KCNC2_RAT
ID KCNC2_RAT Reviewed; 638 AA.
AC P22462; P22461; P22463; Q63735;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Potassium voltage-gated channel subfamily C member 2 {ECO:0000312|RGD:628829};
DE AltName: Full=Potassium channel voltage-gated Shaw-related subfamily C member 2 {ECO:0000312|RGD:628829};
DE AltName: Full=Shaw-like potassium channel {ECO:0000303|PubMed:1879548};
DE AltName: Full=Voltage-gated potassium channel subunit Kv3.2 {ECO:0000303|PubMed:1879548};
GN Name=Kcnc2 {ECO:0000312|RGD:628829};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=2367536; DOI=10.1073/pnas.87.13.5227;
RA McCormack T., de Miera E.C.V.-S., Rudy B.;
RT "Molecular cloning of a member of a third class of Shaker-family K+ channel
RT genes in mammals.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5227-5231(1990).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=2023956; DOI=10.1073/pnas.88.9.4060-b;
RA McCormack T., de Miera E.C.V.-S., Rudy B.;
RT "Molecular cloning of a member of a third class of Shaker-family K+ channel
RT genes in mammals.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4060-4060(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=1879548; DOI=10.1016/0014-5793(91)81026-5;
RA Luneau C.J., Wiedmann R., Smith J.S., Williams J.B.;
RT "Shaw-like rat brain potassium channel cDNA's with divergent 3' ends.";
RL FEBS Lett. 288:163-167(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RX PubMed=1378392; DOI=10.1002/j.1460-2075.1992.tb05312.x;
RA Rettig J., Wunder F., Stocker M., Lichtinghagen R., Mastiaux F., Beckh S.,
RA Kues W., Pedarzani P., Schroeter K.H., Ruppersberg J.P., Veh R., Pongs O.;
RT "Characterization of a Shaw-related potassium channel family in rat
RT brain.";
RL EMBO J. 11:2473-2486(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=1374908; DOI=10.1073/pnas.89.10.4603;
RA Baker H., Pollock J., Ellisman M., Kentros C., Miera E., Serodio P.,
RA Weiser M., Rudy B., Fruhling D.;
RT "Region-specific expression of a K+ channel gene in brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:4603-4607(1992).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=8120636; DOI=10.1523/jneurosci.14-03-00949.1994;
RA Weiser M., Vega-Saenz de Miera E., Kentros C., Moreno H., Franzen L.,
RA Hillman D., Baker H., Rudy B.;
RT "Differential expression of Shaw-related K+ channels in the rat central
RT nervous system.";
RL J. Neurosci. 14:949-972(1994).
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION,
RP PHOSPHORYLATION, MUTAGENESIS OF SER-563 AND SER-564, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=7643197; DOI=10.1523/jneurosci.15-08-05486.1995;
RA Moreno H., Kentros C., Bueno E., Weiser M., Hernandez A.,
RA Vega-Saenz de Miera E., Ponce A., Thornhill W., Rudy B.;
RT "Thalamocortical projections have a K+ channel that is phosphorylated and
RT modulated by cAMP-dependent protein kinase.";
RL J. Neurosci. 15:5486-5501(1995).
RN [8]
RP SUBCELLULAR LOCATION (ISOFORMS 1; 2 AND 3).
RX PubMed=9307441; DOI=10.1007/s002329900278;
RA Ponce A., Vega-Saenz de Miera E., Kentros C., Moreno H., Thornhill B.,
RA Rudy B.;
RT "K+ channel subunit isoforms with divergent carboxy-terminal sequences
RT carry distinct membrane targeting signals.";
RL J. Membr. Biol. 159:149-159(1997).
RN [9]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT,
RP INTERACTION WITH KCNC1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10482766; DOI=10.1152/jn.1999.82.3.1512;
RA Hernandez-Pineda R., Chow A., Amarillo Y., Moreno H., Saganich M.,
RA Vega-Saenz de Miera E.C., Hernandez-Cruz A., Rudy B.;
RT "Kv3.1-Kv3.2 channels underlie a high-voltage-activating component of the
RT delayed rectifier K+ current in projecting neurons from the globus
RT pallidus.";
RL J. Neurophysiol. 82:1512-1528(1999).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10414968; DOI=10.1523/jneurosci.19-15-06394.1999;
RA Baranauskas G., Tkatch T., Surmeier D.J.;
RT "Delayed rectifier currents in rat globus pallidus neurons are attributable
RT to Kv2.1 and Kv3.1/3.2 K(+) channels.";
RL J. Neurosci. 19:6394-6404(1999).
RN [11]
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 [12]
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 [13]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF SER-563 AND SER-564.
RX PubMed=11281123; DOI=10.1111/j.1469-7793.2001.0345k.x;
RA Moreno H., Vega-Saenz de Miera E., Nadal M.S., Amarillo Y., Rudy B.;
RT "Modulation of Kv3 potassium channels expressed in CHO cells by a nitric
RT oxide-activated phosphatase.";
RL J. Physiol. (Lond.) 530:345-358(2001).
RN [14]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INTERACTION WITH KCNC1;
RP KCNE1; KCNE2 AND KCNE3, AND SUBCELLULAR LOCATION.
RX PubMed=14679187; DOI=10.1074/jbc.m310501200;
RA Lewis A., McCrossan Z.A., Abbott G.W.;
RT "MinK, MiRP1, and MiRP2 diversify Kv3.1 and Kv3.2 potassium channel
RT gating.";
RL J. Biol. Chem. 279:7884-7892(2004).
RN [15]
RP TISSUE SPECIFICITY.
RX PubMed=16413129; DOI=10.1016/j.neuroscience.2005.11.047;
RA McDonald A.J., Mascagni F.;
RT "Differential expression of Kv3.1b and Kv3.2 potassium channel subunits in
RT interneurons of the basolateral amygdala.";
RL Neuroscience 138:537-547(2006).
RN [16]
RP INDUCTION.
RX PubMed=18775767; DOI=10.1016/j.neuroscience.2008.08.008;
RA Grabert J., Wahle P.;
RT "Neuronal activity and TrkB ligands influence Kv3.1b and Kv3.2 expression
RT in developing cortical interneurons.";
RL Neuroscience 156:618-629(2008).
RN [17]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=18708127; DOI=10.1016/j.neuroscience.2008.07.035;
RA Grabert J., Wahle P.;
RT "Visual experience regulates Kv3.1b and Kv3.2 expression in developing rat
RT visual cortex.";
RL Neuroscience 158:654-664(2009).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22831914; DOI=10.1016/j.ceca.2012.06.007;
RA Kuznetsov K.I., Grygorov O.O., Maslov V.Y., Veselovsky N.S., Fedulova S.A.;
RT "Kv3 channels modulate calcium signals induced by fast firing patterns in
RT the rat retinal ganglion cells.";
RL Cell Calcium 52:405-411(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:10482766, PubMed:10414968,
CC PubMed:11506885, PubMed:22831914). Homotetramer channels mediate
CC delayed-rectifier voltage-dependent potassium currents that activate
CC rapidly at high-threshold voltages and inactivate slowly
CC (PubMed:2367536, PubMed:1879548, PubMed:8120636, PubMed:7643197,
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 (PubMed:2367536,
CC PubMed:1879548, PubMed:8120636, PubMed:7643197). Can form functional
CC homotetrameric channels 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:10482766, PubMed:14679187). Channel
CC properties may be modulated either by 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 (PubMed:11281123, PubMed:14679187). Contributes to fire
CC sustained trains of very brief action potentials at high frequency in
CC retinal ganglion cells, thalamocortical and suprachiasmatic nucleus
CC (SCN) neurons and in hippocampal and neocortical interneurons
CC (PubMed:10482766, PubMed:10414968, PubMed:11506885, PubMed:22831914).
CC Sustained maximal action potential firing frequency in inhibitory
CC hippocampal interneurons is negatively modulated by histamine H2
CC receptor activation in a cAMP- and protein kinase (PKA)
CC phosphorylation-dependent manner. 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. Required for long-range synchronization of gamma oscillations
CC over distance in the neocortex. Contributes to the modulation of the
CC circadian rhythm of spontaneous action potential firing in
CC suprachiasmatic nucleus (SCN) neurons in a light-dependent manner (By
CC similarity). {ECO:0000250|UniProtKB:Q14B80,
CC ECO:0000269|PubMed:10414968, ECO:0000269|PubMed:10482766,
CC ECO:0000269|PubMed:11281123, ECO:0000269|PubMed:11506885,
CC ECO:0000269|PubMed:14679187, ECO:0000269|PubMed:1879548,
CC ECO:0000269|PubMed:22831914, ECO:0000269|PubMed:2367536,
CC ECO:0000269|PubMed:7643197, ECO:0000269|PubMed:8120636,
CC ECO:0000305|PubMed:10414303, ECO:0000305|PubMed:11506885}.
CC -!- ACTIVITY REGULATION: Inhibited by Stichodactyla helianthus peptide ShK
CC (By similarity). Inhibited by millimolar levels of tetraethylammonium
CC (TEA). Contrary to other channels, inhibited only by millimolar levels
CC of 4-aminopyridine (4-AP) (PubMed:2367536, PubMed:1879548,
CC PubMed:7643197, PubMed:10482766, PubMed:10414303).
CC {ECO:0000250|UniProtKB:Q96PR1, ECO:0000269|PubMed:10482766,
CC ECO:0000269|PubMed:1879548, ECO:0000269|PubMed:2367536,
CC ECO:0000269|PubMed:7643197, 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 (PubMed:2367536, PubMed:1879548, PubMed:8120636,
CC PubMed:7643197, PubMed:10414303, PubMed:11281123, PubMed:14679187).
CC The voltage-dependence of activation and inactivation and other
CC 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 (PubMed:7643197, PubMed:10414303, PubMed:11281123, PubMed:14679187).
CC {ECO:0000269|PubMed:11281123, ECO:0000269|PubMed:14679187,
CC ECO:0000269|PubMed:1879548, ECO:0000269|PubMed:2367536,
CC ECO:0000269|PubMed:7643197, ECO:0000269|PubMed:8120636,
CC ECO:0000305|PubMed:10414303};
CC -!- SUBUNIT: Homotetramer and heterotetramer with other channel-forming
CC alpha subunits, such as KCNC1. Interacts with KCNC1 (PubMed:10482766,
CC PubMed:14679187). Homotetramer or heterotetramer channel activity is
CC regulated by association with modulating ancillary subunits such as
CC KCNE1, KCNE2 and KCNE3, creating a functionally diverse range of
CC channel complexes. Interacts with KCNE1, KCNE2 and KCNE3
CC (PubMed:14679187). {ECO:0000269|PubMed:10482766,
CC ECO:0000269|PubMed:14679187}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10414968,
CC ECO:0000269|PubMed:10482766, ECO:0000269|PubMed:14679187,
CC ECO:0000269|PubMed:1879548, ECO:0000269|PubMed:22831914,
CC ECO:0000269|PubMed:2367536, ECO:0000269|PubMed:7643197,
CC ECO:0000269|PubMed:8120636}; Multi-pass membrane protein {ECO:0000255}.
CC Membrane {ECO:0000269|PubMed:11281123}; Multi-pass membrane protein
CC {ECO:0000255}. Perikaryon {ECO:0000269|PubMed:10482766}. Cell
CC projection, axon {ECO:0000269|PubMed:7643197}. Synapse
CC {ECO:0000269|PubMed:7643197}. Synapse, synaptosome
CC {ECO:0000269|PubMed:7643197}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q14B80}. Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q14B80}. Presynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q14B80}. Note=Localizes on the surface of cell
CC somata, proximal dendrites and axonal membranes. Also detected
CC throughout the neuropil. Localized in starburst cell somata and
CC proximal dendrite processes. Colocalized with GABA in presynaptic
CC terminals. Clustered in patches in somatic and proximal dendritic
CC membrane as well as in axons and presnypatic terminals of GABAergic
CC interneurons; some of these patches are found near postsynaptic sites
CC (By similarity). Colocalizes with parvalbumin in globus pallidus
CC neurons (PubMed:10482766). Localizes in thalamocortical axons and
CC synapses (PubMed:7643197). {ECO:0000250|UniProtKB:Q14B80,
CC ECO:0000269|PubMed:10482766, ECO:0000269|PubMed:7643197}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Apical cell membrane
CC {ECO:0000269|PubMed:9307441}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Apical cell membrane
CC {ECO:0000269|PubMed:9307441}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Basolateral cell membrane
CC {ECO:0000269|PubMed:9307441}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=KV3.2B {ECO:0000303|PubMed:1879548};
CC IsoId=P22462-1; Sequence=Displayed;
CC Name=2; Synonyms=KV3.2C {ECO:0000303|PubMed:1879548};
CC IsoId=P22462-2; Sequence=VSP_001018;
CC Name=3; Synonyms=KV3.2A, KShIIIA.1 {ECO:0000303|PubMed:2367536};
CC IsoId=P22462-3; Sequence=VSP_001019;
CC Name=4;
CC IsoId=P22462-4; Sequence=VSP_001020;
CC -!- TISSUE SPECIFICITY: Expressed in neurons of the visual cortex during
CC postnatal development (PubMed:18708127). Expressed in neurons of the
CC globus pallidus at postnatal age day 7 (P7), onward (PubMed:10482766).
