Target Information

General Information of This Target
Target ID
BTDT00185
Target Name
Potassium voltage-gated channel subfamily H member 6 (KCNH6)
Target Bioclass
Transporter and channel
Uniprot ID
Q9H252
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
KCNH6
Gene ID
81033
Synonym
ERG2; Ether-a-go-go-related gene potassium channel 2; Voltage-gated potassium channel subunit Kv11.2
Sequence
MPVRRGHVAPQNTYLDTIIRKFEGQSRKFLIANAQMENCAIIYCNDGFCELFGYSRVEVM
QQPCTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDG
AVIMFILNFEDLAQLLAKCSSRSLSQRLLSQSFLGSEGSHGRPGGPGPGTGRGKYRTISQ
IPQFTLNFVEFNLEKHRSSSTTEIEIIAPHKVVERTQNVTEKVTQVLSLGADVLPEYKLQ
APRIHRWTILHYSPFKAVWDWLILLLVIYTAVFTPYSAAFLLSDQDESRRGACSYTCSPL
TVVDLIVDIMFVVDIVINFRTTYVNTNDEVVSHPRRIAVHYFKGWFLIDMVAAIPFDLLI
FRTGSDETTTLIGLLKTARLLRLVRVARKLDRYSEYGAAVLFLLMCTFALIAHWLACIWY
AIGNVERPYLEHKIGWLDSLGVQLGKRYNGSDPASGPSVQDKYVTALYFTFSSLTSVGFG
NVSPNTNSEKVFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVKEFIRFHQ
IPNPLRQRLEEYFQHAWSYTNGIDMNAVLKGFPECLQADICLHLHRALLQHCPAFSGAGK
GCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILRDDVVVAILGKNDIFGEP
VSLHAQPGKSSADVRALTYCDLHKIQRADLLEVLDMYPAFAESFWSKLEVTFNLRDAAGG
LHSSPRQAPGSQDHQGFFLSDNQSGSPHELGPQFPSKGYSLLGPGSQNSMGAGPCAPGHP
DAAPPLSISDASGLWPELLQEMPPRHSPQSPQEDPDCWPLKLGSRLEQLQAQMNRLESRV
SSDLSRILQLLQKPMPQGHASYILEAPASNDLALVPIASETTSPGPRLPQGFLPPAQTPS
YGDLDDCSPKHRNSSPRMPHLAVATDKTLAPSSEQEQPEGLWPPLASPLHPLEVQGLICG
PCFSSLPEHLGSVPKQLDFQRHGSDPGFAGSWGH

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Family
the potassium channel family
Function
Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits a slowly activating, rectifying current. Channel properties may be modulated by cAMP and subunit assembly.

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Taxonomy ID
9606
        Click to Show/Hide the Complete Species Lineage
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    Potassium channel toxin gamma-KTx 2.1 Dissociation constant
77 nM
 [1]
 Toxin Info    Beta-theraphotoxin-Gr1a Inhibition rate . [2], [3], [4], [5]
 Toxin Info    Beta-theraphotoxin-Gr1b Inhibition rate . [3], [4], [5]
 Toxin Info    Kappa-theraphotoxin-Gr2c Inhibition rate . [3], [4], [5], [6]
 Toxin Info    Potassium channel toxin gamma-KTx 1.7 Inhibition rate . [7]
 Toxin Info    Potassium channel toxin gamma-KTx 1.8 Inhibition rate . [7]
 Toxin Info    Potassium channel toxin gamma-KTx 1.1 Inhibition rate . [1]
 Toxin Info    M-theraphotoxin-Gr1a IC50
10.9 μM
 [3- 19]
 Toxin Info    Kappa-theraphotoxin-Gr3a IC50
45 μM
 [3- 23]
References
Ref 1 Species diversity and peptide toxins blocking selectivity of ether-a-go-go-related gene subfamily K+ channels in the central nervous system. