KCNC2_MOUSE
ID KCNC2_MOUSE Reviewed; 642 AA.
AC Q14B80;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Potassium voltage-gated channel subfamily C member 2 {ECO:0000312|MGI:MGI:96668};
DE AltName: Full=Shaw-like potassium channel {ECO:0000250|UniProtKB:P22462};
DE AltName: Full=Voltage-gated potassium channel Kv3.2 {ECO:0000303|PubMed:12000114};
GN Name=Kcnc2 {ECO:0000312|MGI:MGI:96668};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10561420; DOI=10.1152/jn.1999.82.5.2476;
RA Erisir A., Lau D., Rudy B., Leonard C.S.;
RT "Function of specific K(+) channels in sustained high-frequency firing of
RT fast-spiking neocortical interneurons.";
RL J. Neurophysiol. 82:2476-2489(1999).
RN [3]
RP REVIEW.
RX PubMed=10414303; DOI=10.1111/j.1749-6632.1999.tb11295.x;
RA Rudy B., Chow A., Lau D., Amarillo Y., Ozaita A., Saganich M., Moreno H.,
RA Nadal M.S., Hernandez-Pineda R., Hernandez-Cruz A., Erisir A., Leonard C.,
RA Vega-Saenz de Miera E.;
RT "Contributions of Kv3 channels to neuronal excitability.";
RL Ann. N. Y. Acad. Sci. 868:304-343(1999).
RN [4]
RP SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10531438; DOI=10.1523/jneurosci.19-21-09332.1999;
RA Chow A., Erisir A., Farb C., Nadal M.S., Ozaita A., Lau D., Welker E.,
RA Rudy B.;
RT "K(+) channel expression distinguishes subpopulations of parvalbumin- and
RT somatostatin-containing neocortical interneurons.";
RL J. Neurosci. 19:9332-9345(1999).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=11124984; DOI=10.1523/jneurosci.20-24-09071.2000;
RA Lau D., Vega-Saenz de Miera E.C., Contreras D., Ozaita A., Harvey M.,
RA Chow A., Noebels J.L., Paylor R., Morgan J.I., Leonard C.S., Rud y B.;
RT "Impaired fast-spiking, suppressed cortical inhibition, and increased
RT susceptibility to seizures in mice lacking Kv3.2 K+ channel proteins.";
RL J. Neurosci. 20:9071-9085(2000).
RN [6]
RP FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=10903572; DOI=10.1038/77693;
RA Atzori M., Lau D., Tansey E.P., Chow A., Ozaita A., Rudy B., McBain C.J.;
RT "H2 histamine receptor-phosphorylation of Kv3.2 modulates interneuron fast
RT spiking.";
RL Nat. Neurosci. 3:791-798(2000).
RN [7]
RP REVIEW.
RX PubMed=11506885; DOI=10.1016/s0166-2236(00)01892-0;
RA Rudy B., McBain C.J.;
RT "Kv3 channels: voltage-gated K+ channels designed for high-frequency
RT repetitive firing.";
RL Trends Neurosci. 24:517-526(2001).
RN [8]
RP INTERACTION WITH KCNC1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12000114; DOI=10.1002/hipo.1104;
RA Tansey E.P., Chow A., Rudy B., McBain C.J.;
RT "Developmental expression of potassium-channel subunit Kv3.2 within
RT subpopulations of mouse hippocampal inhibitory interneurons.";
RL Hippocampus 12:137-148(2002).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=15317859; DOI=10.1523/jneurosci.1275-04.2004;
RA Ozaita A., Petit-Jacques J., Volgyi B., Ho C.S., Joho R.H.,
RA Bloomfield S.A., Rudy B.;
RT "A unique role for Kv3 voltage-gated potassium channels in starburst
RT amacrine cell signaling in mouse retina.";
RL J. Neurosci. 24:7335-7343(2004).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=15917463; DOI=10.1523/jneurosci.0722-05.2005;
RA Goldberg E.M., Watanabe S., Chang S.Y., Joho R.H., Huang Z.J.,
RA Leonard C.S., Rudy B.;
RT "Specific functions of synaptically localized potassium channels in
RT synaptic transmission at the neocortical GABAergic fast-spiking cell
RT synapse.";
RL J. Neurosci. 25:5230-5235(2005).
RN [11]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15852012; DOI=10.1038/nn1448;
RA Itri J.N., Michel S., Vansteensel M.J., Meijer J.H., Colwell C.S.;
RT "Fast delayed rectifier potassium current is required for circadian neural
RT activity.";
RL Nat. Neurosci. 8:650-656(2005).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17761775; DOI=10.1113/jphysiol.2007.141135;
RA Kasten M.R., Rudy B., Anderson M.P.;
RT "Differential regulation of action potential firing in adult murine
RT thalamocortical neurons by Kv3.2, Kv1, and SK potassium and N-type calcium
RT channels.";
RL J. Physiol. (Lond.) 584:565-582(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21414897; DOI=10.1523/jneurosci.5792-10.2011;
RA Kudo T., Loh D.H., Kuljis D., Constance C., Colwell C.S.;
RT "Fast delayed rectifier potassium current: critical for input and output of
RT the circadian system.";
RL J. Neurosci. 31:2746-2755(2011).
RN [15]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=21912965; DOI=10.1007/s12031-011-9648-6;
RA Boda E., Hoxha E., Pini A., Montarolo F., Tempia F.;
RT "Brain expression of Kv3 subunits during development, adulthood and aging
RT and in a murine model of Alzheimer's disease.";
RL J. Mol. Neurosci. 46:606-615(2012).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22539821; DOI=10.1152/jn.00102.2012;
RA Harvey M., Lau D., Civillico E., Rudy B., Contreras D.;
RT "Impaired long-range synchronization of gamma oscillations in the neocortex
RT of a mouse lacking Kv3.2 potassium channels.";
RL J. Neurophysiol. 108:827-833(2012).
CC -!- FUNCTION: Voltage-gated potassium channel that mediates transmembrane
CC potassium transport in excitable membranes, primarily in the brain.
CC Contributes to the regulation of the fast action potential
CC repolarization and in sustained high-frequency firing in neurons of the
CC central nervous system (PubMed:10561420, PubMed:10414303,
CC PubMed:11124984, PubMed:10903572, PubMed:11506885, PubMed:15317859,
CC PubMed:15917463, PubMed:17761775, PubMed:21414897). Homotetramer
CC channels mediate delayed-rectifier voltage-dependent potassium currents
CC that activate rapidly at high-threshold voltages and inactivate slowly
CC (PubMed:10414303). Forms tetrameric channels through which potassium
CC ions pass in accordance with their electrochemical gradient. The
CC channel alternates between opened and closed conformations in response
CC to the voltage difference across the membrane (By similarity). Can form
CC functional homotetrameric and heterotetrameric channels that contain
CC variable proportions of KCNC1, and possibly other family members as
CC well; channel properties depend on the type of alpha subunits that are
CC part of the channel (PubMed:10531438, PubMed:12000114). Channel
CC properties may be modulated by either the association with ancillary
CC subunits, such as KCNE1, KCNE2 and KCNE3 or indirectly by nitric oxide
CC (NO) through a cGMP- and PKG-mediated signaling cascade, slowing
CC channel activation and deactivation of delayed rectifier potassium
CC channels (By similarity). Contributes to fire sustained trains of very
CC brief action potentials at high frequency in thalamocortical and
CC suprachiasmatic nucleus (SCN) neurons, in hippocampal and neocortical
CC interneurons and in retinal ganglion cells (PubMed:10561420,
CC PubMed:10903572, PubMed:11506885, PubMed:17761775). Sustained maximal
CC action potential firing frequency in inhibitory hippocampal
CC interneurons is negatively modulated by histamine H2 receptor
CC activation in a cAMP- and protein kinase (PKA) phosphorylation-
CC dependent manner (PubMed:10903572). Plays a role in maintaining the
CC fidelity of synaptic transmission in neocortical GABAergic interneurons
CC by generating action potential (AP) repolarization at nerve terminals,
CC thus reducing spike-evoked calcium influx and GABA neurotransmitter
CC release (PubMed:15917463). Required for long-range synchronization of
CC gamma oscillations over distance in the neocortex (PubMed:22539821).
CC Contributes to the modulation of the circadian rhythm of spontaneous
CC action potential firing in suprachiasmatic nucleus (SCN) neurons in a
CC light-dependent manner (PubMed:21414897).
CC {ECO:0000250|UniProtKB:P22462, ECO:0000269|PubMed:10531438,
CC ECO:0000269|PubMed:10561420, ECO:0000269|PubMed:10903572,
CC ECO:0000269|PubMed:11124984, ECO:0000269|PubMed:12000114,
CC ECO:0000269|PubMed:15317859, ECO:0000269|PubMed:15917463,
CC ECO:0000269|PubMed:17761775, ECO:0000269|PubMed:21414897,
CC ECO:0000269|PubMed:22539821, ECO:0000305|PubMed:10414303,
CC ECO:0000305|PubMed:11506885}.
