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UniProtKB - P16388 (KCNA1_MOUSE)

Entry version 176 (12 Aug 2020)
Sequence version 1 (01 Aug 1990)
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Protein

Potassium voltage-gated channel subfamily A member 1

Gene

Kcna1

Organism
Mus musculus (Mouse)
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:9736643, PubMed:9581771 PubMed:10191303, PubMed:12611922, PubMed:21966978, PubMed:22158511, PubMed:23473320). Forms tetrameric potassium-selective 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:15361858). 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. 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:15361858). 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:7517498, PubMed:15361858). In contrast, a heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid inactivation (By similarity). Regulates neuronal excitability in hippocampus, especially in mossy fibers and medial perforant path axons, preventing neuronal hyperexcitability (PubMed:23466697). May function as down-stream effector for G protein-coupled receptors and inhibit GABAergic inputs to basolateral amygdala neurons (By similarity). May contribute to the regulation of neurotransmitter release, such as gamma-aminobutyric acid (GABA) release (By similarity). 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 (PubMed:20392939, PubMed:22641786, PubMed:25377007). Required for normal neuromuscular responses (PubMed:9736643). 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 (PubMed:23473320). Required for normal responses to auditory stimuli and precise location of sound sources, but not for sound perception (PubMed:21966978, PubMed:22396426). The use of toxins that block specific channels suggest that it contributes to the regulation of the axonal release of the neurotransmitter dopamine (PubMed:21233214). Required for normal postnatal brain development and normal proliferation of neuronal precursor cells in the brain (PubMed:8995755, PubMed:17250763, PubMed:17315199, PubMed:22411008). 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 similarity19 Publications

Miscellaneous

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 <a href="http://www.uniprot.org/help/function%5Fsection">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 4-aminopyridine (4-AP), tetraethylammonium (TEA) and dendrotoxin (DTX), but not by charybdotoxin (CTX).1 Publication

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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-MMU-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%5Fand%5Ftaxonomy%5Fsection">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):
MBK11 Publication
MKI
Voltage-gated potassium channel subunit Kv1.1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 6

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:96654, 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 & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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%5Flocation%5Fsection">'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%5Flocation%5Fsection">'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

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

A spontaneous mutation leading to a frameshift and truncation of Kcna2 causes megencephaly with a 25% increase of brain weight relative to wild-type. Especially the hippocampus shows increased proliferation of neurons and astrocytes, leading to increased brain volume (PubMed:17315199). Mutant mice appear normal at birth. After 3-4 weeks, they display low body weight, a subtle shakiness in their gait, a preference for a strange sitting position that is maintained for periods ranging from 30 seconds to several minutes, excessive lacrimation and acoustic startle hypersensitivity (PubMed:8995755, PubMed:21966978). The increase in the acoustic startle response is down-regulated by treatment with the anti-epileptic drug valproate (PubMed:21966978). Mutant mice display an abnormal electro-encephalogram with single spikes and waves, when anesthesized (PubMed:21966978). The electric activity of mossy cells from the dentate hilus region is altered and shows increased firing of action potentials, probably due to the absence of functional Kcna1 channels (PubMed:14686897). Heterozygotes show mechanical allodynia, but no increased sensitivity to heat (PubMed:23473320). Homozygotes show no alteration of the islet of Langerhans structure, of the basal levels of insulin secretion and blood glucose levels (PubMed:21483673). Compared to wild-type, they display moderately increased insulin secretion in response to a glucose stimulus (PubMed:21483673). Besides, the frequency of beta cell action potentials is increased (PubMed:21483673).5 Publications

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mice are born at the expected Mendelian rate. After three weeks, mice begin to display episodic eye blinking, twitching of whiskers, forlimb padding, arrested motion and a hyperstartle response. About 50% of the homozygotes die between the third and the fifth week after birth. Surviving mice continue to display spontaneous seizures occurring once or twice every hour throughout adult life (PubMed:9581771). The fecundity of homozygotes is extremely low (PubMed:9581771). Mutant mice display interictal cardiac abnormalities, including a fivefold increase in atrioventricular conduction blocks, brachycardia and premature ventricular contractions; this may lead to sudden unexplained death in epilepsy (PubMed:20392939). Mutant mice have slightly elevated heart rates; they all have a reduced livespan and are subject to sudden death after presumed seizure activity and sinus bradycardia (PubMed:25377007). About 70% of the mutant mice have an enlarged hippocampus and ventral brain cortex (PubMed:17250763). Mutant mice show a temperature-sensitive alteration in neuromuscular transmission, causing nerve hyperexcitability when exposed to cold and delayed repetitive discharge after a single nerve stimulation (PubMed:9736643). After 2 minutes of swimming in cold water, mutant mice have impaired motor control; they fall over when placed on dry ground and exhibit severe neuromyotonia with violent tremors that decrease with time, leading to full recovery after twenty minutes (PubMed:9736643). Mutant mice have an increased frequency of spontaneous postsynaptic currents in Purkinje cells, impaired ability to maintain their balance on a thin stationary rod, but perform as well as wild-type on a rotarod (PubMed:10191303). Mutant mice have a normal hearing threshold, but altered brainstem responses to auditory stimuli and reduced sensitivity to small changes in sound location (PubMed:22396426). Mutant mice display no alteration of the islet of Langerhans, but have reduced blood glucose levels and increased insulin secretion in response to a glucose stimulus (PubMed:21483673).8 Publications

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2429705

DrugCentral

More...DrugCentrali		P16388

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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000539691 – 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 residuei23PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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%5Fprocessing%5Fsection">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 residuei437PhosphoserineBy similarity1
Modified residuei439PhosphoserineBy similarity1
Modified residuei446Phosphoserine; by PKABy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

N-glycosylated.By similarity
Palmitoylated on Cys-243; which may be required for membrane targeting.By similarity
Phosphorylated on tyrosine residues. Phosphorylation increases in response to NRG1; this inhibits channel activity (PubMed:22158511). Phosphorylation at Ser-446 regulates channel activity by down-regulating expression at the cell membrane (By similarity).By similarity1 Publication

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P16388

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

More...PaxDbi		P16388

PeptideAtlas

More...PeptideAtlasi		P16388

PRoteomics IDEntifications database

More...PRIDEi		P16388

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P16388, 1 site

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P16388

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

More...PhosphoSitePlusi		P16388

<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 brain (PubMed:21483673, PubMed:22158511). Detected in the juxtaparanodal regions of the nodes of Ranvier in myelinated axons (PubMed:8361541, PubMed:8046438). Detected in the paranodal region in sciatic nerve (PubMed:9736643). Detected on cell bodies in cerebellum, dorsal and ventral cochlear nucleus, pontine reticular nucleus, mesencephalic trigeminal nucleus, motor trigeminal nucleus and the pricipal sensory trigeminal nucleus (PubMed:8046438). Detected in terminal fields of basket cells in the cerebellum corpus medullare (PubMed:8361541, PubMed:8046438, PubMed:9581771). Detected in hippocampus CA3 pyramidal neurons and in the hilus and stratum moleculare of the dentate gyrus (PubMed:8046438, PubMed:9581771, PubMed:14686897). Detected in the central nucleus and the external nucleus of the inferior colliculus (PubMed:8046438, PubMed:21966978). Detected in fiber tracts in the optic tract, external medullary lamina, stria terminalis, medulla, ventral pallidum and substantia nigra (PubMed:8046438). Detected in neurons from dorsal root ganglion (PubMed:23473320). Detected in neurons in the medial nucleus of the trapezoid body (PubMed:12611922). Detected in midbrain dopamine neuron axon terminals (PubMed:21233214). Detected in brain cortex (PubMed:8046438, PubMed:14686897). Detected in brainstem (PubMed:8361541). Detected in juxtaparanodal regions of the nodes of Ranvier in the vagus nerve, but only at very low levels in the heart (PubMed:20392939, PubMed:22641786). Detected in the islet of Langerhans (PubMed:21483673). Detected at the luminal membrane in distal convoluted tubules in the kidney (at protein level) (PubMed:19307729). Detected in brain (PubMed:2451788, PubMed:9581771). Detected in hippocampus, thalamus, neocortex and ventral brain cortex, including the piriform and entorhinal cortex and the amygdala (PubMed:14686897). Detected in midbrain dopamine neurons (PubMed:21233214). Detected in heart atrium, ventricle, sinoatrial node and atrioventricular node (PubMed:20392939). Detected in the islet of Langerhans (PubMed:21483673).15 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

Down-regulated by high dietary Mg2+ levels.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000047976, Expressed in sciatic nerve and 186 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P16388, MM

<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%5Fsection">'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%5Fsection">'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:8361541). Channel activity is regulated by interaction with the beta subunits KCNAB1 and KCNAB2 (PubMed:15361858).

Identified in a complex with KCNA2 and KCNAB2.

Interacts (via C-terminus) with the PDZ domains of DLG1, DLG2 and DLG4 (By similarity).

Interacts with LGI1 within a complex containing LGI1, KCNA4 and KCNAB1 (By similarity).

Interacts (via N-terminus) with STX1A; this promotes channel inactivation (By similarity).

Interacts (via N-terminus) with the heterodimer formed by GNB1 and GNG2; this promotes channel inactivation (By similarity). Can interact simultaneously with STX1A and the heterodimer formed by GNB1 and GNG2 (By similarity).

Interacts (via cytoplasmic N-terminal domain) with KCNRG; this inhibits channel activity (By similarity).

Interacts with ANK3; this inhibits channel activity (PubMed:23903368).

By similarityCurated3 Publications

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		200876, 9 interactors

Protein interaction database and analysis system

More...IntActi		P16388, 3 interactors

Molecular INTeraction database

More...MINTi		P16388

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000055225

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P16388, protein

<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		P16388

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>Regioni1 – 128Tetramerization domainBy similarityAdd 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-bindingBy similarity3

<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.By similarity
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

Belongs to the potassium channel family. A (Shaker) (TC 1.A.1.2) subfamily. Kv1.1/KCNA1 sub-subfamily. [View classification]Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1545, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000158576

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_011722_4_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P16388

KEGG Orthology (KO)

More...KOi		K04874

Identification of Orthologs from Complete Genome Data

More...OMAi		GHPQDPY

Database of Orthologous Groups

More...OrthoDBi		695337at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P16388

TreeFam database of animal gene trees

More...TreeFami		TF313103

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
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

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		PR01508, KV11CHANNEL
PR01491, KVCHANNEL
PR01496, SHAKERCHANEL

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%5Flength">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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P16388-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTVMSGENAD EASTAPGHPQ 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 ANIRTGNCTT ADQNCVNKSK LLTDV
Length:495
Mass (Da):56,409
Last modified:August 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:iC9249F130E943D3D
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 varies from 35% in the frontal cortex to 75% in the spinal chord.

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

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M30439 Genomic DNA Translation: AAA39711.1
Y00305 mRNA Translation: CAA68408.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS20555.1

Protein sequence database of the Protein Information Resource

More...PIRi		A40090
S09042

NCBI Reference Sequences

More...RefSeqi		NP_034725.3, NM_010595.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000055168; ENSMUSP00000055225; ENSMUSG00000047976
ENSMUST00000203094; ENSMUSP00000144947; ENSMUSG00000047976

Database of genes from NCBI RefSeq genomes

More...GeneIDi		16485

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:16485

UCSC genome browser

More...UCSCi		uc009dvb.1, mouse

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
M30439 Genomic DNA Translation: AAA39711.1
Y00305 mRNA Translation: CAA68408.1
CCDSiCCDS20555.1
PIRiA40090
S09042
RefSeqiNP_034725.3, NM_010595.3

3D structure databases

SMRiP16388
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi200876, 9 interactors
IntActiP16388, 3 interactors
MINTiP16388
STRINGi10090.ENSMUSP00000055225

Chemistry databases

ChEMBLiCHEMBL2429705
DrugCentraliP16388
GuidetoPHARMACOLOGYi538

PTM databases

GlyGeniP16388, 1 site
iPTMnetiP16388
PhosphoSitePlusiP16388

Proteomic databases

MaxQBiP16388
PaxDbiP16388
PeptideAtlasiP16388
PRIDEiP16388

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		22315, 415 antibodies

Genome annotation databases

EnsembliENSMUST00000055168; ENSMUSP00000055225; ENSMUSG00000047976
ENSMUST00000203094; ENSMUSP00000144947; ENSMUSG00000047976
GeneIDi16485
KEGGimmu:16485
UCSCiuc009dvb.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		3736
MGIiMGI:96654, Kcna1

Phylogenomic databases

eggNOGiKOG1545, Eukaryota
GeneTreeiENSGT00940000158576
HOGENOMiCLU_011722_4_0_1
InParanoidiP16388
KOiK04874
OMAiGHPQDPY
OrthoDBi695337at2759
PhylomeDBiP16388
TreeFamiTF313103

Enzyme and pathway databases

ReactomeiR-MMU-1296072, Voltage gated Potassium channels

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		16485, 1 hit in 19 CRISPR screens

Protein Ontology

More...PROi		PR:P16388
RNActiP16388, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000047976, Expressed in sciatic nerve and 186 other tissues
GenevisibleiP16388, MM

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
PRINTSiPR01508, 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...

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 nameiKCNA1_MOUSE
<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: P16388
<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%5Fand%5Fisoforms">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, 1990
Last sequence update: August 1, 1990
Last modified: August 12, 2020
This is version 176 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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