Q61423 · KCNA4_MOUSE

  • Protein
    Potassium voltage-gated channel subfamily A member 4
  • Gene
    Kcna4
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. 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:8020965).
Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (By similarity).
Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation. 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 KCNA4 forms a potassium channel that opens in response to membrane depolarization, followed by rapid spontaneous channel closure (PubMed:8020965).
Likewise, a heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid inactivation (By similarity).

Catalytic activity

GO annotations

AspectTerm
Cellular Componentasymmetric synapse
Cellular Componentaxon
Cellular Componentaxon initial segment
Cellular Componentcell surface
Cellular Componentdendritic shaft
Cellular Componentdendritic spine
Cellular Componentglutamatergic synapse
Cellular Componentmembrane
Cellular Componentplasma membrane
Cellular Componentpostsynaptic membrane
Cellular Componentpresynaptic membrane
Cellular Componentvoltage-gated potassium channel complex
Molecular Functiondelayed rectifier potassium channel activity
Molecular Functionmonoatomic ion channel activity
Molecular Functionpotassium channel activity
Molecular Functionpotassium ion binding
Molecular Functionvoltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential
Molecular Functionvoltage-gated potassium channel activity
Biological Processaction potential
Biological Processpotassium ion transmembrane transport
Biological Processprotein homooligomerization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Potassium voltage-gated channel subfamily A member 4
  • Alternative names
    • Voltage-gated potassium channel subunit Kv1.4

Gene names

    • Name
      Kcna4

Organism names

  • Taxonomic identifier
  • Strains
    • AKR/J
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q61423
  • Secondary accessions
    • Q8CBF8

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane, intramembrane.

TypeIDPosition(s)Description
Topological domain1-305Cytoplasmic
Transmembrane306-327Helical; Name=Segment S1
Topological domain328-371Extracellular
Transmembrane372-393Helical; Name=Segment S2
Topological domain394-404Cytoplasmic
Transmembrane405-425Helical; Name=Segment S3
Topological domain426-440Extracellular
Transmembrane441-461Helical; Voltage-sensor; Name=Segment S4
Topological domain462-476Cytoplasmic
Transmembrane477-498Helical; Name=Segment S5
Topological domain499-512Extracellular
Intramembrane513-524Helical; Name=Pore helix
Intramembrane525-532
Topological domain533-539Extracellular
Transmembrane540-568Helical; Name=Segment S6
Topological domain569-654Cytoplasmic

Keywords

Phenotypes & Variants

Variants

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The viewer provides 32 variants from UniProt as well as other sources including ClinVar and dbSNP.

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Chemistry

PTM/Processing

Features

Showing features for chain, modified residue, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00000539821-654Potassium voltage-gated channel subfamily A member 4
Modified residue122Phosphoserine
Glycosylation353N-linked (GlcNAc...) asparagine
Modified residue600Phosphoserine; by PKA

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in the brain, lens and retina.

Gene expression databases

Interaction

Subunit

Homotetramer and heterotetramer of potassium channel proteins (By similarity).
Interacts with KCNAB1 and KCNAB2 (By similarity).
Interacts with DLG1, DLG2 and DLG4 via their PDZ domains (By similarity).
Interacts with SIGMAR1 (By similarity).
Detected in a complex with KCNA1 (By similarity).
Interacts with KCNA2 (By similarity).
Part of a complex containing KCNA1, KCNAB1 and LGI1 (By similarity).
Interacts (via cytoplasmic N-terminal domain) with KCNRG (By similarity).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q61423Dlg4 Q621083EBI-2309633, EBI-300895

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, motif.

TypeIDPosition(s)Description
Region24-145Disordered
Compositional bias80-99Basic residues
Compositional bias120-140Acidic residues
Region463-476S4-S5 linker
Motif525-530Selectivity filter
Region630-654Disordered
Motif652-654PDZ-binding

Domain

The N-terminus may be important in determining the rate of inactivation of the channel while the tail may play a role in modulation of channel activity and/or targeting of the channel to specific subcellular compartments.
The transmembrane segment S4 functions as a 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.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    654
  • Mass (Da)
    73,470
  • Last updated
    2011-07-27 v2
  • Checksum
    9322A3DC9CBA2AC4
MEVAMVSAESSGCNSHMPYGYAAQARARERERLAHSRAAAAAAVAAATAAVEGTGGSGGGPHHHHQTRGAYSSHDPQGSRGSRRRRRQRTEKKKLHHRQSSFPHCSDLMPSGSEEKILRELSEEEEDEEEEEEEEEEGRFYYSEEDHGDGCSYTDLLPQDDGGGGGYSSVRYSDCCERVVINVSGLRFETQMKTLAQFPETLLGDPEKRTQYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLKRPVNVPFDIFTEEVKFYQLGEEALLKFREDEGFVREEEDRALPENEFKKQIWLLFEYPESSSPARGIAIVSVLVILISIVIFCLETLPEFRDDRDLIMALSAGGHSRLLNDTSAPHLENSGHTIFNDPFFIVETVCIVWFSFEFVVRCFACPSQALFFKNIMNIIDIVSILPYFITLGTDLAQQQGGGNGQQQQAMSFAILRIIRLVRVFRIFKLSRHSKGLQILGHTLRASMRELGLLIFFLFIGVILFSSAVYFAEADEPTTHFQSIPDAFWWAVVTMTTVGYGDMKPITVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETENEEQTQLTQNAVSCPYLPSNLLKKFRSSTSSSLGDKSEYLEMEEGVKESLCGKEEKCQGKGDESETDKNNCSNAKAVETDV

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias80-99Basic residues
Compositional bias120-140Acidic residues
Sequence conflict160in Ref. 1; AAB60668
Sequence conflict395in Ref. 1; AAB60668
Sequence conflict636in Ref. 1; AAB60668

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U03723
EMBL· GenBank· DDBJ
AAB60668.1
EMBL· GenBank· DDBJ
Genomic DNA
AK036112
EMBL· GenBank· DDBJ
BAC29309.1
EMBL· GenBank· DDBJ
mRNA
BX293548
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH466519
EMBL· GenBank· DDBJ
EDL27774.1
EMBL· GenBank· DDBJ
Genomic DNA
BC109014
EMBL· GenBank· DDBJ
AAI09015.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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