O70344 · KCNQ1_CAVPO
- ProteinPotassium voltage-gated channel subfamily KQT member 1
- GeneKCNQ1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids671 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon (By similarity).
Associates with KCNE beta subunits that modulates current kinetics (By similarity).
Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selective outward current (By similarity).
Promotes also a delayed voltage activated potassium current showing outward rectification characteristic (By similarity).
During beta-adrenergic receptor stimulation participates in cardiac repolarization by associating with KCNE1 to form the I(Ks) cardiac potassium current that increases the amplitude and slows down the activation kinetics of outward potassium current I(Ks) (By similarity).
Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current (By similarity).
When associated with KCNE3, forms the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions (By similarity).
This interaction with KCNE3 is reduced by 17beta-estradiol, resulting in the reduction of currents (By similarity).
During conditions of increased substrate load, maintains the driving force for proximal tubular and intestinal sodium ions absorption, gastric acid secretion, and cAMP-induced jejunal chloride ions secretion (By similarity).
Allows the provision of potassium ions to the luminal membrane of the secretory canaliculus in the resting state as well as during stimulated acid secretion (By similarity).
When associated with KCNE2, forms a heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (By similarity).
When associated with KCNE4, inhibits voltage-gated potassium channel activity (By similarity).
When associated with KCNE5, this complex only conducts current upon strong and continued depolarization (By similarity).
Also forms a heterotetramer with KCNQ5 that has a voltage-gated potassium channel activity (By similarity).
Binds with phosphatidylinositol 4,5-bisphosphate (By similarity).
Associates with KCNE beta subunits that modulates current kinetics (By similarity).
Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selective outward current (By similarity).
Promotes also a delayed voltage activated potassium current showing outward rectification characteristic (By similarity).
During beta-adrenergic receptor stimulation participates in cardiac repolarization by associating with KCNE1 to form the I(Ks) cardiac potassium current that increases the amplitude and slows down the activation kinetics of outward potassium current I(Ks) (By similarity).
Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current (By similarity).
When associated with KCNE3, forms the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions (By similarity).
This interaction with KCNE3 is reduced by 17beta-estradiol, resulting in the reduction of currents (By similarity).
During conditions of increased substrate load, maintains the driving force for proximal tubular and intestinal sodium ions absorption, gastric acid secretion, and cAMP-induced jejunal chloride ions secretion (By similarity).
Allows the provision of potassium ions to the luminal membrane of the secretory canaliculus in the resting state as well as during stimulated acid secretion (By similarity).
When associated with KCNE2, forms a heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (By similarity).
When associated with KCNE4, inhibits voltage-gated potassium channel activity (By similarity).
When associated with KCNE5, this complex only conducts current upon strong and continued depolarization (By similarity).
Also forms a heterotetramer with KCNQ5 that has a voltage-gated potassium channel activity (By similarity).
Binds with phosphatidylinositol 4,5-bisphosphate (By similarity).
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended namePotassium voltage-gated channel subfamily KQT member 1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Hystricomorpha > Caviidae > Cavia
Accessions
- Primary accessionO70344
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Note: Colocalized with KCNE3 at the plasma membrane. Upon 17beta-oestradiol treatment, colocalizes with RAB5A at early endosome. Heterotetramer with KCNQ5 is highly retained at the endoplasmic reticulum and is localized outside of lipid raft microdomains. During the early stages of epithelial cell polarization induced by the calcium switch it is removed from the plasma membrane to the endoplasmic reticulum, where it is retained, and redistributed to the basolateral cell surface in a PI3K-dependent manner at a later stage.
Features
Showing features for topological domain, transmembrane, intramembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-122 | Cytoplasmic | ||||
Sequence: MAAASSPPRTERKRGGWGRLLGSRRGSASLAKKCPFSLELAEGGPAGGTLYAPVAPPGALSPGSPAPPASPAAPPAGLELGPRPPVSLDPRVSIYSARRPLLARTHIQGRVYNFLERPTGWK | ||||||
Transmembrane | 123-143 | Helical; Name=Segment S1 | ||||
Sequence: CFVYHFAVFLIVLACLIFSVL | ||||||
Topological domain | 144-148 | Extracellular | ||||
Sequence: STIEQ | ||||||
Transmembrane | 149-169 | Helical; Name=Segment S2 | ||||
Sequence: YAALATGTLFWMEIVLVVFFG | ||||||
Topological domain | 170-196 | Cytoplasmic | ||||
Sequence: TEYVVRLWSAGCRSKYVGIWGRLRFAR | ||||||
Transmembrane | 197-218 | Helical; Name=Segment S3 | ||||
Sequence: KPISIIDLIVVVASMVVLCVGS | ||||||
Topological domain | 219-226 | Extracellular | ||||
Sequence: KGQVFATS | ||||||
Transmembrane | 227-249 | Helical; Voltage-sensor; Name=Segment S4 | ||||
Sequence: AIRGIRFLQILRMLHVDRQGGTW | ||||||
Topological domain | 250-262 | Cytoplasmic | ||||
Sequence: RLLGSVVFIHRQE | ||||||
Transmembrane | 263-283 | Helical; Name=Segment S5 | ||||
Sequence: LITTLYIGFLGLIFSSYFVYL | ||||||
Topological domain | 284-300 | Extracellular | ||||
Sequence: AEKDAVNESGRVEFGSY | ||||||
Intramembrane | 301-321 | Pore-forming; Name=Segment H5 | ||||
Sequence: ADALWWGVVTVTTIGYGDKVP | ||||||
Topological domain | 322-328 | Extracellular | ||||
Sequence: QTWVGKT | ||||||
Transmembrane | 329-349 | Helical; Name=Segment S6 | ||||
Sequence: IASCFSVFAISFFALPAGILG | ||||||
Topological domain | 350-671 | Cytoplasmic | ||||
Sequence: SGFALKVQQKQRQKHFNRQIPAAASLIQTAWRCYAAENPDSSTWKIYVRKPARSHTLLSPSPKPKKSAMVRKKKFKPDKDNGVSPGEKMLTVPHITCDPPEERRPDHFSVDGYDSSVRKSPTLLEVSPTHFMRTNSFAEDLDLEGETLLTPITHVSQLREHHRATIKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMVRIKELQRRLDQSIGKPSLFIPISEKSKDRGSNTIGARLNRVEDKVTQLDQRLVVITDMLHQLLSLHQGGPHSGGGPQMVQPCSEDGSIHPELFLPSNSLPTYEQLTVPQRGPDEAS |
Keywords
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000054021 | 1-671 | Potassium voltage-gated channel subfamily KQT member 1 | |||
Sequence: MAAASSPPRTERKRGGWGRLLGSRRGSASLAKKCPFSLELAEGGPAGGTLYAPVAPPGALSPGSPAPPASPAAPPAGLELGPRPPVSLDPRVSIYSARRPLLARTHIQGRVYNFLERPTGWKCFVYHFAVFLIVLACLIFSVLSTIEQYAALATGTLFWMEIVLVVFFGTEYVVRLWSAGCRSKYVGIWGRLRFARKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRVEFGSYADALWWGVVTVTTIGYGDKVPQTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASLIQTAWRCYAAENPDSSTWKIYVRKPARSHTLLSPSPKPKKSAMVRKKKFKPDKDNGVSPGEKMLTVPHITCDPPEERRPDHFSVDGYDSSVRKSPTLLEVSPTHFMRTNSFAEDLDLEGETLLTPITHVSQLREHHRATIKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMVRIKELQRRLDQSIGKPSLFIPISEKSKDRGSNTIGARLNRVEDKVTQLDQRLVVITDMLHQLLSLHQGGPHSGGGPQMVQPCSEDGSIHPELFLPSNSLPTYEQLTVPQRGPDEAS | ||||||
Modified residue | 27 | Phosphoserine; by PKA | ||||
Sequence: S | ||||||
Glycosylation | 290 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 408 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 410 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation at Ser-27 by PKA; increases delayed rectifier potassium channel activity of the KCNQ1-KCNE1 complex through a macromolecular complex that includes PKA, PP1, and the targeting protein AKAP9.
Ubiquitinated by NEDD4L; promotes internalization. The ubiquitinylated form is internalized through a clathrin-mediated endocytosis by interacting with AP2M1 and is recycled back to the cell membrane via RAB4A and RAB11A.
Deubiquitinated by USP2; counteracts the NEDD4L-specific down-regulation of I(Ks) and restores the membrane localization.
Keywords
- PTM
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Tetramer. Heterotetramer with KCNE1; targets to the membrane raft. Interacts (via C-terminus) with CALM; forms a heterooctameric structure (with 4:4 KCNQ1:CALM stoichiometry) in a calcium-independent manner. Interacts with AKAP9; targets protein kinase A (PKA) catalytic and regulatory subunits and protein phosphatase 1 (PP1) to the KCNQ1-KCNE1 complex, allowing PKA-mediated phosphorylation and increase of delayed rectifier potassium channel activity. Interacts with KCNE2; form a heterooligomer complex that targets to the membrane raft and leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current. Interacts with AP2M1; mediates estrogen-induced internalization via clathrin-coated vesicles. Interacts with NEDD4L; promotes internalization and decreases I(Ks) currents. Interacts with USP2; counteracts the NEDD4L-specific down-regulation of I(Ks) and restore plasma membrane localization. Heterotetramer with KCNQ5; has a voltage-gated potassium channel activity. Interacts with KCNE3; alters membrane raft localization. Interacts with KCNE4; impairs KCNQ1 localization in lipid rafts and inhibits voltage-gated potassium channel activity. Interacts with KCNE5; impairs KCNQ1 localization in lipid rafts and only conducts current upon strong and continued depolarization.
Protein-protein interaction databases
Chemistry
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-29 | Disordered | ||||
Sequence: MAAASSPPRTERKRGGWGRLLGSRRGSAS | ||||||
Compositional bias | 61-81 | Pro residues | ||||
Sequence: SPGSPAPPASPAAPPAGLELG | ||||||
Region | 61-84 | Disordered | ||||
Sequence: SPGSPAPPASPAAPPAGLELGPRP | ||||||
Motif | 313-318 | Selectivity filter | ||||
Sequence: TIGYGD | ||||||
Region | 371-383 | Interaction with CALM | ||||
Sequence: AAASLIQTAWRCY | ||||||
Region | 406-461 | Disordered | ||||
Sequence: LLSPSPKPKKSAMVRKKKFKPDKDNGVSPGEKMLTVPHITCDPPEERRPDHFSVDG | ||||||
Compositional bias | 446-461 | Basic and acidic residues | ||||
Sequence: CDPPEERRPDHFSVDG | ||||||
Region | 516-530 | Interaction with CALM; calcium-dependent | ||||
Sequence: KVIRRMQYFVAKKKF | ||||||
Region | 536-573 | Interaction with KCNE1 C-terminus | ||||
Sequence: PYDVRDVIEQYSQGHLNLMVRIKELQRRLDQSIGKPSL | ||||||
Coiled coil | 586-621 | |||||
Sequence: SNTIGARLNRVEDKVTQLDQRLVVITDMLHQLLSLH | ||||||
Region | 589-617 | Interaction with AKAP9 | ||||
Sequence: IGARLNRVEDKVTQLDQRLVVITDMLHQL | ||||||
Region | 590-621 | C-terminal assembly domain | ||||
Sequence: GARLNRVEDKVTQLDQRLVVITDMLHQLLSLH | ||||||
Region | 621-671 | Disordered | ||||
Sequence: HQGGPHSGGGPQMVQPCSEDGSIHPELFLPSNSLPTYEQLTVPQRGPDEAS |
Domain
The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.
The coiled-coil domain mediates tetramerization.
The segment S6 is involved in the inhibition of voltage-gated potassium channel activity by KCNE4.
The C-terminal assembly domain promotes self-interactiona; allows functional channel.
The C-terminal coiled-coil domain interacts with a single CALM molecule via the first two membrane-proximal helical regions, with CALM forming a clamp-like structure. Binding of CALM C-terminus to the first helical region is calcium-independent but is essential for assembly of the structure. Binding of CALM N-terminus to the second helical region is calcium-dependent and regulates electrophysiological activity of the channel.
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length671
- Mass (Da)74,411
- Last updated2016-01-20 v3
- Checksum68B5ABCE83313557
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0W5V8 | H0W5V8_CAVPO | KCNQ1 | 443 | ||
A0A2C9F1E3 | A0A2C9F1E3_CAVPO | KCNQ1 | 660 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 61-81 | Pro residues | ||||
Sequence: SPGSPAPPASPAAPPAGLELG | ||||||
Sequence conflict | 236 | in Ref. 2; AAC05498 | ||||
Sequence: I → S | ||||||
Compositional bias | 446-461 | Basic and acidic residues | ||||
Sequence: CDPPEERRPDHFSVDG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAKN02038603 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAKN02038605 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAKN02038604 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AF049341 EMBL· GenBank· DDBJ | AAC05498.1 EMBL· GenBank· DDBJ | mRNA | ||
AB032574 EMBL· GenBank· DDBJ | BAA88579.1 EMBL· GenBank· DDBJ | mRNA |