KCNC2_HUMAN
ID KCNC2_HUMAN Reviewed; 638 AA.
AC Q96PR1; B7Z231; F5H030; J3KPP5; Q4LE77; Q86W09; Q8N1V9; Q96PR0;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Potassium voltage-gated channel subfamily C member 2 {ECO:0000312|HGNC:HGNC:6234};
DE AltName: Full=Shaw-like potassium channel {ECO:0000250|UniProtKB:P22462};
DE AltName: Full=Voltage-gated potassium channel Kv3.2 {ECO:0000250|UniProtKB:P22462};
GN Name=KCNC2 {ECO:0000312|HGNC:HGNC:6234};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RX PubMed=8111118; DOI=10.1007/bf00357794;
RA Haas M., Ward D.C., Lee J., Roses A.D., Clarke V., D'Eustachio P., Lau D.,
RA Vega-Saenz de Miera E., Rudy B.;
RT "Localization of Shaw-related K+ channel genes on mouse and human
RT chromosomes.";
RL Mamm. Genome 4:711-715(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Isbrandt D., Pongs O.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6).
RC TISSUE=Amygdala, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R.,
RA Okazaki N., Koga H., Nagase T., Ohara O.;
RT "Preparation of a set of expression-ready clones of mammalian long cDNAs
RT encoding large proteins by the ORF trap cloning method.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
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 [9]
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 [10]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15709110; DOI=10.1124/mol.105.011064;
RA Yan L., Herrington J., Goldberg E., Dulski P.M., Bugianesi R.M.,
RA Slaughter R.S., Banerjee P., Brochu R.M., Priest B.T., Kaczorowski G.J.,
RA Rudy B., Garcia M.L.;
RT "Stichodactyla helianthus peptide, a pharmacological tool for studying
RT Kv3.2 channels.";
RL Mol. Pharmacol. 67:1513-1521(2005).
RN [11]
RP CHROMOSOMAL REARRANGEMENT.
RX PubMed=23475819; DOI=10.1136/jnnp-2012-304555;
RA Rajakulendran S., Roberts J., Koltzenburg M., Hanna M.G., Stewart H.;
RT "Deletion of chromosome 12q21 affecting KCNC2 and ATXN7L3B in a family with
RT neurodevelopmental delay and ataxia.";
RL J. Neurol. Neurosurg. Psych. 84:1255-1257(2013).
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. Homotetramer channels mediate delayed-rectifier
CC voltage-dependent potassium currents that activate rapidly at high-
CC threshold voltages and inactivate slowly. Forms tetrameric channels
CC through which potassium ions pass in accordance with their
CC electrochemical gradient. The channel alternates between opened and
CC closed conformations in response to the voltage difference across the
CC membrane (PubMed:15709110). Can form functional homotetrameric and
CC heterotetrameric channels that contain variable proportions of KCNC1,
CC and possibly other family members as well; channel properties depend on
CC the type of alpha subunits that are part of the channel. Channel
CC properties may be modulated either by the association with ancillary
CC subunits, such as KCNE1, KCNE2 or KCNE3 or indirectly by nitric oxide
CC (NO) through a cGMP- and PKG-mediated signaling cascade, slowing
CC channel activation and deactivation of delayed rectifier potassium
CC channels (By similarity). Contributes to fire sustained trains of very
CC brief action potentials at high frequency in retinal ganglion cells,
CC thalamocortical and suprachiasmatic nucleus (SCN) neurons and in
CC hippocampal and neocortical interneurons (PubMed:15709110). Sustained
CC maximal action potential firing frequency in inhibitory hippocampal
CC interneurons is negatively modulated by histamine H2 receptor
CC activation in a cAMP- and protein kinase (PKA) phosphorylation-
CC dependent manner. Plays a role in maintaining the fidelity of synaptic
CC transmission in neocortical GABAergic interneurons by generating action
CC potential (AP) repolarization at nerve terminals, thus reducing spike-
CC evoked calcium influx and GABA neurotransmitter release. Required for
CC long-range synchronization of gamma oscillations over distance in the
CC neocortex. Contributes to the modulation of the circadian rhythm of
CC spontaneous action potential firing in suprachiasmatic nucleus (SCN)
CC neurons in a light-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:P22462, ECO:0000250|UniProtKB:Q14B80,
CC ECO:0000269|PubMed:15709110, ECO:0000305|PubMed:10414303,
CC ECO:0000305|PubMed:11506885}.
CC -!- ACTIVITY REGULATION: Inhibited by Stichodactyla helianthus peptide ShK
CC (PubMed:15709110). Inhibited by millimolar levels of tetraethylammonium
CC (TEA). Contrary to other channels, inhibited only by millimolar levels
CC of 4-aminopyridine (4-AP) (By similarity).
CC {ECO:0000250|UniProtKB:P22462, ECO:0000269|PubMed:15709110,
CC ECO:0000305|PubMed:10414303}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=Homotetrameric channels expressed in xenopus oocytes or in
CC mammalian non-neuronal cells display delayed-rectifier voltage-
CC dependent potassium currents, that are rapidly activated during
CC membrane depolarization, i.e within a risetime of a few msec. After
CC that, inactivates very slowly, i.e within about >800 msec. Their
CC activation requires a threshold potential at about -10 mV, with a
CC midpoint activation at about 12.1 mV and a steepness parameter of
CC about 8.4 mV. The voltage-dependence of activation and inactivation
CC and other channel characteristics vary depending on the experimental
CC conditions, the expression system, the presence or absence of
CC ancillary subunits and post-translational modifications.
CC {ECO:0000269|PubMed:15709110, ECO:0000305|PubMed:10414303};
CC -!- SUBUNIT: Homotetramer and heterotetramer with other channel-forming
CC alpha subunits, such as KCNC1. Interacts with KCNC1. Homotetramer or
CC heterotetramer channel activity is regulated by association with
CC modulating ancillary subunits such as KCNE1, KCNE2 and KCNE3, creating
CC a functionally diverse range of channel complexes. Interacts with
CC KCNE1, KCNE2 and KCNE3. {ECO:0000250|UniProtKB:P22462,
CC ECO:0000250|UniProtKB:Q14B80}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15709110};
CC Multi-pass membrane protein {ECO:0000255}. Membrane
CC {ECO:0000250|UniProtKB:Q14B80}; Multi-pass membrane protein
CC {ECO:0000255}. Perikaryon {ECO:0000250|UniProtKB:Q14B80}. Cell
CC projection, axon {ECO:0000250|UniProtKB:Q14B80}. Cell projection,
CC dendrite {ECO:0000250|UniProtKB:Q14B80}. Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q14B80}. Presynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q14B80}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:P22462}. Synapse {ECO:0000250|UniProtKB:P22462}.
CC Apical cell membrane {ECO:0000250|UniProtKB:P22462}. Basolateral cell
CC membrane {ECO:0000250|UniProtKB:P22462}. Note=Colocalizes with
CC parvalbumin in globus pallidus neurons. Localizes in thalamocortical
CC axons and synapses. Localizes on the surface of cell somata, proximal
CC dendrites and axonal membranes. Also detected throughout the neuropil.
CC Localized in starburst cell somata and proximal dendrite processes.
CC Colocalized with GABA in presynaptic terminals. Clustered in patches in
CC somatic and proximal dendritic membrane as well as in axons and
CC presnypatic terminals of GABAergic interneurons; some of these patches
CC are found near postsynaptic sites. {ECO:0000250|UniProtKB:P22462,
CC ECO:0000250|UniProtKB:Q14B80}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=Kv3.2b;
CC IsoId=Q96PR1-1; Sequence=Displayed;
CC Name=2; Synonyms=Kv3.2d;
CC IsoId=Q96PR1-2; Sequence=VSP_029271;
CC Name=3; Synonyms=Kv3.2a;
CC IsoId=Q96PR1-3; Sequence=VSP_029272;
CC Name=4; Synonyms=Kv3.2c;
CC IsoId=Q96PR1-4; Sequence=VSP_029269, VSP_029270;
CC Name=5;
CC IsoId=Q96PR1-5; Sequence=VSP_044742;
CC Name=6;
CC IsoId=Q96PR1-6; Sequence=VSP_046002;
CC -!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position. Channel opening and closing is effected by a
CC conformation change that affects the position and orientation of the
CC voltage-sensor paddle formed by S3 and S4 within the membrane. A
CC transmembrane electric field that is positive inside would push the
CC positively charged S4 segment outwards, thereby opening the pore, while
CC a field that is negative inside would pull the S4 segment inwards and
CC close the pore. Changes in the position and orientation of S4 are then
CC transmitted to the activation gate formed by the inner helix bundle via
CC the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}.
CC -!- PTM: Phosphorylated by PKA in cortical synaptosomes. cAMP-dependent
CC phosphorylation inhibits channel activity (By similarity). Histamine H2
CC receptor- and PKA-induced phosphorylation extends action potential
CC spike duration, reduces action potential spike amplitude, sustains
CC maximum firing frequency in hippocampal interneurons; also reduces the
CC incidence of high-frequency oscillations in hippocampal CA3 pyramidal
CC cell layers. {ECO:0000250|UniProtKB:P22462,
CC ECO:0000250|UniProtKB:Q14B80}.
CC -!- DISEASE: Note=A chromosomal aberration involving KCNC2 has been found
CC in a mother and her two children with varying degrees of
CC neurodevelopmental delay and cerebellar ataxia. One child also exhibits
CC episodes of unresponsiveness suggestive of absence seizures and facial
CC dysmorphism. Deletion at 12q21.1 deletes exons 3-5 of KCNC2.
CC {ECO:0000269|PubMed:23475819}.
CC -!- SIMILARITY: Belongs to the potassium channel family. C (Shaw) (TC
CC 1.A.1.2) subfamily. Kv3.2/KCNC2 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE06076.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF268896; AAL27272.1; -; mRNA.
DR EMBL; AF268897; AAL27273.1; -; mRNA.
DR EMBL; AY243473; AAO89503.1; -; mRNA.
DR EMBL; AY118169; AAM81577.1; -; mRNA.
DR EMBL; AK094720; BAC04407.1; -; mRNA.
DR EMBL; AK294269; BAH11717.1; -; mRNA.
DR EMBL; AK309245; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB209994; BAE06076.1; ALT_INIT; mRNA.
DR EMBL; AC073525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC130405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97287.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW97288.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW97289.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW97291.1; -; Genomic_DNA.
DR EMBL; BC093635; AAH93635.1; -; mRNA.
DR EMBL; BC111991; AAI11992.1; -; mRNA.
DR CCDS; CCDS58255.1; -. [Q96PR1-5]
DR CCDS; CCDS58256.1; -. [Q96PR1-2]
DR CCDS; CCDS58257.1; -. [Q96PR1-6]
DR CCDS; CCDS9005.1; -. [Q96PR1-3]
DR CCDS; CCDS9006.1; -. [Q96PR1-4]
DR CCDS; CCDS9007.1; -. [Q96PR1-1]
DR RefSeq; NP_001247426.1; NM_001260497.1. [Q96PR1-6]
DR RefSeq; NP_001247427.1; NM_001260498.1. [Q96PR1-2]
DR RefSeq; NP_001247428.1; NM_001260499.1. [Q96PR1-5]
DR RefSeq; NP_631874.1; NM_139136.3. [Q96PR1-3]
DR RefSeq; NP_631875.1; NM_139137.3. [Q96PR1-1]
DR RefSeq; NP_715624.1; NM_153748.2. [Q96PR1-4]
DR RefSeq; XP_006719445.1; XM_006719382.3. [Q96PR1-3]
DR AlphaFoldDB; Q96PR1; -.
DR SMR; Q96PR1; -.
DR BioGRID; 109949; 1.
DR STRING; 9606.ENSP00000449253; -.
DR ChEMBL; CHEMBL2363009; -.
DR DrugBank; DB06637; Dalfampridine.
DR DrugBank; DB00228; Enflurane.
DR DrugBank; DB01110; Miconazole.
DR DrugBank; DB01069; Promethazine.
DR DrugCentral; Q96PR1; -.
DR GuidetoPHARMACOLOGY; 549; -.
DR GlyGen; Q96PR1; 2 sites.
DR iPTMnet; Q96PR1; -.
DR PhosphoSitePlus; Q96PR1; -.
DR BioMuta; KCNC2; -.
DR DMDM; 74752079; -.
DR EPD; Q96PR1; -.
DR MassIVE; Q96PR1; -.
DR PaxDb; Q96PR1; -.
DR PeptideAtlas; Q96PR1; -.
DR PRIDE; Q96PR1; -.
DR ProteomicsDB; 25209; -.
DR ProteomicsDB; 77738; -. [Q96PR1-1]
DR ProteomicsDB; 77739; -. [Q96PR1-2]
DR ProteomicsDB; 77740; -. [Q96PR1-3]
DR ProteomicsDB; 77741; -. [Q96PR1-4]
DR TopDownProteomics; Q96PR1-4; -. [Q96PR1-4]
DR ABCD; Q96PR1; 3 sequenced antibodies.
DR Antibodypedia; 17155; 267 antibodies from 30 providers.
DR DNASU; 3747; -.
DR Ensembl; ENST00000298972.5; ENSP00000298972.1; ENSG00000166006.14. [Q96PR1-3]
DR Ensembl; ENST00000350228.6; ENSP00000319877.2; ENSG00000166006.14. [Q96PR1-4]
DR Ensembl; ENST00000393288.2; ENSP00000376966.2; ENSG00000166006.14. [Q96PR1-6]
DR Ensembl; ENST00000540018.5; ENSP00000438423.1; ENSG00000166006.14. [Q96PR1-5]
DR Ensembl; ENST00000548513.5; ENSP00000449941.1; ENSG00000166006.14. [Q96PR1-3]
DR Ensembl; ENST00000549446.6; ENSP00000449253.2; ENSG00000166006.14. [Q96PR1-1]
DR Ensembl; ENST00000550433.5; ENSP00000448301.1; ENSG00000166006.14. [Q96PR1-2]
DR GeneID; 3747; -.
DR KEGG; hsa:3747; -.
DR MANE-Select; ENST00000549446.6; ENSP00000449253.2; NM_139137.4; NP_631875.1.
DR UCSC; uc001sxe.5; human. [Q96PR1-1]
DR CTD; 3747; -.
DR DisGeNET; 3747; -.
DR GeneCards; KCNC2; -.
DR HGNC; HGNC:6234; KCNC2.
DR HPA; ENSG00000166006; Tissue enriched (brain).
DR MIM; 176256; gene.
DR neXtProt; NX_Q96PR1; -.
DR OpenTargets; ENSG00000166006; -.
DR PharmGKB; PA35490; -.
DR VEuPathDB; HostDB:ENSG00000166006; -.
DR eggNOG; KOG3713; Eukaryota.
DR GeneTree; ENSGT00940000157371; -.
DR HOGENOM; CLU_011722_4_3_1; -.
DR InParanoid; Q96PR1; -.
DR OMA; ELNTACN; -.
DR OrthoDB; 1123666at2759; -.
DR PhylomeDB; Q96PR1; -.
DR TreeFam; TF352511; -.
DR PathwayCommons; Q96PR1; -.
DR Reactome; R-HSA-1296072; Voltage gated Potassium channels.
DR Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR SIGNOR; Q96PR1; -.
DR BioGRID-ORCS; 3747; 19 hits in 1068 CRISPR screens.
DR ChiTaRS; KCNC2; human.
DR GeneWiki; KCNC2; -.
DR GenomeRNAi; 3747; -.
DR Pharos; Q96PR1; Tclin.
DR PRO; PR:Q96PR1; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q96PR1; protein.
DR Bgee; ENSG00000166006; Expressed in prefrontal cortex and 52 other tissues.
DR ExpressionAtlas; Q96PR1; baseline and differential.
DR Genevisible; Q96PR1; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0030673; C:axolemma; IEA:Ensembl.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0032590; C:dendrite membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0032809; C:neuronal cell body membrane; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS: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; ISS:UniProtKB.
DR GO; GO:0043195; C:terminal bouton; IEA:Ensembl.
DR GO; GO:0031982; C:vesicle; IEA:Ensembl.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR GO; GO:0099508; F:voltage-gated ion channel activity involved in regulation of presynaptic membrane potential; IEA:Ensembl.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISS:UniProtKB.
DR GO; GO:0001508; P:action potential; IEA:Ensembl.
DR GO; GO:0071242; P:cellular response to ammonium ion; IEA:Ensembl.
DR GO; GO:0071732; P:cellular response to nitric oxide; ISS:UniProtKB.
DR GO; GO:0097237; P:cellular response to toxic substance; IEA:Ensembl.
DR GO; GO:0021759; P:globus pallidus development; IEA:Ensembl.
DR GO; GO:0038060; P:nitric oxide-cGMP-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; IEA:Ensembl.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0051291; P:protein heterooligomerization; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0014075; P:response to amine; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0009642; P:response to light intensity; IEA:Ensembl.
DR GO; GO:0032026; P:response to magnesium ion; IEA:Ensembl.
DR GO; GO:1990089; P:response to nerve growth factor; IEA:Ensembl.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR Gene3D; 1.20.120.350; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR InterPro; IPR003974; K_chnl_volt-dep_Kv3.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR028325; VG_K_chnl.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01498; SHAWCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection;
KW Chromosomal rearrangement; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Phosphoprotein; Postsynaptic cell membrane; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Synapse;
KW Synaptosome; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..638
FT /note="Potassium voltage-gated channel subfamily C member
FT 2"
FT /id="PRO_0000310416"
FT TOPO_DOM 1..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
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..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
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..402
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..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 38..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..442
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT REGION 538..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..72
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 539..593
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044742"
FT VAR_SEQ 539..558
FT /note="VLSGDDSTGSEPPLSPPERL -> DNCKEVVITGYTQAEARSLT (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_029269"
FT VAR_SEQ 559..638
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_029270"
FT VAR_SEQ 594..638
FT /note="GYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIPSIL -> VLY
FT RIYHGLLTAEKGTVEFSHTKDYTGNRLLLLNVP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8111118"
FT /id="VSP_029271"
FT VAR_SEQ 594..638
FT /note="GYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIPSIL -> DNC
FT KEVVITGYTQAEARSLT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8111118"
FT /id="VSP_029272"
FT VAR_SEQ 595..638
FT /note="YEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIPSIL -> IRNG
FT HSILHHLDNGTKCHYLRIIF (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046002"
FT CONFLICT 31
FT /note="G -> V (in Ref. 3; AK309245)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="P -> S (in Ref. 4; BAE06076)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="F -> S (in Ref. 3; BAH11717)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="Q -> H (in Ref. 3; AK309245)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 638 AA; 70226 MW; 211CAF8395A58C5D CRC64;
MGKIENNERV ILNVGGTRHE TYRSTLKTLP GTRLALLASS EPPGDCLTTA GDKLQPSPPP
LSPPPRAPPL SPGPGGCFEG GAGNCSSRGG RASDHPGGGR EFFFDRHPGV FAYVLNYYRT
GKLHCPADVC GPLFEEELAF WGIDETDVEP CCWMTYRQHR DAEEALDIFE TPDLIGGDPG
DDEDLAAKRL GIEDAAGLGG PDGKSGRWRR LQPRMWALFE DPYSSRAARF IAFASLFFIL
VSITTFCLET HEAFNIVKNK TEPVINGTSV VLQYEIETDP ALTYVEGVCV VWFTFEFLVR
IVFSPNKLEF IKNLLNIIDF VAILPFYLEV GLSGLSSKAA KDVLGFLRVV RFVRILRIFK
LTRHFVGLRV LGHTLRASTN EFLLLIIFLA LGVLIFATMI YYAERVGAQP NDPSASEHTQ
FKNIPIGFWW AVVTMTTLGY GDMYPQTWSG MLVGALCALA GVLTIAMPVP VIVNNFGMYY
SLAMAKQKLP RKRKKHIPPA PQASSPTFCK TELNMACNST QSDTCLGKDN RLLEHNRSVL
SGDDSTGSEP PLSPPERLPI RRSSTRDKNR RGETCFLLTT GDYTCASDGG IRKGYEKSRS
LNNIAGLAGN ALRLSPVTSP YNSPCPLRRS RSPIPSIL
