true2007-11-132024-01-24174KCNC2_HUMANLocalization of Shaw-related K+ channel genes on mouse and human chromosomes.Haas M.Ward D.C.Lee J.Roses A.D.Clarke V.D'Eustachio P.Lau D.Vega-Saenz de Miera E.Rudy B.doi:10.1007/bf003577941993Mamm. Genome4711-715NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3)Isbrandt D.Pongs O.2002-06EMBL/GenBank/DDBJNUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T.Suzuki Y.Nishikawa T.Otsuki T.Sugiyama T.Irie R.Wakamatsu A.Hayashi K.Sato H.Nagai K.Kimura K.Makita H.Sekine M.Obayashi M.Nishi T.Shibahara T.Tanaka T.Ishii S.Yamamoto J.Saito K.Kawai Y.Isono Y.Nakamura Y.Nagahari K.Murakami K.Yasuda T.Iwayanagi T.Wagatsuma M.Shiratori A.Sudo H.Hosoiri T.Kaku Y.Kodaira H.Kondo H.Sugawara M.Takahashi M.Kanda K.Yokoi T.Furuya T.Kikkawa E.Omura Y.Abe K.Kamihara K.Katsuta N.Sato K.Tanikawa M.Yamazaki M.Ninomiya K.Ishibashi T.Yamashita H.Murakawa K.Fujimori K.Tanai H.Kimata M.Watanabe M.Hiraoka S.Chiba Y.Ishida S.Ono Y.Takiguchi S.Watanabe S.Yosida M.Hotuta T.Kusano J.Kanehori K.Takahashi-Fujii A.Hara H.Tanase T.-O.Nomura Y.Togiya S.Komai F.Hara R.Takeuchi K.Arita M.Imose N.Musashino K.Yuuki H.Oshima A.Sasaki N.Aotsuka S.Yoshikawa Y.Matsunawa H.Ichihara T.Shiohata N.Sano S.Moriya S.Momiyama H.Satoh N.Takami S.Terashima Y.Suzuki O.Nakagawa S.Senoh A.Mizoguchi H.Goto Y.Shimizu F.Wakebe H.Hishigaki H.Watanabe T.Sugiyama A.Takemoto M.Kawakami B.Yamazaki M.'Watanabe K.Kumagai A.Itakura S.Fukuzumi Y.Fujimori Y.Komiyama M.Tashiro H.Tanigami A.Fujiwara T.Ono T.Yamada K.Fujii Y.Ozaki K.Hirao M.Ohmori Y.Kawabata A.Hikiji T.Kobatake N.Inagaki H.Ikema Y.Okamoto S.Okitani R.Kawakami T.Noguchi S.Itoh T.Shigeta K.Senba T.Matsumura K.Nakajima Y.Mizuno T.Morinaga M.Sasaki M.Togashi T.Oyama M.Hata H.Watanabe M.'Komatsu T.Mizushima-Sugano J.Satoh T.Shirai Y.Takahashi Y.Nakagawa K.Okumura K.Nagase T.Nomura N.Kikuchi H.Masuho Y.Yamashita R.Nakai K.Yada T.Nakamura Y.'Ohara O.Isogai T.Sugano S.doi:10.1038/ng12852004Nat. Genet.3640-45NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6)AmygdalaThalamusPreparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method.Nakajima D.Saito K.Yamakawa H.Kikuno R.F.Nakayama M.Ohara R.Okazaki N.Koga H.Nagase T.Ohara O.2005-03EMBL/GenBank/DDBJNUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)BrainThe finished DNA sequence of human chromosome 12.Scherer S.E.Muzny D.M.Buhay C.J.Chen R.Cree A.Ding Y.Dugan-Rocha S.Gill R.Gunaratne P.Harris R.A.Hawes A.C.Hernandez J.Hodgson A.V.Hume J.Jackson A.Khan Z.M.Kovar-Smith C.Lewis L.R.Lozado R.J.Metzker M.L.Milosavljevic A.Miner G.R.Montgomery K.T.Morgan M.B.Nazareth L.V.Scott G.Sodergren E.Song X.-Z.Steffen D.Lovering R.C.Wheeler D.A.Worley K.C.Yuan Y.Zhang Z.Adams C.Q.Ansari-Lari M.A.Ayele M.Brown M.J.Chen G.Chen Z.Clerc-Blankenburg K.P.Davis C.Delgado O.Dinh H.H.Draper H.Gonzalez-Garay M.L.Havlak P.Jackson L.R.Jacob L.S.Kelly S.H.Li L.Li Z.Liu J.Liu W.Lu J.Maheshwari M.Nguyen B.