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Protein

Potassium voltage-gated channel subfamily A member 1

Gene

Kcna1

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 and the central nervous system, but also in the kidney. Contributes to the regulation of the membrane potential and nerve signaling, and prevents neuronal hyperexcitability (PubMed:12177193, PubMed:17855588, PubMed:22206926). Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient (PubMed:23725331). The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:2539643). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNA7, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (PubMed:2348860, PubMed:12177193, PubMed:10896669, PubMed:23725331). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation of delayed rectifier potassium channels (PubMed:10896669, PubMed:12114518). In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Homotetrameric KCNA1 forms a delayed-rectifier potassium channel that opens in response to membrane depolarization, followed by slow spontaneous channel closure (PubMed:2348860, PubMed:8038169, PubMed:12681381, PubMed:22206926, PubMed:23725331). In contrast, a heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid inactivation (PubMed:2348860). Regulates neuronal excitability in hippocampus, especially in mossy fibers and medial perforant path axons, preventing neuronal hyperexcitability. Response to toxins that are selective for KCNA1, respectively for KCNA2, suggests that heteromeric potassium channels composed of both KCNA1 and KCNA2 play a role in pacemaking and regulate the output of deep cerebellar nuclear neurons (PubMed:12177193, PubMed:23318870). May function as down-stream effector for G protein-coupled receptors and inhibit GABAergic inputs to basolateral amygdala neurons (PubMed:16306173). May contribute to the regulation of neurotransmitter release, such as gamma-aminobutyric acid (GABA) release (PubMed:17869444). Plays a role in regulating the generation of action potentials and preventing hyperexcitability in myelinated axons of the vagus nerve, and thereby contributes to the regulation of heart contraction (By similarity). Required for normal neuromuscular responses (PubMed:22206926). Regulates the frequency of neuronal action potential firing in response to mechanical stimuli, and plays a role in the perception of pain caused by mechanical stimuli, but does not play a role in the perception of pain due to heat stimuli (By similarity). Required for normal responses to auditory stimuli and precise location of sound sources, but not for sound perception (By similarity). The use of toxins that block specific channels suggest that it contributes to the regulation of the axonal release of the neurotransmitter dopamine (By similarity). Required for normal postnatal brain development and normal proliferation of neuronal precursor cells in the brain (By similarity). Plays a role in the reabsorption of Mg2+ in the distal convoluted tubules in the kidney and in magnesium ion homeostasis, probably via its effect on the membrane potential (By similarity).By similarity1 Publication12 Publications

Miscellaneous

A missense mutation at Ser-309 is the cause of the autosomal dominant myokymia and seizures (ADMS) phenotype. Homozygous and heterozygous rats are born at the expected Mendelian rate. After 6 weeks, heterozygous rats begin to display muscle twitching, startle responses and spontaneous convulsive seizures; over 80% of the animals are dead after 30 weeks. After 16 weeks, they display lower body weight compared to wild-type. The rats exhibit severe periodic seizures with characteristic alterations in their cortical and hippocampal electroencephalogram, similar to rodent models of temporal lobe epilepsy. Homozygous rats display impaired development starting 14 days after birth, with reduced body weight, tremors, motor incoordination, spontaneous convulsive seizures; none survive past 18 days after birth.1 Publication
The delay or D-type current observed in hippocampus pyramidal neurons is probably mediated by potassium channels containing KCNA2 plus KCNA1 or other family members. It is activated at about -50 mV, i.e. below the action potential threshold, and is characterized by slow inactivation, extremely slow recovery from inactivation, sensitivity to dendrotoxin (DTX) and to 4-aminopyridine (4-AP).1 Publication

<p>This subsection of the ‘Function’ 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 4-aminopyridine (4-AP) and by tetraethylammonium (TEA) (PubMed:2539643). Inhibited by kaliotoxin (KTX) (PubMed:23725331).3 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

<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 A member 1
Alternative name(s):
RBKI1 Publication
RCK12 Publications
Voltage-gated potassium channel subunit Kv1.1
<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:Kcna1
<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 4

