Target Information

General Information of This Target
Target ID
BTDT10248
Target Name
Shaker-IR
Target Bioclass
Transporter and channel
Taxonomy ID
7227
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Kingdom: Metazoa
Phylum: Arthropoda
Class: Insecta
Order: Diptera
Family: Drosophilidae
Genus: Drosophila
Species: Drosophila melanogaster
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    SVSP (H43R) Inhibition rate . [1]
 Toxin Info    Defensin-like protein 1 Inhibition rate . [2]
 Toxin Info    Beta/kappa-theraphotoxin-Gi1a Inhibition rate . [3]
 Toxin Info    Crotamine Inhibition rate . [4]
 Toxin Info    Potassium channel toxin alpha-KTx 1.11 Inhibition rate . [5]
 Toxin Info    Toxin PhcrTx2 Inhibition rate . [6]
 Toxin Info    U-Asilidin(12)-Dg3b Inhibition rate . [7], [8]
 Toxin Info    Potassium channel toxin alpha-KTx 10.4 Inhibition rate . [9]
 Toxin Info    Potassium channel toxin alpha-KTx 2.16 Inhibition rate . [9]
 Toxin Info    Potassium channel toxin alpha-KTx 2.17 Inhibition rate . [9]
 Toxin Info    Potassium channel toxin alpha-KTx 8.8 Inhibition rate . [10]
 Toxin Info    Potassium channel toxin TsTXK-beta Inhibition rate . [11]
 Toxin Info    Thrombin-like enzyme collinein-1 Inhibition rate . [1- 14]
 Toxin Info    Apamin Inhibition rate . [15- 32]
 Toxin Info    Neurotoxin beta-KTx 14.3 Inhibition rate . [33]
 Toxin Info    U-actitoxin-Oulsp1 Inhibition rate . [34]
 Toxin Info    Potassium channel gamma toxin gamma-KTx 1.9 Inhibition rate . [9]
 Toxin Info    Plant antimicrobial peptide domain-containing protein_Q2D_K3D_K6Y_Q7R_R18K_R19K_K23E Inhibition rate . [35]
 Toxin Info    Potassium channel toxin alpha-KTx (N30P) Inhibition rate
10 %
 [36]
 Toxin Info    Potassium channel toxin epsilon-KTx 1.1 Inhibition rate
10 %
 [37]
 Toxin Info    Pi-stichotoxin-Hcr5b Inhibition rate
10 %
 [38]
 Toxin Info    Potassium channel toxin AbeTx1 Inhibition rate
15 %
 [39]
 Toxin Info    Potassium channel toxin alpha-KTx 3.13 Inhibition rate
19 %
 [40]
 Toxin Info    Kappa-actitoxin-Ate1a Inhibition rate
23 %
 [41]
 Toxin Info    Potassium channel toxin epsilon-KTx 1.2 Inhibition rate
27 %
 [37]
 Toxin Info    Potassium channel toxin MeuTXKalpha3 Inhibition rate
28 %
 [36]
 Toxin Info    Scorpine Inhibition rate
36 %
 [42]
 Toxin Info    Potassium channel toxin alpha-KTx 19.2 Inhibition rate
65 %
 [43]
 Toxin Info    Potassium channel toxin alpha-KTx 31.1 Inhibition rate
100 %
 [44]
 Toxin Info    Mesomartoxin IC50
0.054 nM
 [45]
 Toxin Info    Kunitz-type conkunitzin-S1 IC50
0.95 nM
 [46], [47], [48]
 Toxin Info    Potassium channel toxin alpha-KTx 2.15 IC50
22 nM
 [9]
 Toxin Info    Kappa-actitoxin-Bcs3b IC50
49.14 nM
 [49]
 Toxin Info    Kappa-actitoxin-Bcs4a IC50
94.25 nM
 [50]
 Toxin Info    PI-stichotoxin-Hcr2g IC50
114.9 nM
 [51]
 Toxin Info    Kappa-actitoxin-Bcs3a IC50
247.69 nM
 [49]
 Toxin Info    PI-stichotoxin-Hcr2f IC50
433.1 nM
 [51]
 Toxin Info    Conotoxin AsXIVA IC50
824 nM
 [52]
 Toxin Info    Kappa-theraphotoxin-Gr1a IC50
6 μM
 [53- 59]
References
Ref 1 Beyond hemostasis: a snake venom serine protease with potassium channel blocking and potential antitumor activities. Sci Rep. 2020 Mar 11;10(1):4476. doi: 10.1038/s41598-020-61258-x.
