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Protein

Potassium voltage-gated channel subfamily C member 2

Gene

Kcnc2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain. Contributes to the regulation of the fast action potential repolarization and in sustained high-frequency firing in neurons of the central nervous system (PubMed:10482766, PubMed:10414968, PubMed:11506885, PubMed:22831914). Homotetramer channels mediate delayed-rectifier voltage-dependent potassium currents that activate rapidly at high-threshold voltages and inactivate slowly (PubMed:2367536, PubMed:1879548, PubMed:8120636, PubMed:7643197, PubMed:10414303). Forms tetrameric channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:2367536, PubMed:1879548, PubMed:8120636, PubMed:7643197). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNC1, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (PubMed:10482766, PubMed:14679187). Channel properties may be modulated either by the association with ancillary subunits, such as KCNE1, KCNE2 and KCNE3 or indirectly by nitric oxide (NO) through a cGMP- and PKG-mediated signaling cascade, slowing channel activation and deactivation of delayed rectifier potassium channels (PubMed:11281123, PubMed:14679187). Contributes to fire sustained trains of very brief action potentials at high frequency in retinal ganglion cells, thalamocortical and suprachiasmatic nucleus (SCN) neurons and in hippocampal and neocortical interneurons (PubMed:10482766, PubMed:10414968, PubMed:11506885, PubMed:22831914). Sustained maximal action potential firing frequency in inhibitory hippocampal interneurons is negatively modulated by histamine H2 receptor activation in a cAMP- and protein kinase (PKA) phosphorylation-dependent manner. Plays a role in maintaining the fidelity of synaptic transmission in neocortical GABAergic interneurons by generating action potential (AP) repolarization at nerve terminals, thus reducing spike-evoked calcium influx and GABA neurotransmitter release. Required for long-range synchronization of gamma oscillations over distance in the neocortex. Contributes to the modulation of the circadian rhythm of spontaneous action potential firing in suprachiasmatic nucleus (SCN) neurons in a light-dependent manner (By similarity).By similarity2 Publications10 Publications

Enzyme regulationi

Inhibited by Stichodactyla helianthus peptide ShK (By similarity). Inhibited by millimolar levels of tetraethylammonium (TEA). Contrary to other channels, inhibited only by millimolar levels of 4-aminopyridine (4-AP) (PubMed:2367536, PubMed:1879548, PubMed:7643197, PubMed:10482766, PubMed:10414303).By similarity1 Publication4 Publications

Kineticsi

Homotetrameric channels expressed in xenopus oocytes or in mammalian non-neuronal cells display delayed-rectifier voltage-dependent potassium currents, that are rapidly activated during membrane depolarization, i.e within a risetime of a few msec. After that, inactivates very slowly, i.e within about >800 msec. Their activation requires a threshold potential at about -10 mV, with a midpoint activation at about 12.1 mV and a steepness parameter of about 8.4 mV (PubMed:2367536, PubMed:1879548, PubMed:8120636, PubMed:7643197, PubMed:10414303, PubMed:11281123, PubMed:14679187). The voltage-dependence of activation and inactivation and other channel characteristics vary depending on the experimental conditions, the expression system, the presence or absence of ancillary subunits and post-translational modifications (PubMed:7643197, PubMed:10414303, PubMed:11281123, PubMed:14679187).1 Publication

6 Publications

      GO - Molecular functioni

      • delayed rectifier potassium channel activity Source: UniProtKB
      • ion channel binding Source: UniProtKB
      • voltage-gated potassium channel activity Source: UniProtKB

      GO - Biological processi

      • action potential Source: Ensembl
      • cellular response to ammonium ion Source: RGD
      • cellular response to nitric oxide Source: UniProtKB
      • cellular response to toxic substance Source: RGD
      • globus pallidus development Source: RGD
      • ion transmembrane transport Source: RGD
      • nitric oxide-cGMP-mediated signaling pathway Source: UniProtKB
      • positive regulation of potassium ion transmembrane transport Source: RGD
      • potassium ion transmembrane transport Source: UniProtKB
      • protein heterooligomerization Source: UniProtKB
      • protein homooligomerization Source: UniProtKB
      • response to amine Source: RGD
      • response to ethanol Source: RGD
      • response to light intensity Source: RGD
      • response to magnesium ion Source: RGD
      • response to nerve growth factor Source: RGD
      • response to organic cyclic compound Source: RGD
      • response to toxic substance Source: RGD
      Complete GO annotation...

      Keywords - Molecular functioni

      Ion channel, Potassium channel, Voltage-gated channel

      Keywords - Biological processi

      Ion transport, Potassium transport, Transport

      Keywords - Ligandi

      Potassium

      Enzyme and pathway databases

      ReactomeiREACT_297045. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
      REACT_352543. Voltage gated Potassium channels.

      Names & Taxonomyi

      Protein namesi
      Recommended name:
      Potassium voltage-gated channel subfamily C member 2Imported
      Alternative name(s):
      Potassium channel voltage-gated Shaw-related subfamily C member 2Imported
      Shaw-like potassium channel1 Publication
      Voltage-gated potassium channel subunit Kv3.21 Publication
      Gene namesi
      Name:Kcnc2Imported
      OrganismiRattus norvegicus (Rat)
      Taxonomic identifieri10116 [NCBI]
      Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
      ProteomesiUP000002494 Componenti: Chromosome 7

      Organism-specific databases

      RGDi628829. Kcnc2.

      Subcellular locationi

      Isoform 1 :
      Isoform 2 :
      Isoform 3 :

      Topology

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Topological domaini1 – 229229CytoplasmicSequence AnalysisAdd
      BLAST
      Transmembranei230 – 24819Helical; Name=Segment S1Sequence AnalysisAdd
      BLAST
      Transmembranei284 – 30320Helical; Name=Segment S2Sequence AnalysisAdd
      BLAST
      Topological domaini304 – 31411CytoplasmicSequence AnalysisAdd
      BLAST
      Transmembranei315 – 33723Helical; Name=Segment S3Sequence AnalysisAdd
      BLAST
      Transmembranei346 – 36823Helical; Voltage-sensor; Name=Segment S4Sequence AnalysisAdd
      BLAST
      Topological domaini369 – 38113CytoplasmicSequence AnalysisAdd
      BLAST
      Transmembranei382 – 40120Helical; Name=Segment S5Sequence AnalysisAdd
      BLAST
      Transmembranei451 – 47323Helical; Name=Segment S6Sequence AnalysisAdd
      BLAST
      Topological domaini474 – 638165CytoplasmicSequence AnalysisAdd
      BLAST

      GO - Cellular componenti

      • apical plasma membrane Source: UniProtKB
      • axolemma Source: RGD
      • axon Source: UniProtKB
      • basolateral plasma membrane Source: RGD
      • dendrite Source: RGD
      • integral component of membrane Source: GO_Central
      • integral component of plasma membrane Source: UniProtKB
      • neuronal cell body Source: RGD
      • neuronal cell body membrane Source: UniProtKB
      • perikaryon Source: UniProtKB
      • plasma membrane Source: UniProtKB
      • postsynaptic membrane Source: UniProtKB
      • presynaptic membrane Source: UniProtKB
      • synapse Source: UniProtKB
      • terminal bouton Source: RGD
      • vesicle Source: RGD
      • voltage-gated potassium channel complex Source: UniProtKB
      Complete GO annotation...

      Keywords - Cellular componenti

      Cell junction, Cell membrane, Cell projection, Membrane, Postsynaptic cell membrane, Synapse, Synaptosome

      Pathology & Biotechi

      Mutagenesis

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Mutagenesisi563 – 5631S → A: Does not abolish channel activity inhibition in presence of nitric oxide (NO); when associated with A-564. Absence of channel activity inhibition in presence of cAMP; when associated with A-564. 2 Publications
      Mutagenesisi564 – 5641S → A: Does not abolish channel activity inhibition in presence of nitric oxide (NO); when associated with A-564. Absence of channel activity inhibition in presence of cAMP; when associated with A-563. 2 Publications

      PTM / Processingi

      Molecule processing

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Chaini1 – 638638Potassium voltage-gated channel subfamily C member 2PRO_0000054054Add
      BLAST

      Amino acid modifications

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Glycosylationi259 – 2591N-linked (GlcNAc...)Sequence Analysis
      Glycosylationi266 – 2661N-linked (GlcNAc...)Sequence Analysis
      Modified residuei564 – 5641Phosphoserine; by PKASequence Analysis

      Post-translational modificationi

      Phosphorylated by PKA in cortical synaptosomes (PubMed:7643197). cAMP-dependent phosphorylation inhibits channel activity (PubMed:7643197). Histamine H2 receptor- and PKA-induced phosphorylation extends action potential spike duration, reduces action potential spike amplitude, sustains maximum firing frequency in hippocampal interneurons; also reduces the incidence of high-frequency oscillations in hippocampal CA3 pyramidal cell layers (By similarity).By similarity1 Publication

      Keywords - PTMi

      Glycoprotein, Phosphoprotein

      Proteomic databases

      PaxDbiP22462.

      Expressioni

      Tissue specificityi

      Expressed in neurons of the visual cortex during postnatal development (PubMed:18708127). Expressed in neurons of the globus pallidus at postnatal age day 7 (P7), onward (PubMed:10482766). Expressed in thalamic relay neurons. Expressed in neurons in layer IV and deeper cortical layers of the neocortex. Expressed in hippocampal interneurons (PubMed:7643197). Expressed in nonpyramidal interneurons in the basolateral amygdala (PubMed:16413129). Expressed in retinal ganglion cells (at protein level) (PubMed:22831914). Widely expressed in the brain (PubMed:1879548, PubMed:8120636). Expressed in numerous thalamic relay neurons throughout the dorsal thalamus. Expressed in interneurons of the deep layers V-VI of the cerebral cortex, the CA1 and CA3 pyramidal and dentate gyrus (DG) granule cells of the hippocampus, in neurons of the caudate-putamen, globus pallidus and subthalamic nucleus. Also expressed in the optic layer of interior colliculus, the inferior colliculus, the red nucleus, the medial geniculate, the ventral lateral lemiscus, the reticulotegmental nucleus and in the deep cerebellar nuclei (PubMed:1374908, PubMed:8120636, PubMed:7643197, PubMed:18708127). Expressed in globus pallidus (GP) neurons (PubMed:10414968).9 Publications

      Inductioni

      Up-regulated in visual cortex during the second postnatal week from dark-reared animals (at protein level). Down-regulated in visual cortex by active visual experience until postnatal day P40 of dark-reared animals (PubMed:18708127). Down-regulated by chronic action potential activity deprivation in organotypic culture of the visual cortex (PubMed:18775767).2 Publications

      Gene expression databases

      GenevestigatoriP22462.

      Interactioni

      Subunit structurei

      Homotetramer and heterotetramer with other channel-forming alpha subunits, such as KCNC1. Interacts with KCNC1 (PubMed:10482766, PubMed:14679187). Homotetramer or heterotetramer channel activity is regulated by association with modulating ancillary subunits such as KCNE1, KCNE2 and KCNE3, creating a functionally diverse range of channel complexes. Interacts with KCNE1, KCNE2 and KCNE3 (PubMed:14679187).2 Publications

      Protein-protein interaction databases

      BioGridi251521. 1 interaction.

      Structurei

      3D structure databases

      ProteinModelPortaliP22462.
      SMRiP22462. Positions 101-160.
      ModBaseiSearch...
      MobiDBiSearch...

      Family & Domainsi

      Motif

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Motifi437 – 4426Selectivity filterBy similarity

      Compositional bias

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Compositional biasi56 – 9944Gly/Pro-rich (insert)Add
      BLAST

      Domaini

      The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region.By similarity

      Sequence similaritiesi

      Keywords - Domaini

      Transmembrane, Transmembrane helix

      Phylogenomic databases

      eggNOGiCOG1226.
      GeneTreeiENSGT00760000118846.
      HOGENOMiHOG000231012.
      HOVERGENiHBG105862.
      InParanoidiP22462.
      KOiK04888.
      OMAiMCLGKDN.
      OrthoDBiEOG7CRTPP.
      PhylomeDBiP22462.
      TreeFamiTF352511.

