Q61423 · KCNA4_MOUSE
- ProteinPotassium voltage-gated channel subfamily A member 4
- GeneKcna4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids654 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- K+(in) = K+(out)
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | asymmetric synapse | |
Cellular Component | axon | |
Cellular Component | axon initial segment | |
Cellular Component | cell surface | |
Cellular Component | dendritic shaft | |
Cellular Component | dendritic spine | |
Cellular Component | glutamatergic synapse | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Cellular Component | postsynaptic membrane | |
Cellular Component | presynaptic membrane | |
Cellular Component | voltage-gated potassium channel complex | |
Molecular Function | delayed rectifier potassium channel activity | |
Molecular Function | monoatomic ion channel activity | |
Molecular Function | potassium channel activity | |
Molecular Function | potassium ion binding | |
Molecular Function | voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential | |
Molecular Function | voltage-gated potassium channel activity | |
Biological Process | action potential | |
Biological Process | potassium ion transmembrane transport | |
Biological Process | protein homooligomerization |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePotassium voltage-gated channel subfamily A member 4
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ61423
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane, intramembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-305 | Cytoplasmic | ||||
Sequence: MEVAMVSAESSGCNSHMPYGYAAQARARERERLAHSRAAAAAAVAAATAAVEGTGGSGGGPHHHHQTRGAYSSHDPQGSRGSRRRRRQRTEKKKLHHRQSSFPHCSDLMPSGSEEKILRELSEEEEDEEEEEEEEEEGRFYYSEEDHGDGCSYTDLLPQDDGGGGGYSSVRYSDCCERVVINVSGLRFETQMKTLAQFPETLLGDPEKRTQYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLKRPVNVPFDIFTEEVKFYQLGEEALLKFREDEGFVREEEDRALPENEFKKQIWLLFEYPESSS | ||||||
Transmembrane | 306-327 | Helical; Name=Segment S1 | ||||
Sequence: PARGIAIVSVLVILISIVIFCL | ||||||
Topological domain | 328-371 | Extracellular | ||||
Sequence: ETLPEFRDDRDLIMALSAGGHSRLLNDTSAPHLENSGHTIFNDP | ||||||
Transmembrane | 372-393 | Helical; Name=Segment S2 | ||||
Sequence: FFIVETVCIVWFSFEFVVRCFA | ||||||
Topological domain | 394-404 | Cytoplasmic | ||||
Sequence: CPSQALFFKNI | ||||||
Transmembrane | 405-425 | Helical; Name=Segment S3 | ||||
Sequence: MNIIDIVSILPYFITLGTDLA | ||||||
Topological domain | 426-440 | Extracellular | ||||
Sequence: QQQGGGNGQQQQAMS | ||||||
Transmembrane | 441-461 | Helical; Voltage-sensor; Name=Segment S4 | ||||
Sequence: FAILRIIRLVRVFRIFKLSRH | ||||||
Topological domain | 462-476 | Cytoplasmic | ||||
Sequence: SKGLQILGHTLRASM | ||||||
Transmembrane | 477-498 | Helical; Name=Segment S5 | ||||
Sequence: RELGLLIFFLFIGVILFSSAVY | ||||||
Topological domain | 499-512 | Extracellular | ||||
Sequence: FAEADEPTTHFQSI | ||||||
Intramembrane | 513-524 | Helical; Name=Pore helix | ||||
Sequence: PDAFWWAVVTMT | ||||||
Intramembrane | 525-532 | |||||
Sequence: TVGYGDMK | ||||||
Topological domain | 533-539 | Extracellular | ||||
Sequence: PITVGGK | ||||||
Transmembrane | 540-568 | Helical; Name=Segment S6 | ||||
Sequence: IVGSLCAIAGVLTIALPVPVIVSNFNYFY | ||||||
Topological domain | 569-654 | Cytoplasmic | ||||
Sequence: HRETENEEQTQLTQNAVSCPYLPSNLLKKFRSSTSSSLGDKSEYLEMEEGVKESLCGKEEKCQGKGDESETDKNNCSNAKAVETDV |
Keywords
- Cellular component
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 32 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000053982 | 1-654 | Potassium voltage-gated channel subfamily A member 4 | |||
Sequence: MEVAMVSAESSGCNSHMPYGYAAQARARERERLAHSRAAAAAAVAAATAAVEGTGGSGGGPHHHHQTRGAYSSHDPQGSRGSRRRRRQRTEKKKLHHRQSSFPHCSDLMPSGSEEKILRELSEEEEDEEEEEEEEEEGRFYYSEEDHGDGCSYTDLLPQDDGGGGGYSSVRYSDCCERVVINVSGLRFETQMKTLAQFPETLLGDPEKRTQYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLKRPVNVPFDIFTEEVKFYQLGEEALLKFREDEGFVREEEDRALPENEFKKQIWLLFEYPESSSPARGIAIVSVLVILISIVIFCLETLPEFRDDRDLIMALSAGGHSRLLNDTSAPHLENSGHTIFNDPFFIVETVCIVWFSFEFVVRCFACPSQALFFKNIMNIIDIVSILPYFITLGTDLAQQQGGGNGQQQQAMSFAILRIIRLVRVFRIFKLSRHSKGLQILGHTLRASMRELGLLIFFLFIGVILFSSAVYFAEADEPTTHFQSIPDAFWWAVVTMTTVGYGDMKPITVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETENEEQTQLTQNAVSCPYLPSNLLKKFRSSTSSSLGDKSEYLEMEEGVKESLCGKEEKCQGKGDESETDKNNCSNAKAVETDV | ||||||
Modified residue | 122 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 353 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 600 | Phosphoserine; by PKA | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
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).
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q61423 | Dlg4 Q62108 | 3 | EBI-2309633, EBI-300895 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 24-145 | Disordered | ||||
Sequence: QARARERERLAHSRAAAAAAVAAATAAVEGTGGSGGGPHHHHQTRGAYSSHDPQGSRGSRRRRRQRTEKKKLHHRQSSFPHCSDLMPSGSEEKILRELSEEEEDEEEEEEEEEEGRFYYSEE | ||||||
Compositional bias | 80-99 | Basic residues | ||||
Sequence: RGSRRRRRQRTEKKKLHHRQ | ||||||
Compositional bias | 120-140 | Acidic residues | ||||
Sequence: ELSEEEEDEEEEEEEEEEGRF | ||||||
Region | 463-476 | S4-S5 linker | ||||
Sequence: KGLQILGHTLRASM | ||||||
Motif | 525-530 | Selectivity filter | ||||
Sequence: TVGYGD | ||||||
Region | 630-654 | Disordered | ||||
Sequence: CQGKGDESETDKNNCSNAKAVETDV | ||||||
Motif | 652-654 | PDZ-binding | ||||
Sequence: TDV |
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
Belongs to the potassium channel family. A (Shaker) (TC 1.A.1.2) subfamily. Kv1.4/KCNA4 sub-subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length654
- Mass (Da)73,470
- Last updated2011-07-27 v2
- Checksum9322A3DC9CBA2AC4
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 80-99 | Basic residues | ||||
Sequence: RGSRRRRRQRTEKKKLHHRQ | ||||||
Compositional bias | 120-140 | Acidic residues | ||||
Sequence: ELSEEEEDEEEEEEEEEEGRF | ||||||
Sequence conflict | 160 | in Ref. 1; AAB60668 | ||||
Sequence: D → E | ||||||
Sequence conflict | 395 | in Ref. 1; AAB60668 | ||||
Sequence: P → T | ||||||
Sequence conflict | 636 | in Ref. 1; AAB60668 | ||||
Sequence: E → D |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |