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

 KCNC2_RAT               Reviewed;         638 AA.
P22462; P22461; P22463; Q63735;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-AUG-1991, sequence version 1.
29-SEP-2021, entry version 174.
RecName: Full=Potassium voltage-gated channel subfamily C member 2 {ECO:0000312|RGD:628829};
AltName: Full=Potassium channel voltage-gated Shaw-related subfamily C member 2 {ECO:0000312|RGD:628829};
AltName: Full=Shaw-like potassium channel {ECO:0000303|PubMed:1879548};
AltName: Full=Voltage-gated potassium channel subunit Kv3.2 {ECO:0000303|PubMed:1879548};
Name=Kcnc2 {ECO:0000312|RGD:628829};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, BIOPHYSICOCHEMICAL
PROPERTIES, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
TISSUE=Brain;
PubMed=2367536; DOI=10.1073/pnas.87.13.5227;
McCormack T., de Miera E.C.V.-S., Rudy B.;
"Molecular cloning of a member of a third class of Shaker-family K+ channel
genes in mammals.";
Proc. Natl. Acad. Sci. U.S.A. 87:5227-5231(1990).
[2]
SEQUENCE REVISION.
PubMed=2023956; DOI=10.1073/pnas.88.9.4060-b;
McCormack T., de Miera E.C.V.-S., Rudy B.;
"Molecular cloning of a member of a third class of Shaker-family K+ channel
genes in mammals.";
Proc. Natl. Acad. Sci. U.S.A. 88:4060-4060(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, BIOPHYSICOCHEMICAL
PROPERTIES, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Brain;
PubMed=1879548; DOI=10.1016/0014-5793(91)81026-5;
Luneau C.J., Wiedmann R., Smith J.S., Williams J.B.;
"Shaw-like rat brain potassium channel cDNA's with divergent 3' ends.";
FEBS Lett. 288:163-167(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
PubMed=1378392; DOI=10.1002/j.1460-2075.1992.tb05312.x;
Rettig J., Wunder F., Stocker M., Lichtinghagen R., Mastiaux F., Beckh S.,
Kues W., Pedarzani P., Schroeter K.H., Ruppersberg J.P., Veh R., Pongs O.;
"Characterization of a Shaw-related potassium channel family in rat
brain.";
EMBO J. 11:2473-2486(1992).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=1374908; DOI=10.1073/pnas.89.10.4603;
Baker H., Pollock J., Ellisman M., Kentros C., Miera E., Serodio P.,
Weiser M., Rudy B., Fruhling D.;
"Region-specific expression of a K+ channel gene in brain.";
Proc. Natl. Acad. Sci. U.S.A. 89:4603-4607(1992).
[6]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=8120636; DOI=10.1523/jneurosci.14-03-00949.1994;
Weiser M., Vega-Saenz de Miera E., Kentros C., Moreno H., Franzen L.,
Hillman D., Baker H., Rudy B.;
"Differential expression of Shaw-related K+ channels in the rat central
nervous system.";
J. Neurosci. 14:949-972(1994).
[7]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION,
PHOSPHORYLATION, MUTAGENESIS OF SER-563 AND SER-564, SUBCELLULAR LOCATION,
AND TISSUE SPECIFICITY.
PubMed=7643197; DOI=10.1523/jneurosci.15-08-05486.1995;
Moreno H., Kentros C., Bueno E., Weiser M., Hernandez A.,
Vega-Saenz de Miera E., Ponce A., Thornhill W., Rudy B.;
"Thalamocortical projections have a K+ channel that is phosphorylated and
modulated by cAMP-dependent protein kinase.";
J. Neurosci. 15:5486-5501(1995).
[8]
SUBCELLULAR LOCATION (ISOFORMS 1; 2 AND 3).
PubMed=9307441; DOI=10.1007/s002329900278;
Ponce A., Vega-Saenz de Miera E., Kentros C., Moreno H., Thornhill B.,
Rudy B.;
"K+ channel subunit isoforms with divergent carboxy-terminal sequences
carry distinct membrane targeting signals.";
J. Membr. Biol. 159:149-159(1997).
[9]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT,
INTERACTION WITH KCNC1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10482766; DOI=10.1152/jn.1999.82.3.1512;
Hernandez-Pineda R., Chow A., Amarillo Y., Moreno H., Saganich M.,
Vega-Saenz de Miera E.C., Hernandez-Cruz A., Rudy B.;
"Kv3.1-Kv3.2 channels underlie a high-voltage-activating component of the
delayed rectifier K+ current in projecting neurons from the globus
pallidus.";
J. Neurophysiol. 82:1512-1528(1999).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10414968; DOI=10.1523/jneurosci.19-15-06394.1999;
Baranauskas G., Tkatch T., Surmeier D.J.;
"Delayed rectifier currents in rat globus pallidus neurons are attributable
to Kv2.1 and Kv3.1/3.2 K(+) channels.";
J. Neurosci. 19:6394-6404(1999).
[11]
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).
[12]
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).
[13]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF SER-563 AND SER-564.
PubMed=11281123; DOI=10.1111/j.1469-7793.2001.0345k.x;
Moreno H., Vega-Saenz de Miera E., Nadal M.S., Amarillo Y., Rudy B.;
"Modulation of Kv3 potassium channels expressed in CHO cells by a nitric
oxide-activated phosphatase.";
J. Physiol. (Lond.) 530:345-358(2001).
[14]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INTERACTION WITH KCNC1;
KCNE1; KCNE2 AND KCNE3, AND SUBCELLULAR LOCATION.
PubMed=14679187; DOI=10.1074/jbc.m310501200;
Lewis A., McCrossan Z.A., Abbott G.W.;
"MinK, MiRP1, and MiRP2 diversify Kv3.1 and Kv3.2 potassium channel
gating.";
J. Biol. Chem. 279:7884-7892(2004).
[15]
TISSUE SPECIFICITY.
PubMed=16413129; DOI=10.1016/j.neuroscience.2005.11.047;
McDonald A.J., Mascagni F.;
"Differential expression of Kv3.1b and Kv3.2 potassium channel subunits in
interneurons of the basolateral amygdala.";
Neuroscience 138:537-547(2006).
[16]
INDUCTION.
PubMed=18775767; DOI=10.1016/j.neuroscience.2008.08.008;
Grabert J., Wahle P.;
"Neuronal activity and TrkB ligands influence Kv3.1b and Kv3.2 expression
in developing cortical interneurons.";
Neuroscience 156:618-629(2008).
[17]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=18708127; DOI=10.1016/j.neuroscience.2008.07.035;
Grabert J., Wahle P.;
"Visual experience regulates Kv3.1b and Kv3.2 expression in developing rat
visual cortex.";
Neuroscience 158:654-664(2009).
[18]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=22831914; DOI=10.1016/j.ceca.2012.06.007;
Kuznetsov K.I., Grygorov O.O., Maslov V.Y., Veselovsky N.S., Fedulova S.A.;
"Kv3 channels modulate calcium signals induced by fast firing patterns in
the rat retinal ganglion cells.";
Cell Calcium 52:405-411(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:10482766, PubMed:10414968,
PubMed:11506885, PubMed:22831914). Homotetramer channels mediate
delayed-rectifier voltage-dependent potassium currents that activate
rapidly at high-threshold voltages and inactivate slowly
(PubMed:2367536, PubMed:1879548, PubMed:8120636, PubMed:7643197,
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 (PubMed:2367536,
PubMed:1879548, PubMed:8120636, PubMed:7643197). Can form functional
homotetrameric channels 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:10482766, PubMed:14679187). Channel
properties may be modulated either by 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 (PubMed:11281123, PubMed:14679187). Contributes to fire
sustained trains of very brief action potentials at high frequency in
retinal ganglion cells, thalamocortical and suprachiasmatic nucleus
(SCN) neurons and in hippocampal and neocortical interneurons
(PubMed:10482766, PubMed:10414968, PubMed:11506885, PubMed:22831914).