      Family and domain databases

      Gene3Di1.20.120.350. 1 hit.
      InterProiIPR000210. BTB/POZ-like.
      IPR011333. BTB/POZ_fold.
      IPR027359. Channel_four-helix_dom.
      IPR005821. Ion_trans_dom.
      IPR003091. K_chnl.
      IPR003968. K_chnl_volt-dep_Kv.
      IPR003974. K_chnl_volt-dep_Kv3.
      IPR003131. T1-type_BTB.
      IPR028325. VG_K_chnl.
      [Graphical view]
      PANTHERiPTHR11537. PTHR11537. 1 hit.
      PfamiPF02214. BTB_2. 1 hit.
      PF00520. Ion_trans. 1 hit.
      [Graphical view]
      PRINTSiPR00169. KCHANNEL.
      PR01491. KVCHANNEL.
      PR01498. SHAWCHANNEL.
      SMARTiSM00225. BTB. 1 hit.
      [Graphical view]
      SUPFAMiSSF54695. SSF54695. 2 hits.

      Sequences (4)i

      Sequence statusi: Complete.

      This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

      Isoform 1 (identifier: P22462-1) [UniParc]FASTAAdd to basket

      Also known as: KV3.2B1 Publication

      This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

      « Hide

              10         20         30         40         50
      MGKIENNERV ILNVGGTRHE TYRSTLKTLP GTRLALLASS EPQGDCLTAA
      60 70 80 90 100
      GDKLQPLPPP LSPPPRPPPL SPVPSGCFEG GAGNCSSHGG NGSDHPGGGR
      110 120 130 140 150
      EFFFDRHPGV FAYVLNYYRT GKLHCPADVC GPLFEEELAF WGIDETDVEP
      160 170 180 190 200
      CCWMTYRQHR DAEEALDIFE TPDLIGGDPG DDEDLGGKRL GIEDAAGLGG
      210 220 230 240 250
      PDGKSGRWRK LQPRMWALFE DPYSSRAARF IAFASLFFIL VSITTFCLET
      260 270 280 290 300
      HEAFNIVKNK TEPVINGTSA VLQYEIETDP ALTYVEGVCV VWFTFEFLVR
      310 320 330 340 350
      IVFSPNKLEF IKNLLNIIDF VAILPFYLEV GLSGLSSKAA KDVLGFLRVV
      360 370 380 390 400
      RFVRILRIFK LTRHFVGLRV LGHTLRASTN EFLLLIIFLA LGVLIFATMI
      410 420 430 440 450
      YYAERVGAQP NDPSASEHTQ FKNIPIGFWW AVVTMTTLGY GDMYPQTWSG
      460 470 480 490 500
      MLVGALCALA GVLTIAMPVP VIVNNFGMYY SLAMAKQKLP RKRKKHIPPA
      510 520 530 540 550
      PLASSPTFCK TELNMACNST QSDTCLGKEN RLLEHNRSVL SGDDSTGSEP
      560 570 580 590 600
      PLSPPERLPI RRSSTRDKNR RGETCFLLTT GDYTCASDGG IRKGYEKSRS
      610 620 630
      LNNIAGLAGN ALRLSPVTSP YNSPCPLRRS RSPIPSIL
      Length:638
      Mass (Da):70,191
      Last modified:August 1, 1991 - v1
      Checksum:i25C102B4CCE53BF4
      GO
      Isoform 2 (identifier: P22462-2) [UniParc]FASTAAdd to basket

      Also known as: KV3.2C1 Publication

      The sequence of this isoform differs from the canonical sequence as follows:
           594-638: GYEKSRSLNN...RSRSPIPSIL → ASTLEPMEST...CPTGSSFPTL

      Show »
      Length:635
      Mass (Da):69,887
      Checksum:i3F3D0386C5EC0C23
      GO
      Isoform 3 (identifier: P22462-3) [UniParc]FASTAAdd to basket

      Also known as: KV3.2A, KShIIIA.11 Publication

      The sequence of this isoform differs from the canonical sequence as follows:
           594-638: GYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIPSIL → DNCKDVVITGYTQAEARSLT

      Show »
      Length:613
      Mass (Da):67,551
      Checksum:iEA2E740D2E95F7E1
      GO
      Isoform 4 (identifier: P22462-4) [UniParc]FASTAAdd to basket

      The sequence of this isoform differs from the canonical sequence as follows:
           594-638: GYEKSRSLNN...RSRSPIPSIL → VLYRIYHGFLPAENGTLRFSHSKDCTGNFCY

      Show »
      Length:624
      Mass (Da):68,976
      Checksum:iA29A2E25DC33E99A
      GO

      Experimental Info

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Sequence conflicti2 – 21G → S in CAA44643 (PubMed:1378392).Curated

      Alternative sequence

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Alternative sequencei594 – 63845GYEKS…IPSIL → ASTLEPMESTSQTKGDTRPE AHWNCAHLLNFGCPTGSSFP TL in isoform 2. 1 PublicationVSP_001018Add
      BLAST
      Alternative sequencei594 – 63845GYEKS…IPSIL → DNCKDVVITGYTQAEARSLT in isoform 3. 1 PublicationVSP_001019Add
      BLAST
      Alternative sequencei594 – 63845GYEKS…IPSIL → VLYRIYHGFLPAENGTLRFS HSKDCTGNFCY in isoform 4. 1 PublicationVSP_001020Add
      BLAST

      Sequence databases

      Select the link destinations:
      EMBLi
      GenBanki
      DDBJi
      Links Updated
      M34052 mRNA. Translation: AAA42142.1.
      M59211 mRNA. Translation: AAA41819.1.
      M59313 mRNA. Translation: AAA41820.1. Sequence problems.
      X62839 mRNA. Translation: CAA44643.1.
      M84203 mRNA. Translation: AAA42143.1.
      PIRiA39402.
      B45292.
      S22703.
      RefSeqiNP_631962.1. NM_139216.1. [P22462-3]
      NP_631963.1. NM_139217.1. [P22462-1]
      XP_006241389.1. XM_006241327.2. [P22462-1]
      UniGeneiRn.9733.

      Genome annotation databases

      EnsembliENSRNOT00000005690; ENSRNOP00000005690; ENSRNOG00000004077. [P22462-3]
      ENSRNOT00000005700; ENSRNOP00000005700; ENSRNOG00000004077. [P22462-4]
      ENSRNOT00000005773; ENSRNOP00000005773; ENSRNOG00000004077. [P22462-1]
      ENSRNOT00000049943; ENSRNOP00000049641; ENSRNOG00000004077. [P22462-2]
      GeneIDi246153.
      KEGGirno:246153.
      UCSCiRGD:628829. rat. [P22462-1]

      Keywords - Coding sequence diversityi

      Alternative splicing

      Cross-referencesi

      Sequence databases

      Select the link destinations:
      EMBLi
      GenBanki
      DDBJi
      Links Updated
      M34052 mRNA. Translation: AAA42142.1.
      M59211 mRNA. Translation: AAA41819.1.
      M59313 mRNA. Translation: AAA41820.1. Sequence problems.
      X62839 mRNA. Translation: CAA44643.1.
      M84203 mRNA. Translation: AAA42143.1.
      PIRiA39402.
      B45292.
      S22703.
      RefSeqiNP_631962.1. NM_139216.1. [P22462-3]
      NP_631963.1. NM_139217.1. [P22462-1]
      XP_006241389.1. XM_006241327.2. [P22462-1]
      UniGeneiRn.9733.

      3D structure databases

      ProteinModelPortaliP22462.
      SMRiP22462. Positions 101-160.
      ModBaseiSearch...
      MobiDBiSearch...

      Protein-protein interaction databases

      BioGridi251521. 1 interaction.

      Chemistry

      GuidetoPHARMACOLOGYi549.

      Proteomic databases

      PaxDbiP22462.

      Protocols and materials databases

      Structural Biology KnowledgebaseSearch...

      Genome annotation databases

      EnsembliENSRNOT00000005690; ENSRNOP00000005690; ENSRNOG00000004077. [P22462-3]
      ENSRNOT00000005700; ENSRNOP00000005700; ENSRNOG00000004077. [P22462-4]
      ENSRNOT00000005773; ENSRNOP00000005773; ENSRNOG00000004077. [P22462-1]
      ENSRNOT00000049943; ENSRNOP00000049641; ENSRNOG00000004077. [P22462-2]
      GeneIDi246153.
      KEGGirno:246153.
      UCSCiRGD:628829. rat. [P22462-1]

      Organism-specific databases

      CTDi3747.
      RGDi628829. Kcnc2.

