General Information of This Target
Target ID
BTDT10223
Target Name
Potassium voltage-gated channel subfamily KQT member 1
Target Bioclass
Transporter and channel
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N.A.
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    Potassium channel toxin alpha-KTx 28.1 Dissociation constant
11.69 μM
[1]
 Toxin Info    U-scoloptoxin(15)-Sm2a Effect . [2], [3]
 Toxin Info    Apamin Inhibition rate . [4- 21]
 Toxin Info    Kappa-theraphotoxin-Ps1a Inhibition rate . [22], [23], [24]
 Toxin Info    Kappa-actitoxin-Ael2a Inhibition rate . [25- 31]
 Toxin Info    Potassium channel toxin alpha-KTx 8.2 Inhibition rate
4 %
[1- 36]
 Toxin Info    Potassium channel toxin kappa-KTx 2.7 Inhibition rate
17.8 %
[1- 39]
 Toxin Info    Potassium channel toxin alpha-KTx 11.1 Inhibition rate
21.43 %
[1- 41]
 Toxin Info    Potassium channel toxin alpha-KTx 9.1 Inhibition rate
23.3 %
[1- 43]
 Toxin Info    Potassium channel toxin alpha-KTx 29.1 Inhibition rate
27.7 %
[1- 44]
 Toxin Info    Potassium channel toxin alpha-KTx 29.2 Inhibition rate
27.7 %
[1]
 Toxin Info    Potassium channel toxin alpha-KTx 29.3 Inhibition rate
27.7 %
[1- 44]
 Toxin Info    Potassium channel toxin kappa-KTx 2.8 Inhibition rate
44.9 %
[1- 39]
 Toxin Info    Mu-scoloptoxin(15)-Ssm1a IC50
2.8 μM
[45]
References
Ref 1 Structural and functional diversity of acidic scorpion potassium channel toxins. PLoS One. 2012;7(4):e35154. doi: 10.1371/journal.pone.0035154. Epub 2012 Apr 12.
Ref 2 Clawing through evolution: toxin diversification and convergence in the ancient lineage Chilopoda (centipedes). Mol Biol Evol. 2014 Aug;31(8):2124-48. doi: 10.1093/molbev/msu162. Epub 2014 May 20.
Ref 3 A Centipede Toxin Family Defines an Ancient Class of CS Defensins. Structure. 2019 Feb 5;27(2):315-326.e7. doi: 10.1016/j.str.2018.10.022. Epub 2018 Dec 13.
Ref 4 The precursors of the bee venom constituents apamin and MCD peptide are encoded by two genes in tandem which share the same 3'-exon. J Biol Chem. 1995 May 26;270(21):12704-8. doi: 10.1074/jbc.270.21.12704.
Ref 5 The peptide components of bee venom. Eur J Biochem. 1976 Jan 15;61(2):369-76. doi: 10.1111/j.1432-1033.1976.tb10030.x.
Ref 6 Apamin as a selective blocker of the calcium-dependent potassium channel in neuroblastoma cells: voltage-clamp and biochemical characterization of the toxin receptor. Proc Natl Acad Sci U S A. 1982 Feb;79(4):1308-12. doi: 10.1073/pnas.79.4.1308.
Ref 7 Apamin, a blocker of the calcium-activated potassium channel, induces neurodegeneration of Purkinje cells exclusively. Brain Res. 1997 Dec 19;778(2):405-8. doi: 10.1016/s0006-8993(97)01165-7.
Ref 8 Determinants of apamin and d-tubocurarine block in SK potassium channels. J Biol Chem. 1997 Sep 12;272(37):23195-200. doi: 10.1074/jbc.272.37.23195.
Ref 9 Pharmacological characterization of small-conductance Ca(2+)-activated K(+) channels stably expressed in HEK 293 cells. Br J Pharmacol. 2000 Mar;129(5):991-9. doi: 10.1038/sj.bjp.0703120.
Ref 10 SK3 is an important component of K(+) channels mediating the afterhyperpolarization in cultured rat SCG neurones. J Physiol. 2001 Sep 1;535(Pt 2):323-34. doi: 10.1111/j.1469-7793.2001.00323.x.
Ref 11 Apamin interacts with all subtypes of cloned small-conductance Ca2+-activated K+ channels. Pflugers Arch. 2001 Jan;441(4):544-50. doi: 10.1007/s004240000447.