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. 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. Required for long-range synchronization of gamma oscillations
over distance in the neocortex. Contributes to the modulation of the
circadian rhythm of spontaneous action potential firing in
suprachiasmatic nucleus (SCN) neurons in a light-dependent manner (By
similarity). {ECO:0000250|UniProtKB:Q14B80,
ECO:0000269|PubMed:10414968, ECO:0000269|PubMed:10482766,
ECO:0000269|PubMed:11281123, ECO:0000269|PubMed:11506885,
ECO:0000269|PubMed:14679187, ECO:0000269|PubMed:1879548,
ECO:0000269|PubMed:22831914, ECO:0000269|PubMed:2367536,
ECO:0000269|PubMed:7643197, ECO:0000269|PubMed:8120636,
ECO:0000305|PubMed:10414303, ECO:0000305|PubMed:11506885}.
-!- ACTIVITY REGULATION: Inhibited by Stichodactyla helianthus peptide ShK
(By similarity). Inhibited by millimolar levels of tetraethylammonium
(TEA). Contrary to other channels, inhibited only by millimolar levels
of 4-aminopyridine (4-AP) (PubMed:2367536, PubMed:1879548,
PubMed:7643197, PubMed:10482766, PubMed:10414303).
{ECO:0000250|UniProtKB:Q96PR1, ECO:0000269|PubMed:10482766,
ECO:0000269|PubMed:1879548, ECO:0000269|PubMed:2367536,
ECO:0000269|PubMed:7643197, 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 (PubMed:2367536, PubMed:1879548, PubMed:8120636,
PubMed:7643197, PubMed:10414303, PubMed:11281123, PubMed:14679187).
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
(PubMed:7643197, PubMed:10414303, PubMed:11281123, PubMed:14679187).
{ECO:0000269|PubMed:11281123, ECO:0000269|PubMed:14679187,
ECO:0000269|PubMed:1879548, ECO:0000269|PubMed:2367536,
ECO:0000269|PubMed:7643197, ECO:0000269|PubMed:8120636,
ECO:0000305|PubMed:10414303};
-!- SUBUNIT: Homotetramer and heterotetramer with other channel-forming
alpha subunits, such as KCNC1. Interacts with KCNC1 (PubMed:10482766,
PubMed:14679187). 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
(PubMed:14679187). {ECO:0000269|PubMed:10482766,
ECO:0000269|PubMed:14679187}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10414968,
ECO:0000269|PubMed:10482766, ECO:0000269|PubMed:14679187,
ECO:0000269|PubMed:1879548, ECO:0000269|PubMed:22831914,
ECO:0000269|PubMed:2367536, ECO:0000269|PubMed:7643197,
ECO:0000269|PubMed:8120636}; Multi-pass membrane protein {ECO:0000255}.
Membrane {ECO:0000269|PubMed:11281123}; Multi-pass membrane protein
{ECO:0000255}. Perikaryon {ECO:0000269|PubMed:10482766}. Cell
projection, axon {ECO:0000269|PubMed:7643197}. Cell junction, synapse
{ECO:0000269|PubMed:7643197}. Cell junction, synapse, synaptosome
{ECO:0000269|PubMed:7643197}. Cell projection, dendrite
{ECO:0000250|UniProtKB:Q14B80}. Cell junction, synapse, postsynaptic
cell membrane {ECO:0000250|UniProtKB:Q14B80}. Cell junction, synapse,
presynaptic cell membrane {ECO:0000250|UniProtKB:Q14B80}.
Note=Localizes on the surface of cell somata, proximal dendrites and
axonal membranes. Also detected throughout the neuropil. Localized in
starburst cell somata and proximal dendrite processes. Colocalized with
GABA in presynaptic terminals. 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 (By similarity). Colocalizes with parvalbumin
in globus pallidus neurons (PubMed:10482766). Localizes in
thalamocortical axons and synapses (PubMed:7643197).