      Phylogenomic databases

      eggNOGiCOG1226.
      GeneTreeiENSGT00760000118846.
      HOGENOMiHOG000231012.
      HOVERGENiHBG105862.
      InParanoidiP22462.
      KOiK04888.
      OMAiMCLGKDN.
      OrthoDBiEOG7CRTPP.
      PhylomeDBiP22462.
      TreeFamiTF352511.

      Enzyme and pathway databases

      ReactomeiREACT_297045. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
      REACT_352543. Voltage gated Potassium channels.

      Miscellaneous databases

      NextBioi623450.
      PROiP22462.

      Gene expression databases

      GenevestigatoriP22462.

      Family and domain databases

      Gene3Di1.20.120.350. 1 hit.
      InterProiIPR000210. BTB/POZ-like.
      IPR011333. BTB/POZ_fold.
      IPR027359. Channel_four-helix_dom.
      IPR005821. Ion_trans_dom.
      IPR003091. K_chnl.
      IPR003968. K_chnl_volt-dep_Kv.
      IPR003974. K_chnl_volt-dep_Kv3.
      IPR003131. T1-type_BTB.
      IPR028325. VG_K_chnl.
      [Graphical view]
      PANTHERiPTHR11537. PTHR11537. 1 hit.
      PfamiPF02214. BTB_2. 1 hit.
      PF00520. Ion_trans. 1 hit.
      [Graphical view]
      PRINTSiPR00169. KCHANNEL.
      PR01491. KVCHANNEL.
      PR01498. SHAWCHANNEL.
      SMARTiSM00225. BTB. 1 hit.
      [Graphical view]
      SUPFAMiSSF54695. SSF54695. 2 hits.
      ProtoNetiSearch...

