General Information of This Target
Target ID
BTDT00149
Target Name
Potassium voltage-gated channel subfamily A member 6 (Kcna6)
Target Bioclass
Transporter and channel
Uniprot ID
Q61923
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
Kcna6
Gene ID
16494
Synonym
MK1.6; Voltage-gated potassium channel subunit Kv1.6
Sequence
MRSEKSLTLAAPGEVRGPEGEQQDAGEFQEAEGGGGCCSSERLVINISGLRFETQLRTLS
LFPDTLLGDPGRRVRFFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFMEE
IRFYQLGEEALAAFREDEGCLPEGGEDEKPLPSQPFQRQVWLLFEYPESSGPARGIAIVS
VLVILISIVIFCLETLPQFRADGRGGSNEGSGTRLSPASRSHEEEDEDEDSYAFPGSIPS
GGLGTGGTSSLSTLGGSFFTDPFFLVETLCIVWFTFELLVRFSACPSKAAFFRNIMNIID
LVAIFPYFITLGTELVQRHEQQSVSGGSGQNGQQAMSLAILRVIRLVRVFRIFKLSRHSK
GLQILGKTLQASMRELGLLIFFLFIGVILFSSAVYFAEADDVDSLFPSIPDAFWWAVVTM
TTVGYGDMYPMTVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEQEEQGQYTHV
TCGQPTPDLKATDNGLGKPDFAEASRERRPSYLPTPHRAYAEKRMLTEV

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Family
the potassium channel family
Function
Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium- selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA6, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel. Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation. Homotetrameric channels display rapid activation and slow inactivation.

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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    Mu-conotoxin GIIIA Inhibition rate . [1- 13]
 Toxin Info    Kappa-theraphotoxin-Sc1a Inhibition rate . [14]
 Toxin Info    Delta-theraphotoxin-Hm1a Inhibition rate
1 %
[14], [15], [16], [17]
 Toxin Info    Kappa-theraphotoxin-Hm2a Inhibition rate
13 %
[14]
 Toxin Info    Mu-conotoxin SIIIA Inhibition rate
54 %
[9- 43]
 Toxin Info    Mu-conotoxin PIIIA Inhibition rate
80 %
[2- 47]
 Toxin Info    Beta-defensin 3 IC50
600 nM
[48]
References
Ref 1 Evolution of separate predation- and defence-evoked venoms in carnivorous cone snails. Nat Commun. 2014 Mar 24;5:3521. doi: 10.1038/ncomms4521.
Ref 2 Definition of the M-conotoxin superfamily: characterization of novel peptides from molluscivorous Conus venoms. Biochemistry. 2005 Jun 7;44(22):8176-86. doi: 10.1021/bi047541b.
Ref 3 The amino acid sequences of homologous hydroxyproline-containing myotoxins from the marine snail Conus geographus venom. FEBS Lett. 1983 May 8;155(2):277-80. doi: 10.1016/0014-5793(82)80620-0.
Ref 4 Disulfide pairings in geographutoxin I, a peptide neurotoxin from Conus geographus. FEBS Lett. 1990 May 7;264(1):29-32. doi: 10.1016/0014-5793(90)80756-9.
Ref 5 Action of derivatives of mu-conotoxin GIIIA on sodium channels. Single amino acid substitutions in the toxin separately affect association and dissociation rates. Biochemistry. 1992 Sep 8;31(35):8229-38. doi: 10.1021/bi00150a016.
Ref 6 Distinction among neuronal subtypes of voltage-activated sodium channels by mu-conotoxin PIIIA. J Neurosci. 2000 Jan 1;20(1):76-80. doi: 10.1523/JNEUROSCI.20-01-00076.2000.
Ref 7 Role of hydroxyprolines in the in vitro oxidative folding and biological activity of conotoxins. Biochemistry. 2008 Feb 12;47(6):1741-51. doi: 10.1021/bi701934m. Epub 2008 Jan 12.