Organism-specific databases

Rat genome database

More...
RGDi
2949 Kcna1

<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; 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 – 164CytoplasmicBy similarityAdd BLAST164
<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>Transmembranei165 – 186Helical; Name=Segment S1By similarityAdd BLAST22
Topological domaini187 – 220ExtracellularBy similarityAdd BLAST34
Transmembranei221 – 242Helical; Name=Segment S2By similarityAdd BLAST22
Topological domaini243 – 253CytoplasmicBy similarityAdd BLAST11
Transmembranei254 – 274Helical; Name=Segment S3By similarityAdd BLAST21
Topological domaini275 – 287ExtracellularBy similarityAdd BLAST13
Transmembranei288 – 308Helical; Voltage-sensor; Name=Segment S4By similarityAdd BLAST21
Topological domaini309 – 323CytoplasmicBy similarityAdd BLAST15
Transmembranei324 – 345Helical; Name=Segment S5By similarityAdd BLAST22
Topological domaini346 – 359ExtracellularBy similarityAdd BLAST14
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei360 – 371Helical; Name=Pore helixBy similarityAdd BLAST12
Intramembranei372 – 379By similarity8
Topological domaini380 – 386ExtracellularBy similarity7
Transmembranei387 – 415Helical; Name=Segment S6By similarityAdd BLAST29
Topological domaini416 – 495CytoplasmicBy similarityAdd BLAST80

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasmic vesicle, Endoplasmic reticulum, Membrane, Synapse

<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>Mutagenesisi309S → T in ADMS: Dominant negative mutation that abolishes channel activity; leads to myokymia, neuromyotonia, spontaneous epileptic seizures and premature death. 1 Publication1
Mutagenesisi352A → R: Is not blocked by the scorpion mesomartoxin. 1 Publication1
Mutagenesisi355H → Q: Is not blocked by the scorpion mesomartoxin. 1 Publication1
Mutagenesisi357S → P: Is not blocked by the scorpion mesomartoxin. 1 Publication1
Mutagenesisi379Y → V: Is blocked by the scorpion mesomartoxin, with an IC(50)=16.60 nM. 1 Publication1
Mutagenesisi381V → T: Is not blocked by the scorpion mesomartoxin. 1 Publication1
Mutagenesisi443R → C: Abolishes phosphorylation by PKA; when associated with A-446. 1
Mutagenesisi446S → A: Abolishes phosphorylation by PKA; when associated with C-443. 1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5190

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
538

<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_00000539701 – 495Potassium voltage-gated channel subfamily A member 1Add BLAST495

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei23PhosphoserineCombined sources1
<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>Glycosylationi207N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi243S-palmitoyl cysteineBy similarity1
Modified residuei322Phosphoserine; by PKASequence analysis1
Modified residuei437PhosphoserineCombined sources1
Modified residuei439PhosphoserineCombined sources1
Modified residuei446Phosphoserine; by PKA1 Publication1

<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

Palmitoylated on Cys-243; which may be required for membrane targeting.By similarity
N-glycosylated.2 Publications
Phosphorylated on tyrosine residues. Phosphorylation increases in response to NRG1; this inhibits channel activity (By similarity). Phosphorylated by PKA (PubMed:8038169, PubMed:12681381). Phosphorylation at Ser-446 regulates channel activity by down-regulating expression at the cell membrane (By similarity).By similarity2 Publications

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

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

More...
PaxDbi
P10499

PRoteomics IDEntifications database

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PRIDEi
P10499

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P10499

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

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PhosphoSitePlusi
P10499

<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

Detected in hippocampus, in the middle third of the molecular layer of the dentate gyrus and in stratum radiatum and stratum oriens (PubMed:9334400). Detected in the mossy fiber zone in the hippocampus CA3 region, at or near axon terminals (PubMed:9334400). Detected in brain cortex, at basket cell terminals (PubMed:9334400). Detected adjacent to nodes of Ranvier in juxtaparanodal zones in spinal cord nerve fibers, but also in paranodal regions in some myelinated spinal cord axons (PubMed:11086297). Detected in juxtaparanodal regions adjacent to the nodes of Ranvier in myelinated axons in cerebellar white matter (PubMed:9334400). Detected in sensory neurons (PubMed:17855588). Detected in neurons from the medial nucleus of the trapezoid body (PubMed:12177193). Detected in basolateral amygdala (PubMed:16306173). Detected in the paraventricular nucleus of the hypothalamus (PubMed:17869444). Detected in the islet of Langerhans (at protein level) (PubMed:21483673). Detected in the islet of Langerhans (PubMed:21483673).6 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSRNOG00000019750 Expressed in 3 organ(s), highest expression level in brain

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P10499 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 KCNA2, KCNA4, KCNA5, KCNA6 and KCNA7 (PubMed:10896669, PubMed:10884227). Channel activity is regulated by interaction with the beta subunits KCNAB1 and KCNAB2 (PubMed:9334400, PubMed:12114518). Identified in a complex with KCNA2 and KCNAB2 (PubMed:10896669, PubMed:11086297, PubMed:23318870, PubMed:10884227). Interacts (via C-terminus) with the PDZ domains of DLG1, DLG2 and DLG4. Interacts with LGI1 within a complex containing LGI1, KCNA4 and KCNAB1. Interacts (via cytoplasmic N-terminal domain) with KCNRG; this inhibits channel activity (By similarity). Interacts with ANK3; this inhibits channel activity (By similarity). Interacts (via N-terminus) with STX1A; this promotes channel inactivation (PubMed:12114518). Interacts (via N-terminus) with the heterodimer formed by GNB1 and GNG2; this promotes channel inactivation (PubMed:12114518). Can interact simultaneously with STX1A and the heterodimer formed by GNB1 and GNG2 (PubMed:12114518).By similarity8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
DLG4P783522EBI-631463,EBI-80389From Homo sapiens.

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
246675, 3 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P10499

Protein interaction database and analysis system

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IntActi
P10499, 2 interactors

Molecular INTeraction database

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MINTi
P10499

STRING: functional protein association networks

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STRINGi
10116.ENSRNOP00000026731

<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

Secondary structure

1495
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P10499

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

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SMRi
P10499

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P10499

<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>Regioni1 – 128Tetramerization domainCuratedAdd BLAST128
Regioni310 – 323S4-S5 linkerBy similarityAdd BLAST14

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>Motifi372 – 377Selectivity filterBy similarity6
Motifi493 – 495PDZ-bindingCurated3

<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 cytoplasmic N-terminus is important for tetramerization and for interaction with the beta subunits that promote rapid channel closure.1 Publication
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

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eggNOGi
KOG1545 Eukaryota
COG1226 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000158576

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000231015

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG052230

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P10499

KEGG Orthology (KO)

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KOi
K04874

Identification of Orthologs from Complete Genome Data

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OMAi
IHRIDNT

Database of Orthologous Groups

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OrthoDBi
EOG091G10NU

Database for complete collections of gene phylogenies

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PhylomeDBi
P10499

TreeFam database of animal gene trees

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TreeFami
TF313103

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.20.120.350, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR000210 BTB/POZ_dom
IPR005821 Ion_trans_dom
IPR003968 K_chnl_volt-dep_Kv
IPR003972 K_chnl_volt-dep_Kv1
IPR004048 K_chnl_volt-dep_Kv1.1
IPR011333 SKP1/BTB/POZ_sf
IPR003131 T1-type_BTB
IPR028325 VG_K_chnl
IPR027359 Volt_channel_dom_sf

The PANTHER Classification System

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PANTHERi
PTHR11537 PTHR11537, 1 hit

Pfam protein domain database

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

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00169 KCHANNEL
PR01508 KV11CHANNEL
PR01491 KVCHANNEL
PR01496 SHAKERCHANEL

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00225 BTB, 1 hit

Superfamily database of structural and functional annotation

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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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<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.

P10499-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTVMSGENAD EASAAPGHPQ DGSYPRQADH DDHECCERVV INISGLRFET
60 70 80 90 100
QLKTLAQFPN TLLGNPKKRM RYFDPLRNEY FFDRNRPSFD AILYYYQSGG
110 120 130 140 150
RLRRPVNVPL DMFSEEIKFY ELGEEAMEKF REDEGFIKEE ERPLPEKEYQ
160 170 180 190 200
RQVWLLFEYP ESSGPARVIA IVSVMVILIS IVIFCLETLP ELKDDKDFTG
210 220 230 240 250
TIHRIDNTTV IYTSNIFTDP FFIVETLCII WFSFELVVRF FACPSKTDFF
260 270 280 290 300
KNIMNFIDIV AIIPYFITLG TEIAEQEGNQ KGEQATSLAI LRVIRLVRVF
310 320 330 340 350
RIFKLSRHSK GLQILGQTLK ASMRELGLLI FFLFIGVILF SSAVYFAEAE
360 370 380 390 400
EAESHFSSIP DAFWWAVVSM TTVGYGDMYP VTIGGKIVGS LCAIAGVLTI
410 420 430 440 450
ALPVPVIVSN FNYFYHRETE GEEQAQLLHV SSPNLASDSD LSRRSSSTIS
460 470 480 490
KSEYMEIEED MNNSIAHYRQ ANIRTGNCTA TDQNCVNKSK LLTDV
Length:495
Mass (Da):56,379
Last modified:April 1, 1990 - 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:i29804463133F5D31
GO

<p>This subsection of the ‘Sequence’ section provides information relevant to all types of RNA editing events (conversion, insertion, deletion of nucleotides) that lead to one or more amino acid changes compared to the translation of the non-edited RNA version.<p><a href='/help/rna_editing' target='_top'>More...</a></p>RNA editingi

Edited at position 400.1 Publication
Partially edited. RNA editing is at an average of 50% in the whole brain.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti400I → V in RNA edited version. 1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X12589 mRNA Translation: CAA31102.1
M26161 mRNA Translation: AAA41982.1

Protein sequence database of the Protein Information Resource

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PIRi
B39113

NCBI Reference Sequences

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RefSeqi
NP_775118.1, NM_173095.3

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Rn.9769

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000026731; ENSRNOP00000026731; ENSRNOG00000019750

Database of genes from NCBI RefSeq genomes

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GeneIDi
24520

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:24520

UCSC genome browser

More...
UCSCi
RGD:2949 rat

Keywords - Coding sequence diversityi

RNA editing

<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
X12589 mRNA Translation: CAA31102.1
M26161 mRNA Translation: AAA41982.1
PIRiB39113
RefSeqiNP_775118.1, NM_173095.3
UniGeneiRn.9769

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EXBX-ray2.10E27-129[»]
ProteinModelPortaliP10499
SMRiP10499
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246675, 3 interactors
CORUMiP10499
IntActiP10499, 2 interactors
MINTiP10499
STRINGi10116.ENSRNOP00000026731

Chemistry databases

ChEMBLiCHEMBL5190
GuidetoPHARMACOLOGYi538

PTM databases

iPTMnetiP10499
PhosphoSitePlusiP10499

Proteomic databases

PaxDbiP10499
PRIDEiP10499

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026731; ENSRNOP00000026731; ENSRNOG00000019750
GeneIDi24520
KEGGirno:24520
UCSCiRGD:2949 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3736
RGDi2949 Kcna1

Phylogenomic databases

eggNOGiKOG1545 Eukaryota
COG1226 LUCA
GeneTreeiENSGT00940000158576
HOGENOMiHOG000231015
HOVERGENiHBG052230
InParanoidiP10499
KOiK04874
OMAiIHRIDNT
OrthoDBiEOG091G10NU
PhylomeDBiP10499
TreeFamiTF313103

Enzyme and pathway databases

ReactomeiR-RNO-1296072 Voltage gated Potassium channels

Miscellaneous databases

EvolutionaryTraceiP10499

Protein Ontology

More...
PROi
PR:P10499

Gene expression databases

BgeeiENSRNOG00000019750 Expressed in 3 organ(s), highest expression level in brain
GenevisibleiP10499 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
IPR003972 K_chnl_volt-dep_Kv1
IPR004048 K_chnl_volt-dep_Kv1.1
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
PRINTSiPR00169 KCHANNEL
PR01508 KV11CHANNEL
PR01491 KVCHANNEL
PR01496 SHAKERCHANEL
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 nameiKCNA1_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: P10499
<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: April 1, 1990
Last sequence update: April 1, 1990
Last modified: December 5, 2018
This is version 168 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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