Ref 2 The antifungal plant defensin AtPDF2.3 from Arabidopsis thaliana blocks potassium channels. Sci Rep. 2016 Aug 30;6:32121. doi: 10.1038/srep32121.
Ref 3 GiTx1(/-theraphotoxin-Gi1a), a novel toxin from the venom of Brazilian tarantula Grammostola iheringi (Mygalomorphae, Theraphosidae): Isolation, structural assessments and activity on voltage-gated ion channels. Biochimie. 2020 Sep;176:138-149. doi: 10.1016/j.biochi.2020.07.008. Epub 2020 Jul 24.
Ref 4 Crotamine pharmacology revisited: novel insights based on the inhibition of KV channels. Mol Pharmacol. 2012 Jul;82(1):90-6. doi: 10.1124/mol.112.078188. Epub 2012 Apr 12.
Ref 5 Slotoxin, alphaKTx1.11, a new scorpion peptide blocker of MaxiK channels that differentiates between alpha and alpha+beta (beta1 or beta4) complexes. FEBS Lett. 2001 Sep 21;505(3):369-73. doi: 10.1016/s0014-5793(01)02791-0.
Ref 6 PhcrTx2, a New Crab-Paralyzing Peptide Toxin from the Sea Anemone Phymanthus crucifer. Toxins (Basel). 2018 Feb 7;10(2):72. doi: 10.3390/toxins10020072.
Ref 7 Buzz Kill: Function and Proteomic Composition of Venom from the Giant Assassin Fly Dolopus genitalis (Diptera: Asilidae). Toxins (Basel). 2018 Nov 5;10(11):456. doi: 10.3390/toxins10110456.
Ref 8 Weaponisation 'on the fly': Convergent recruitment of knottin and defensin peptide scaffolds into the venom of predatory assassin flies. Insect Biochem Mol Biol. 2020 Mar;118:103310. doi: 10.1016/j.ibmb.2019.103310. Epub 2019 Dec 21.
Ref 9 Isolation, chemical and functional characterization of several new K(+)-channel blocking peptides from the venom of the scorpion Centruroides tecomanus. Toxicon. 2016 Jun 1;115:1-12. doi: 10.1016/j.toxicon.2016.02.017. Epub 2016 Feb 26.
Ref 10 C-Terminal residues in small potassium channel blockers OdK1 and OSK3 from scorpion venom fine-tune the selectivity. Biochim Biophys Acta Proteins Proteom. 2017 May;1865(5):465-472. doi: 10.1016/j.bbapap.2017.02.001. Epub 2017 Feb 4.
Ref 11 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 12 Expression of a new serine protease from Crotalus durissus collilineatus venom in Pichia pastoris and functional comparison with the native enzyme. Appl Microbiol Biotechnol. 2015 Dec;99(23):9971-86. doi: 10.1007/s00253-015-6836-2. Epub 2015 Jul 31.
Ref 13 Functional and biological insights of rCollinein-1, a recombinant serine protease from Crotalus durissus collilineatus. J Venom Anim Toxins Incl Trop Dis. 2019 Apr 8;25:e147118. doi: 10.1590/1678-9199-JVATITD-1471-18. eCollection 2019.