CC -!- ACTIVITY REGULATION: Inhibited by millimolar levels of
CC tetraethylammonium (TEA). Contrary to other channels, inhibited only by
CC millimolar levels of 4-aminopyridine (4-AP). Inhibited by Stichodactyla
CC helianthus peptide ShK. {ECO:0000250|UniProtKB:P22462,
CC ECO:0000250|UniProtKB:Q96PR1, ECO:0000305|PubMed:10414303}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=Homotetrameric channels expressed in xenopus oocytes or in
CC mammalian non-neuronal cells display delayed-rectifier voltage-
CC dependent potassium currents, that are rapidly activated during
CC membrane depolarization, i.e within a risetime of a few msec. After
CC that, inactivates very slowly, i.e within about >800 msec. Their
CC activation requires a threshold potential at about -10 mV, with a
CC midpoint activation at about 12.1 mV and a steepness parameter of
CC about 8.4 mV. The voltage-dependence of activation and inactivation
CC and other channel characteristics vary depending on the experimental
CC conditions, the expression system, the presence or absence of
CC ancillary subunits and post-translational modifications.
CC {ECO:0000305|PubMed:10414303};
CC -!- SUBUNIT: Homotetramer and heterotetramer with other channel-forming
CC alpha subunits, such as KCNC1 (PubMed:10531438). Interacts with KCNC1
CC (PubMed:10531438, PubMed:12000114). Homotetramer or heterotetramer
CC channel activity is regulated by association with modulating ancillary
CC subunits such as KCNE1, KCNE2 and KCNE3, creating a functionally
CC diverse range of channel complexes. Interacts with KCNE1, KCNE2 and
CC KCNE3 (By similarity). {ECO:0000250|UniProtKB:P22462,
CC ECO:0000269|PubMed:10531438, ECO:0000269|PubMed:12000114}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10531438,
CC ECO:0000269|PubMed:10561420, ECO:0000269|PubMed:10903572,
CC ECO:0000269|PubMed:11124984, ECO:0000269|PubMed:15317859,
CC ECO:0000269|PubMed:15917463, ECO:0000269|PubMed:17761775,
CC ECO:0000269|PubMed:21414897, ECO:0000269|PubMed:22539821}; Multi-pass
CC membrane protein {ECO:0000255}. Membrane {ECO:0000269|PubMed:12000114};
CC Multi-pass membrane protein {ECO:0000255}. Perikaryon
CC {ECO:0000269|PubMed:10531438, ECO:0000269|PubMed:10903572,
CC ECO:0000269|PubMed:12000114, ECO:0000269|PubMed:15317859,
CC ECO:0000269|PubMed:15852012}. Cell projection, axon
CC {ECO:0000269|PubMed:10903572}. Cell projection, dendrite
CC {ECO:0000269|PubMed:10531438, ECO:0000269|PubMed:10903572,
CC ECO:0000269|PubMed:12000114, ECO:0000269|PubMed:15317859}. Postsynaptic
CC cell membrane {ECO:0000269|PubMed:10531438}. Presynaptic cell membrane
CC {ECO:0000269|PubMed:10531438}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:P22462}. Synapse {ECO:0000250|UniProtKB:P22462}.
CC Apical cell membrane {ECO:0000250|UniProtKB:P22462}. Basolateral cell
CC membrane {ECO:0000250|UniProtKB:P22462}. Note=Colocalizes with
CC parvalbumin in globus pallidus neurons. Localizes in thalamocortical
CC axons and synapses (By similarity). Localizes on the surface of cell
CC somata, proximal dendrites and axonal membranes (PubMed:12000114,
CC PubMed:10903572). Also detected throughout the neuropil
CC (PubMed:12000114). Localized in starburst cell somata and proximal
CC dendrite processes (PubMed:15317859). Colocalized with GABA in
CC presynaptic terminals (PubMed:10531438). Clustered in patches in
CC somatic and proximal dendritic membrane as well as in axons and
CC presnypatic terminals of GABAergic interneurons; some of these patches
CC are found near postsynaptic sites (PubMed:10531438).
CC {ECO:0000250|UniProtKB:P22462, ECO:0000269|PubMed:10531438,
CC ECO:0000269|PubMed:10903572, ECO:0000269|PubMed:12000114,
CC ECO:0000269|PubMed:15317859}.
CC -!- TISSUE SPECIFICITY: Weakly expressed in the brain at postnatal age day
CC 7 (P7) and increased at P60 (PubMed:21912965). Not detectable in
CC newborn hippocampus. Expressed weakly at P7 in the early developing
CC hippocampus, increasing progressively and reaching a plateau of
CC expression at P14 that is maintained throughout P51. Expressed in
CC paravalbumin- and somatostain-containing inhibitory interneurons of the
CC hippocampus; in the CA1/CA3 stratum oriens-alveus and stratum
CC pyramidale and in cells within the hilus and subgranular layer of the
CC dentate gyrus (DG) (PubMed:12000114, PubMed:10903572). Strongly
CC expressed in parvalbumin (PV)-containing fast-spiking GABAergic
CC inhibitor interneurons in deep cortical layers V and VI
CC (PubMed:10531438). Also expressed in non-fast-spiking calbindin
CC (CB)- and/or somatostatin (SOM)-containing interneurons in deep
CC cortical layers V and VI (PubMed:10531438). Expressed in starburst
CC amacrine cells of the retina in the inner nuclear layer (INL) and
CC ganglion cell layer (GCL) (PubMed:15317859). Expressed in the
CC suprachiasmatic nucleus (SCN) (at protein level) (PubMed:15852012,
CC PubMed:21414897). Expressed in the early developing brain, increasing
CC progressively until P14 (PubMed:21912965).
CC {ECO:0000269|PubMed:10531438, ECO:0000269|PubMed:10903572,
CC ECO:0000269|PubMed:12000114, ECO:0000269|PubMed:15317859,
CC ECO:0000269|PubMed:15852012, ECO:0000269|PubMed:21414897,
CC ECO:0000269|PubMed:21912965}.
CC -!- DEVELOPMENTAL STAGE: Weakly expressed in the brain at 14 dpc (at
CC protein level) (PubMed:21912965). Expressed in the brain at 14 dpc
CC (PubMed:21912965). {ECO:0000269|PubMed:21912965}.
CC -!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position. Channel opening and closing is effected by a
CC conformation change that affects the position and orientation of the
CC voltage-sensor paddle formed by S3 and S4 within the membrane. A
CC transmembrane electric field that is positive inside would push the
CC positively charged S4 segment outwards, thereby opening the pore, while
CC a field that is negative inside would pull the S4 segment inwards and
CC close the pore. Changes in the position and orientation of S4 are then
CC transmitted to the activation gate formed by the inner helix bundle via
CC the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}.
CC -!- PTM: Phosphorylated by PKA in cortical synaptosomes. cAMP-dependent
CC phosphorylation inhibits channel activity (By similarity). Histamine H2
CC receptor- and PKA-induced phosphorylation extends action potential
CC spike duration, reduces action potential spike amplitude, sustains
CC maximum firing frequency in hippocampal interneurons; also reduces the
CC incidence of high-frequency oscillations in hippocampal CA3 pyramidal
CC cell layers (PubMed:10903572). {ECO:0000250|UniProtKB:P63142,
CC ECO:0000269|PubMed:10903572}.
CC -!- DISRUPTION PHENOTYPE: Mice are healthy, grow normally, are fertile and
CC show no evidence of severe sensory or motor abnormalities
CC (PubMed:11124984). Show increased seizure susceptibility and reduced
CC long-range synchronization of gamma oscillations over distance in the
CC neocortex (PubMed:22539821). Thalamocortical neurons show a strong
CC attenuation in maximal peak firing rates, with larger spikes and slower
CC action potential repolarization (PubMed:17761775). Neocortical
CC GABAergic interneurons display broader spikes and sustain lower trains
CC of high-frequency spikes without accommodation or spike doublets in
CC rapid succession (PubMed:11124984, PubMed:22539821). Histamine H2
CC receptor- and PKA-induced hippocampal inhibitory interneurons display
CC no maximal sustainable firing frequency modulation (PubMed:10903572).
CC Double knockout of KCNC2 and KCNC1 exhibited disrupted daily rhythms in
CC wheel-running behavior (PubMed:21414897). Display smaller outward
CC currents and slower deactivation in starburst amacrine cells compared
CC with KCNC2 knockout mice (PubMed:15317859). Neocortical GABAergic
CC interneuron terminals display also a reduced rate of spike
CC repolarization, broader spike, increased calcium influx and release of
CC GABA neurotransmitter (PubMed:15917463). Suprachiasmatic nucleus (SCN)
CC neurons display a reduction in the magnitude of fast delayed rectifier
CC potassium currents, wider action potentials, reduced spontaneous firing
CC activity during the day and reduced NMDA-evoked increase firing
CC responses during the night (PubMed:21414897).