{ECO:0000250|UniProtKB:Q14B80, ECO:0000269|PubMed:10482766,
ECO:0000269|PubMed:7643197}.
-!- SUBCELLULAR LOCATION: [Isoform 1]: Apical cell membrane
{ECO:0000269|PubMed:9307441}.
-!- SUBCELLULAR LOCATION: [Isoform 2]: Apical cell membrane
{ECO:0000269|PubMed:9307441}.
-!- SUBCELLULAR LOCATION: [Isoform 3]: Basolateral cell membrane
{ECO:0000269|PubMed:9307441}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=KV3.2B {ECO:0000303|PubMed:1879548};
IsoId=P22462-1; Sequence=Displayed;
Name=2; Synonyms=KV3.2C {ECO:0000303|PubMed:1879548};
IsoId=P22462-2; Sequence=VSP_001018;
Name=3; Synonyms=KV3.2A, KShIIIA.1 {ECO:0000303|PubMed:2367536};
IsoId=P22462-3; Sequence=VSP_001019;
Name=4;
IsoId=P22462-4; Sequence=VSP_001020;
-!- TISSUE SPECIFICITY: Expressed in neurons of the visual cortex during
postnatal development (PubMed:18708127). Expressed in neurons of the
globus pallidus at postnatal age day 7 (P7), onward (PubMed:10482766).
Expressed in thalamic relay neurons. Expressed in neurons in layer IV
and deeper cortical layers of the neocortex. Expressed in hippocampal
interneurons (PubMed:7643197). Expressed in nonpyramidal interneurons
in the basolateral amygdala (PubMed:16413129). Expressed in retinal
ganglion cells (at protein level) (PubMed:22831914). Widely expressed
in the brain (PubMed:1879548, PubMed:8120636). Expressed in numerous
thalamic relay neurons throughout the dorsal thalamus. Expressed in
interneurons of the deep layers V-VI of the cerebral cortex, the CA1
and CA3 pyramidal and dentate gyrus (DG) granule cells of the
hippocampus, in neurons of the caudate-putamen, globus pallidus and
subthalamic nucleus. Also expressed in the optic layer of interior
colliculus, the inferior colliculus, the red nucleus, the medial
geniculate, the ventral lateral lemiscus, the reticulotegmental nucleus
and in the deep cerebellar nuclei (PubMed:1374908, PubMed:8120636,
PubMed:7643197, PubMed:18708127). Expressed in globus pallidus (GP)
neurons (PubMed:10414968). {ECO:0000269|PubMed:10414968,
ECO:0000269|PubMed:10482766, ECO:0000269|PubMed:1374908,
ECO:0000269|PubMed:16413129, ECO:0000269|PubMed:18708127,
ECO:0000269|PubMed:1879548, ECO:0000269|PubMed:22831914,
ECO:0000269|PubMed:7643197, ECO:0000269|PubMed:8120636}.
-!- INDUCTION: Up-regulated in visual cortex during the second postnatal
week from dark-reared animals (at protein level). Down-regulated in
visual cortex by active visual experience until postnatal day P40 of
dark-reared animals (PubMed:18708127). Down-regulated by chronic action
potential activity deprivation in organotypic culture of the visual
cortex (PubMed:18775767). {ECO:0000269|PubMed:18708127,
ECO:0000269|PubMed:18775767}.
-!- 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 (PubMed:7643197).
cAMP-dependent phosphorylation inhibits channel activity
(PubMed:7643197). 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 (By similarity).
{ECO:0000250|UniProtKB:P63142, ECO:0000269|PubMed:7643197}.
-!- 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; M34052; AAA42142.1; -; mRNA.
EMBL; M59211; AAA41819.1; -; mRNA.
EMBL; M59313; AAA41820.1; ALT_SEQ; mRNA.