Ref 14 Towards toxin PEGylation: The example of rCollinein-1, a snake venom thrombin-like enzyme, as a PEGylated biopharmaceutical prototype. Int J Biol Macromol. 2021 Nov 1;190:564-573. doi: 10.1016/j.ijbiomac.2021.09.004. Epub 2021 Sep 7.
Ref 15 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 16 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 17 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 18 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 19 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 20 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 21 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 22 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 23 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 24 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 25 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 26 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 27 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 28 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 29 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 30 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 31 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 32 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 33 Beta-KTx14.3, a scorpion toxin, blocks the human potassium channel KCNQ1. Biochim Biophys Acta Proteins Proteom. 2023 Jul 1;1871(4):140906. doi: 10.1016/j.bbapap.2023.140906. Epub 2023 Mar 12.
Ref 34 Sunanda, Punnepalli, et al. "Identification, chemical synthesis, structure, and function of a new KV1 channel blocking peptide from Oulactis sp." Peptide Science 110.4 (2018): e24073.
Ref 35 Structural similarity between defense peptide from wheat and scorpion neurotoxin permits rational functional design. J Biol Chem. 2014 May 16;289(20):14331-40. doi: 10.1074/jbc.M113.530477. Epub 2014 Mar 26.
Ref 36 A single-point mutation enhances dual functionality of a scorpion toxin. Comp Biochem Physiol C Toxicol Pharmacol. 2016 Jan;179:72-8. doi: 10.1016/j.cbpc.2015.09.002. Epub 2015 Sep 7.
Ref 37 Structural and Functional Elucidation of Peptide Ts11 Shows Evidence of a Novel Subfamily of Scorpion Venom Toxins. Toxins (Basel). 2016 Sep 30;8(10):288. doi: 10.3390/toxins8100288.
Ref 38 A Tale of Toxin Promiscuity: The Versatile Pharmacological Effects of Hcr 1b-2 Sea Anemone Peptide on Voltage-Gated Ion Channels. Mar Drugs. 2022 Feb 17;20(2):147. doi: 10.3390/md20020147.
Ref 39 AbeTx1 Is a Novel Sea Anemone Toxin with a Dual Mechanism of Action on Shaker-Type K? Channels Activation. Mar Drugs. 2018 Oct 1;16(10):360. doi: 10.3390/md16100360.
Ref 40 A potent potassium channel blocker from Mesobuthus eupeus scorpion venom. Biochimie. 2010 Dec;92(12):1847-53. doi: 10.1016/j.biochi.2010.08.003. Epub 2010 Aug 14.
Ref 41 PHAB toxins: a unique family of predatory sea anemone toxins evolving via intra-gene concerted evolution defines a new peptide fold. Cell Mol Life Sci. 2018 Dec;75(24):4511-4524. doi: 10.1007/s00018-018-2897-6. Epub 2018 Aug 14.
Ref 42 Structural and functional studies of scorpine: A channel blocker and cytolytic peptide. Toxicon. 2023 Jan 15;222:106985. doi: 10.1016/j.toxicon.2022.106985. Epub 2022 Nov 24.
Ref 43 Characterization of Kbot21 Reveals Novel Side Chain Interactions of Scorpion Toxins Inhibiting Voltage-Gated Potassium Channels. PLoS One. 2015 Sep 23;10(9):e0137611. doi: 10.1371/journal.pone.0137611. eCollection 2015.
Ref 44 Kbot55, purified from Buthus occitanus tunetanus venom, represents the first member of a novel -KTx subfamily. Peptides. 2016 Jun;80:4-8. doi: 10.1016/j.peptides.2015.05.015. Epub 2015 Jun 14.
Ref 45 Mesomartoxin, a new K(v)1.2-selective scorpion toxin interacting with the channel selectivity filter. Biochem Pharmacol. 2015 Jan 15;93(2):232-9. doi: 10.1016/j.bcp.2014.12.002. Epub 2014 Dec 13.
