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Potassium voltage-gated channel subfamily KQT member 1 (house mouse)

Protein
Encoding Gene
Dates
  • Create:
    2017-04-15
  • Modify:
    2025-01-17
Description
A voltage-gated potassium channel subunit KCNQ1 that is encoded in the genome of mouse.
Pore-forming subunit of the voltage-gated potassium (Kv) channel involved in the regulation of cardiomyocyte excitability and important in normal development and functions of myocardium, inner ear, stomach and colon (By similarity) (PMID: 11120752, PMID: 15004216, PMID: 16314573). Associates with KCNE beta subunits that modulates current kinetics (By similarity) (PMID: 15004216, PMID: 17597584). Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selective outward current (By similarity) (PMID: 8900282). Promotes also a delayed voltage activated potassium current showing outward rectification characteristic (By similarity). During beta-adrenergic receptor stimulation participates in cardiac increases the amplitude and slows down the activation kinetics of outward potassium current I(Ks) (By similarity) (PMID: 15004216, PMID: 17597584). 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 (PMID: 16314573). 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 (PMID: 19491250). 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; has a voltage-gated potassium channel activity (By similarity). Binds with phosphatidylinositol 4,5-bisphosphate (By similarity). KCNQ1-KCNE2 channel associates with Na(+)-coupled myo-inositol symporter in the apical membrane of choroid plexus epithelium and regulates the myo-inositol gradient between blood and cerebrospinal fluid with an impact on neuron excitability (PMID: 24595108).

1 Names and Identifiers

1.1 Synonyms

  • Potassium voltage-gated channel subfamily KQT member 1
  • IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1
  • KQT-like 1
  • Voltage-gated potassium channel subunit Kv7.1

1.2 Other Identifiers

1.2.1 RefSeq Accession

1.2.2 UniProt ID

1.2.3 PRO ID

1.2.4 Guide to PHARMACOLOGY Target ID

1.2.5 GlyCosmos Protein

1.2.6 STRING Protein ID

1.2.7 Wikidata

1.2.8 IntAct Protein

1.2.9 InterPro Protein

3 Sequence

>sp|P97414|KCNQ1_MOUSE Potassium voltage-gated channel subfamily KQT member 1 (Run BLAST)

MDTASSPPSAERKRAGWSRLLGARRGSAVVKKCPFSLELAEGGPEGSTVYAPIAPTGAPGLAPPMSTPVSPAPAPADLGPRPRVSLDPRVSIYSARRPLLARTHIQGRVYNFLERPTGWKCFVYHFTVFLIVLVCLIFSVLSTIEQYAALATGTLFWMEIVLVVFFGTEYVVRLWSAGCRSKYVGIWGRLRFARKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRIEFGSYADALWWGVVTVTTIGYGDKVPQTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASLIQTAWRCYAAENPDSATWKIYVRKPARSHTLLSPSPKPKKSVMVKKKKFKLDKDNGMSPGEKMFNVPHITYDPPEDRRPDHFSIDGYDSSVRKSPTLLEVSTPHFLRTNSFAEDLDLEGETLLTPITHVSQLRDHHRATIKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMVRIKELQRRLDQSIGKPSLFIPISEKSKDRGSNTIGARLNRVEDKVTQLDQRLVIITDMLHQLLSMQQGGPTCNSRSQVVASNEGGSINPELFLPSNSLPTYEQLTVPQTGPDEGS

4 3D Structures

4.1 AlphaFold Structures

Highly accurate protein structure prediction with AlphaFold. Nature. 2021 Aug;596(7873):583-589. DOI:10.1038/s41586-021-03819-2. PMID:34265844; PMCID:PMC8371605

5 Domains

5.1 CDD Domains

5.2 InterPro Domains

6 Interactions and Pathways

6.1 Chemical-Protein Interactions

6.2 Interactions

6.3 Pathways

7 Biochemical Reactions

8 Literature

8.1 Consolidated References

9 Classification

9.1 IUPHAR / BPS Guide to PHARMACOLOGY Target Classification

10 Information Sources

  1. NCBI Protein
    LICENSE
    NCBI Website and Data Usage Policies and Disclaimers
    https://www.ncbi.nlm.nih.gov/home/about/policies/
  2. PubChem
  3. GlyCosmos Glycoscience Portal
    LICENSE
    All copyrightable parts of the datasets in GlyCosmos are under the Creative Commons Attribution (CC BY 4.0) License.
    https://glycosmos.org/license
  4. IntAct Molecular Interaction Database
    LICENSE
    Creative Commons Attribution 4.0 International (CC BY 4.0) License
    https://www.ebi.ac.uk/intact/about#license_privacy
  5. InterPro
    LICENSE
    All of the InterPro, Pfam, PRINTS and SFLD downloadable data provided on the InterPro website is freely available under CC0 1.0 Universal (CC0 1.0) Public Domain Dedication.
    https://www.ebi.ac.uk/interpro/about/license/
  6. IUPHAR/BPS Guide to PHARMACOLOGY
    LICENSE
    The Guide to PHARMACOLOGY database is licensed under the Open Data Commons Open Database License (ODbL) https://opendatacommons.org/licenses/odbl/. Its contents are licensed under a Creative Commons Attribution-ShareAlike 4.0 International License (http://creativecommons.org/licenses/by-sa/4.0/)
    https://www.guidetopharmacology.org/about.jsp#license
    Guide to Pharmacology Target Classification
    https://www.guidetopharmacology.org/targets.jsp
  7. NCBI Conserved Domains (CDD)
    LICENSE
    NCBI Website and Data Usage Policies and Disclaimers
    https://www.ncbi.nlm.nih.gov/home/about/policies/
  8. Protein Ontology
    LICENSE
    PRO is distributed under the Creative Commons CC-BY 4.0 license (https://creativecommons.org/licenses/by/4.0/).
  9. UniProt
    LICENSE
    We have chosen to apply the Creative Commons Attribution (CC BY 4.0, http://creativecommons.org/licenses/by/4.0/) License to all copyrightable parts of our databases.
    https://www.uniprot.org/help/license
  10. STRING: functional protein association networks
  11. Wikidata
    Potassium voltage-gated channel, subfamily Q, member 1
    https://www.wikidata.org/wiki/Q14865158
  12. AlphaFold DB
    LICENSE
    All of the data provided is freely available for both academic and commercial use under Creative Commons Attribution 4.0 (CC-BY 4.0) licence terms.
    https://alphafold.ebi.ac.uk/faq
  13. Rhea - annotated reactions database
    LICENSE
    Rhea has chosen to apply the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/). This means that you are free to copy, distribute, display and make commercial use of the database in all legislations, provided you credit (cite) Rhea.
    https://www.rhea-db.org/help/license-disclaimer
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