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Potassium voltage-gated channel subfamily A member 1 (MBK1) (MKI) (Voltage-gated potassium channel subunit Kv1.1)

 KCNA1_MOUSE             Reviewed;         495 AA.
P16388;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 1.
20-JUN-2018, entry version 162.
RecName: Full=Potassium voltage-gated channel subfamily A member 1;
AltName: Full=MBK1 {ECO:0000303|PubMed:2451788};
AltName: Full=MKI;
AltName: Full=Voltage-gated potassium channel subunit Kv1.1;
Name=Kcna1;
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 [GENOMIC DNA].
PubMed=2305265; DOI=10.1126/science.2305265;
Chandy K.G., Williams C.B., Spencer R.H., Aguilar B.A., Ghanshani S.,
Tempel B.L., Gutman G.A.;
"A family of three mouse potassium channel genes with intronless
coding regions.";
Science 247:973-975(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=2451788; DOI=10.1038/332837a0;
Tempel B.L., Jan Y.N., Jan L.Y.;
"Cloning of a probable potassium channel gene from mouse brain.";
Nature 332:837-839(1988).
[3]
SUBUNIT, INTERACTION WITH KCNA2, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=8361541; DOI=10.1038/365075a0;
Wang H., Kunkel D.D., Martin T.M., Schwartzkroin P.A., Tempel B.L.;
"Heteromultimeric K+ channels in terminal and juxtaparanodal regions
of neurons.";
Nature 365:75-79(1993).
[4]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=8046438;
Wang H., Kunkel D.D., Schwartzkroin P.A., Tempel B.L.;
"Localization of Kv1.1 and Kv1.2, two K channel proteins, to synaptic
terminals, somata, and dendrites in the mouse brain.";
J. Neurosci. 14:4588-4599(1994).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
PubMed=7517498;
Grissmer S., Nguyen A.N., Aiyar J., Hanson D.C., Mather R.J.,
Gutman G.A., Karmilowicz M.J., Auperin D.D., Chandy K.G.;
"Pharmacological characterization of five cloned voltage-gated K+
channels, types Kv1.1, 1.2, 1.3, 1.5, and 3.1, stably expressed in
mammalian cell lines.";
Mol. Pharmacol. 45:1227-1234(1994).
[6]
DISEASE, AND FUNCTION.
PubMed=8995755; DOI=10.1007/s003359900259;
Donahue L.R., Cook S.A., Johnson K.R., Bronson R.T., Davisson M.T.;
"Megencephaly: a new mouse mutation on chromosome 6 that causes
hypertrophy of the brain.";
Mamm. Genome 7:871-876(1996).
[7]
DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
PubMed=9736643;
Zhou L., Zhang C.L., Messing A., Chiu S.Y.;
"Temperature-sensitive neuromuscular transmission in Kv1.1 null mice:
role of potassium channels under the myelin sheath in young nerves.";
J. Neurosci. 18:7200-7215(1998).
[8]
DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=9581771; DOI=10.1016/S0896-6273(00)81018-1;
Smart S.L., Lopantsev V., Zhang C.L., Robbins C.A., Wang H.,
Chiu S.Y., Schwartzkroin P.A., Messing A., Tempel B.L.;
"Deletion of the K(V)1.1 potassium channel causes epilepsy in mice.";
Neuron 20:809-819(1998).
[9]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=10191303;
Zhang C.L., Messing A., Chiu S.Y.;
"Specific alteration of spontaneous GABAergic inhibition in cerebellar
Purkinje cells in mice lacking the potassium channel Kv1. 1.";
J. Neurosci. 19:2852-2864(1999).
[10]
DISEASE, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=14686897; DOI=10.1111/j.1460-9568.2003.03044.x;
Petersson S., Persson A.S., Johansen J.E., Ingvar M., Nilsson J.,
Klement G., Arhem P., Schalling M., Lavebratt C.;
"Truncation of the Shaker-like voltage-gated potassium channel, Kv1.1,
causes megencephaly.";
Eur. J. Neurosci. 18:3231-3240(2003).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12611922; DOI=10.1113/jphysiol.2002.035568;
Brew H.M., Hallows J.L., Tempel B.L.;
"Hyperexcitability and reduced low threshold potassium currents in
auditory neurons of mice lacking the channel subunit Kv1.1.";
J. Physiol. (Lond.) 548:1-20(2003).
[12]
RNA EDITING OF POSITION 400.
PubMed=12907802; DOI=10.1126/science.1086763;
Hoopengardner B., Bhalla T., Staber C., Reenan R.;
"Nervous system targets of RNA editing identified by comparative
genomics.";
Science 301:832-836(2003).
[13]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH KCNAB1.
PubMed=15361858; DOI=10.1038/nsmb825;
Bhalla T., Rosenthal J.J., Holmgren M., Reenan R.;
"Control of human potassium channel inactivation by editing of a small
mRNA hairpin.";
Nat. Struct. Mol. Biol. 11:950-956(2004).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[15]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=17250763; DOI=10.1186/1471-2202-8-10;
Persson A.S., Westman E., Wang F.H., Khan F.H., Spenger C.,
Lavebratt C.;
"Kv1.1 null mice have enlarged hippocampus and ventral cortex.";
BMC Neurosci. 8:10-10(2007).
[16]
DISEASE, AND FUNCTION.
PubMed=17315199; DOI=10.1002/hipo.20268;
Almgren M., Persson A.S., Fenghua C., Witgen B.M., Schalling M.,
Nyengaard J.R., Lavebratt C.;
"Lack of potassium channel induces proliferation and survival causing
increased neurogenesis and two-fold hippocampus enlargement.";
Hippocampus 17:292-304(2007).
[17]
REVIEW.
PubMed=17917103; DOI=10.1007/s12035-007-8001-0;
Baranauskas G.;
"Ionic channel function in action potential generation: current
perspective.";
Mol. Neurobiol. 35:129-150(2007).
[18]
TISSUE SPECIFICITY.
PubMed=19307729; DOI=10.1172/JCI36948;
Glaudemans B., van der Wijst J., Scola R.H., Lorenzoni P.J.,
Heister A., van der Kemp A.W., Knoers N.V., Hoenderop J.G.,
Bindels R.J.;
"A missense mutation in the Kv1.1 voltage-gated potassium channel-
encoding gene KCNA1 is linked to human autosomal dominant
hypomagnesemia.";
J. Clin. Invest. 119:936-942(2009).
[19]
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).
[20]
DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=20392939; DOI=10.1523/JNEUROSCI.5591-09.2010;
Glasscock E., Yoo J.W., Chen T.T., Klassen T.L., Noebels J.L.;
"Kv1.1 potassium channel deficiency reveals brain-driven cardiac
dysfunction as a candidate mechanism for sudden unexplained death in
epilepsy.";
J. Neurosci. 30:5167-5175(2010).
[21]
DISEASE, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=21966978; DOI=10.1111/j.1460-9568.2011.07834.x;
Fisahn A., Lavebratt C., Canlon B.;
"Acoustic startle hypersensitivity in Mceph mice and its effect on
hippocampal excitability.";
Eur. J. Neurosci. 34:1121-1130(2011).
[22]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=21233214; DOI=10.1074/jbc.M110.153262;
Fulton S., Thibault D., Mendez J.A., Lahaie N., Tirotta E.,
Borrelli E., Bouvier M., Tempel B.L., Trudeau L.E.;
"Contribution of Kv1.2 voltage-gated potassium channel to D2
autoreceptor regulation of axonal dopamine overflow.";
J. Biol. Chem. 286:9360-9372(2011).
[23]
TISSUE SPECIFICITY, DISEASE, AND DISRUPTION PHENOTYPE.
PubMed=21483673; DOI=10.1371/journal.pone.0018213;
Ma Z., Lavebratt C., Almgren M., Portwood N., Forsberg L.E.,
Branstrom R., Berglund E., Falkmer S., Sundler F., Wierup N.,
Bjorklund A.;
"Evidence for presence and functional effects of Kv1.1 channels in
beta-cells: general survey and results from mceph/mceph mice.";
PLoS ONE 6:E18213-E18213(2011).
[24]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=22396426; DOI=10.1523/JNEUROSCI.1958-11.2012;
Allen P.D., Ison J.R.;
"Kcna1 gene deletion lowers the behavioral sensitivity of mice to
small changes in sound location and increases asynchronous brainstem
auditory evoked potentials but does not affect hearing thresholds.";
J. Neurosci. 32:2538-2543(2012).
[25]
FUNCTION.