Ref 46 Production of recombinant Conkunitzin-S1 in Escherichia coli. Protein Expr Purif. 2006 Jun;47(2):640-4. doi: 10.1016/j.pep.2006.01.019. Epub 2006 Feb 20.
Ref 47 Conkunitzin-S1 is the first member of a new Kunitz-type neurotoxin family. Structural and functional characterization. J Biol Chem. 2005 Jun 24;280(25):23766-70. doi: 10.1074/jbc.C500064200. Epub 2005 Apr 15.
Ref 48 Structure of conkunitzin-S1, a neurotoxin and Kunitz-fold disulfide variant from cone snail. Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):980-90. doi: 10.1107/S0907444906021123. Epub 2006 Aug 19.
Ref 49 Biochemical and electrophysiological characterization of two sea anemone type 1 potassium toxins from a geographically distant population of Bunodosoma caissarum. Mar Drugs. 2013 Mar 6;11(3):655-79. doi: 10.3390/md11030655.
Ref 50 BcsTx3 is a founder of a novel sea anemone toxin family of potassium channel blocker. FEBS J. 2013 Oct;280(19):4839-52. doi: 10.1111/febs.12456. Epub 2013 Aug 23.
Ref 51 Kunitz-Type Peptides from the Sea Anemone Heteractis crispa Demonstrate Potassium Channel Blocking and Anti-Inflammatory Activities. Biomedicines. 2020 Nov 4;8(11):473. doi: 10.3390/biomedicines8110473.
Ref 52 Efficient enzymatic cyclization of an inhibitory cystine knot-containing peptide. Biotechnol Bioeng. 2016 Oct;113(10):2202-12. doi: 10.1002/bit.25993. Epub 2016 Aug 9.
Ref 53 An inhibitor of the Kv2.1 potassium channel isolated from the venom of a Chilean tarantula. Neuron. 1995 Oct;15(4):941-9. doi: 10.1016/0896-6273(95)90184-1.
Ref 54 Hanatoxin modifies the gating of a voltage-dependent K+ channel through multiple binding sites. Neuron. 1997 Apr;18(4):665-73. doi: 10.1016/s0896-6273(00)80306-2.
Ref 55 Mapping the receptor site for hanatoxin, a gating modifier of voltage-dependent K+ channels. Neuron. 1997 Apr;18(4):675-82. doi: 10.1016/s0896-6273(00)80307-4.
Ref 56 Gating modifier toxins reveal a conserved structural motif in voltage-gated Ca2+ and K+ channels. Proc Natl Acad Sci U S A. 1998 Jul 21;95(15):8585-9. doi: 10.1073/pnas.95.15.8585.
Ref 57 Voltage-sensor activation with a tarantula toxin as cargo. Nature. 2005 Aug 11;436(7052):857-60. doi: 10.1038/nature03873.
Ref 58 Gating modifier peptides as probes of pancreatic beta-cell physiology. Toxicon. 2007 Feb;49(2):231-8. doi: 10.1016/j.toxicon.2006.09.012. Epub 2006 Sep 23.
Ref 59 Solution structure of hanatoxin1, a gating modifier of voltage-dependent K(+) channels: common surface features of gating modifier toxins. J Mol Biol. 2000 Mar 31;297(3):771-80. doi: 10.1006/jmbi.2000.3609.
Ref 60 Experimental conversion of a defensin into a neurotoxin: implications for origin of toxic function. Mol Biol Evol. 2014 Mar;31(3):546-59. doi: 10.1093/molbev/msu038. Epub 2014 Jan 14.
Ref 61 First report on BaltCRP, a cysteine-rich secretory protein (CRISP) from Bothrops alternatus venom: Effects on potassium channels and inflammatory processes. Int J Biol Macromol. 2019 Nov 1;140:556-567. doi: 10.1016/j.ijbiomac.2019.08.108. Epub 2019 Aug 14.
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