Target Information

General Information of This Target
Target ID
BTDT00072
Target Name
Potassium voltage-gated channel subfamily C member 1 (Kcnc1)
Target Bioclass
Transporter and channel
Uniprot ID
P25122
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
Kcnc1
Gene ID
25327
Synonym
NGK2; RAW2; Voltage-gated potassium channel subunit Kv3.1; Voltage-gated potassium channel subunit Kv4
Sequence
MGQGDESERIVINVGGTRHQTYRSTLRTLPGTRLAWLAEPDAHSHFDYDPRADEFFFDRH
PGVFAHILNYYRTGKLHCPADVCGPLYEEELAFWGIDETDVEPCCWMTYRQHRDAEEALD
SFGGAPLDNSADDADADGPGDSGDGEDELEMTKRLALSDSPDGRPGGFWRRWQPRIWALF
EDPYSSRYARYVAFASLFFILVSITTFCLETHERFNPIVNKTEIENVRNGTQVRYYREAE
TEAFLTYIEGVCVVWFTFEFLMRVVFCPNKVEFIKNSLNIIDFVAILPFYLEVGLSGLSS
KAAKDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFA
TMIYYAERIGAQPNDPSASEHTHFKNIPIGFWWAVVTMTTLGYGDMYPQTWSGMLVGALC
ALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPKKKKKHIPRPPQLGSPNYCKSVVNSPH
HSTQSDTCPLAQEEILEINRADSKLNGEVAKAALANEDCPHIDQALTPDEGLPFTRSGTR
ERYGPCFLLSTGEYACPPGGGMRKDLCKESPVIAKYMPTEAVRVT

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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
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    Kappa-actitoxin-Bcs3a Inhibition rate . [1]
 Toxin Info    Kappa-actitoxin-Bcs3b Inhibition rate . [1]
 Toxin Info    Kunitz-type conkunitzin-S1 Inhibition rate . [2], [3], [4]
 Toxin Info    Kunitz-type serine protease inhibitor homolog alpha-dendrotoxin Inhibition rate . [5]
 Toxin Info    Potassium channel toxin alpha-KTx 1.16 Inhibition rate . [6]
 Toxin Info    Potassium channel toxin alpha-KTx 1.17 Inhibition rate . [6]
 Toxin Info    Potassium channel toxin alpha-KTx 12.2 Inhibition rate . [7]
 Toxin Info    Mu-theraphotoxin-Pspp1 Inhibition rate . [8]
 Toxin Info    Potassium channel toxin alpha-KTx 4.1 Inhibition rate . [7]
 Toxin Info    Potassium channel toxin kappa-KTx 2.5 Inhibition rate . [9]
 Toxin Info    Potassium channel toxin TsTXK-beta Inhibition rate . [10]
 Toxin Info    U-actitoxin-Oulsp1 Inhibition rate . [11]
 Toxin Info    Potassium channel toxin alpha-KTx 12.1 Inhibition rate . [7]
 Toxin Info    APETx2 Inhibition rate . [12- 21]
 Toxin Info    KappaPI-actitoxin-Ael3a Inhibition rate . [22], [23]
 Toxin Info    APETx2 Inhibition rate . [12- 21]
References
Ref 1 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 2 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 3 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 4 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 5 Characterization of a Shaw-related potassium channel family in rat brain. EMBO J. 1992 Jul;11(7):2473-86. doi: 10.1002/j.1460-2075.1992.tb05312.x.
Ref 6 K(V)1.2 channel-specific blocker from Mesobuthus eupeus scorpion venom: Structural basis of selectivity. Neuropharmacology. 2018 Dec;143:228-238. doi: 10.1016/j.neuropharm.2018.09.030. Epub 2018 Sep 22.
Ref 7 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 8 Chemical Synthesis, Proper Folding, Na(v) Channel Selectivity Profile and Analgesic Properties of the Spider Peptide Phlotoxin 1. Toxins (Basel). 2019 Jun 21;11(6):367. doi: 10.3390/toxins11060367.
Ref 9 The new kappa-KTx 2.5 from the scorpion Opisthacanthus cayaporum. Peptides. 2011 Jul;32(7):1509-17. doi: 10.1016/j.peptides.2011.05.017. Epub 2011 May 23.
Ref 10 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 11 Structure, folding and stability of a minimal homologue from Anemonia sulcata of the sea anemone potassium channel blocker ShK. Peptides. 2018 Jan;99:169-178. doi: 10.1016/j.peptides.2017.10.001. Epub 2017 Oct 6.
Ref 12 A new sea anemone peptide, APETx2, inhibits ASIC3, a major acid-sensitive channel in sensory neurons. EMBO J. 2004 Apr 7;23(7):1516-25. doi: 10.1038/sj.emboj.7600177. Epub 2004 Mar 25.
Ref 13 ASIC3, a sensor of acidic and primary inflammatory pain. EMBO J. 2008 Nov 19;27(22):3047-55. doi: 10.1038/emboj.2008.213. Epub 2008 Oct 16.
Ref 14 Chemical synthesis and folding of APETx2, a potent and selective inhibitor of acid sensing ion channel 3. Toxicon. 2009 Jul;54(1):56-61. doi: 10.1016/j.toxicon.2009.03.014. Epub 2009 Mar 21.
Ref 15 Expression in Pichia pastoris and characterization of APETx2, a specific inhibitor of acid sensing ion channel 3. Toxicon. 2010 Dec;56(8):1388-97. doi: 10.1016/j.toxicon.2010.08.004. Epub 2010 Sep 9.
Ref 16 Inhibition of voltage-gated Na(+) currents in sensory neurones by the sea anemone toxin APETx2. Br J Pharmacol. 2012 Apr;165(7):2167-77. doi: 10.1111/j.1476-5381.2011.01674.x.
Ref 17 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 18 Cyclisation increases the stability of the sea anemone peptide APETx2 but decreases its activity at acid-sensing ion channel 3. Mar Drugs. 2012 Jul;10(7):1511-1527. doi: 10.3390/md10071511. Epub 2012 Jul 16.
Ref 19 Functional expression in Escherichia coli of the disulfide-rich sea anemone peptide APETx2, a potent blocker of acid-sensing ion channel 3. Mar Drugs. 2012 Jul;10(7):1605-1618. doi: 10.3390/md10071605. Epub 2012 Jul 23.
Ref 20 Solution structure of APETx2, a specific peptide inhibitor of ASIC3 proton-gated channels. Protein Sci. 2005 Aug;14(8):2003-10. doi: 10.1110/ps.051378905. Epub 2005 Jun 29.
Ref 21 Understanding the molecular basis of toxin promiscuity: the analgesic sea anemone peptide APETx2 interacts with acid-sensing ion channel 3 and hERG channels via overlapping pharmacophores. J Med Chem. 2014 Nov 13;57(21):9195-203. doi: 10.1021/jm501400p. Epub 2014 Nov 4.
Ref 22 A bifunctional sea anemone peptide with Kunitz type protease and potassium channel inhibiting properties. Biochem Pharmacol. 2011 Jul 1;82(1):81-90. doi: 10.1016/j.bcp.2011.03.023. Epub 2011 Apr 6.
Ref 23 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.
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