CC Expressed in thalamic relay neurons. Expressed in neurons in layer IV
CC and deeper cortical layers of the neocortex. Expressed in hippocampal
CC interneurons (PubMed:7643197). Expressed in nonpyramidal interneurons
CC in the basolateral amygdala (PubMed:16413129). Expressed in retinal
CC ganglion cells (at protein level) (PubMed:22831914). Widely expressed
CC in the brain (PubMed:1879548, PubMed:8120636). Expressed in numerous
CC thalamic relay neurons throughout the dorsal thalamus. Expressed in
CC interneurons of the deep layers V-VI of the cerebral cortex, the CA1
CC and CA3 pyramidal and dentate gyrus (DG) granule cells of the
CC hippocampus, in neurons of the caudate-putamen, globus pallidus and
CC subthalamic nucleus. Also expressed in the optic layer of interior
CC colliculus, the inferior colliculus, the red nucleus, the medial
CC geniculate, the ventral lateral lemiscus, the reticulotegmental nucleus
CC and in the deep cerebellar nuclei (PubMed:1374908, PubMed:8120636,
CC PubMed:7643197, PubMed:18708127). Expressed in globus pallidus (GP)
CC neurons (PubMed:10414968). {ECO:0000269|PubMed:10414968,
CC ECO:0000269|PubMed:10482766, ECO:0000269|PubMed:1374908,
CC ECO:0000269|PubMed:16413129, ECO:0000269|PubMed:18708127,
CC ECO:0000269|PubMed:1879548, ECO:0000269|PubMed:22831914,
CC ECO:0000269|PubMed:7643197, ECO:0000269|PubMed:8120636}.
CC -!- INDUCTION: Up-regulated in visual cortex during the second postnatal
CC week from dark-reared animals (at protein level). Down-regulated in
CC visual cortex by active visual experience until postnatal day P40 of
CC dark-reared animals (PubMed:18708127). Down-regulated by chronic action
CC potential activity deprivation in organotypic culture of the visual
CC cortex (PubMed:18775767). {ECO:0000269|PubMed:18708127,
CC ECO:0000269|PubMed:18775767}.
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 (PubMed:7643197).
CC cAMP-dependent phosphorylation inhibits channel activity
CC (PubMed:7643197). Histamine H2 receptor- and PKA-induced
CC phosphorylation extends action potential spike duration, reduces action
CC potential spike amplitude, sustains maximum firing frequency in
CC hippocampal interneurons; also reduces the incidence of high-frequency
CC oscillations in hippocampal CA3 pyramidal cell layers (By similarity).
CC {ECO:0000250|UniProtKB:P63142, ECO:0000269|PubMed:7643197}.
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; M34052; AAA42142.1; -; mRNA.
DR EMBL; M59211; AAA41819.1; -; mRNA.
DR EMBL; M59313; AAA41820.1; ALT_SEQ; mRNA.
DR EMBL; X62839; CAA44643.1; -; mRNA.
DR EMBL; M84203; AAA42143.1; -; mRNA.
DR PIR; A39402; A39402.
DR PIR; B45292; B45292.
DR PIR; S22703; S22703.
DR RefSeq; NP_631962.1; NM_139216.1. [P22462-3]
DR RefSeq; NP_631963.1; NM_139217.1. [P22462-1]
DR RefSeq; XP_006241389.1; XM_006241327.3. [P22462-1]
DR RefSeq; XP_017450149.1; XM_017594660.1. [P22462-1]
DR RefSeq; XP_017450150.1; XM_017594661.1. [P22462-2]
DR RefSeq; XP_017450151.1; XM_017594662.1. [P22462-4]
DR RefSeq; XP_017450152.1; XM_017594663.1. [P22462-3]
DR AlphaFoldDB; P22462; -.
DR SMR; P22462; -.
DR BioGRID; 251521; 1.
DR STRING; 10116.ENSRNOP00000005773; -.
DR DrugCentral; P22462; -.
DR GuidetoPHARMACOLOGY; 549; -.