PubMed=22411008; DOI=10.1113/jphysiol.2012.228486;
Yang S.B., Mclemore K.D., Tasic B., Luo L., Jan Y.N., Jan L.Y.;
"Kv1.1-dependent control of hippocampal neuron number as revealed by
mosaic analysis with double markers.";
J. Physiol. (Lond.) 590:2645-2658(2012).
[26]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=22641786; DOI=10.1113/jphysiol.2012.235606;
Glasscock E., Qian J., Kole M.J., Noebels J.L.;
"Transcompartmental reversal of single fibre hyperexcitability in
juxtaparanodal Kv1.1-deficient vagus nerve axons by activation of
nodal KCNQ channels.";
J. Physiol. (Lond.) 590:3913-3926(2012).
[27]
FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=22158511; DOI=10.1038/nn.3006;
Li K.X., Lu Y.M., Xu Z.H., Zhang J., Zhu J.M., Zhang J.M., Cao S.X.,
Chen X.J., Chen Z., Luo J.H., Duan S., Li X.M.;
"Neuregulin 1 regulates excitability of fast-spiking neurons through
Kv1.1 and acts in epilepsy.";
Nat. Neurosci. 15:267-273(2012).
[28]
FUNCTION.
PubMed=23466697; DOI=10.1016/j.nbd.2013.02.009;
Simeone T.A., Simeone K.A., Samson K.K., Kim D.Y., Rho J.M.;
"Loss of the Kv1.1 potassium channel promotes pathologic sharp waves
and high frequency oscillations in in vitro hippocampal slices.";
Neurobiol. Dis. 54:68-81(2013).
[29]
FUNCTION, DISEASE, AND TISSUE SPECIFICITY.
PubMed=23473320; DOI=10.1016/j.neuron.2012.12.035;
Hao J., Padilla F., Dandonneau M., Lavebratt C., Lesage F., Noel J.,
Delmas P.;
"Kv1.1 channels act as mechanical brake in the senses of touch and
pain.";
Neuron 77:899-914(2013).
[30]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=25377007; DOI=10.1111/epi.12793;
Moore B.M., Jerry Jou C., Tatalovic M., Kaufman E.S., Kline D.D.,
Kunze D.L.;
"The Kv1.1 null mouse, a model of sudden unexpected death in epilepsy
(SUDEP).";
Epilepsia 55:1808-1816(2014).
[31]
INTERACTION WITH ANK3, AND INDUCTION BY MAGNESIUM.
PubMed=23903368; DOI=10.1038/ki.2013.280;
San-Cristobal P., Lainez S., Dimke H., de Graaf M.J., Hoenderop J.G.,
Bindels R.J.;
"Ankyrin-3 is a novel binding partner of the voltage-gated potassium
channel Kv1.1 implicated in renal magnesium handling.";
Kidney Int. 85:94-102(2014).
-!- FUNCTION: Voltage-gated potassium channel that mediates
transmembrane potassium transport in excitable membranes,
primarily in the brain and the central nervous system, but also in
the kidney. Contributes to the regulation of the membrane
potential and nerve signaling, and prevents neuronal
hyperexcitability (PubMed:9736643, PubMed:9581771 PubMed:10191303,
PubMed:12611922, PubMed:21966978, PubMed:22158511,
PubMed:23473320). Forms tetrameric potassium-selective channels
through which potassium ions pass in accordance with their
electrochemical gradient. The channel alternates between opened
and closed conformations in response to the voltage difference
across the membrane (PubMed:15361858). Can form functional
homotetrameric channels and heterotetrameric channels that contain
variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNA7,
and possibly other family members as well; channel properties
depend on the type of alpha subunits that are part of the channel.
Channel properties are modulated by cytoplasmic beta subunits that
regulate the subcellular location of the alpha subunits and
promote rapid inactivation of delayed rectifier potassium channels
(PubMed:15361858). In vivo, membranes probably contain a mixture
of heteromeric potassium channel complexes, making it difficult to
assign currents observed in intact tissues to any particular
potassium channel family member. Homotetrameric KCNA1 forms a
delayed-rectifier potassium channel that opens in response to
membrane depolarization, followed by slow spontaneous channel
closure (PubMed:7517498, PubMed:15361858). In contrast, a
heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid
inactivation (By similarity). Regulates neuronal excitability in
hippocampus, especially in mossy fibers and medial perforant path
axons, preventing neuronal hyperexcitability (PubMed:23466697).
May function as down-stream effector for G protein-coupled
receptors and inhibit GABAergic inputs to basolateral amygdala
neurons (By similarity). May contribute to the regulation of
neurotransmitter release, such as gamma-aminobutyric acid (GABA)
release (By similarity). Plays a role in regulating the generation
of action potentials and preventing hyperexcitability in
myelinated axons of the vagus nerve, and thereby contributes to
the regulation of heart contraction (PubMed:20392939,
PubMed:22641786, PubMed:25377007). Required for normal
neuromuscular responses (PubMed:9736643). Regulates the frequency
of neuronal action potential firing in response to mechanical
stimuli, and plays a role in the perception of pain caused by
mechanical stimuli, but does not play a role in the perception of
pain due to heat stimuli (PubMed:23473320). Required for normal
responses to auditory stimuli and precise location of sound
sources, but not for sound perception (PubMed:21966978,
PubMed:22396426). The use of toxins that block specific channels
suggest that it contributes to the regulation of the axonal
release of the neurotransmitter dopamine (PubMed:21233214).
Required for normal postnatal brain development and normal
proliferation of neuronal precursor cells in the brain
(PubMed:8995755, PubMed:17250763, PubMed:17315199,
PubMed:22411008). Plays a role in the reabsorption of Mg(2+) in
the distal convoluted tubules in the kidney and in magnesium ion
homeostasis, probably via its effect on the membrane potential (By
similarity). {ECO:0000250|UniProtKB:P10499,
ECO:0000250|UniProtKB:Q09470, ECO:0000269|PubMed:10191303,
ECO:0000269|PubMed:12611922, ECO:0000269|PubMed:15361858,
ECO:0000269|PubMed:17250763, ECO:0000269|PubMed:17315199,
ECO:0000269|PubMed:20392939, ECO:0000269|PubMed:21233214,
ECO:0000269|PubMed:21966978, ECO:0000269|PubMed:22158511,
ECO:0000269|PubMed:22396426, ECO:0000269|PubMed:22411008,
ECO:0000269|PubMed:22641786, ECO:0000269|PubMed:23466697,
ECO:0000269|PubMed:23473320, ECO:0000269|PubMed:25377007,
ECO:0000269|PubMed:7517498, ECO:0000269|PubMed:8995755,
ECO:0000269|PubMed:9581771, ECO:0000269|PubMed:9736643}.
-!- ENZYME REGULATION: Inhibited by 4-aminopyridine (4-AP),
tetraethylammonium (TEA) and dendrotoxin (DTX), but not by
charybdotoxin (CTX). {ECO:0000269|PubMed:7517498}.
-!- SUBUNIT: Homotetramer and heterotetramer with other channel-
forming alpha subunits, such as KCNA2, KCNA4, KCNA5, KCNA6 and
KCNA7 (PubMed:8361541). Channel activity is regulated by
interaction with the beta subunits KCNAB1 and KCNAB2
(PubMed:15361858). Identified in a complex with KCNA2 and KCNAB2.
Interacts (via C-terminus) with the PDZ domains of DLG1, DLG2 and
DLG4 (By similarity). Interacts with LGI1 within a complex
containing LGI1, KCNA4 and KCNAB1 (By similarity). Interacts (via
N-terminus) with STX1A; this promotes channel inactivation (By
similarity). Interacts (via N-terminus) with the heterodimer
formed by GNB1 and GNG2; this promotes channel inactivation (By
similarity). Can interact simultaneously with STX1A and the
heterodimer formed by GNB1 and GNG2 (By similarity). Interacts
(via cytoplasmic N-terminal domain) with KCNRG; this inhibits
channel activity (By similarity). Interacts with ANK3; this
inhibits channel activity (PubMed:23903368).
{ECO:0000250|UniProtKB:P10499, ECO:0000250|UniProtKB:Q09470,
ECO:0000269|PubMed:15361858, ECO:0000269|PubMed:23903368,
ECO:0000269|PubMed:8361541, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15361858,
ECO:0000269|PubMed:7517498}; Multi-pass membrane protein
{ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:20392939,
ECO:0000269|PubMed:21233214, ECO:0000269|PubMed:8046438,
ECO:0000269|PubMed:8361541, ECO:0000269|PubMed:9581771,
ECO:0000269|PubMed:9736643}. Membrane
{ECO:0000269|PubMed:22158511}. Perikaryon
{ECO:0000269|PubMed:12611922, ECO:0000269|PubMed:8046438}. Cell
projection, dendrite {ECO:0000269|PubMed:8046438}. Cell junction
{ECO:0000269|PubMed:8046438}. Cell junction, synapse
{ECO:0000269|PubMed:8046438}. Cytoplasmic vesicle
{ECO:0000269|PubMed:12611922}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:P10499}. Cell junction, synapse,
presynaptic cell membrane {ECO:0000250|UniProtKB:P10499}.
Note=Homotetrameric KCNA1 is primarily located in the endoplasmic
reticulum. Interaction with KCNA2 and KCNAB2 or with KCNA4 and
KCNAB2 promotes expression at the cell membrane (By similarity).
Detected at axon terminals (PubMed:21233214).
{ECO:0000250|UniProtKB:P10499, ECO:0000269|PubMed:21233214}.
-!- TISSUE SPECIFICITY: Detected in brain (PubMed:21483673,
PubMed:22158511). Detected in the juxtaparanodal regions of the
nodes of Ranvier in myelinated axons (PubMed:8361541,
PubMed:8046438). Detected in the paranodal region in sciatic nerve
(PubMed:9736643). Detected on cell bodies in cerebellum, dorsal
and ventral cochlear nucleus, pontine reticular nucleus,
mesencephalic trigeminal nucleus, motor trigeminal nucleus and the
pricipal sensory trigeminal nucleus (PubMed:8046438). Detected in
terminal fields of basket cells in the cerebellum corpus medullare
(PubMed:8361541, PubMed:8046438, PubMed:9581771). Detected in
hippocampus CA3 pyramidal neurons and in the hilus and stratum
moleculare of the dentate gyrus (PubMed:8046438, PubMed:9581771,
PubMed:14686897). Detected in the central nucleus and the external
nucleus of the inferior colliculus (PubMed:8046438,
PubMed:21966978). Detected in fiber tracts in the optic tract,
external medullary lamina, stria terminalis, medulla, ventral
pallidum and substantia nigra (PubMed:8046438). Detected in
neurons from dorsal root ganglion (PubMed:23473320). Detected in
neurons in the medial nucleus of the trapezoid body
(PubMed:12611922). Detected in midbrain dopamine neuron axon
terminals (PubMed:21233214). Detected in brain cortex
(PubMed:8046438, PubMed:14686897). Detected in brainstem
(PubMed:8361541). Detected in juxtaparanodal regions of the nodes
of Ranvier in the vagus nerve, but only at very low levels in the
heart (PubMed:20392939, PubMed:22641786). Detected in the islet of
Langerhans (PubMed:21483673). Detected at the luminal membrane in
distal convoluted tubules in the kidney (at protein level)
(PubMed:19307729). Detected in brain (PubMed:2451788,
PubMed:9581771). Detected in hippocampus, thalamus, neocortex and
ventral brain cortex, including the piriform and entorhinal cortex
and the amygdala (PubMed:14686897). Detected in midbrain dopamine
neurons (PubMed:21233214). Detected in heart atrium, ventricle,
sinoatrial node and atrioventricular node (PubMed:20392939).
Detected in the islet of Langerhans (PubMed:21483673).
{ECO:0000269|PubMed:12611922, ECO:0000269|PubMed:14686897,
ECO:0000269|PubMed:19307729, ECO:0000269|PubMed:20392939,
ECO:0000269|PubMed:21233214, ECO:0000269|PubMed:21483673,
ECO:0000269|PubMed:21966978, ECO:0000269|PubMed:22158511,
ECO:0000269|PubMed:22641786, ECO:0000269|PubMed:23473320,
ECO:0000269|PubMed:2451788, ECO:0000269|PubMed:8046438,
ECO:0000269|PubMed:8361541, ECO:0000269|PubMed:9581771,
ECO:0000269|PubMed:9736643}.
-!- INDUCTION: Down-regulated by high dietary Mg(2+) levels.
{ECO:0000269|PubMed:23903368}.
-!- DOMAIN: The cytoplasmic N-terminus is important for
tetramerization and for interaction with the beta subunits that
promote rapid channel closure. {ECO:0000250|UniProtKB:P10499}.
-!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor
and is characterized by a series of positively charged amino acids
at every third position. Channel opening and closing is effected
by a conformation change that affects the position and orientation
of the voltage-sensor paddle formed by S3 and S4 within the
membrane. A transmembrane electric field that is positive inside
would push the positively charged S4 segment outwards, thereby
opening the pore, while a field that is negative inside would pull
the S4 segment inwards and close the pore. Changes in the position
and orientation of S4 are then transmitted to the activation gate
formed by the inner helix bundle via the S4-S5 linker region.
{ECO:0000250|UniProtKB:P63142}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P10499}.
-!- PTM: Palmitoylated on Cys-243; which may be required for membrane
targeting. {ECO:0000250|UniProtKB:Q09470}.
-!- PTM: Phosphorylated on tyrosine residues. Phosphorylation
increases in response to NRG1; this inhibits channel activity
(PubMed:22158511). Phosphorylation at Ser-446 regulates channel
activity by down-regulating expression at the cell membrane (By
similarity). {ECO:0000250|UniProtKB:Q09470,
ECO:0000269|PubMed:22158511}.
-!- RNA EDITING: Modified_positions=400 {ECO:0000269|PubMed:12907802};
Note=Partially edited. RNA editing varies from 35% in the frontal
cortex to 75% in the spinal chord.;
-!- DISEASE: Note=A spontaneous mutation leading to a frameshift and
truncation of Kcna2 causes megencephaly with a 25% increase of
brain weight relative to wild-type. Especially the hippocampus
shows increased proliferation of neurons and astrocytes, leading
to increased brain volume (PubMed:17315199). Mutant mice appear
normal at birth. After 3-4 weeks, they display low body weight, a
subtle shakiness in their gait, a preference for a strange sitting
position that is maintained for periods ranging from 30 seconds to
several minutes, excessive lacrimation and acoustic startle
hypersensitivity (PubMed:8995755, PubMed:21966978). The increase
in the acoustic startle response is down-regulated by treatment
with the anti-epileptic drug valproate (PubMed:21966978). Mutant
mice display an abnormal electro-encephalogram with single spikes
and waves, when anesthesized (PubMed:21966978). The electric
activity of mossy cells from the dentate hilus region is altered
and shows increased firing of action potentials, probably due to
the absence of functional Kcna1 channels (PubMed:14686897).
Heterozygotes show mechanical allodynia, but no increased
sensitivity to heat (PubMed:23473320). Homozygotes show no
alteration of the islet of Langerhans structure, of the basal
levels of insulin secretion and blood glucose levels
(PubMed:21483673). Compared to wild-type, they display moderately
increased insulin secretion in response to a glucose stimulus
(PubMed:21483673). Besides, the frequency of beta cell action
potentials is increased (PubMed:21483673).
{ECO:0000269|PubMed:14686897, ECO:0000269|PubMed:17315199,
ECO:0000269|PubMed:21483673, ECO:0000269|PubMed:21966978,
ECO:0000269|PubMed:8995755}.
-!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian
rate. After three weeks, mice begin to display episodic eye
blinking, twitching of whiskers, forlimb padding, arrested motion
and a hyperstartle response. About 50% of the homozygotes die
between the third and the fifth week after birth. Surviving mice
continue to display spontaneous seizures occurring once or twice
every hour throughout adult life (PubMed:9581771). The fecundity
of homozygotes is extremely low (PubMed:9581771). Mutant mice
display interictal cardiac abnormalities, including a fivefold
increase in atrioventricular conduction blocks, brachycardia and
premature ventricular contractions; this may lead to sudden
unexplained death in epilepsy (PubMed:20392939). Mutant mice have
slightly elevated heart rates; they all have a reduced livespan
and are subject to sudden death after presumed seizure activity
and sinus bradycardia (PubMed:25377007). About 70% of the mutant
mice have an enlarged hippocampus and ventral brain cortex
(PubMed:17250763). Mutant mice show a temperature-sensitive
alteration in neuromuscular transmission, causing nerve
hyperexcitability when exposed to cold and delayed repetitive
discharge after a single nerve stimulation (PubMed:9736643). After
2 minutes of swimming in cold water, mutant mice have impaired
motor control; they fall over when placed on dry ground and
exhibit severe neuromyotonia with violent tremors that decrease
with time, leading to full recovery after twenty minutes
(PubMed:9736643). Mutant mice have an increased frequency of
spontaneous postsynaptic currents in Purkinje cells, impaired
ability to maintain their balance on a thin stationary rod, but
perform as well as wild-type on a rotarod (PubMed:10191303).
Mutant mice have a normal hearing threshold, but altered brainstem
responses to auditory stimuli and reduced sensitivity to small
changes in sound location (PubMed:22396426). Mutant mice display
no alteration of the islet of Langerhans, but have reduced blood
glucose levels and increased insulin secretion in response to a
glucose stimulus (PubMed:21483673). {ECO:0000269|PubMed:10191303,
ECO:0000269|PubMed:17250763, ECO:0000269|PubMed:20392939,
ECO:0000269|PubMed:21483673, ECO:0000269|PubMed:22396426,
ECO:0000269|PubMed:25377007, ECO:0000269|PubMed:9581771,
ECO:0000269|PubMed:9736643}.
-!- MISCELLANEOUS: The delay or D-type current observed in hippocampus
pyramidal neurons is probably mediated by potassium channels
containing KCNA2 plus KCNA1 or other family members. It is
activated at about -50 mV, i.e. below the action potential
threshold, and is characterized by slow inactivation, extremely
slow recovery from inactivation, sensitivity to dendrotoxin (DTX)
and to 4-aminopyridine (4-AP). {ECO:0000305|PubMed:17917103}.
-!- SIMILARITY: Belongs to the potassium channel family. A (Shaker)
(TC 1.A.1.2) subfamily. Kv1.1/KCNA1 sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M30439; AAA39711.1; -; Genomic_DNA.
EMBL; Y00305; CAA68408.1; -; mRNA.
CCDS; CCDS20555.1; -.
PIR; A40090; A40090.
PIR; S09042; S09042.
RefSeq; NP_034725.3; NM_010595.3.
UniGene; Mm.40424; -.
ProteinModelPortal; P16388; -.
SMR; P16388; -.
BioGrid; 200876; 3.
IntAct; P16388; 3.
MINT; P16388; -.
STRING; 10090.ENSMUSP00000055225; -.
ChEMBL; CHEMBL2429705; -.
GuidetoPHARMACOLOGY; 538; -.
iPTMnet; P16388; -.
PhosphoSitePlus; P16388; -.
MaxQB; P16388; -.
PaxDb; P16388; -.
PeptideAtlas; P16388; -.
PRIDE; P16388; -.
Ensembl; ENSMUST00000055168; ENSMUSP00000055225; ENSMUSG00000047976.
Ensembl; ENSMUST00000203094; ENSMUSP00000144947; ENSMUSG00000047976.
GeneID; 16485; -.
KEGG; mmu:16485; -.
UCSC; uc009dvb.1; mouse.
CTD; 3736; -.
MGI; MGI:96654; Kcna1.
eggNOG; KOG1545; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00760000118846; -.
HOGENOM; HOG000231015; -.
HOVERGEN; HBG052230; -.
InParanoid; P16388; -.
KO; K04874; -.
OMA; AHYRQAN; -.
OrthoDB; EOG091G10NU; -.
PhylomeDB; P16388; -.
TreeFam; TF313103; -.
Reactome; R-MMU-1296072; Voltage gated Potassium channels.
PRO; PR:P16388; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000047976; -.
Genevisible; P16388; MM.
GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0043679; C:axon terminus; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
GO; GO:0044224; C:juxtaparanode region of axon; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0033270; C:paranode region of axon; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0034705; C:potassium channel complex; ISO:MGI.
GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
GO; GO:0045202; C:synapse; IDA:UniProtKB.
GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
GO; GO:0005251; F:delayed rectifier potassium channel activity; IDA:UniProtKB.
GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB.
GO; GO:0007420; P:brain development; IMP:UniProtKB.
GO; GO:0010644; P:cell communication by electrical coupling; ISS:UniProtKB.
GO; GO:0034613; P:cellular protein localization; ISO:MGI.
GO; GO:0071286; P:cellular response to magnesium ion; IMP:UniProtKB.
GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IMP:UniProtKB.
GO; GO:0050976; P:detection of mechanical stimulus involved in sensory perception of touch; IMP:UniProtKB.
GO; GO:0021766; P:hippocampus development; IMP:UniProtKB.
GO; GO:0010960; P:magnesium ion homeostasis; ISS:UniProtKB.
GO; GO:0007405; P:neuroblast proliferation; IMP:UniProtKB.
GO; GO:0050905; P:neuromuscular process; IMP:UniProtKB.
GO; GO:0019228; P:neuronal action potential; IMP:UniProtKB.
GO; GO:0023041; P:neuronal signal transduction; ISS:UniProtKB.
GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; ISO:MGI.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
GO; GO:0042391; P:regulation of membrane potential; ISS:UniProtKB.
GO; GO:0006937; P:regulation of muscle contraction; ISS:UniProtKB.
GO; GO:0001964; P:startle response; IMP:UniProtKB.
Gene3D; 1.20.120.350; -; 1.
InterPro; IPR000210; BTB/POZ_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR003968; K_chnl_volt-dep_Kv.
InterPro; IPR003972; K_chnl_volt-dep_Kv1.
InterPro; IPR004048; K_chnl_volt-dep_Kv1.1.
InterPro; IPR011333; SKP1/BTB/POZ_sf.
InterPro; IPR003131; T1-type_BTB.
InterPro; IPR028325; VG_K_chnl.
InterPro; IPR027359; Volt_channel_dom_sf.
PANTHER; PTHR11537; PTHR11537; 1.
Pfam; PF02214; BTB_2; 1.
Pfam; PF00520; Ion_trans; 1.
PRINTS; PR00169; KCHANNEL.
PRINTS; PR01508; KV11CHANNEL.
PRINTS; PR01491; KVCHANNEL.
PRINTS; PR01496; SHAKERCHANEL.
SMART; SM00225; BTB; 1.
SUPFAM; SSF54695; SSF54695; 1.
1: Evidence at protein level;
Cell junction; Cell membrane; Cell projection; Complete proteome;
Cytoplasmic vesicle; Endoplasmic reticulum; Glycoprotein; Ion channel;
Ion transport; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
Potassium; Potassium channel; Potassium transport; Reference proteome;
RNA editing; Synapse; Transmembrane; Transmembrane helix; Transport;
Voltage-gated channel.
CHAIN 1 495 Potassium voltage-gated channel subfamily
A member 1.
/FTId=PRO_0000053969.
TOPO_DOM 1 164 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 165 186 Helical; Name=Segment S1.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 187 220 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 221 242 Helical; Name=Segment S2.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 243 253 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 254 274 Helical; Name=Segment S3.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 275 287 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 288 308 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 309 323 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 324 345 Helical; Name=Segment S5.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 346 359 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
INTRAMEM 360 371 Helical; Name=Pore helix.
{ECO:0000250|UniProtKB:P63142}.
INTRAMEM 372 379 {ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 380 386 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 387 415 Helical; Name=Segment S6.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 416 495 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
REGION 1 128 Tetramerization domain.
{ECO:0000250|UniProtKB:P10499}.
REGION 310 323 S4-S5 linker.
{ECO:0000250|UniProtKB:P63142}.
MOTIF 372 377 Selectivity filter.
{ECO:0000250|UniProtKB:P63142}.
MOTIF 493 495 PDZ-binding. {ECO:0000250}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000250|UniProtKB:P10499}.
MOD_RES 322 322 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 437 437 Phosphoserine.
{ECO:0000250|UniProtKB:P10499}.
MOD_RES 439 439 Phosphoserine.
{ECO:0000250|UniProtKB:P10499}.
MOD_RES 446 446 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:Q09470}.
LIPID 243 243 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:Q09470}.
CARBOHYD 207 207 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 400 400 I -> V (in RNA edited version).
SEQUENCE 495 AA; 56409 MW; C9249F130E943D3D CRC64;
MTVMSGENAD EASTAPGHPQ DGSYPRQADH DDHECCERVV INISGLRFET QLKTLAQFPN
TLLGNPKKRM RYFDPLRNEY FFDRNRPSFD AILYYYQSGG RLRRPVNVPL DMFSEEIKFY
ELGEEAMEKF REDEGFIKEE ERPLPEKEYQ RQVWLLFEYP ESSGPARVIA IVSVMVILIS
IVIFCLETLP ELKDDKDFTG TIHRIDNTTV IYTSNIFTDP FFIVETLCII WFSFELVVRF
FACPSKTDFF KNIMNFIDIV AIIPYFITLG TEIAEQEGNQ KGEQATSLAI LRVIRLVRVF
RIFKLSRHSK GLQILGQTLK ASMRELGLLI FFLFIGVILF SSAVYFAEAE EAESHFSSIP
DAFWWAVVSM TTVGYGDMYP VTIGGKIVGS LCAIAGVLTI ALPVPVIVSN FNYFYHRETE
GEEQAQLLHV SSPNLASDSD LSRRSSSTIS KSEYMEIEED MNNSIAHYRQ ANIRTGNCTT
ADQNCVNKSK LLTDV


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