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 174 (29 Sep 2021)
Sequence version 1 (01 Aug 1991)
Previous versions | rss
Add a publicationFeedback
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

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

DrugCentral

More...
DrugCentrali
P22462

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 or proteolytic cleavage.<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

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
P22462, 2 sites

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 brain and 15 other tissues

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 the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P22462

Database of comparative protein structure models

More...
ModBasei
Search...

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni47 – 75DisorderedSequence analysisAdd BLAST29
Regioni538 – 572DisorderedSequence analysisAdd BLAST35

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 type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi56 – 74Pro residuesSequence analysisAdd BLAST19

<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

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000157371

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_011722_4_3_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P22462

Identification of Orthologs from Complete Genome Data

More...
OMAi
IRHETYT

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 <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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

SMRiP22462
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi251521, 1 interactor
STRINGi10116.ENSRNOP00000005773

Chemistry databases

DrugCentraliP22462
GuidetoPHARMACOLOGYi549

PTM databases

GlyGeniP22462, 2 sites
PhosphoSitePlusiP22462

Proteomic databases

PaxDbiP22462

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...
ABCDi
P22462, 3 sequenced antibodies

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
GeneTreeiENSGT00940000157371
HOGENOMiCLU_011722_4_3_1
InParanoidiP22462
OMAiIRHETYT
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 brain and 15 other tissues
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

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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: September 29, 2021
This is version 174 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

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