Target Information

General Information of This Target
Target ID
BTDT00128
Target Name
Potassium voltage-gated channel subfamily C member 4 (KCNC4)
Target Bioclass
Transporter and channel
Uniprot ID
Q03721
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
KCNC4
Gene ID
3749
Synonym
KSHIIIC; Voltage-gated potassium channel subunit Kv3.4
Sequence
MISSVCVSSYRGRKSGNKPPSKTCLKEEMAKGEASEKIIINVGGTRHETYRSTLRTLPGT
RLAWLADPDGGGRPETDGGGVGSSGSSGGGGCEFFFDRHPGVFAYVLNYYRTGKLHCPAD
VCGPLFEEELTFWGIDETDVEPCCWMTYRQHRDAEEALDIFESPDGGGSGAGPSDEAGDD
ERELALQRLGPHEGGAGHGAGSGGCRGWQPRMWALFEDPYSSRAARVVAFASLFFILVSI
TTFCLETHEAFNIDRNVTEILRVGNITSVHFRREVETEPILTYIEGVCVLWFTLEFLVRI
VCCPDTLDFVKNLLNIIDFVAILPFYLEVGLSGLSSKAARDVLGFLRVVRFVRILRIFKL
TRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERIGARPSDPRGNDHTDF
KNIPIGFWWAVVTMTTLGYGDMYPKTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYS
LAMAKQKLPKKRKKHVPRPAQLESPMYCKSEETSPRDSTCSDTSPPAREEGMIERKRADS
KQNGDANAVLSDEEGAGLTQPLASSPTPEERRALRRSTTRDRNKKAAACFLLSTGDYACA
DGSVRKGTFVLRDLPLQHSPEAACPPTAGTLFLPH

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Family
the potassium channel family
Function
This protein mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.

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Taxonomy ID
9606
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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    Kappa-LhTx-1 Inhibition rate . [1]
 Toxin Info    Kappa-HfTx2 (C1G,T2Y,A3G,S4Y,K5T,Q6S,C7N,W8A) Inhibition rate . [2]
 Toxin Info    Tamapin Inhibition rate
3 %
 [2]
 Toxin Info    Fungal defensin plectasin Inhibition rate
5 %
 [2]
 Toxin Info    Delta/kappa-actitoxin-Avd4a Inhibition rate
65 %
 [3- 8]
References
Ref 1 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 2 Synthesis and Pharmacological Evaluation of a Novel Peptide Based on Anemonia sulcata BDS-I Toxin as a New K(V)3.4 Inhibitor Exerting a Neuroprotective Effect Against Amyloid- Peptide. Front Chem. 2019 Jul 9;7:479. doi: 10.3389/fchem.2019.00479. eCollection 2019.
Ref 3 Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3.4. J Biol Chem. 1998 Mar 20;273(12):6744-9. doi: 10.1074/jbc.273.12.6744.
Ref 4 Modulation of Kv3 subfamily potassium currents by the sea anemone toxin BDS: significance for CNS and biophysical studies. J Neurosci. 2005 Sep 21;25(38):8735-45. doi: 10.1523/JNEUROSCI.2119-05.2005.
Ref 5 Modulation of neuronal sodium channels by the sea anemone peptide BDS-I. J Neurophysiol. 2012 Jun;107(11):3155-67. doi: 10.1152/jn.00785.2011. Epub 2012 Mar 21.
Ref 6 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 7 A proton nuclear magnetic resonance study of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: sequential and stereospecific resonance assignment and secondary structure. Biochemistry. 1989 Mar 7;28(5):2178-87. doi: 10.1021/bi00431a032.
Ref 8 Determination of the three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing. Biochemistry. 1989 Mar 7;28(5):2188-98. doi: 10.1021/bi00431a033.
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