-V.Okwuonu G.O.Pasternak S.Perez L.M.Plopper F.J.H.Santibanez J.Shen H.Tabor P.E.Verduzco D.Waldron L.Wang Q.Williams G.A.Zhang J.Zhou J.Allen C.C.Amin A.G.Anyalebechi V.Bailey M.Barbaria J.A.Bimage K.E.Bryant N.P.Burch P.E.Burkett C.E.Burrell K.L.Calderon E.Cardenas V.Carter K.Casias K.Cavazos I.Cavazos S.R.Ceasar H.Chacko J.Chan S.N.Chavez D.Christopoulos C.Chu J.Cockrell R.Cox C.D.Dang M.Dathorne S.R.David R.Davis C.M.Davy-Carroll L.Deshazo D.R.Donlin J.E.D'Souza L.Eaves K.A.Egan A.Emery-Cohen A.J.Escotto M.Flagg N.Forbes L.D.Gabisi A.M.Garza M.Hamilton C.Henderson N.Hernandez O.Hines S.Hogues M.E.Huang M.Idlebird D.G.Johnson R.Jolivet A.Jones S.Kagan R.King L.M.Leal B.Lebow H.Lee S.LeVan J.M.Lewis L.C.London P.Lorensuhewa L.M.Loulseged H.Lovett D.A.Lucier A.Lucier R.L.Ma J.Madu R.C.Mapua P.Martindale A.D.Martinez E.Massey E.Mawhiney S.Meador M.G.Mendez S.Mercado C.Mercado I.C.Merritt C.E.Miner Z.L.Minja E.Mitchell T.Mohabbat F.Mohabbat K.Montgomery B.Moore N.Morris S.Munidasa M.Ngo R.N.Nguyen N.B.Nickerson E.Nwaokelemeh O.O.Nwokenkwo S.Obregon M.Oguh M.Oragunye N.Oviedo R.J.Parish B.J.Parker D.N.Parrish J.Parks K.L.Paul H.A.Payton B.A.Perez A.Perrin W.Pickens A.Primus E.L.Pu L.-L.Puazo M.Quiles M.M.Quiroz J.B.Rabata D.Reeves K.Ruiz S.J.Shao H.Sisson I.Sonaike T.Sorelle R.P.Sutton A.E.Svatek A.F.Svetz L.A.Tamerisa K.S.Taylor T.R.Teague B.Thomas N.Thorn R.D.Trejos Z.Y.Trevino B.K.Ukegbu O.N.Urban J.B.Vasquez L.I.Vera V.A.Villasana D.M.Wang L.Ward-Moore S.Warren J.T.Wei X.White F.Williamson A.L.Wleczyk R.Wooden H.S.Wooden S.H.Yen J.Yoon L.Yoon V.Zorrilla S.E.Nelson D.Kucherlapati R.Weinstock G.Gibbs R.A.doi:10.1038/nature045692006Nature440346-351NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]Mural R.J.Istrail S.Sutton G.G.Florea L.Halpern A.L.Mobarry C.M.Lippert R.Walenz B.Shatkay H.Dew I.Miller J.R.Flanigan M.J.Edwards N.J.Bolanos R.Fasulo D.Halldorsson B.V.Hannenhalli S.Turner R.Yooseph S.Lu F.Nusskern D.R.Shue B.C.Zheng X.H.Zhong F.Delcher A.L.Huson D.H.Kravitz S.A.Mouchard L.Reinert K.Remington K.A.Clark A.G.Waterman M.S.Eichler E.E.Adams M.D.Hunkapiller M.W.Myers E.W.Venter J.C.2006-12EMBL/GenBank/DDBJNUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).The MGC Project Teamdoi:10.1101/gr.25965042004Genome Res.142121-2127NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4)Contributions of Kv3 channels to neuronal excitability.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.doi:10.1111/j.1749-6632.1999.tb11295.x1999Ann. N. Y. Acad. Sci.868304-343REVIEWKv3 channels: voltage-gated K+ channels designed for high-frequency repetitive firing.Rudy B.McBain C.J.doi:10.1016/s0166-2236(00)01892-02001Trends Neurosci.24517-526REVIEWStichodactyla helianthus peptide, a pharmacological tool for studying Kv3.2 channels.Yan L.Herrington J.Goldberg E.Dulski P.M.Bugianesi R.M.Slaughter R.S.Banerjee P.Brochu R.M.Priest B.T.Kaczorowski G.J.Rudy B.Garcia M.L.doi:10.1124/mol.105.0110642005Mol. Pharmacol.671513-1521FUNCTIONBIOPHYSICOCHEMICAL PROPERTIESACTIVITY REGULATIONSUBCELLULAR LOCATIONDeletion of chromosome 12q21 affecting KCNC2 and ATXN7L3B in a family with neurodevelopmental delay and ataxia.Rajakulendran S.Roberts J.Koltzenburg M.Hanna M.G.Stewart