO:0000250|UniProtKB:O00180,
CC ECO:0000250|UniProtKB:O08581, ECO:0000269|PubMed:12855359,
CC ECO:0000269|PubMed:9843722}.
CC -!- TISSUE SPECIFICITY: Detected in brain and in kidney cortex and medulla,
CC especially at the renal brush border membranes of the proximal
CC convoluted tubules, in distal tubules and on intercalated cells of the
CC collecting duct (PubMed:9843722). Detected cerebellum granule neurons
CC (PubMed:25305496). Detected in astrocytes in hippocampus stratum
CC radiatum (PubMed:19571146). Highly expressed in the stria vascularis in
CC the cochlea (PubMed:12855359). Detected in neurons in Scarpa's ganglion
CC in the inner ear, at nerve terminals in the crista ampullaris, in
CC supporting cells and dark cells, but not in hair cells
CC (PubMed:18838117) (at protein level). Detected in the brain cerebellar
CC granule cell layer, amygdala, thalamus reticular nucleus, habenula,
CC mesencephalic trigeminal neurons, neocortex and piriform cortex, and at
CC lower levels in the olfactory bulb (PubMed:11567039). Detected
CC cerebellum granule neurons (PubMed:23169818, PubMed:25305496). Detected
CC in Scarpa's ganglia and crista ampullaris in the inner ear
CC (PubMed:18838117). {ECO:0000269|PubMed:11567039,
CC ECO:0000269|PubMed:12855359, ECO:0000269|PubMed:18838117,
CC ECO:0000269|PubMed:19571146, ECO:0000269|PubMed:23169818,
CC ECO:0000269|PubMed:25305496, ECO:0000269|PubMed:9843722}.
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 -!- MISCELLANEOUS: When the external pH is lowered, it takes about 8
CC minutes till the channel has reached a new, stable state characterized
CC by increased Na(+) permeability. Likewise, when raising the pH back to
CC 7.4, it takes about 12 minutes for the channel to regain its original
CC selectivity for K(+). {ECO:0000269|PubMed:22948150}.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000255}.
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DR EMBL; AF022819; AAD09336.1; -; mRNA.
DR EMBL; BC061807; AAH61807.1; -; mRNA.
DR RefSeq; NP_067720.1; NM_021688.3.
DR PDB; 7SK0; EM; 3.33 A; A/B=1-336.
DR PDB; 7SK1; EM; 3.43 A; A/B=1-336.
DR PDBsum; 7SK0; -.
DR PDBsum; 7SK1; -.
DR AlphaFoldDB; Q9Z2T2; -.
DR SMR; Q9Z2T2; -.
DR STRING; 10116.ENSRNOP00000027058; -.
DR GlyGen; Q9Z2T2; 1 site.
DR iPTMnet; Q9Z2T2; -.
DR PhosphoSitePlus; Q9Z2T2; -.
DR PaxDb; Q9Z2T2; -.
DR Ensembl; ENSRNOT00000027058; ENSRNOP00000027058; ENSRNOG00000019937.
DR GeneID; 59324; -.
DR KEGG; rno:59324; -.
DR UCSC; RGD:621447; rat.
DR CTD; 3775; -.
DR RGD; 621447; Kcnk1.
DR eggNOG; KOG1418; Eukaryota.
DR GeneTree; ENSGT00940000155293; -.
DR HOGENOM; CLU_022504_6_0_1; -.
DR InParanoid; Q9Z2T2; -.
DR OMA; MVAIVHA; -.
DR OrthoDB; 1211599at2759; -.
DR PhylomeDB; Q9Z2T2; -.
DR TreeFam; TF313947; -.
DR Reactome; R-RNO-1299308; Tandem of pore domain in a weak inwardly rectifying K+ channels (TWIK).
DR Reactome; R-RNO-5576886; Phase 4 - resting membrane potential.
DR PRO; PR:Q9Z2T2; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000019937; Expressed in cerebellum and 15 other tissues.
DR Genevisible; Q9Z2T2; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0031526; C:brush border membrane; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:1902937; C:inward rectifier potassium channel complex; ISO:RGD.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0034705; C:potassium channel complex; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0097060; C:synaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; ISO:RGD.
DR GO; GO:0005267; F:potassium channel activity; ISS:UniProtKB.
DR GO; GO:0022841; F:potassium ion leak channel activity; IDA: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:0060075; P:regulation of resting membrane potential; ISS:UniProtKB.
DR GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR003092; 2pore_dom_K_chnl_TASK.
DR InterPro; IPR005408; 2pore_dom_K_chnl_TWIK.
DR InterPro; IPR001779; 2pore_dom_K_chnl_TWIK1.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR11003; PTHR11003; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PIRSF; PIRSF038061; K_channel_subfamily_K_type; 1.
DR PRINTS; PR01333; 2POREKCHANEL.
DR PRINTS; PR01096; TWIK1CHANNEL.
DR PRINTS; PR01586; TWIKCHANNEL.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Cytoplasmic vesicle;
KW Disulfide bond; Endosome; Glycoprotein; Ion channel; Ion transport;
KW Isopeptide bond; 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_0000299071"
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 COMPBIAS 318..336
FT /note="Polar residues"
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:0007744|PubMed:22673903"
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 CROSSLNK 274
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT MUTAGEN 274
FT /note="K->E: Strongly increases channel activity."
FT /evidence="ECO:0000269|PubMed:19571146,
FT ECO:0000269|PubMed:22948150"
FT HELIX 25..66
FT /evidence="ECO:0007829|PDB:7SK0"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:7SK0"
FT HELIX 72..88
FT /evidence="ECO:0007829|PDB:7SK0"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:7SK1"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:7SK0"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:7SK0"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:7SK0"
FT HELIX 128..160
FT /evidence="ECO:0007829|PDB:7SK0"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:7SK0"
FT HELIX 176..195
FT /evidence="ECO:0007829|PDB:7SK0"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:7SK0"
FT HELIX 212..224
FT /evidence="ECO:0007829|PDB:7SK0"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:7SK0"
FT HELIX 242..269
FT /evidence="ECO:0007829|PDB:7SK0"
FT HELIX 271..279
FT /evidence="ECO:0007829|PDB:7SK0"
SQ 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
