Target Information

General Information of This Target
Target ID
BTDT00095
Target Name
Potassium voltage-gated channel subfamily C member 1 (KCNC1)
Target Bioclass
Transporter and channel
Uniprot ID
P48547
3D Structure
Download
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
KCNC1
Gene ID
3746
Synonym
NGK2; Voltage-gated potassium channel subunit Kv3.1; Voltage-gated potassium channel subunit Kv4
Sequence
MGQGDESERIVINVGGTRHQTYRSTLRTLPGTRLAWLAEPDAHSHFDYDPRADEFFFDRH
PGVFAHILNYYRTGKLHCPADVCGPLYEEELAFWGIDETDVEPCCWMTYRQHRDAEEALD
SFGGAPLDNSADDADADGPGDSGDGEDELEMTKRLALSDSPDGRPGGFWRRWQPRIWALF
EDPYSSRYARYVAFASLFFILVSITTFCLETHERFNPIVNKTEIENVRNGTQVRYYREAE
TEAFLTYIEGVCVVWFTFEFLMRVIFCPNKVEFIKNSLNIIDFVAILPFYLEVGLSGLSS
KAAKDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFA
TMIYYAERIGAQPNDPSASEHTHFKNIPIGFWWAVVTMTTLGYGDMYPQTWSGMLVGALC
ALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPKKKKKHIPRPPQLGSPNYCKSVVNSPH
HSTQSDTCPLAQEEILEINRAGRKPLRGMSI

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Family
the potassium channel family
Function
Voltage-gated potassium channel that plays an important role in the rapid repolarization of fast-firing brain neurons. The channel opens in response to the voltage difference across the membrane, forming a potassium-selective channel through which potassium ions pass in accordance with their electrochemical gradient. Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNC2, and possibly other family members as well. Contributes to fire sustained trains of very brief action potentials at high frequency in pallidal neurons.

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Taxonomy ID
9606
TCDB ID
1.A.1.2.24
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Kingdom: Metazoa
Phylum: Chordata
Class: Mammalia
Order: Primates
Family: Hominidae
Genus: Homo
Species: Homo sapiens
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    N.vectensis toxin 4 Effect . [1]
 Toxin Info    N.vectensis toxin 5 Effect . [1]
 Toxin Info    Crotamine Inhibition rate . [2]
 Toxin Info    Kappa-actitoxin-Bgr1a Inhibition rate . [3]
 Toxin Info    Potassium channel toxin alpha-KTx 3.13 Inhibition rate . [4]
 Toxin Info    Toxin PhcrTx2 Inhibition rate . [5]
 Toxin Info    Kappa-LhTx-1 Inhibition rate . [6]
 Toxin Info    Kappa-actitoxin-Bcs4a Inhibition rate . [7]
 Toxin Info    Potassium channel toxin AbeTx1 Inhibition rate . [8]
 Toxin Info    Potassium channel toxin alpha-KTx 8.8 Inhibition rate . [9]
 Toxin Info    Potassium channel toxin epsilon-KTx 1.1 Inhibition rate . [10]
 Toxin Info    Potassium channel toxin epsilon-KTx 1.2 Inhibition rate . [10]
 Toxin Info    U-actitoxin-Oulsp1 Inhibition rate . [11]
 Toxin Info    Potassium channel toxin AbeTx1 Inhibition rate . [8]
 Toxin Info    Pi-stichotoxin-Hcr5b Inhibition rate . [12]
 Toxin Info    Apamin Inhibition rate . [13- 30]
 Toxin Info    Kappa-actitoxin-Ate1a Inhibition rate . [31]
 Toxin Info    Potassium channel toxin alpha-KTx 3.6 Inhibition rate . [4]
 Toxin Info    Potassium channel toxin alpha-KTx 21.1 Inhibition rate . [32- 36]
 Toxin Info    Potassium channel toxin alpha-KTx 16.2 Inhibition rate . [37]
 Toxin Info    Potassium channel toxin alpha-KTx 21.1 Inhibition rate
5 %
 [34]
References
Ref 1 The Birth and Death of Toxins with Distinct Functions: A Case Study in the Sea Anemone Nematostella. Mol Biol Evol. 2019 Sep 1;36(9):2001-2012. doi: 10.1093/molbev/msz132.
Ref 2 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 3 A potassium-channel toxin from the sea anemone Bunodosoma granulifera, an inhibitor for Kv1 channels. Revision of the amino acid sequence, disulfide-bridge assignment, chemical synthesis, and biological activity. Eur J Biochem. 1997 Feb 15;244(1):192-202. doi: 10.1111/j.1432-1033.1997.00192.x.
Ref 4 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 5 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 6 Variation of Two S3b Residues in K(V)4.1-4.3 Channels Underlies Their Different Modulations by Spider Toxin -LhTx-1. Front Pharmacol. 2021 Jun 10;12:692076. doi: 10.3389/fphar.2021.692076. eCollection 2021.
Ref 7 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 8 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 9 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 10 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 11 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 12 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 13 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 14 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 15 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 16 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 17 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 18 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 19 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 20 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 21 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 22 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 23 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 24 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 25 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 26 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 27 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 28 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 29 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 30 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 31 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 32 Proteomic endorsed transcriptomic profiles of venom glands from Tityus obscurus and T. serrulatus scorpions. PLoS One. 2018 Mar 21;13(3):e0193739. doi: 10.1371/journal.pone.0193739. eCollection 2018.
Ref 33 Novel components of Tityus serrulatus venom: A transcriptomic approach. Toxicon. 2021 Jan 15;189:91-104. doi: 10.1016/j.toxicon.2020.11.001. Epub 2020 Nov 10.
Ref 34 Purification and characterization of Ts15, the first member of a new -KTX subfamily from the venom of the Brazilian scorpion Tityus serrulatus. Toxicon. 2011 Jul;58(1):54-61. doi: 10.1016/j.toxicon.2011.05.001. Epub 2011 May 13.
Ref 35 Moving pieces in a venomic puzzle: unveiling post-translationally modified toxins from Tityus serrulatus. J Proteome Res. 2013 Jul 5;12(7):3460-70. doi: 10.1021/pr4003068. Epub 2013 Jun 13.
Ref 36 Influence of post-starvation extraction time and prey-specific diet in Tityus serrulatus scorpion venom composition and hyaluronidase activity. Toxicon. 2014 Nov;90:326-36. doi: 10.1016/j.toxicon.2014.08.064. Epub 2014 Sep 6.
Ref 37 Recombinant expression and functional characterization of martentoxin: a selective inhibitor for BK channel ( + 4). Toxins (Basel). 2014 Apr 22;6(4):1419-33. doi: 10.3390/toxins6041419.
Ref 38 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 39 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.
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