H.doi:10.1136/jnnp-2012-3045552013J. Neurol. Neurosurg. Psych.841255-1257CHROMOSOMAL REARRANGEMENTA de novo heterozygous mutation in KCNC2 gene implicated in severe developmental and epileptic encephalopathy.Vetri L.Cali F.Vinci M.Amato C.Roccella M.Granata T.Freri E.Solazzi R.Romano V.Elia M.doi:10.1016/j.ejmg.2020.1038482020Eur. J. Med. Genet.63103848VARIANT DEE103 LEU-471INVOLVEMENT IN DEE103Whole-exome sequencing in NF1-related West syndrome leads to the identification of KCNC2 as a novel candidate gene for epilepsy.Rademacher A.Schwarz N.Seiffert S.Pendziwiat M.Rohr A.van Baalen A.Helbig I.Weber Y.Muhle H.doi:10.1055/s-0040-17105242020Neuropediatrics51368-372VARIANT DEE103 TYR-167INVOLVEMENT IN DEE103CHARACTERIZATION OF VARIANT DEE103 TYR-167A recurrent de novo variant supports KCNC2 involvement in the pathogenesis of developmental and epileptic encephalopathy.Rydzanicz M.Zwolinski P.Gasperowicz P.Pollak A.Kostrzewa G.Walczak A.Konarzewska M.Ploski R.doi:10.1002/ajmg.a.624552021Am. J. Med. Genet. A1853384-3389VARIANT DEE103 LEU-471INVOLVEMENT IN DEE103Emerging evidence of genotype-phenotype associations of developmental and epileptic encephalopathy due to KCNC2 mutation: Identification of novel R405G.Wang S.Yu Y.Wang X.Deng X.Ma J.Liu Z.Gu W.Sun D.doi:10.3389/fnmol.2022.9502552022Front. Mol. Neurosci.15950255VARIANT DEE103 GLY-405CHARACTERIZATION OF VARIANT DEE103 GLY-405Spectrum of phenotypic, genetic, and functional characteristics in patients with epilepsy with KCNC2 pathogenic variants.Schwarz N.Seiffert S.Pendziwiat M.Rademacher A.V.Bruenger T.Hedrich U.B.S.Augustijn P.B.Baier H.Bayat A.Bisulli F.Buono R.J.Bruria B.Z.Doyle M.G.Guerrini R.Heimer G.Iacomino M.Kearney H.Klein K.M.Kousiappa I.Kunz W.S.Lerche H.Licchetta L.Lohmann E.Minardi R.McDonald M.Montgomery S.Mulahasanovic L.Oegema R.Ortal B.Papacostas S.S.Ragona F.Granata T.Reif P.S.Rosenow F.Rothschild A.Scudieri P.Striano P.Tinuper P.Tanteles G.A.Vetro A.Zahnert F.Goldberg E.M.Zara F.Lal D.May P.Muhle H.Helbig I.Weber Y.doi:10.1212/wnl.00000000002006602022Neurology98e2046-e2059VARIANTS DEE103 TRP-125; GLY-135; LYS-351 AND ALA-437CHARACTERIZATION OF VARIANTS DEE103 TRP-125; GLY-135 AND ALA-437VARIANTS SER-219 AND CYS-382CHARACTERIZATION OF VARIANT SER-219Different initiation.1DalfampridineEnfluraneMiconazolePromethazine2 sites, No reported glycans2 sites3 sequenced antibodies294 antibodies from 30 providershumanKCNC2Tissue enriched (brain)genephenotypeEukaryotaVoltage gated Potassium channelsGlucagon-like Peptide-1 (GLP1) regulates insulin secretion19 hits in 1154 CRISPR screenshumanTclinProteinExpressed in prefrontal cortex and 52 other cell types or tissuesbaseline and differentialHSBTB_KCNC2_4Voltage-gated potassium channels. Chain CBTB/POZ_domIon_trans_domK_chnl_volt-dep_KvK_chnl_volt-dep_Kv3SKP1/BTB/POZ_sfT1-type_BTBVolt_channel_dom_sfPOTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY C MEMBER 2VOLTAGE-GATED POTASSIUM CHANNELBTB_2Ion_transKCHANNELKVCHANNELSHAWCHANNELBTBPOZ domainVoltage-gated potassium channelsPotassium voltage-gated channel subfamily C member 2Shaw-like potassium channelVoltage-gated potassium channel Kv3.2KCNC2Voltage-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. Homotetramer channels mediate delayed-rectifier voltage-dependent potassium currents that activate rapidly at high-threshold voltages and inactivate slowly. 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:15709110). Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNC1, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel. Channel properties may be modulated either by the association with ancillary subunits, such as KCNE1, KCNE2 or KCNE3 or indirectly by nitric oxide (NO) through a cGMP- and PKG-mediated signaling cascade, slowing channel activation and deactivation of delayed rectifier potassium channels (By similarity). Contributes to fire sustained trains of very brief action potentials at high frequency in retinal ganglion cells, thalamocortical and suprachiasmatic nucleus (SCN) neurons and in hippocampal and neocortical interneurons (PubMed:15709110). 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).Inhibited by Stichodactyla helianthus peptide ShK (PubMed:15709110). Inhibited by millimolar levels of tetraethylammonium (TEA). Contrary to other channels, inhibited only by millimolar levels of 4-aminopyridine (4-AP) (By similarity).Homotetrameric channels expressed in xenopus oocytes or in mammalian non-neuronal cells display delayed-rectifier voltage-dependent potassium currents, that are rapidly activated during membrane depolarization, i.e within a risetime of a few msec. After that, inactivates very slowly, i.e within about >800 msec. Their activation requires a threshold potential at about -10 mV, with a midpoint activation at about 12.1 mV and a steepness parameter of about 8.4 mV. The voltage-dependence of activation and inactivation and other channel characteristics vary depending on the experimental conditions, the expression system, the presence or absence of ancillary subunits and post-translational modifications.Homotetramer and heterotetramer with other channel-forming alpha subunits, such as KCNC1. Interacts with KCNC1. 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.Colocalizes with parvalbumin in globus pallidus neurons. Localizes in thalamocortical axons and synapses. 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.The transmembrane segment S4 functions as a 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.Phosphorylated by PKA in cortical synaptosomes. cAMP-dependent phosphorylation inhibits channel activity (By similarity). Histamine H2 receptor- and PKA-induced phosphorylation extends action potential spike duration, reduces action potential spike amplitude, sustains maximum firing frequency in hippocampal interneurons; also reduces the incidence of high-frequency oscillations in hippocampal CA3 pyramidal cell layers.A chromosomal aberration involving KCNC2 has been found in a mother and her two children with varying degrees of neurodevelopmental delay and cerebellar ataxia. One child also exhibits episodes of unresponsiveness suggestive of absence seizures and facial dysmorphism. Deletion at 12q21.1 deletes exons 3-5 of KCNC2.The disease is caused by variants affecting the gene represented in this entry.Belongs to the potassium channel family. C (Shaw) (TC 1.A.1.2) subfamily. Kv3.2/KCNC2 sub-subfamily.Potassium voltage-gated channel subfamily C member 2702261638Cytoplasmic229Helical; Name=Segment S1230250Helical; Name=Segment S2284303Cytoplasmic304313Helical; Name=Segment S3314334Helical; Voltage-sensor; Name=Segment S4346368Cytoplasmic369381Helical; Name=Segment S5382402Helical; Name=Segment S6453473Cytoplasmic474Disordered3893Selectivity filter437442Disordered538572Pro residues5672Phosphoserine600N-linked (GlcNAc...) asparagine259N-linked (GlcNAc...) asparagine266In isoform 5.539593In isoform 4.DNCKEVVITGYTQAEARSLT558In isoform 4.559In isoform 2.VLYRIYHGLLTAEKGTVEFSHTKDYTGNRLLLLNVP594In isoform 3.DNCKEVVITGYTQAEARSLTIn isoform 6.IRNGHSILHHLDNGTKCHYLRIIF595In DEE103; affects voltage-gated potassium channel activity; when expressed in Xenopus laevis oocytes, it results in a shift in voltage dependence of activation to more hyperpolarized potentials and a slower deactivation time.W125In DEE103; affects voltage-gated potassium channel activity; when expressed in Xenopus laevis oocytes, it results in a shift in voltage dependence of activation to more hyperpolarized potentials and a slower deactivation time.G135In DEE103; affects voltage-gated potassium channel activity; when expressed in Xenopus laevis oocytes, it causes a shift in voltage dependence of steady-state activation to more hyperpolarized potentials and results in a significant reduction of potassium currents.Y167Found in a patient with generalized epilepsy; likely pathogenic; loss of voltage-gated potassium channel activity; no current is detected when mutant channels are expressed in Xenopus laevis oocytes.S219In DEE103.K351Found in a patient with myoclonic-atonic epilepsy; uncertain significance.CIn DEE103; affects voltage-gated potassium channel activity; results in a shift in voltage dependence of activation to more hyperpolarized potentials.G405In DEE103; affects voltage-gated potassium channel activity; when expressed in Xenopus laevis oocytes, it results in a shift in voltage dependence of activation to more hyperpolarized potentials and a slower deactivation time.AIn DEE103.L471V31S305S476H4872001-12-01170226a8cef8a9fb4c27b86df85f481d1e32c91Kv3.2bMGKIENNERVILNVGGTRHETYRSTLKTLPGTRLALLASSEPPGDCLTTAGDKLQPSPPPLSPPPRAPPLSPGPGGCFEGGAGNCSSRGGRASDHPGGGREFFFDRHPGVFAYVLNYYRTGKLHCPADVCGPLFEEELAFWGIDETDVEPCCWMTYRQHRDAEEALDIFETPDLIGGDPGDDEDLAAKRLGIEDAAGLGGPDGKSGRWRRLQPRMWALFEDPYSSRAARFIAFASLFFILVSITTFCLETHEAFNIVKNKTEPVINGTSVVLQYEIETDPALTYVEGVCVVWFTFEFLVRIVFSPNKLEFIKNLLNIIDFVAILPFYLEVGLSGLSSKAAKDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERVGAQPNDPSASEHTQFKNIPIGFWWAVVTMTTLGYGDMYPQTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPRKRKKHIPPAPQASSPTFCKTELNMACNSTQSDTCLGKDNRLLEHNRSVLSGDDSTGSEPPLSPPERLPIRRSSTRDKNRRGETCFLLTTGDYTCASDGGIRKGYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIPSIL2Kv3.2dMGKIENNERVILNVGGTRHETYRSTLKTLPGTRLALLASSEPPGDCLTTAGDKLQPSPPPLSPPPRAPPLSPGPGGCFEGGAGNCSSRGGRASDHPGGGREFFFDRHPGVFAYVLNYYRTGKLHCPADVCGPLFEEELAFWGIDETDVEPCCWMTYRQHRDAEEALDIFETPDLIGGDPGDDEDLAAKRLGIEDAAGLGGPDGKSGRWRRLQPRMWALFEDPYSSRAARFIAFASLFFILVSITTFCLETHEAFNIVKNKTEPVINGTSVVLQYEIETDPALTYVEGVCVVWFTFEFLVRIVFSPNKLEFIKNLLNIIDFVAILPFYLEVGLSGLSSKAAKDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERVGAQPNDPSASEHTQFKNIPIGFWWAVVTMTTLGYGDMYPQTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPRKRKKHIPPAPQASSPTFCKTELNMACNSTQSDTCLGKDNRLLEHNRSVLSGDDSTGSEPPLSPPERLPIRRSSTRDKNRRGETCFLLTTGDYTCASDGGIRKVLYRIYHGLLTAEKGTVEFSHTKDYTGNRLLLLNVP3Kv3.2aMGKIENNERVILNVGGTRHETYRSTLKTLPGTRLALLASSEPPGDCLTTAGDKLQPSPPPLSPPPRAPPLSPGPGGCFEGGAGNCSSRGGRASDHPGGGREFFFDRHPGVFAYVLNYYRTGKLHCPADVCGPLFEEELAFWGIDETDVEPCCWMTYRQHRDAEEALDIFETPDLIGGDPGDDEDLAAKRLGIEDAAGLGGPDGKSGRWRRLQPRMWALFEDPYSSRAARFIAFASLFFILVSITTFCLETHEAFNIVKNKTEPVINGTSVVLQYEIETDPALTYVEGVCVVWFTFEFLVRIVFSPNKLEFIKNLLNIIDFVAILPFYLEVGLSGLSSKAAKDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERVGAQPNDPSASEHTQFKNIPIGFWWAVVTMTTLGYGDMYPQTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPRKRKKHIPPAPQASSPTFCKTELNMACNSTQSDTCLGKDNRLLEHNRSVLSGDDSTGSEPPLSPPERLPIRRSSTRDKNRRGETCFLLTTGDYTCASDGGIRKDNCKEVVITGYTQAEARSLT4Kv3.2cMGKIENNERVILNVGGTRHETYRSTLKTLPGTRLALLASSEPPGDCLTTAGDKLQPSPPPLSPPPRAPPLSPGPGGCFEGGAGNCSSRGGRASDHPGGGREFFFDRHPGVFAYVLNYYRTGKLHCPADVCGPLFEEELAFWGIDETDVEPCCWMTYRQHRDAEEALDIFETPDLIGGDPGDDEDLAAKRLGIEDAAGLGGPDGKSGRWRRLQPRMWALFEDPYSSRAARFIAFASLFFILVSITTFCLETHEAFNIVKNKTEPVINGTSVVLQYEIETDPALTYVEGVCVVWFTFEFLVRIVFSPNKLEFIKNLLNIIDFVAILPFYLEVGLSGLSSKAAKDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERVGAQPNDPSASEHTQFKNIPIGFWWAVVTMTTLGYGDMYPQTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPRKRKKHIPPAPQASSPTFCKTELNMACNSTQSDTCLGKDNRLLEHNRSDNCKEVVITGYTQAEARSLT5MGKIENNERVILNVGGTRHETYRSTLKTLPGTRLALLASSEPPGDCLTTAGDKLQPSPPPLSPPPRAPPLSPGPGGCFEGGAGNCSSRGGRASDHPGGGREFFFDRHPGVFAYVLNYYRTGKLHCPADVCGPLFEEELAFWGIDETDVEPCCWMTYRQHRDAEEALDIFETPDLIGGDPGDDEDLAAKRLGIEDAAGLGGPDGKSGRWRRLQPRMWALFEDPYSSRAARFIAFASLFFILVSITTFCLETHEAFNIVKNKTEPVINGTSVVLQYEIETDPALTYVEGVCVVWFTFEFLVRIVFSPNKLEFIKNLLNIIDFVAILPFYLEVGLSGLSSKAAKDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERVGAQPNDPSASEHTQFKNIPIGFWWAVVTMTTLGYGDMYPQTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPRKRKKHIPPAPQASSPTFCKTELNMACNSTQSDTCLGKDNRLLEHNRSGYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIPSIL6MGKIENNERVILNVGGTRHETYRSTLKTLPGTRLALLASSEPPGDCLTTAGDKLQPSPPPLSPPPRAPPLSPGPGGCFEGGAGNCSSRGGRASDHPGGGREFFFDRHPGVFAYVLNYYRTGKLHCPADVCGPLFEEELAFWGIDETDVEPCCWMTYRQHRDAEEALDIFETPDLIGGDPGDDEDLAAKRLGIEDAAGLGGPDGKSGRWRRLQPRMWALFEDPYSSRAARFIAFASLFFILVSITTFCLETHEAFNIVKNKTEPVINGTSVVLQYEIETDPALTYVEGVCVVWFTFEFLVRIVFSPNKLEFIKNLLNIIDFVAILPFYLEVGLSGLSSKAAKDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERVGAQPNDPSASEHTQFKNIPIGFWWAVVTMTTLGYGDMYPQTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPRKRKKHIPPAPQASSPTFCKTELNMACNSTQSDTCLGKDNRLLEHNRSVLSGDDSTGSEPPLSPPERLPIRRSSTRDKNRRGETCFLLTTGDYTCASDGGIRKGIRNGHSILHHLDNGTKCHYLRIIFtruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetrue