Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 163 (08 May 2019)
Sequence version 1 (01 Aug 1991)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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 Publication6 Publications

      <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

      GO - Biological processi

      <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

      Molecular functionIon channel, Potassium channel, Voltage-gated channel
      Biological processIon transport, Potassium transport, Transport
      LigandPotassium

      Enzyme and pathway databases

      Reactome - a knowledgebase of biological pathways and processes

      More...
      Reactomei
      R-RNO-1296072 Voltage gated Potassium channels
      R-RNO-381676 Glucagon-like Peptide-1 (GLP1) regulates insulin secretion

      <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

      <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
      <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
      Name:Kcnc2Imported
      <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
      <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
      <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
      <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
      • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

      Organism-specific databases

      Rat genome database

      More...
      RGDi
      628829 Kcnc2

      <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

      Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

      Topology

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 229CytoplasmicSequence analysisAdd BLAST229
      <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei230 – 248Helical; Name=Segment S1Sequence analysisAdd BLAST19
      Transmembranei284 – 303Helical; Name=Segment S2Sequence analysisAdd BLAST20
      Topological domaini304 – 314CytoplasmicSequence analysisAdd BLAST11
      Transmembranei315 – 337Helical; Name=Segment S3Sequence analysisAdd BLAST23
      Transmembranei346 – 368Helical; Voltage-sensor; Name=Segment S4Sequence analysisAdd BLAST23
      Topological domaini369 – 381CytoplasmicSequence analysisAdd BLAST13
      Transmembranei382 – 401Helical; Name=Segment S5Sequence analysisAdd BLAST20
      Transmembranei451 – 473Helical; Name=Segment S6Sequence analysisAdd BLAST23
      Topological domaini474 – 638CytoplasmicSequence analysisAdd BLAST165

      Keywords - Cellular componenti

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

      <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

      Mutagenesis

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi563S → 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 Publications1
      Mutagenesisi564S → 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 Publications1

      Chemistry databases

      IUPHAR/BPS Guide to PHARMACOLOGY

      More...
      GuidetoPHARMACOLOGYi
      549

      <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

      Molecule processing

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000540541 – 638Potassium voltage-gated channel subfamily C member 2Add BLAST638

      Amino acid modifications

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi259N-linked (GlcNAc...) asparagineSequence analysis1
      Glycosylationi266N-linked (GlcNAc...) asparagineSequence analysis1
      <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei564Phosphoserine; by PKASequence analysis1
      Modified residuei600PhosphoserineBy similarity1

      <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

      PaxDb, a database of protein abundance averages across all three domains of life

      More...
      PaxDbi
      P22462

      PRoteomics IDEntifications database

      More...
      PRIDEi
      P22462

      PTM databases

      Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

      More...
      PhosphoSitePlusi
      P22462

      <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

      <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

      <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>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

      Bgee dataBase for Gene Expression Evolution

      More...
      Bgeei
      ENSRNOG00000004077 Expressed in 5 organ(s), highest expression level in brain

      Genevisible search portal to normalized and curated expression data from Genevestigator

      More...
      Genevisiblei
      P22462 RN

      <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

      <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

      GO - Molecular functioni

      Protein-protein interaction databases

      The Biological General Repository for Interaction Datasets (BioGrid)

      More...
      BioGridi
      251521, 1 interactor

      STRING: functional protein association networks

      More...
      STRINGi
      10116.ENSRNOP00000005773

      <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

      Motif

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi437 – 442Selectivity filterBy similarity6

      Compositional bias

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi56 – 99Gly/Pro-rich (insert)Add BLAST44

      <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

      <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

      Keywords - Domaini

      Transmembrane, Transmembrane helix

      Phylogenomic databases

      evolutionary genealogy of genes: Non-supervised Orthologous Groups

      More...
      eggNOGi
      KOG3713 Eukaryota
      COG1226 LUCA

      Ensembl GeneTree

      More...
      GeneTreei
      ENSGT00940000157371

      The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

      More...
      HOGENOMi
      HOG000231012

      InParanoid: Eukaryotic Ortholog Groups

      More...
      InParanoidi
      P22462

      KEGG Orthology (KO)

      More...
      KOi
      K04888

      Identification of Orthologs from Complete Genome Data

      More...
      OMAi
      YEGTLTW

      Database of Orthologous Groups

      More...
      OrthoDBi
      818306at2759

      Database for complete collections of gene phylogenies

      More...
      PhylomeDBi
      P22462

      TreeFam database of animal gene trees

      More...
      TreeFami
      TF352511

      Family and domain databases

      Gene3D Structural and Functional Annotation of Protein Families

      More...
      Gene3Di
      1.20.120.350, 1 hit

      Integrated resource of protein families, domains and functional sites

      More...
      InterProi
      View protein in InterPro
      IPR000210 BTB/POZ_dom
      IPR005821 Ion_trans_dom
      IPR003968 K_chnl_volt-dep_Kv
      IPR003974 K_chnl_volt-dep_Kv3
      IPR011333 SKP1/BTB/POZ_sf
      IPR003131 T1-type_BTB
      IPR028325 VG_K_chnl
      IPR027359 Volt_channel_dom_sf

      The PANTHER Classification System

      More...
      PANTHERi
      PTHR11537 PTHR11537, 1 hit

      Pfam protein domain database

      More...
      Pfami
      View protein in Pfam
      PF02214 BTB_2, 1 hit
      PF00520 Ion_trans, 1 hit

      Protein Motif fingerprint database; a protein domain database

      More...
      PRINTSi
      PR01491 KVCHANNEL
      PR01498 SHAWCHANNEL

      Simple Modular Architecture Research Tool; a protein domain database

      More...
      SMARTi
      View protein in SMART
      SM00225 BTB, 1 hit

      Superfamily database of structural and functional annotation

      More...
      SUPFAMi
      SSF54695 SSF54695, 1 hit

      <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4)i

      <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

      This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> 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
      <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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)DescriptionActionsGraphical viewLength
      <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti2G → S in CAA44643 (PubMed:1378392).Curated1

      Alternative sequence

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_001018594 – 638GYEKS…IPSIL → ASTLEPMESTSQTKGDTRPE AHWNCAHLLNFGCPTGSSFP TL in isoform 2. 1 PublicationAdd BLAST45
      Alternative sequenceiVSP_001019594 – 638GYEKS…IPSIL → DNCKDVVITGYTQAEARSLT in isoform 3. 1 PublicationAdd BLAST45
      Alternative sequenceiVSP_001020594 – 638GYEKS…IPSIL → VLYRIYHGFLPAENGTLRFS HSKDCTGNFCY in isoform 4. 1 PublicationAdd BLAST45

      Sequence databases

      Select the link destinations:

      EMBL nucleotide sequence database

      More...
      EMBLi

      GenBank nucleotide sequence database

      More...
      GenBanki

      DNA Data Bank of Japan; a nucleotide sequence database

      More...
      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

      Protein sequence database of the Protein Information Resource

      More...
      PIRi
      A39402
      B45292
      S22703

      NCBI Reference Sequences

      More...
      RefSeqi
      NP_631962.1, NM_139216.1 [P22462-3]
      NP_631963.1, NM_139217.1 [P22462-1]
      XP_006241389.1, XM_006241327.3 [P22462-1]
      XP_017450149.1, XM_017594660.1 [P22462-1]
      XP_017450150.1, XM_017594661.1 [P22462-2]
      XP_017450151.1, XM_017594662.1 [P22462-4]
      XP_017450152.1, XM_017594663.1 [P22462-3]

      Genome annotation databases

      Ensembl eukaryotic genome annotation project

      More...
      Ensembli
      ENSRNOT00000005690; ENSRNOP00000005690; ENSRNOG00000004077 [P22462-3]
      ENSRNOT00000005773; ENSRNOP00000005773; ENSRNOG00000004077 [P22462-1]

      Database of genes from NCBI RefSeq genomes

      More...
      GeneIDi
      246153

      KEGG: Kyoto Encyclopedia of Genes and Genomes

      More...
      KEGGi
      rno:246153

      UCSC genome browser

      More...
      UCSCi
      RGD:628829 rat [P22462-1]

      Keywords - Coding sequence diversityi

      Alternative splicing

      <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

      <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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_006241327.3 [P22462-1]
      XP_017450149.1, XM_017594660.1 [P22462-1]
      XP_017450150.1, XM_017594661.1 [P22462-2]
      XP_017450151.1, XM_017594662.1 [P22462-4]
      XP_017450152.1, XM_017594663.1 [P22462-3]

      3D structure databases

      Database of comparative protein structure models

      More...
      ModBasei
      Search...

      MobiDB: a database of protein disorder and mobility annotations

      More...
      MobiDBi
      Search...

      SWISS-MODEL Interactive Workspace

      More...
      SWISS-MODEL-Workspacei
      Submit a new modelling project...

      Protein-protein interaction databases

      BioGridi251521, 1 interactor
      STRINGi10116.ENSRNOP00000005773

      Chemistry databases

      GuidetoPHARMACOLOGYi549

      PTM databases

      PhosphoSitePlusiP22462

      Proteomic databases

      PaxDbiP22462
      PRIDEiP22462

      Protocols and materials databases

      Structural Biology KnowledgebaseSearch...

      Genome annotation databases

      EnsembliENSRNOT00000005690; ENSRNOP00000005690; ENSRNOG00000004077 [P22462-3]
      ENSRNOT00000005773; ENSRNOP00000005773; ENSRNOG00000004077 [P22462-1]
      GeneIDi246153
      KEGGirno:246153
      UCSCiRGD:628829 rat [P22462-1]

      Organism-specific databases

      Comparative Toxicogenomics Database

      More...
      CTDi
      3747
      RGDi628829 Kcnc2

      Phylogenomic databases

      eggNOGiKOG3713 Eukaryota
      COG1226 LUCA
      GeneTreeiENSGT00940000157371
      HOGENOMiHOG000231012
      InParanoidiP22462
      KOiK04888
      OMAiYEGTLTW
      OrthoDBi818306at2759
      PhylomeDBiP22462
      TreeFamiTF352511

      Enzyme and pathway databases

      ReactomeiR-RNO-1296072 Voltage gated Potassium channels
      R-RNO-381676 Glucagon-like Peptide-1 (GLP1) regulates insulin secretion

      Miscellaneous databases

      Protein Ontology

      More...
      PROi
      PR:P22462

      Gene expression databases

      BgeeiENSRNOG00000004077 Expressed in 5 organ(s), highest expression level in brain
      GenevisibleiP22462 RN

      Family and domain databases

      Gene3Di1.20.120.350, 1 hit
      InterProiView protein in InterPro
      IPR000210 BTB/POZ_dom
      IPR005821 Ion_trans_dom
      IPR003968 K_chnl_volt-dep_Kv
      IPR003974 K_chnl_volt-dep_Kv3
      IPR011333 SKP1/BTB/POZ_sf
      IPR003131 T1-type_BTB
      IPR028325 VG_K_chnl
      IPR027359 Volt_channel_dom_sf
      PANTHERiPTHR11537 PTHR11537, 1 hit
      PfamiView protein in Pfam
      PF02214 BTB_2, 1 hit
      PF00520 Ion_trans, 1 hit
      PRINTSiPR01491 KVCHANNEL
      PR01498 SHAWCHANNEL
      SMARTiView protein in SMART
      SM00225 BTB, 1 hit
      SUPFAMiSSF54695 SSF54695, 1 hit

      ProtoNet; Automatic hierarchical classification of proteins

      More...
      ProtoNeti
      Search...

      <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

      <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiKCNC2_RAT
      <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P22462
      Secondary accession number(s): P22461, P22463, Q63735
      <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
      Last sequence update: August 1, 1991
      Last modified: May 8, 2019
      This is version 163 of the entry and version 1 of the sequence. See complete history.
      <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
      Annotation programChordata Protein Annotation Program

      <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

      Keywords - Technical termi

      Complete proteome, Reference proteome

      Documents

      1. SIMILARITY comments
        Index of protein domains and families
      UniProt is an ELIXIR core data resource
      Main funding by: National Institutes of Health

      We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

      Do not show this banner again