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Potassium voltage-gated channel subfamily C member 2 (Shaw-like potassium channel) (Voltage-gated potassium channel Kv3.2)

 KCNC2_MOUSE             Reviewed;         642 AA.
Q14B80;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
22-AUG-2006, sequence version 1.
12-SEP-2018, entry version 94.
RecName: Full=Potassium voltage-gated channel subfamily C member 2 {ECO:0000312|MGI:MGI:96668};
AltName: Full=Shaw-like potassium channel {ECO:0000250|UniProtKB:P22462};
AltName: Full=Voltage-gated potassium channel Kv3.2 {ECO:0000303|PubMed:12000114};
Name=Kcnc2 {ECO:0000312|MGI:MGI:96668};
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 [LARGE SCALE MRNA].
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).
[2]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10561420;
Erisir A., Lau D., Rudy B., Leonard C.S.;
"Function of specific K(+) channels in sustained high-frequency firing
of fast-spiking neocortical interneurons.";
J. Neurophysiol. 82:2476-2489(1999).
[3]
REVIEW.
PubMed=10414303; DOI=10.1111/j.1749-6632.1999.tb11295.x;
Rudy B., Chow A., Lau D., Amarillo Y., Ozaita A., Saganich M.,
Moreno H., Nadal M.S., Hernandez-Pineda R., Hernandez-Cruz A.,
Erisir A., Leonard C., Vega-Saenz de Miera E.;
"Contributions of Kv3 channels to neuronal excitability.";
Ann. N. Y. Acad. Sci. 868:304-343(1999).
[4]
SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10531438;
Chow A., Erisir A., Farb C., Nadal M.S., Ozaita A., Lau D., Welker E.,
Rudy B.;
"K(+) channel expression distinguishes subpopulations of
parvalbumin- and somatostatin-containing neocortical interneurons.";
J. Neurosci. 19:9332-9345(1999).
[5]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=11124984;
Lau D., Vega-Saenz de Miera E.C., Contreras D., Ozaita A., Harvey M.,
Chow A., Noebels J.L., Paylor R., Morgan J.I., Leonard C.S., Rud y B.;
"Impaired fast-spiking, suppressed cortical inhibition, and increased
susceptibility to seizures in mice lacking Kv3.2 K+ channel
proteins.";
J. Neurosci. 20:9071-9085(2000).
[6]
FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
AND DISRUPTION PHENOTYPE.
PubMed=10903572; DOI=10.1038/77693;
Atzori M., Lau D., Tansey E.P., Chow A., Ozaita A., Rudy B.,
McBain C.J.;
"H2 histamine receptor-phosphorylation of Kv3.2 modulates interneuron
fast spiking.";
Nat. Neurosci. 3:791-798(2000).
[7]
REVIEW.
PubMed=11506885; DOI=10.1016/S0166-2236(00)01892-0;
Rudy B., McBain C.J.;
"Kv3 channels: voltage-gated K+ channels designed for high-frequency
repetitive firing.";
Trends Neurosci. 24:517-526(2001).
[8]
INTERACTION WITH KCNC1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12000114; DOI=10.1002/hipo.1104;
Tansey E.P., Chow A., Rudy B., McBain C.J.;
"Developmental expression of potassium-channel subunit Kv3.2 within
subpopulations of mouse hippocampal inhibitory interneurons.";
Hippocampus 12:137-148(2002).
[9]
FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
SPECIFICITY.
PubMed=15317859; DOI=10.1523/JNEUROSCI.1275-04.2004;
Ozaita A., Petit-Jacques J., Volgyi B., Ho C.S., Joho R.H.,
Bloomfield S.A., Rudy B.;
"A unique role for Kv3 voltage-gated potassium channels in starburst
amacrine cell signaling in mouse retina.";
J. Neurosci. 24:7335-7343(2004).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=15917463; DOI=10.1523/JNEUROSCI.0722-05.2005;
Goldberg E.M., Watanabe S., Chang S.Y., Joho R.H., Huang Z.J.,
Leonard C.S., Rudy B.;
"Specific functions of synaptically localized potassium channels in
synaptic transmission at the neocortical GABAergic fast-spiking cell
synapse.";
J. Neurosci. 25:5230-5235(2005).
[11]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15852012; DOI=10.1038/nn1448;
Itri J.N., Michel S., Vansteensel M.J., Meijer J.H., Colwell C.S.;
"Fast delayed rectifier potassium current is required for circadian
neural activity.";
Nat. Neurosci. 8:650-656(2005).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=17761775; DOI=10.1113/jphysiol.2007.141135;
Kasten M.R., Rudy B., Anderson M.P.;
"Differential regulation of action potential firing in adult murine
thalamocortical neurons by Kv3.2, Kv1, and SK potassium and N-type
calcium channels.";
J. Physiol. (Lond.) 584:565-582(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, AND 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).
[14]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=21414897; DOI=10.1523/JNEUROSCI.5792-10.2011;
Kudo T., Loh D.H., Kuljis D., Constance C., Colwell C.S.;
"Fast delayed rectifier potassium current: critical for input and
output of the circadian system.";
J. Neurosci. 31:2746-2755(2011).
[15]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=21912965; DOI=10.1007/s12031-011-9648-6;
Boda E., Hoxha E., Pini A., Montarolo F., Tempia F.;
"Brain expression of Kv3 subunits during development, adulthood and
aging and in a murine model of Alzheimer's disease.";
J. Mol. Neurosci. 46:606-615(2012).
[16]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=22539821; DOI=10.1152/jn.00102.2012;
Harvey M., Lau D., Civillico E., Rudy B., Contreras D.;
"Impaired long-range synchronization of gamma oscillations in the
neocortex of a mouse lacking Kv3.2 potassium channels.";
J. Neurophysiol. 108:827-833(2012).
-!- FUNCTION: Voltage-gated potassium channel that mediates
transmembrane potassium transport in excitable membranes,
primarily in the brain. Contributes to the regulation of the fast
action potential repolarization and in sustained high-frequency
firing in neurons of the central nervous system (PubMed:10561420,
PubMed:10414303, PubMed:11124984, PubMed:10903572,
PubMed:11506885, PubMed:15317859, PubMed:15917463,
PubMed:17761775, PubMed:21414897). Homotetramer channels mediate
delayed-rectifier voltage-dependent potassium currents that
activate rapidly at high-threshold voltages and inactivate slowly
(PubMed:10414303). Forms tetrameric 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 (By similarity). Can form functional homotetrameric and
heterotetrameric channels that contain variable proportions of
KCNC1, and possibly other family members as well; channel
properties depend on the type of alpha subunits that are part of
the channel (PubMed:10531438, PubMed:12000114). Channel properties
may be modulated by either the association with ancillary
subunits, such as KCNE1, KCNE2 and KCNE3 or indirectly by nitric
oxide (NO) through a cGMP- and PKG-mediated signaling cascade,
slowing channel activation and deactivation of delayed rectifier
potassium channels (By similarity). Contributes to fire sustained
trains of very brief action potentials at high frequency in
thalamocortical and suprachiasmatic nucleus (SCN) neurons, in
hippocampal and neocortical interneurons and in retinal ganglion
cells (PubMed:10561420, PubMed:10903572, PubMed:11506885,
PubMed:17761775). Sustained maximal action potential firing
frequency in inhibitory hippocampal interneurons is negatively
modulated by histamine H2 receptor activation in a cAMP- and
protein kinase (PKA) phosphorylation-dependent manner
(PubMed:10903572). Plays a role in maintaining the fidelity of
synaptic transmission in neocortical GABAergic interneurons by
generating action potential (AP) repolarization at nerve
terminals, thus reducing spike-evoked calcium influx and GABA
neurotransmitter release (PubMed:15917463). Required for long-
range synchronization of gamma oscillations over distance in the
neocortex (PubMed:22539821). Contributes to the modulation of the
circadian rhythm of spontaneous action potential firing in
suprachiasmatic nucleus (SCN) neurons in a light-dependent manner
(PubMed:21414897). {ECO:0000250|UniProtKB:P22462,
ECO:0000269|PubMed:10531438, ECO:0000269|PubMed:10561420,
ECO:0000269|PubMed:10903572, ECO:0000269|PubMed:11124984,
ECO:0000269|PubMed:12000114, ECO:0000269|PubMed:15317859,
ECO:0000269|PubMed:15917463, ECO:0000269|PubMed:17761775,
ECO:0000269|PubMed:21414897, ECO:0000269|PubMed:22539821,
ECO:0000305|PubMed:10414303, ECO:0000305|PubMed:11506885}.
-!- ACTIVITY REGULATION: Inhibited by millimolar levels of
tetraethylammonium (TEA). Contrary to other channels, inhibited
only by millimolar levels of 4-aminopyridine (4-AP). Inhibited by
Stichodactyla helianthus peptide ShK.
{ECO:0000250|UniProtKB:P22462, ECO:0000250|UniProtKB:Q96PR1,
ECO:0000305|PubMed:10414303}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Note=Homotetrameric channels expressed in xenopus oocytes or in
mammalian non-neuronal cells display delayed-rectifier voltage-
dependent potassium currents, that are rapidly activated during
membrane depolarization, i.e within a risetime of a few msec.
After that, inactivates very slowly, i.e within about >800 msec.
Their activation requires a threshold potential at about -10 mV,
with a midpoint activation at about 12.1 mV and a steepness
parameter of about 8.4 mV. The voltage-dependence of activation
and inactivation and other channel characteristics vary
depending on the experimental conditions, the expression system,
the presence or absence of ancillary subunits and post-
translational modifications. {ECO:0000305|PubMed:10414303};
-!- SUBUNIT: Homotetramer and heterotetramer with other channel-
forming alpha subunits, such as KCNC1 (PubMed:10531438). Interacts
with KCNC1 (PubMed:10531438, PubMed:12000114). Homotetramer or
heterotetramer channel activity is regulated by association with
modulating ancillary subunits such as KCNE1, KCNE2 and KCNE3,
creating a functionally diverse range of channel complexes.
Interacts with KCNE1, KCNE2 and KCNE3 (By similarity).
{ECO:0000250|UniProtKB:P22462, ECO:0000269|PubMed:10531438,
ECO:0000269|PubMed:12000114}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10531438,
ECO:0000269|PubMed:10561420, ECO:0000269|PubMed:10903572,
ECO:0000269|PubMed:11124984, ECO:0000269|PubMed:15317859,
ECO:0000269|PubMed:15917463, ECO:0000269|PubMed:17761775,
ECO:0000269|PubMed:21414897, ECO:0000269|PubMed:22539821}; Multi-
pass membrane protein {ECO:0000255}. Membrane
{ECO:0000269|PubMed:12000114}; Multi-pass membrane protein
{ECO:0000255}. Perikaryon {ECO:0000269|PubMed:10531438,
ECO:0000269|PubMed:10903572, ECO:0000269|PubMed:12000114,
ECO:0000269|PubMed:15317859, ECO:0000269|PubMed:15852012}. Cell
projection, axon {ECO:0000269|PubMed:10903572}. Cell projection,
dendrite {ECO:0000269|PubMed:10531438,
ECO:0000269|PubMed:10903572, ECO:0000269|PubMed:12000114,
ECO:0000269|PubMed:15317859}. Cell junction, synapse, postsynaptic
cell membrane {ECO:0000269|PubMed:10531438}. Cell junction,
synapse, presynaptic cell membrane {ECO:0000269|PubMed:10531438}.
Cell junction, synapse, synaptosome
{ECO:0000250|UniProtKB:P22462}. Cell junction, synapse
{ECO:0000250|UniProtKB:P22462}. Apical cell membrane
{ECO:0000250|UniProtKB:P22462}. Basolateral cell membrane
{ECO:0000250|UniProtKB:P22462}. Note=Colocalizes with parvalbumin
in globus pallidus neurons. Localizes in thalamocortical axons and
synapses (By similarity). Localizes on the surface of cell somata,
proximal dendrites and axonal membranes (PubMed:12000114,
PubMed:10903572). Also detected throughout the neuropil
(PubMed:12000114). Localized in starburst cell somata and proximal
dendrite processes (PubMed:15317859). Colocalized with GABA in
presynaptic terminals (PubMed:10531438). Clustered in patches in
somatic and proximal dendritic membrane as well as in axons and
presnypatic terminals of GABAergic interneurons; some of these
patches are found near postsynaptic sites (PubMed:10531438).
{ECO:0000250|UniProtKB:P22462, ECO:0000269|PubMed:10531438,
ECO:0000269|PubMed:10903572, ECO:0000269|PubMed:12000114,
ECO:0000269|PubMed:15317859}.
-!- TISSUE SPECIFICITY: Weakly expressed in the brain at postnatal age
day 7 (P7) and increased at P60 (PubMed:21912965). Not detectable
in newborn hippocampus. Expressed weakly at P7 in the early
developing hippocampus, increasing progressively and reaching a
plateau of expression at P14 that is maintained throughout P51.
Expressed in paravalbumin- and somatostain-containing inhibitory
interneurons of the hippocampus; in the CA1/CA3 stratum oriens-
alveus and stratum pyramidale and in cells within the hilus and
subgranular layer of the dentate gyrus (DG) (PubMed:12000114,
PubMed:10903572). Strongly expressed in parvalbumin (PV)-
containing fast-spiking GABAergic inhibitor interneurons in deep
cortical layers V and VI (PubMed:10531438). Also expressed in non-
fast-spiking calbindin (CB)- and/or somatostatin (SOM)-containing
interneurons in deep cortical layers V and VI (PubMed:10531438).
Expressed in starburst amacrine cells of the retina in the inner
nuclear layer (INL) and ganglion cell layer (GCL)
(PubMed:15317859). Expressed in the suprachiasmatic nucleus (SCN)
(at protein level) (PubMed:15852012, PubMed:21414897). Expressed
in the early developing brain, increasing progressively until P14
(PubMed:21912965). {ECO:0000269|PubMed:10531438,
ECO:0000269|PubMed:10903572, ECO:0000269|PubMed:12000114,
ECO:0000269|PubMed:15317859, ECO:0000269|PubMed:15852012,
ECO:0000269|PubMed:21414897, ECO:0000269|PubMed:21912965}.
-!- DEVELOPMENTAL STAGE: Weakly expressed in the brain at 14 dpc (at
protein level) (PubMed:21912965). Expressed in the brain at 14 dpc
(PubMed:21912965). {ECO:0000269|PubMed:21912965}.
-!- 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: Phosphorylated by PKA in cortical synaptosomes. cAMP-
dependent phosphorylation inhibits channel activity (By
similarity). Histamine H2 receptor- and PKA-induced
phosphorylation extends action potential spike duration, reduces
action potential spike amplitude, sustains maximum firing
frequency in hippocampal interneurons; also reduces the incidence
of high-frequency oscillations in hippocampal CA3 pyramidal cell
layers (PubMed:10903572). {ECO:0000250|UniProtKB:P63142,
ECO:0000269|PubMed:10903572}.
-!- DISRUPTION PHENOTYPE: Mice are healthy, grow normally, are fertile
and show no evidence of severe sensory or motor abnormalities
(PubMed:11124984). Show increased seizure susceptibility and
reduced long-range synchronization of gamma oscillations over
distance in the neocortex (PubMed:22539821). Thalamocortical
neurons show a strong attenuation in maximal peak firing rates,
with larger spikes and slower action potential repolarization
(PubMed:17761775). Neocortical GABAergic interneurons display
broader spikes and sustain lower trains of high-frequency spikes
without accommodation or spike doublets in rapid succession
(PubMed:11124984, PubMed:22539821). Histamine H2 receptor- and
PKA-induced hippocampal inhibitory interneurons display no maximal
sustainable firing frequency modulation (PubMed:10903572). Double
knockout of KCNC2 and KCNC1 exhibited disrupted daily rhythms in
wheel-running behavior (PubMed:21414897). Display smaller outward
currents and slower deactivation in starburst amacrine cells
compared with KCNC2 knockout mice (PubMed:15317859). Neocortical
GABAergic interneuron terminals display also a reduced rate of
spike repolarization, broader spike, increased calcium influx and
release of GABA neurotransmitter (PubMed:15917463).
Suprachiasmatic nucleus (SCN) neurons display a reduction in the
magnitude of fast delayed rectifier potassium currents, wider
action potentials, reduced spontaneous firing activity during the
day and reduced NMDA-evoked increase firing responses during the
night (PubMed:21414897). {ECO:0000269|PubMed:10903572,
ECO:0000269|PubMed:11124984, ECO:0000269|PubMed:15317859,
ECO:0000269|PubMed:15917463, ECO:0000269|PubMed:17761775,
ECO:0000269|PubMed:21414897, ECO:0000269|PubMed:22539821}.
-!- SIMILARITY: Belongs to the potassium channel family. C (Shaw) (TC
1.A.1.2) subfamily. Kv3.2/KCNC2 sub-subfamily. {ECO:0000305}.
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EMBL; BC116289; AAI16290.1; -; mRNA.
EMBL; BC116290; AAI16291.1; -; mRNA.
RefSeq; XP_006513748.1; XM_006513685.3.
RefSeq; XP_006513750.1; XM_006513687.3.
RefSeq; XP_006513751.1; XM_006513688.1.
RefSeq; XP_006513752.1; XM_006513689.3.
RefSeq; XP_006513753.1; XM_006513690.2.
UniGene; Mm.336242; -.
ProteinModelPortal; Q14B80; -.
STRING; 10090.ENSMUSP00000089814; -.
iPTMnet; Q14B80; -.
PhosphoSitePlus; Q14B80; -.
PaxDb; Q14B80; -.
PRIDE; Q14B80; -.
Ensembl; ENSMUST00000092175; ENSMUSP00000089814; ENSMUSG00000035681.
GeneID; 268345; -.
UCSC; uc007hao.1; mouse.
CTD; 3747; -.
MGI; MGI:96668; Kcnc2.
eggNOG; KOG3713; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00760000118846; -.
HOGENOM; HOG000231012; -.
HOVERGEN; HBG105862; -.
InParanoid; Q14B80; -.
PhylomeDB; Q14B80; -.
Reactome; R-MMU-1296072; Voltage gated Potassium channels.
Reactome; R-MMU-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
ChiTaRS; Kcnc2; mouse.
PRO; PR:Q14B80; -.
Proteomes; UP000000589; Chromosome 10.
ExpressionAtlas; Q14B80; baseline and differential.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0030673; C:axolemma; ISO:MGI.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0032809; C:neuronal cell body membrane; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0043195; C:terminal bouton; ISO:MGI.
GO; GO:0031982; C:vesicle; ISO:MGI.
GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
GO; GO:0005251; F:delayed rectifier potassium channel activity; ISS:UniProtKB.
GO; GO:0044325; F:ion channel binding; IPI:UniProtKB.
GO; GO:0005249; F:voltage-gated potassium channel activity; ISS:UniProtKB.
