General Information of This Target
Target ID
BTDT00206
Target Name
Potassium voltage-gated channel subfamily KQT member 1 (Kcnq1)
Target Bioclass
Transporter and channel
Uniprot ID
Q9Z0N7
3D Structure
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2D Sequence
3D Structure
Source
Predict by Alphafold2
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Alphafold Parameters: msa_mode: mmseqs2_uniref_env model_type: auto num_recycles: auto
Gene Name
Kcnq1
Gene ID
84020
Synonym
IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1; KQT-like 1; Voltage-gated potassium channel subunit Kv7.1
Sequence
MDTASSPPNAERKRAGWGRLLGARRGSAGLAKKCPFSLELAEGGPTGGTVYAPIAPTGAP
GLAPPMSPPVSPVPAPADLGPRPRVSLDPRVSIYSTRRPLLARTHIQGRVYNFLERPTGW
KCFVYHFTVFLIVLVCLIFSVLSTIEQYAALATGTLFWMEIVLVVFFGTEYVVRLWSAGC
RSKYVGIWGRLRFARKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLH
VDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRIEFGSYA
DALWWGVVTVTTIGYGDKVPQTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQR
QKHFNRQIPAAASLIQTAWRCYAAENPDSSTWKIYVRKPARSHTLLSPSPKPKKSVMVKK
KKFKLDKDNGLSPGEKIFNVPHITCDPPEDRRPDHFSIDGYDSSVRKSPTLLEVSTPHFL
RTNSFAEDLDLEGETLLTPITHVSQLRDHHRATIKVIRRMQYFVAKKKFQQARKPYDVRD
VIEQYSQGHLNLMVRIKELQRRLDQSIGKPSLFIPISEKSKDRGSNTIGARLNRVEDKVT
QLDQRLVIITDMLHQLLSLQQGGPTCNNRSQVVASDERGSINPELFLPSNSLPTYEQLTV
PQTGPDEGS

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Family
the potassium channel family
Function
Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon. Associates with KCNE beta subunits that modulates current kinetics . Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selective outward current . Promotes also a delayed voltage activated potassium current showing outward rectification characteristic. 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) . Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current. When associated with KCNE3, forms the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions. This interaction with KCNE3 is reduced by 17beta- estradiol, resulting in the reduction of currents. 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. 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. 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. When associated with KCNE4, inhibits voltage-gated potassium channel activity. When associated with KCNE5, this complex only conducts current upon strong and continued depolarization. Also forms a heterotetramer with KCNQ5 that has a voltage- gated potassium channel activity. Binds with phosphatidylinositol 4,5-bisphosphate. 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.

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Taxonomy ID
10116
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Kingdom: Metazoa
Phylum: Chordata
Class: Mammalia
Order: Rodentia
Family: Muridae
Genus: Rattus
Species: Rattus norvegicus
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    Potassium channel toxin alpha-KTx 4.1 Inhibition rate . [1]
 Toxin Info    Potassium channel toxin TsTXK-beta Inhibition rate . [2]
 Toxin Info    Potassium channel toxin gamma-KTx 1.1 Inhibition rate . [3- 14]
 Toxin Info    Potassium channel toxin alpha-KTx 12.2 Inhibition rate
5 %
[1]
 Toxin Info    Potassium channel toxin alpha-KTx 12.1 Inhibition rate
5 %
[1]
References
Ref 1 Electrophysiological characterization of Ts6 and Ts7, K? channel toxins isolated through an improved Tityus serrulatus venom purification procedure. Toxins (Basel). 2014 Feb 28;6(3):892-913. doi: 10.3390/toxins6030892.
Ref 2 Ts8 scorpion toxin inhibits the Kv4.2 channel and produces nociception in?vivo. Toxicon. 2016 Sep 1;119:244-52. doi: 10.1016/j.toxicon.2016.06.014. Epub 2016 Jun 23.
Ref 3 A large number of novel Ergtoxin-like genes and ERG K+-channels blocking peptides from scorpions of the genus Centruroides. FEBS Lett. 2002 Dec 4;532(1-2):121-6. doi: 10.1016/s0014-5793(02)03652-9.
Ref 4 A toxin to nervous, cardiac, and endocrine ERG K+ channels isolated from Centruroides noxius scorpion venom. FASEB J. 1999 May;13(8):953-62.
Ref 5 Disulfide bridges of ergtoxin, a member of a new sub-family of peptide blockers of the ether-a-go-go-related K+ channel. FEBS Lett. 2000 Aug 18;479(3):156-7. doi: 10.1016/s0014-5793(00)01891-3.
Ref 6 Mapping the receptor site for ergtoxin, a specific blocker of ERG channels. FEBS Lett. 2002 Jan 2;510(1-2):45-9. doi: 10.1016/s0014-5793(01)03218-5.
Ref 7 Mapping the binding site of a human ether-a-go-go-related gene-specific peptide toxin (ErgTx) to the channel's outer vestibule. J Biol Chem. 2002 May 10;277(19):16403-11. doi: 10.1074/jbc.M200460200. Epub 2002 Feb 25.
Ref 8 Preferential closed channel blockade of HERG potassium currents by chemically synthesised BeKm-1 scorpion toxin. FEBS Lett. 2003 Jul 17;547(1-3):20-6. doi: 10.1016/s0014-5793(03)00662-8.
Ref 9 Species diversity and peptide toxins blocking selectivity of ether-a-go-go-related gene subfamily K+ channels in the central nervous system. Mol Pharmacol. 2006 May;69(5):1673-83. doi: 10.1124/mol.105.019729. Epub 2006 Feb 23.
Ref 10 Mechanism of block of the hERG K+ channel by the scorpion toxin CnErg1. Biophys J. 2007 Jun 1;92(11):3915-29. doi: 10.1529/biophysj.106.101956. Epub 2007 Mar 16.
Ref 11 Recombinant expression of the toxic peptide ErgTx1 and role of Met35 on its stability and function. Peptides. 2011 Mar;32(3):560-7. doi: 10.1016/j.peptides.2010.06.018. Epub 2010 Jun 30.
Ref 12 Positive selection-guided mutational analysis revealing two key functional sites of scorpion ERG K(+) channel toxins. Biochem Biophys Res Commun. 2012 Dec 7;429(1-2):111-6. doi: 10.1016/j.bbrc.2012.10.065. Epub 2012 Oct 24.
Ref 13 Solution structure of CnErg1 (Ergtoxin), a HERG specific scorpion toxin. FEBS Lett. 2003 Mar 27;539(1-3):138-42. doi: 10.1016/s0014-5793(03)00216-3.
Ref 14 Exploring structural features of the interaction between the scorpion toxinCnErg1 and ERG K+ channels. Proteins. 2004 Aug 1;56(2):367-75. doi: 10.1002/prot.20102.
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