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 24-JAN-2024, entry version 184. 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 CC voltage-dependent potassium currents, that are rapidly activated CC during membrane depolarization, i.e within a risetime of a few msec. CC After that, inactivates very slowly, i.e within about >800 msec. CC Their activation requires a threshold potential at about -10 mV, with CC a 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 a voltage-sensor and CC is 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) CC (TC 1.A.1.2) subfamily. Kv3.2/KCNC2 sub-subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_017450152.1; XM_017594663.1. DR AlphaFoldDB; P22462; -. DR SMR; P22462; -. DR BioGRID; 251521; 1. DR STRING; 10116.ENSRNOP00000005773; -. DR DrugCentral; P22462; -. DR GuidetoPHARMACOLOGY; 549; -. DR GlyCosmos; P22462; 2 sites, No reported glycans. DR GlyGen; P22462; 2 sites. DR PhosphoSitePlus; P22462; -. DR PaxDb; 10116-ENSRNOP00000005773; -. DR ABCD; P22462; 3 sequenced antibodies. DR Ensembl; ENSRNOT00000005690.5; ENSRNOP00000005690.2; ENSRNOG00000004077.9. [P22462-3] DR Ensembl; ENSRNOT00000005773.8; ENSRNOP00000005773.4; ENSRNOG00000004077.9. [P22462-1] DR Ensembl; ENSRNOT00000099049.1; ENSRNOP00000084708.1; ENSRNOG00000004077.9. [P22462-2] DR Ensembl; ENSRNOT00000105247.1; ENSRNOP00000088724.1; ENSRNOG00000004077.9. [P22462-4] DR Ensembl; ENSRNOT00055020968; ENSRNOP00055016940; ENSRNOG00055012317. [P22462-1] DR Ensembl; ENSRNOT00060006183; ENSRNOP00060004592; ENSRNOG00060003730. [P22462-1] DR Ensembl; ENSRNOT00065022805; ENSRNOP00065017701; ENSRNOG00065013851. [P22462-1] DR GeneID; 246153; -. DR KEGG; rno:246153; -. DR UCSC; RGD:628829; rat. [P22462-1] DR AGR; RGD:628829; -. 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; FYADAMM; -. DR OrthoDB; 1478695at2759; -. 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 cell types or tissues. 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:0043679; C:axon terminus; IBA:GO_Central. 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:0098982; C:GABA-ergic synapse; IDA:SynGO. 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; IDA:SynGO. 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 monoatomic 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:monoatomic ion transmembrane transport; IDA:RGD. DR GO; GO:0038060; P:nitric oxide-cGMP-mediated signaling pathway; IDA:UniProtKB. DR GO; GO:0021554; P:optic nerve development; IEP:RGD. DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; 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 CDD; cd18415; BTB_KCNC2_4; 1. DR Gene3D; 1.10.287.70; -; 1. DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 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; IPR027359; Volt_channel_dom_sf. DR PANTHER; PTHR11537:SF172; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY C MEMBER 2; 1. DR PANTHER; PTHR11537; VOLTAGE-GATED POTASSIUM CHANNEL; 1. DR Pfam; PF02214; BTB_2; 1. DR Pfam; PF00520; Ion_trans; 1. DR PRINTS; PR00169; KCHANNEL. DR PRINTS; PR01491; KVCHANNEL. DR PRINTS; PR01498; SHAWCHANNEL. DR SMART; SM00225; BTB; 1. DR SUPFAM; SSF54695; POZ domain; 1. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1. DR Genevisible; P22462; RN. 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 FT A-564. Absence of channel activity inhibition in presence FT of 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 FT A-564. Absence of channel activity inhibition in presence FT of 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 //