EMBL; X62839; CAA44643.1; -; mRNA.
EMBL; M84203; AAA42143.1; -; mRNA.
PIR; A39402; A39402.
PIR; B45292; B45292.
PIR; S22703; S22703.
RefSeq; NP_631962.1; NM_139216.1. [P22462-3]
RefSeq; NP_631963.1; NM_139217.1. [P22462-1]
RefSeq; XP_006241389.1; XM_006241327.3. [P22462-1]
RefSeq; XP_017450149.1; XM_017594660.1. [P22462-1]
RefSeq; XP_017450150.1; XM_017594661.1. [P22462-2]
RefSeq; XP_017450151.1; XM_017594662.1. [P22462-4]
RefSeq; XP_017450152.1; XM_017594663.1. [P22462-3]
SMR; P22462; -.
BioGRID; 251521; 1.
STRING; 10116.ENSRNOP00000005773; -.
DrugCentral; P22462; -.
GuidetoPHARMACOLOGY; 549; -.
GlyGen; P22462; 2 sites.
PhosphoSitePlus; P22462; -.
PaxDb; P22462; -.
ABCD; P22462; 3 sequenced antibodies.
Ensembl; ENSRNOT00000005690; ENSRNOP00000005690; ENSRNOG00000004077. [P22462-3]
Ensembl; ENSRNOT00000005773; ENSRNOP00000005773; ENSRNOG00000004077. [P22462-1]
GeneID; 246153; -.
KEGG; rno:246153; -.
UCSC; RGD:628829; rat. [P22462-1]
CTD; 3747; -.
RGD; 628829; Kcnc2.
eggNOG; KOG3713; Eukaryota.
GeneTree; ENSGT00940000157371; -.
HOGENOM; CLU_011722_4_3_1; -.
InParanoid; P22462; -.
OMA; IRHETYT; -.
OrthoDB; 818306at2759; -.
PhylomeDB; P22462; -.
TreeFam; TF352511; -.
Reactome; R-RNO-1296072; Voltage gated Potassium channels.
Reactome; R-RNO-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
PRO; PR:P22462; -.
Proteomes; UP000002494; Chromosome 7.
Bgee; ENSRNOG00000004077; Expressed in brain and 15 other tissues.
Genevisible; P22462; RN.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0030673; C:axolemma; IDA:RGD.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0032590; C:dendrite membrane; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0032809; C:neuronal cell body membrane; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
GO; GO:0045202; C:synapse; IDA:UniProtKB.
GO; GO:0043195; C:terminal bouton; IDA:RGD.
GO; GO:0031982; C:vesicle; IDA:RGD.
GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
GO; GO:0005251; F:delayed rectifier potassium channel activity; IDA:UniProtKB.
GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
GO; GO:0099508; F:voltage-gated ion channel activity involved in regulation of presynaptic membrane potential; IDA:SynGO.
GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB.
GO; GO:0001508; P:action potential; ISO:RGD.
GO; GO:0071242; P:cellular response to ammonium ion; IEP:RGD.
GO; GO:0071732; P:cellular response to nitric oxide; IDA:UniProtKB.
GO; GO:0097237; P:cellular response to toxic substance; IMP:RGD.
GO; GO:0021759; P:globus pallidus development; IEP:RGD.
GO; GO:0034220; P:ion transmembrane transport; IDA:RGD.
GO; GO:0038060; P:nitric oxide-cGMP-mediated signaling pathway; IDA:UniProtKB.
GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IDA:RGD.
GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; IDA:RGD.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0051291; P:protein heterooligomerization; IDA:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
GO; GO:0014075; P:response to amine; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0009642; P:response to light intensity; IEP:RGD.
GO; GO:0032026; P:response to magnesium ion; IEP:RGD.
GO; GO:1990089; P:response to nerve growth factor; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0009636; P:response to toxic substance; IEP:RGD.
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; PR01491; KVCHANNEL.
PRINTS; PR01498; SHAWCHANNEL.
SMART; SM00225; BTB; 1.
SUPFAM; SSF54695; SSF54695; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Cell projection;
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..638
/note="Potassium voltage-gated channel subfamily C member
2"
/id="PRO_0000054054"
TOPO_DOM 1..229
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 230..248
/note="Helical; Name=Segment S1"
/evidence="ECO:0000255"
TRANSMEM 284..303
/note="Helical; Name=Segment S2"
/evidence="ECO:0000255"
TOPO_DOM 304..314
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 315..337
/note="Helical; Name=Segment S3"
/evidence="ECO:0000255"
TRANSMEM 346..368
/note="Helical; Voltage-sensor; Name=Segment S4"
/evidence="ECO:0000255"
TOPO_DOM 369..381
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 382..401
/note="Helical; Name=Segment S5"
/evidence="ECO:0000255"
TRANSMEM 451..473
/note="Helical; Name=Segment S6"
/evidence="ECO:0000255"
TOPO_DOM 474..638
/note="Cytoplasmic"
/evidence="ECO:0000255"
REGION 47..75
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 538..572
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOTIF 437..442
/note="Selectivity filter"
/evidence="ECO:0000250"
COMPBIAS 56..74
/note="Pro residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 564
/note="Phosphoserine; by PKA"
/evidence="ECO:0000255"
MOD_RES 600
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q14B80"
CARBOHYD 259
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 266
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
VAR_SEQ 594..638
/note="GYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIPSIL -> AST
LEPMESTSQTKGDTRPEAHWNCAHLLNFGCPTGSSFPTL (in isoform 2)"
/evidence="ECO:0000303|PubMed:1879548"
/id="VSP_001018"
VAR_SEQ 594..638
/note="GYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIPSIL -> DNC
KDVVITGYTQAEARSLT (in isoform 3)"
/evidence="ECO:0000303|PubMed:2367536"
/id="VSP_001019"
VAR_SEQ 594..638
/note="GYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIPSIL -> VLY
RIYHGFLPAENGTLRFSHSKDCTGNFCY (in isoform 4)"
/evidence="ECO:0000303|PubMed:1378392"
/id="VSP_001020"
MUTAGEN 563
/note="S->A: Does not abolish channel activity inhibition
in presence of nitric oxide (NO); when associated with A-
564. Absence of channel activity inhibition in presence of
cAMP; when associated with A-564."
/evidence="ECO:0000269|PubMed:11281123,
ECO:0000269|PubMed:7643197"
MUTAGEN 564
/note="S->A: Does not abolish channel activity inhibition
in presence of nitric oxide (NO); when associated with A-
564. Absence of channel activity inhibition in presence of
cAMP; when associated with A-563."
/evidence="ECO:0000269|PubMed:11281123,
ECO:0000269|PubMed:7643197"
CONFLICT 2
/note="G -> S (in Ref. 4; CAA44643)"
/evidence="ECO:0000305"
SEQUENCE 638 AA; 70191 MW; 25C102B4CCE53BF4 CRC64;
MGKIENNERV ILNVGGTRHE TYRSTLKTLP GTRLALLASS EPQGDCLTAA GDKLQPLPPP
LSPPPRPPPL SPVPSGCFEG GAGNCSSHGG NGSDHPGGGR EFFFDRHPGV FAYVLNYYRT
GKLHCPADVC GPLFEEELAF WGIDETDVEP CCWMTYRQHR DAEEALDIFE TPDLIGGDPG
DDEDLGGKRL GIEDAAGLGG PDGKSGRWRK LQPRMWALFE DPYSSRAARF IAFASLFFIL
VSITTFCLET HEAFNIVKNK TEPVINGTSA VLQYEIETDP ALTYVEGVCV VWFTFEFLVR
IVFSPNKLEF IKNLLNIIDF VAILPFYLEV GLSGLSSKAA KDVLGFLRVV RFVRILRIFK
LTRHFVGLRV LGHTLRASTN EFLLLIIFLA LGVLIFATMI YYAERVGAQP NDPSASEHTQ
FKNIPIGFWW AVVTMTTLGY GDMYPQTWSG MLVGALCALA GVLTIAMPVP VIVNNFGMYY
SLAMAKQKLP RKRKKHIPPA PLASSPTFCK TELNMACNST QSDTCLGKEN RLLEHNRSVL
SGDDSTGSEP PLSPPERLPI RRSSTRDKNR RGETCFLLTT GDYTCASDGG IRKGYEKSRS
LNNIAGLAGN ALRLSPVTSP YNSPCPLRRS RSPIPSIL


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WP2272: Pathogenic Escherichia coli infection
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WP201: Ptf1a related regulatory pathway
WP1614: 1- and 2-Methylnaphthalene degradation
WP1644: DNA replication
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WP731: Sterol regulatory element binding protein related
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WP1693: Purine metabolism
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WP1937: Transport of vitamins, nucleosides, and related molecules
WP1566: Citrate cycle (TCA cycle)
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WP2292: Chemokine signaling pathway
WP1663: Homologous recombination
WP1680: Oxidative phosphorylation
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WP2080: TFs Regulate miRNAs related to cardiac hypertrophy
WP1655: Geraniol degradation
WP1672: Mismatch repair

Related Genes :
[Kcnc2] Potassium voltage-gated channel subfamily C member 2 (Potassium channel voltage-gated Shaw-related subfamily C member 2) (Shaw-like potassium channel) (Voltage-gated potassium channel subunit Kv3.2)
[KCNC2] Potassium voltage-gated channel subfamily C member 2 (Shaw-like potassium channel) (Voltage-gated potassium channel Kv3.2)
[Kcnc2] Potassium voltage-gated channel subfamily C member 2 (Shaw-like potassium channel) (Voltage-gated potassium channel Kv3.2)
[Kcnc1] Potassium voltage-gated channel subfamily C member 1 (NGK2) (Voltage-gated potassium channel subunit Kv3.1) (Voltage-gated potassium channel subunit Kv4)
[Kcnc1] Potassium voltage-gated channel subfamily C member 1 (NGK2) (RAW2) (Voltage-gated potassium channel subunit Kv3.1) (Voltage-gated potassium channel subunit Kv4)
[KCNC1] Potassium voltage-gated channel subfamily C member 1 (NGK2) (Voltage-gated potassium channel subunit Kv3.1) (Voltage-gated potassium channel subunit Kv4)
[Kcnc3] Potassium voltage-gated channel subfamily C member 3 (KSHIIID) (Voltage-gated potassium channel subunit Kv3.3)
[Kcnc4] Potassium voltage-gated channel subfamily C member 4 (Raw3) (Voltage-gated potassium channel subunit Kv3.4)
[KCNC4 C1orf30] Potassium voltage-gated channel subfamily C member 4 (KSHIIIC) (Voltage-gated potassium channel subunit Kv3.4)
[KCNC3] Potassium voltage-gated channel subfamily C member 3 (KSHIIID) (Voltage-gated potassium channel subunit Kv3.3)
[Kcnc4] Potassium voltage-gated channel subfamily C member 4 (Voltage-gated potassium channel subunit Kv3.4)
[Kcna3] Potassium voltage-gated channel subfamily A member 3 (RCK3) (RGK5) (Voltage-gated potassium channel subunit Kv1.3) (Voltage-gated potassium channel subunit Kv3)
[Kcnb1] Potassium voltage-gated channel subfamily B member 1 (Delayed rectifier potassium channel 1) (DRK1) (Voltage-gated potassium channel subunit Kv2.1)
[KCNH2 CERG ERG] Potassium voltage-gated channel subfamily H member 2 (Ether-a-go-go-related gene potassium channel 1) (DERG) (ERG-1) (Eag-related protein 1) (Ether-a-go-go-related protein 1) (c-ERG) (Voltage-gated potassium channel subunit Kv11.1)
[Kcnd2 Kiaa1044 MNCb-7013] Potassium voltage-gated channel subfamily D member 2 (Voltage-gated potassium channel subunit Kv4.2)
[Kcne2] Potassium voltage-gated channel subfamily E member 2 (MinK-related peptide 1) (Minimum potassium ion channel-related peptide 1) (Potassium channel subunit beta MiRP1)
[KCNA4 KCNA4L] Potassium voltage-gated channel subfamily A member 4 (HPCN2) (Voltage-gated K(+) channel HuKII) (Voltage-gated potassium channel HBK4) (Voltage-gated potassium channel HK1) (Voltage-gated potassium channel subunit Kv1.4)
[KCNH2 ERG ERG1 HERG] Potassium voltage-gated channel subfamily H member 2 (Eag homolog) (Ether-a-go-go-related gene potassium channel 1) (ERG-1) (Eag-related protein 1) (Ether-a-go-go-related protein 1) (H-ERG) (hERG-1) (hERG1) (Voltage-gated potassium channel subunit Kv11.1)
[KCNH6 ERG2] Potassium voltage-gated channel subfamily H member 6 (Ether-a-go-go-related gene potassium channel 2) (ERG-2) (Eag-related protein 2) (Ether-a-go-go-related protein 2) (hERG-2) (hERG2) (Voltage-gated potassium channel subunit Kv11.2)
[Kcna4] Potassium voltage-gated channel subfamily A member 4 (Voltage-gated potassium channel subunit Kv1.4)
[Kcnh2 Erg Merg1] Potassium voltage-gated channel subfamily H member 2 (Ether-a-go-go-related gene potassium channel 1) (ERG-1) (Eag-related protein 1) (Ether-a-go-go-related protein 1) (MERG) (Voltage-gated potassium channel subunit Kv11.1)
[KCNA2] Potassium voltage-gated channel subfamily A member 2 (NGK1) (Voltage-gated K(+) channel HuKIV) (Voltage-gated potassium channel HBK5) (Voltage-gated potassium channel subunit Kv1.2)
[Kcnh6 Erg2] Potassium voltage-gated channel subfamily H member 6 (Ether-a-go-go-related gene potassium channel 2) (ERG-2) (Eag-related protein 2) (Ether-a-go-go-related protein 2) (Voltage-gated potassium channel subunit Kv11.2)
[Kcna2] Potassium voltage-gated channel subfamily A member 2 (MK2) (Voltage-gated potassium channel subunit Kv1.2)
[Kcnh2 Erg] Potassium voltage-gated channel subfamily H member 2 (Ether-a-go-go-related gene potassium channel 1) (ERG-1) (Eag-related protein 1) (Ether-a-go-go-related protein 1) (RERG) (r-ERG) (Voltage-gated potassium channel subunit Kv11.1)
[Kcne2] Potassium voltage-gated channel subfamily E member 2 (MinK-related peptide 1) (Minimum potassium ion channel-related peptide 1) (Potassium channel subunit beta MiRP1)
[Kcnb1] Potassium voltage-gated channel subfamily B member 1 (Voltage-gated potassium channel subunit Kv2.1) (mShab)
[Kcne1] Potassium voltage-gated channel subfamily E member 1 (Delayed rectifier potassium channel subunit IsK) (IKs producing slow voltage-gated potassium channel subunit beta Mink) (Minimal potassium channel)
[Kcnh1 Eag] Potassium voltage-gated channel subfamily H member 1 (Ether-a-go-go potassium channel 1) (EAG channel 1) (EAG1) (m-eag) (Voltage-gated potassium channel subunit Kv10.1)
[KCNQ2] Potassium voltage-gated channel subfamily KQT member 2 (KQT-like 2) (Neuroblastoma-specific potassium channel subunit alpha KvLQT2) (Voltage-gated potassium channel subunit Kv7.2)

Bibliography :