DR GlyGen; P22462; 2 sites.
DR PhosphoSitePlus; P22462; -.
DR PaxDb; P22462; -.
DR ABCD; P22462; 3 sequenced antibodies.
DR Ensembl; ENSRNOT00000005690; ENSRNOP00000005690; ENSRNOG00000004077. [P22462-3]
DR Ensembl; ENSRNOT00000005773; ENSRNOP00000005773; ENSRNOG00000004077. [P22462-1]
DR Ensembl; ENSRNOT00000099049; ENSRNOP00000084708; ENSRNOG00000004077. [P22462-2]
DR Ensembl; ENSRNOT00000105247; ENSRNOP00000088724; ENSRNOG00000004077. [P22462-4]
DR GeneID; 246153; -.
DR KEGG; rno:246153; -.
DR UCSC; RGD:628829; rat. [P22462-1]
DR CTD; 3747; -.
DR RGD; 628829; Kcnc2.
DR eggNOG; KOG3713; Eukaryota.
DR GeneTree; ENSGT00940000157371; -.
DR HOGENOM; CLU_011722_4_3_1; -.
DR InParanoid; P22462; -.
DR OMA; ELNTACN; -.
DR OrthoDB; 818306at2759; -.
DR PhylomeDB; P22462; -.
DR TreeFam; TF352511; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR Reactome; R-RNO-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR PRO; PR:P22462; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000004077; Expressed in frontal cortex and 3 other tissues.
DR Genevisible; P22462; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0030673; C:axolemma; IDA:RGD.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
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; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
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; IDA:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0031982; C:vesicle; IDA:RGD.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IDA: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; IDA:SynGO.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB.
DR GO; GO:0001508; P:action potential; ISO:RGD.
DR GO; GO:0071242; P:cellular response to ammonium ion; IEP:RGD.
DR GO; GO:0071732; P:cellular response to nitric oxide; IDA:UniProtKB.
DR GO; GO:0097237; P:cellular response to toxic substance; IMP:RGD.
DR GO; GO:0021759; P:globus pallidus development; IEP:RGD.
DR GO; GO:0034220; P:ion transmembrane transport; IDA:RGD.
DR GO; GO:0038060; P:nitric oxide-cGMP-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IDA:RGD.
DR GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; IDA:RGD.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0051291; P:protein heterooligomerization; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0014075; P:response to amine; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0009642; P:response to light intensity; IEP:RGD.
DR GO; GO:0032026; P:response to magnesium ion; IEP:RGD.
DR GO; GO:1990089; P:response to nerve growth factor; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; IEP:RGD.
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 Alternative splicing; Cell membrane; Cell projection; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Synapse; Synaptosome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..638
FT /note="Potassium voltage-gated channel subfamily C member
FT 2"
FT /id="PRO_0000054054"
FT TOPO_DOM 1..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..248
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..303
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..337
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..368
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..401
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..473
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..638
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 47..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 437..442
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 564
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14B80"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 594..638
FT /note="GYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIPSIL -> AST
FT LEPMESTSQTKGDTRPEAHWNCAHLLNFGCPTGSSFPTL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1879548"
FT /id="VSP_001018"
FT VAR_SEQ 594..638
FT /note="GYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIPSIL -> DNC
FT KDVVITGYTQAEARSLT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:2367536"
FT /id="VSP_001019"
FT VAR_SEQ 594..638
FT /note="GYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIPSIL -> VLY
FT RIYHGFLPAENGTLRFSHSKDCTGNFCY (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:1378392"
FT /id="VSP_001020"
FT MUTAGEN 563
FT /note="S->A: Does not abolish channel activity inhibition
FT in presence of nitric oxide (NO); when associated with A-
FT 564. Absence of channel activity inhibition in presence of
FT cAMP; when associated with A-564."
FT /evidence="ECO:0000269|PubMed:11281123,
FT ECO:0000269|PubMed:7643197"
FT MUTAGEN 564
FT /note="S->A: Does not abolish channel activity inhibition
FT in presence of nitric oxide (NO); when associated with A-
FT 564. Absence of channel activity inhibition in presence of
FT cAMP; when associated with A-563."
FT /evidence="ECO:0000269|PubMed:11281123,
FT ECO:0000269|PubMed:7643197"
FT CONFLICT 2
FT /note="G -> S (in Ref. 4; CAA44643)"
FT /evidence="ECO:0000305"
SQ 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