Ref 8 Pruning nature: Biodiversity-derived discovery of novel sodium channel blocking conotoxins from Conus bullatus. Toxicon. 2009 Jan;53(1):90-8. doi: 10.1016/j.toxicon.2008.10.017. Epub 2008 Nov 20.
Ref 9 -Conotoxins that differentially block sodium channels NaV1.1 through 1.8 identify those responsible for action potentials in sciatic nerve. Proc Natl Acad Sci U S A. 2011 Jun 21;108(25):10302-7. doi: 10.1073/pnas.1107027108. Epub 2011 Jun 7.
Ref 10 NMR Structure of -Conotoxin GIIIC: Leucine 18 Induces Local Repacking of the N-Terminus Resulting in Reduced Na(V) Channel Potency. Molecules. 2018 Oct 22;23(10):2715. doi: 10.3390/molecules23102715.
Ref 11 Solution structure of mu-conotoxin GIIIA analysed by 2D-NMR and distance geometry calculations. FEBS Lett. 1991 Jan 28;278(2):160-6. doi: 10.1016/0014-5793(91)80107-e.
Ref 12 Tertiary structure of conotoxin GIIIA in aqueous solution. Biochemistry. 1991 Jul 16;30(28):6908-16. doi: 10.1021/bi00242a014.
Ref 13 Structure-activity relationships of mu-conotoxin GIIIA: structure determination of active and inactive sodium channel blocker peptides by NMR and simulated annealing calculations. Biochemistry. 1992 Dec 22;31(50):12577-84. doi: 10.1021/bi00165a006.
Ref 14 Novel tarantula toxins for subtypes of voltage-dependent potassium channels in the Kv2 and Kv4 subfamilies. Mol Pharmacol. 2002 Jul;62(1):48-57. doi: 10.1124/mol.62.1.48.
Ref 15 Selective spider toxins reveal a role for the Nav1.1 channel in mechanical pain. Nature. 2016 Jun 23;534(7608):494-9. doi: 10.1038/nature17976. Epub 2016 Jun 6.
Ref 16 A selective Na(V)1.1 activator with potential for treatment of Dravet syndrome epilepsy. Biochem Pharmacol. 2020 Nov;181:113991. doi: 10.1016/j.bcp.2020.113991. Epub 2020 Apr 23.
Ref 17 Selective Na(V)1.1 activation rescues Dravet syndrome mice from seizures and premature death. Proc Natl Acad Sci U S A. 2018 Aug 21;115(34):E8077-E8085. doi: 10.1073/pnas.1804764115. Epub 2018 Aug 3.
Ref 18 A novel conotoxin from Conus striatus, mu-SIIIA, selectively blocking rat tetrodotoxin-resistant sodium channels. Toxicon. 2006 Jan;47(1):122-32. doi: 10.1016/j.toxicon.2005.10.008. Epub 2005 Dec 1.
Ref 19 Novel conotoxins from Conus striatus and Conus kinoshitai selectively block TTX-resistant sodium channels. Biochemistry. 2005 May 17;44(19):7259-65. doi: 10.1021/bi0473408.
Ref 20 A Lewis Acid-Controlled Enantiodivergent Epoxidation of Aldehydes. ACS Catal. 2023 Oct 6;13(19):13117-13126. doi: 10.1021/acscatal.3c03929. Epub 2023 Sep 25.
Ref 21 Retraction of "Effect of Fluoride Layer Growth on the Deposition Rate under Different Microchannel Structures". ACS Omega. 2024 Feb 28;9(10):12291. doi: 10.1021/acsomega.4c01652. eCollection 2024 Mar 12.
Ref 22 Retraction of "Assessing the Weathering Performance and Functionality of Nanoparticle-Enhanced High-Pressure Laminates for Building Facade Applications". ACS Omega. 2024 Mar 1;9(10):12290. doi: 10.1021/acsomega.4c01411. eCollection 2024 Mar 12.
Ref 23 Correction to "Digoxin-Mediated Inhibition of Potential Hypoxia-Related Angiogenic Repair in Modulated Electro-Hyperthermia (mEHT)-Treated Murine Triple-Negative Breast Cancer Model". ACS Pharmacol Transl Sci. 2024 Feb 28;7(3):904. doi: 10.1021/acsptsci.4c00094. eCollection 2024 Mar 8.
Ref 24 Correction to 1,2,3-Triazole Tethered Hybrid Capsaicinoids as Antiproliferative Agents Active against Lung Cancer Cells (A549). ACS Omega. 2024 Feb 20;9(9):11026. doi: 10.1021/acsomega.4c00155. eCollection 2024 Mar 5.
Ref 25 Correction to "Dual-Surfactant-Capped Ag Nanoparticles as a Highly Selective and Sensitive Colorimetric Sensor for Citrate Detection". ACS Omega. 2024 Feb 22;9(9):11025. doi: 10.1021/acsomega.3c09929. eCollection 2024 Mar 5.
Ref 26 Colloidal Stability of PFSA-Ionomer Dispersions. Part I. Single-Ion Electrostatic Interaction Potential Energies. Langmuir. 2024 Apr 2;40(13):6654-6665. doi: 10.1021/acs.langmuir.3c03903. Epub 2024 Mar 8.
Ref 27 Correction to "Searching for the Rules of Electrochemical Nitrogen Fixation". ACS Catal. 2024 Feb 14;14(5):3169-3170. doi: 10.1021/acscatal.4c00448. eCollection 2024 Mar 1.
Ref 28 Correction to "Quantification and Mapping of Alkylation in the Human Genome Reveal Single Nucleotide Resolution Precursors of Mutational Signatures". ACS Cent Sci. 2024 Jan 25;10(2):487. doi: 10.1021/acscentsci.3c01597. eCollection 2024 Feb 28.
Ref 29 Correction to "Characterization of Proteins Extracted from Ulva sp., Padina sp., and Laurencia sp. Macroalgae Using Green Technology: Effect of In Vitro Digestion on Antioxidant and ACE-I Inhibitory Activity". ACS Omega. 2024 Feb 16;9(8):9848. doi: 10.1021/acsomega.4c00407. eCollection 2024 Feb 27.
Ref 30 Erratum: Antibacterial Efficacy of ZnO/Bentonite (Clay) Nanocomposites against Multidrug-Resistant Escherichia coli. ACS Omega. 2024 Feb 15;9(8):9847. doi: 10.1021/acsomega.4c00630. eCollection 2024 Feb 27.
Ref 31 Low-Cost Nonfused-Ring Electron Acceptors Enabled by Noncovalent Conformational Locks. Acc Chem Res. 2024 Mar 19;57(6):981-991. doi: 10.1021/acs.accounts.3c00813. Epub 2024 Mar 3.
Ref 32 Retraction of "Hydrogenolysis of Polyethylene and Polypropylene into Propane over Cobalt-Based Catalysts". JACS Au. 2024 Feb 7;4(2):865. doi: 10.1021/jacsau.4c00090. eCollection 2024 Feb 26.
Ref 33 Correction to "Comprehensive Study of Preparation of Carboxy Group-Containing Cellulose Fibers from Dry-Lap Kraft Pulps by Catalytic Oxidation with Solid NaOCl". ACS Sustain Chem Eng. 2024 Feb 6;12(7):2921-2923. doi: 10.1021/acssuschemeng.4c00215. eCollection 2024 Feb 19.
Ref 34 Correction to "Dissolution Behavior of Polycyclic Aromatic Hydrocarbons in Heavy Oil in the Presence of Supercritical Cyclohexane". ACS Omega. 2024 Jan 31;9(6):7269. doi: 10.1021/acsomega.4c00064. eCollection 2024 Feb 13.
Ref 35 Retraction of "Fe(3)O(4) Nanoparticles Grown on Cellulose/GO Hydrogels as Advanced Catalytic Materials for the Heterogeneous Fenton-like Reaction". ACS Omega. 2024 Jan 31;9(6):7270. doi: 10.1021/acsomega.4c00561. eCollection 2024 Feb 13.
Ref 36 Correction to "Ligand Chromophore Modification Approach for Predictive Incremental Tuning of Metal-Organic Framework Color". Chem Mater. 2024 Jan 19;36(3):1773. doi: 10.1021/acs.chemmater.3c03160. eCollection 2024 Feb 13.
Ref 37 Correction to "Electrospun Nanofibrous UV Filters with Bidirectional Actuation Properties Based on Salmon Sperm DNA/Silk Fibroin for Biomedical Applications". ACS Omega. 2024 Jan 25;9(5):6025. doi: 10.1021/acsomega.4c00072. eCollection 2024 Feb 6.
Ref 38 Correction to "Iterative Dual-Metal and Energy Transfer Catalysis Enables Stereodivergence in Alkyne Difunctionalization: Carboboration as Case Study". ACS Catal. 2024 Jan 22;14(3):1976. doi: 10.1021/acscatal.4c00200. eCollection 2024 Feb 2.
Ref 39 Correction to "Nanotechnology Impact on Chemical-Enhanced Oil Recovery: A Review and Bibliometric Analysis of Recent Developments". ACS Omega. 2024 Jan 15;9(4):5083. doi: 10.1021/acsomega.3c10450. eCollection 2024 Jan 30.
Ref 40 Neuronally micro-conotoxins from Conus striatus utilize an alpha-helical motif to target mammalian sodium channels. J Biol Chem. 2008 Aug 1;283(31):21621-8. doi: 10.1074/jbc.M802852200. Epub 2008 Jun 3.
Ref 41 N- and C-terminal extensions of -conotoxins increase potency and selectivity for neuronal sodium channels. Biopolymers. 2012;98(2):161-5. doi: 10.1002/bip.22032. Epub 2012 Feb 10.
Ref 42 A novel -conopeptide, CnIIIC, exerts potent and preferential inhibition of NaV1.2/1.4 channels and blocks neuronal nicotinic acetylcholine receptors. Br J Pharmacol. 2012 Jul;166(5):1654-68. doi: 10.1111/j.1476-5381.2012.01837.x.
Ref 43 Structure, dynamics, and selectivity of the sodium channel blocker mu-conotoxin SIIIA. Biochemistry. 2008 Oct 14;47(41):10940-9. doi: 10.1021/bi801010u. Epub 2008 Sep 18.
Ref 44 mu-Conotoxin PIIIA, a new peptide for discriminating among tetrodotoxin-sensitive Na channel subtypes. J Neurosci. 1998 Jun 15;18(12):4473-81. doi: 10.1523/JNEUROSCI.18-12-04473.1998.
Ref 45 Co-expression of Na(V) subunits alters the kinetics of inhibition of voltage-gated sodium channels by pore-blocking -conotoxins. Br J Pharmacol. 2013 Apr;168(7):1597-610. doi: 10.1111/bph.12051.
Ref 46 Structurally diverse -conotoxin PIIIA isomers block sodium channel NaV 1.4. Angew Chem Int Ed Engl. 2012 Apr 23;51(17):4058-61. doi: 10.1002/anie.201107011. Epub 2012 Mar 12.
Ref 47 Solution structure of mu-conotoxin PIIIA, a preferential inhibitor of persistent tetrodotoxin-sensitive sodium channels. J Biol Chem. 2002 Jul 26;277(30):27247-55. doi: 10.1074/jbc.M201611200. Epub 2002 May 2.
Ref 48 Mouse -Defensin 3, A Defensin Inhibitor of Both Its Endogenous and Exogenous Potassium Channels. Molecules. 2018 Jun 20;23(6):1489. doi: 10.3390/molecules23061489.
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