CC {ECO:0000269|PubMed:10903572, ECO:0000269|PubMed:11124984,
CC ECO:0000269|PubMed:15317859, ECO:0000269|PubMed:15917463,
CC ECO:0000269|PubMed:17761775, ECO:0000269|PubMed:21414897,
CC ECO:0000269|PubMed:22539821}.
CC -!- SIMILARITY: Belongs to the potassium channel family. C (Shaw) (TC
CC 1.A.1.2) subfamily. Kv3.2/KCNC2 sub-subfamily. {ECO:0000305}.
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DR EMBL; BC116289; AAI16290.1; -; mRNA.
DR EMBL; BC116290; AAI16291.1; -; mRNA.
DR CCDS; CCDS88085.1; -.
DR RefSeq; XP_006513748.1; XM_006513685.3.
DR RefSeq; XP_006513750.1; XM_006513687.3.
DR RefSeq; XP_006513751.1; XM_006513688.1.
DR RefSeq; XP_006513752.1; XM_006513689.3.
DR RefSeq; XP_006513753.1; XM_006513690.2.
DR AlphaFoldDB; Q14B80; -.
DR SMR; Q14B80; -.
DR STRING; 10090.ENSMUSP00000089814; -.
DR GlyGen; Q14B80; 2 sites.
DR iPTMnet; Q14B80; -.
DR PhosphoSitePlus; Q14B80; -.
DR PaxDb; Q14B80; -.
DR PRIDE; Q14B80; -.
DR ProteomicsDB; 269259; -.
DR ABCD; Q14B80; 3 sequenced antibodies.
DR Antibodypedia; 17155; 267 antibodies from 30 providers.
DR DNASU; 268345; -.
DR Ensembl; ENSMUST00000092175; ENSMUSP00000089814; ENSMUSG00000035681.
DR GeneID; 268345; -.
DR UCSC; uc007hao.1; mouse.
DR CTD; 3747; -.
DR MGI; MGI:96668; Kcnc2.
DR VEuPathDB; HostDB:ENSMUSG00000035681; -.
DR eggNOG; KOG3713; Eukaryota.
DR GeneTree; ENSGT00940000157371; -.
DR InParanoid; Q14B80; -.
DR OrthoDB; 818306at2759; -.
DR PhylomeDB; Q14B80; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR Reactome; R-MMU-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR BioGRID-ORCS; 268345; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Kcnc2; mouse.
DR PRO; PR:Q14B80; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q14B80; protein.
DR Bgee; ENSMUSG00000035681; Expressed in lateral geniculate body and 113 other tissues.
DR ExpressionAtlas; Q14B80; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0030673; C:axolemma; ISO:MGI.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0032590; C:dendrite membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0032809; C:neuronal cell body membrane; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR GO; GO:0099508; F:voltage-gated ion channel activity involved in regulation of presynaptic membrane potential; ISO:MGI.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISS:UniProtKB.
DR GO; GO:0001508; P:action potential; IMP:MGI.
DR GO; GO:0071242; P:cellular response to ammonium ion; IEA:Ensembl.
DR GO; GO:0071732; P:cellular response to nitric oxide; ISS:UniProtKB.
DR GO; GO:0097237; P:cellular response to toxic substance; ISO:MGI.
DR GO; GO:0021759; P:globus pallidus development; IEA:Ensembl.
DR GO; GO:0034220; P:ion transmembrane transport; ISO:MGI.
DR GO; GO:0038060; P:nitric oxide-cGMP-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; ISO:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0051291; P:protein heterooligomerization; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0014075; P:response to amine; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0009642; P:response to light intensity; IEA:Ensembl.
DR GO; GO:0032026; P:response to magnesium ion; IEA:Ensembl.
DR GO; GO:1990089; P:response to nerve growth factor; IEA:Ensembl.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR Gene3D; 1.20.120.350; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR InterPro; IPR003974; K_chnl_volt-dep_Kv3.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR028325; VG_K_chnl.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01498; SHAWCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Phosphoprotein; Postsynaptic cell membrane; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Synapse;
KW Synaptosome; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..642
FT /note="Potassium voltage-gated channel subfamily C member
FT 2"
FT /id="PRO_0000310417"
FT TOPO_DOM 1..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..372
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..642
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 45..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 441..446
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 56..74
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ 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