Ref 12 An amino acid outside the pore region influences apamin sensitivity in small conductance Ca2+-activated K+ channels. J Biol Chem. 2007 Feb 9;282(6):3478-86. doi: 10.1074/jbc.M607213200. Epub 2006 Dec 1.
Ref 13 Apamin reduces neuromuscular transmission by activating inhibitory muscarinic M(2) receptors on motor nerve terminals. Eur J Pharmacol. 2010 Jan 25;626(2-3):239-43. doi: 10.1016/j.ejphar.2009.09.064. Epub 2009 Oct 8.
Ref 14 Allosteric block of KCa2 channels by apamin. J Biol Chem. 2010 Aug 27;285(35):27067-27077. doi: 10.1074/jbc.M110.110072. Epub 2010 Jun 18.
Ref 15 The small neurotoxin apamin blocks not only small conductance Ca(2+) activated K(+) channels (SK type) but also the voltage dependent Kv1.3 channel. Eur Biophys J. 2017 Sep;46(6):517-523. doi: 10.1007/s00249-016-1196-0. Epub 2017 Jan 20.
Ref 16 Apamin inhibits TNF-- and IFN--induced inflammatory cytokines and chemokines via suppressions of NF-B signaling pathway and STAT in human keratinocytes. Pharmacol Rep. 2017 Oct;69(5):1030-1035. doi: 10.1016/j.pharep.2017.04.006. Epub 2017 Apr 18.
Ref 17 Apamin Suppresses LPS-Induced Neuroinflammatory Responses by Regulating SK Channels and TLR4-Mediated Signaling Pathways. Int J Mol Sci. 2020 Jun 17;21(12):4319. doi: 10.3390/ijms21124319.
Ref 18 Apamin from bee venom suppresses inflammation in a murine model of gouty arthritis. J Ethnopharmacol. 2020 Jul 15;257:112860. doi: 10.1016/j.jep.2020.112860. Epub 2020 Apr 11.
Ref 19 Antioxidative, Antiapoptotic, and Anti-Inflammatory Effects of Apamin in a Murine Model of Lipopolysaccharide-Induced Acute Kidney Injury. Molecules. 2020 Dec 3;25(23):5717. doi: 10.3390/molecules25235717.
Ref 20 Solution structure of apamin determined by nuclear magnetic resonance and distance geometry. Biochemistry. 1988 Nov 1;27(22):8491-8. doi: 10.1021/bi00422a029.
Ref 21 Binding and toxicity of apamin. Characterization of the active site. Eur J Biochem. 1991 Mar 28;196(3):639-45. doi: 10.1111/j.1432-1033.1991.tb15860.x.
Ref 22 Effects of phrixotoxins on the Kv4 family of potassium channels and implications for the role of Ito1 in cardiac electrogenesis. Br J Pharmacol. 1999 Jan;126(1):251-63. doi: 10.1038/sj.bjp.0702283.
Ref 23 Studies examining the relationship between the chemical structure of protoxin II and its activity on voltage gated sodium channels. J Med Chem. 2014 Aug 14;57(15):6623-31. doi: 10.1021/jm500687u. Epub 2014 Jul 24.
Ref 24 Solution structure of Phrixotoxin 1, a specific peptide inhibitor of Kv4 potassium channels from the venom of the theraphosid spider Phrixotrichus auratus. Protein Sci. 2004 May;13(5):1197-208. doi: 10.1110/ps.03584304.
Ref 25 APETx1, a new toxin from the sea anemone Anthopleura elegantissima, blocks voltage-gated human ether-a-go-go-related gene potassium channels. Mol Pharmacol. 2003 Jul;64(1):59-69. doi: 10.1124/mol.64.1.59.
Ref 26 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 27 APETx1 from sea anemone Anthopleura elegantissima is a gating modifier peptide toxin of the human ether-a-go-go- related potassium channel. Mol Pharmacol. 2007 Aug;72(2):259-68. doi: 10.1124/mol.107.035840. Epub 2007 May 1.
Ref 28 A natural point mutation changes both target selectivity and mechanism of action of sea anemone toxins. FASEB J. 2012 Dec;26(12):5141-51. doi: 10.1096/fj.12-218479. Epub 2012 Sep 12.
Ref 29 Development of a rational nomenclature for naming peptide and protein toxins from sea anemones. Toxicon. 2012 Sep 15;60(4):539-50. doi: 10.1016/j.toxicon.2012.05.020. Epub 2012 Jun 5.
Ref 30 Defensin-neurotoxin dyad in a basally branching metazoan sea anemone. FEBS J. 2017 Oct;284(19):3320-3338. doi: 10.1111/febs.14194. Epub 2017 Sep 6.
Ref 31 Solution structure of APETx1 from the sea anemone Anthopleura elegantissima: a new fold for an HERG toxin. Proteins. 2005 May 1;59(2):380-6. doi: 10.1002/prot.20425.
Ref 32 Genomic organization of three neurotoxins active on small conductance Ca2+-activated potassium channels from the scorpion Buthus martensi Karsch. FEBS Lett. 1999 Jun 11;452(3):360-4. doi: 10.1016/s0014-5793(99)00651-1.
Ref 33 Scorpion Toxin, BmP01, Induces Pain by Targeting TRPV1 Channel. Toxins (Basel). 2015 Sep 14;7(9):3671-87. doi: 10.3390/toxins7093671.
Ref 34 Characterization of four toxins from Buthus martensi scorpion venom, which act on apamin-sensitive Ca2+-activated K+ channels. Eur J Biochem. 1997 Apr 15;245(2):457-64. doi: 10.1111/j.1432-1033.1997.00457.x.
Ref 35 Solution structure of BmP01 from the venom of scorpion Buthus martensii Karsch. Biochem Biophys Res Commun. 2000 Oct 5;276(3):1148-54. doi: 10.1006/bbrc.2000.3435.
Ref 36 Molecular diversity and functional evolution of scorpion potassium channel toxins. Mol Cell Proteomics. 2011 Feb;10(2):M110.002832. doi: 10.1074/mcp.M110.002832. Epub 2010 Sep 30.
Ref 37 Molecular diversity of toxic components from the scorpion Heterometrus petersii venom revealed by proteomic and transcriptome analysis. Proteomics. 2010 Jul;10(13):2471-85. doi: 10.1002/pmic.200900763.
Ref 38 Genomic and structural characterization of Kunitz-type peptide LmKTT-1a highlights diversity and evolution of scorpion potassium channel toxins. PLoS One. 2013;8(4):e60201. doi: 10.1371/journal.pone.0060201. Epub 2013 Apr 3.
Ref 39 Purification, molecular cloning and functional characterization of HelaTx1 (Heterometrus laoticus): the first member of a new -KTX subfamily. Biochem Pharmacol. 2012 May 1;83(9):1307-17. doi: 10.1016/j.bcp.2012.01.021. Epub 2012 Jan 24.
Ref 40 A unified nomenclature for short-chain peptides isolated from scorpion venoms: alpha-KTx molecular subfamilies. Trends Pharmacol Sci. 1999 Nov;20(11):444-7. doi: 10.1016/s0165-6147(99)01398-x.
Ref 41 A subfamily of acidic alpha-K(+) toxins. J Biol Chem. 2004 Jan 23;279(4):2781-9. doi: 10.1074/jbc.M311029200. Epub 2003 Oct 14.
Ref 42 Molecular cloning and sequencing of two 'short chain' and two 'long chain' K(+) channel-blocking peptides from the Chinese scorpion Buthus martensii Karsch. FEBS Lett. 1999 Sep 3;457(3):509-14. doi: 10.1016/s0014-5793(99)01101-1.
Ref 43 Solution structure of BmP02, a new potassium channel blocker from the venom of the Chinese scorpion Buthus martensi Karsch. Biochemistry. 2000 Nov 14;39(45):13669-75. doi: 10.1021/bi000860s.
Ref 44 Comparative venom gland transcriptome analysis of the scorpion Lychas mucronatus reveals intraspecific toxic gene diversity and new venomous components. BMC Genomics. 2010 Jul 28;11:452. doi: 10.1186/1471-2164-11-452.
Ref 45 Centipedes subdue giant prey by blocking KCNQ channels. Proc Natl Acad Sci U S A. 2018 Feb 13;115(7):1646-1651. doi: 10.1073/pnas.1714760115. Epub 2018 Jan 22.
Ref 46 Inhibition of Kv2.1 Potassium Channels by MiDCA1, A Pre-Synaptically Active PLA(2)-Type Toxin from Micrurus dumerilii carinicauda Coral Snake Venom. Toxins (Basel). 2019 Jun 12;11(6):335. doi: 10.3390/toxins11060335.
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