      Publicationsi

      1. "Molecular cloning of a member of a third class of Shaker-family K+ channel genes in mammals."
        McCormack T., de Miera E.C.V.-S., Rudy B.
        Proc. Natl. Acad. Sci. U.S.A. 87:5227-5231(1990) [PubMed] [Europe PMC] [Abstract]
        Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR LOCATION.
        Tissue: Brain.
      2. "Molecular cloning of a member of a third class of Shaker-family K+ channel genes in mammals."
        McCormack T., de Miera E.C.V.-S., Rudy B.
        Proc. Natl. Acad. Sci. U.S.A. 88:4060-4060(1991) [PubMed] [Europe PMC] [Abstract]
        Cited for: SEQUENCE REVISION.
      3. "Shaw-like rat brain potassium channel cDNA's with divergent 3' ends."
        Luneau C.J., Wiedmann R., Smith J.S., Williams J.B.
        FEBS Lett. 288:163-167(1991) [PubMed] [Europe PMC] [Abstract]
        Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
        Tissue: Brain.
      4. "Characterization of a Shaw-related potassium channel family in rat brain."
        Rettig J., Wunder F., Stocker M., Lichtinghagen R., Mastiaux F., Beckh S., Kues W., Pedarzani P., Schroeter K.H., Ruppersberg J.P., Veh R., Pongs O.
        EMBO J. 11:2473-2486(1992) [PubMed] [Europe PMC] [Abstract]
        Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
      5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      6. "Differential expression of Shaw-related K+ channels in the rat central nervous system."
        Weiser M., Vega-Saenz de Miera E., Kentros C., Moreno H., Franzen L., Hillman D., Baker H., Rudy B.
        J. Neurosci. 14:949-972(1994) [PubMed] [Europe PMC] [Abstract]
        Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      7. "Thalamocortical projections have a K+ channel that is phosphorylated and modulated by cAMP-dependent protein kinase."
        Moreno H., Kentros C., Bueno E., Weiser M., Hernandez A., Vega-Saenz de Miera E., Ponce A., Thornhill W., Rudy B.
        J. Neurosci. 15:5486-5501(1995) [PubMed] [Europe PMC] [Abstract]
        Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, PHOSPHORYLATION, MUTAGENESIS OF SER-563 AND SER-564, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      8. "K+ channel subunit isoforms with divergent carboxy-terminal sequences carry distinct membrane targeting signals."
        Ponce A., Vega-Saenz de Miera E., Kentros C., Moreno H., Thornhill B., Rudy B.
        J. Membr. Biol. 159:149-159(1997) [PubMed] [Europe PMC] [Abstract]
        Cited for: SUBCELLULAR LOCATION (ISOFORMS 1; 2 AND 3).
      9. "Kv3.1-Kv3.2 channels underlie a high-voltage-activating component of the delayed rectifier K+ current in projecting neurons from the globus pallidus."
        Hernandez-Pineda R., Chow A., Amarillo Y., Moreno H., Saganich M., Vega-Saenz de Miera E.C., Hernandez-Cruz A., Rudy B.
        J. Neurophysiol. 82:1512-1528(1999) [PubMed] [Europe PMC] [Abstract]
        Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT, INTERACTION WITH KCNC1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      10. "Delayed rectifier currents in rat globus pallidus neurons are attributable to Kv2.1 and Kv3.1/3.2 K(+) channels."
        Baranauskas G., Tkatch T., Surmeier D.J.
        J. Neurosci. 19:6394-6404(1999) [PubMed] [Europe PMC] [Abstract]
        Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      11. Cited for: REVIEW.
      12. "Kv3 channels: voltage-gated K+ channels designed for high-frequency repetitive firing."
        Rudy B., McBain C.J.
        Trends Neurosci. 24:517-526(2001) [PubMed] [Europe PMC] [Abstract]
        Cited for: REVIEW.
      13. "Modulation of Kv3 potassium channels expressed in CHO cells by a nitric oxide-activated phosphatase."
        Moreno H., Vega-Saenz de Miera E., Nadal M.S., Amarillo Y., Rudy B.
        J. Physiol. (Lond.) 530:345-358(2001) [PubMed] [Europe PMC] [Abstract]
        Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-563 AND SER-564.
      14. "MinK, MiRP1, and MiRP2 diversify Kv3.1 and Kv3.2 potassium channel gating."
        Lewis A., McCrossan Z.A., Abbott G.W.
        J. Biol. Chem. 279:7884-7892(2004) [PubMed] [Europe PMC] [Abstract]
        Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INTERACTION WITH KCNC1; KCNE1; KCNE2 AND KCNE3, SUBCELLULAR LOCATION.
      15. "Differential expression of Kv3.1b and Kv3.2 potassium channel subunits in interneurons of the basolateral amygdala."
        McDonald A.J., Mascagni F.
        Neuroscience 138:537-547(2006) [PubMed] [Europe PMC] [Abstract]
        Cited for: TISSUE SPECIFICITY.
      16. "Neuronal activity and TrkB ligands influence Kv3.1b and Kv3.2 expression in developing cortical interneurons."
        Grabert J., Wahle P.
        Neuroscience 156:618-629(2008) [PubMed] [Europe PMC] [Abstract]
        Cited for: INDUCTION.
      17. "Visual experience regulates Kv3.1b and Kv3.2 expression in developing rat visual cortex."
        Grabert J., Wahle P.
        Neuroscience 158:654-664(2009) [PubMed] [Europe PMC] [Abstract]
        Cited for: TISSUE SPECIFICITY, INDUCTION.
      18. "Kv3 channels modulate calcium signals induced by fast firing patterns in the rat retinal ganglion cells."
        Kuznetsov K.I., Grygorov O.O., Maslov V.Y., Veselovsky N.S., Fedulova S.A.
        Cell Calcium 52:405-411(2012) [PubMed] [Europe PMC] [Abstract]
        Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

      Entry informationi

      Entry nameiKCNC2_RAT
      AccessioniPrimary (citable) accession number: P22462
      Secondary accession number(s): P22461, P22463, Q63735
      Entry historyi
      Integrated into UniProtKB/Swiss-Prot: August 1, 1991
      Last sequence update: August 1, 1991
      Last modified: May 27, 2015
      This is version 135 of the entry and version 1 of the sequence. [Complete history]
      Entry statusiReviewed (UniProtKB/Swiss-Prot)
      Annotation programChordata Protein Annotation Program

      Miscellaneousi

      Keywords - Technical termi

      Complete proteome, Reference proteome

      Documents

      1. SIMILARITY comments
        Index of protein domains and families

      External Data

      Dasty 3

      Similar proteinsi

      Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
      100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
      90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
      50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.