GO; GO:0001508; P:action potential; IMP:MGI.
GO; GO:0071732; P:cellular response to nitric oxide; ISS:UniProtKB.
GO; GO:0097237; P:cellular response to toxic substance; ISO:MGI.
GO; GO:0034220; P:ion transmembrane transport; ISO:MGI.
GO; GO:0038060; P:nitric oxide-cGMP-mediated signaling pathway; ISS:UniProtKB.
GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; ISO:MGI.
GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; ISO:MGI.
GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
GO; GO:0051291; P:protein heterooligomerization; ISS:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; ISS: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; IPR003974; K_chnl_volt-dep_Kv3.
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; PR01491; KVCHANNEL.
PRINTS; PR01498; SHAWCHANNEL.
SMART; SM00225; BTB; 1.
SUPFAM; SSF54695; SSF54695; 2.
1: Evidence at protein level;
Cell junction; Cell membrane; Cell projection; Complete proteome;
Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein;
Postsynaptic cell membrane; Potassium; Potassium channel;
Potassium transport; Reference proteome; Synapse; Synaptosome;
Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 642 Potassium voltage-gated channel subfamily
C member 2.
/FTId=PRO_0000310417.
TOPO_DOM 1 233 Cytoplasmic. {ECO:0000255}.
TRANSMEM 234 254 Helical; Name=Segment S1. {ECO:0000255}.
TRANSMEM 287 307 Helical; Name=Segment S2. {ECO:0000255}.
TOPO_DOM 308 317 Cytoplasmic. {ECO:0000255}.
TRANSMEM 318 338 Helical; Name=Segment S3. {ECO:0000255}.
TRANSMEM 350 372 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000255}.
TOPO_DOM 373 385 Cytoplasmic. {ECO:0000255}.
TRANSMEM 386 406 Helical; Name=Segment S5. {ECO:0000255}.
TRANSMEM 457 477 Helical; Name=Segment S6. {ECO:0000255}.
TOPO_DOM 478 642 Cytoplasmic. {ECO:0000255}.
MOTIF 441 446 Selectivity filter. {ECO:0000250}.
COMPBIAS 56 103 Gly/Pro-rich (insert).
MOD_RES 604 604 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 263 263 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 270 270 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 642 AA; 70503 MW; 2B9B6D29A40A80E3 CRC64;
MGKIESNERV ILNVGGTRHE TYRSTLKTLP GTRLALLASS EPQGDCLTAA GDKLQPLPPP
LSPPPRPPPL SPVPSGCFEG GAGNCSSHGG NGGNGGSDHP GGGREFFFDR HPGVFAYVLN
YYRTGKLHCP ADVCGPLFEE ELAFWGIDET DVEPCCWMTY RQHRDAEEAL DIFETPDLIG
GDPGDDEDLA AKRLGIEDAA GLGGPDGKSG RWRKLQPRMW ALFEDPYSSR AARFIAFASL
FFILVSITTF CLETHEAFNI VKNKTEPVIN GTSPVLQYEI ETDPALTYVE GVCVVWFTFE
FLVRIVFSPN KLEFIKNLLN IIDFVAILPF YLEVGLSGLS SKAAKDVLGF LRVVRFVRIL
RIFKLTRHFV GLRVLGHTLR ASTNEFLLLI IFLALGVLIF ATMIYYAERV GAQPNDPSAS
EHTQFKNIPI GFWWAVVTMT TLGYGDMYPQ TWSGMLVGAL CALAGVLTIA MPVPVIVNNF
GMYYSLAMAK QKLPRKRKKH IPPAPLASSP TFCKTELNMA CNSTQSDTCL GKENRLLEHN
RSVLSGDDST GSEPPLSPPE RLPIRRSSTR DKNRRGETCF LLTTGDYTCA SDGGIRKGYE
KSRSLNNIAG LAGNALRLSP VTSPYNSPCP LRRSRSPIPS IL


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