Target Information

General Information of This Target
Target ID
BTDT00053
Target Name
Potassium voltage-gated channel subfamily C member 1 (Kcnc1)
Target Bioclass
Transporter and channel
Uniprot ID
P15388
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
16502
Synonym
NGK2; Voltage-gated potassium channel subunit Kv3.1; Voltage-gated potassium channel subunit Kv4
Sequence
MGQGDESERIVINVGGTRHQTYRSTLRTLPGTRLAWLAEPDAHSHFDYDPRADEFFFDRH
PGVFAHILNYYRTGKLHCPADVCGPLYEEELAFWGIDETDVEPCCWMTYRQHRDAEEALD
SFGGAPLDNSADDADADGPGDSGDGEDELEMTKRLALSDSPDGRPGGFWRRWQPRIWALF
EDPYSSRYARYVAFASLFFILVSITTFCLETHERFNPIVNKTEIENVRNGTQVRYYREAE
TEAFLTYIEGVCVVWFTFEFLMRVVFCPNKVEFIKNSLNIIDFVAILPFYLEVGLSGLSS
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
10090
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Kingdom: Metazoa
Phylum: Chordata
Class: Mammalia
Order: Rodentia
Family: Muridae
Genus: Mus
Species: Mus musculus
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    OsK1 (E16K,K20D,T36Y) Inhibition rate . [1]
 Toxin Info    OsK1 (E16K) Inhibition rate . [1]
 Toxin Info    Potassium channel toxin ShK ([pTyr][AEEA]) Inhibition rate . [2]
 Toxin Info    Potassium channel toxin ShK (K22[Dap]) Inhibition rate . [3]
 Toxin Info    Toxin II.10.4 (T7P,D9Q) Inhibition rate . [4]
 Toxin Info    OsK1 Inhibition rate . [1]
 Toxin Info    OsK1 (E14A,K18D) Inhibition rate . [5]
 Toxin Info    OsK1 (E15K,K19D) Inhibition rate . [5]
 Toxin Info    Bs6 Inhibition rate . [1]
 Toxin Info    Potassium channel toxin alpha-KTx 3.7 Inhibition rate . [1]
 Toxin Info    OsK1 (E16K,K20D) Inhibition rate . [5]
 Toxin Info    [D20]- OsK1 Inhibition rate . [1]
 Toxin Info    Kappa-stichotoxin-She3a Inhibition rate . [3]
 Toxin Info    Kappa-theraphotoxin-Gr1a Inhibition rate . [6- 12]
References
Ref 1 K+ channel types targeted by synthetic OSK1, a toxin from Orthochirus scrobiculosus scorpion venom. Biochem J. 2005 Jan 1;385(Pt 1):95-104. doi: 10.1042/BJ20041379.
Ref 2 Targeting effector memory T cells with a selective peptide inhibitor of Kv1.3 channels for therapy of autoimmune diseases. Mol Pharmacol. 2005 Apr;67(4):1369-81. doi: 10.1124/mol.104.008193. Epub 2005 Jan 21.
Ref 3 ShK-Dap22, a potent Kv1.3-specific immunosuppressive polypeptide. J Biol Chem. 1998 Dec 4;273(49):32697-707. doi: 10.1074/jbc.273.49.32697.
Ref 4 Cobatoxin 1 from Centruroides noxius scorpion venom: chemical synthesis, three-dimensional structure in solution, pharmacology and docking on K+ channels. Biochem J. 2004 Jan 1;377(Pt 1):37-49. doi: 10.1042/BJ20030977.
Ref 5 Pharmacological profiling of Orthochirus scrobiculosus toxin 1 analogs with a trimmed N-terminal domain. Mol Pharmacol. 2006 Jan;69(1):354-62. doi: 10.1124/mol.105.017210. Epub 2005 Oct 18.
Ref 6 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 7 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 8 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 9 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 10 Voltage-sensor activation with a tarantula toxin as cargo. Nature. 2005 Aug 11;436(7052):857-60. doi: 10.1038/nature03873.
Ref 11 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 12 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.
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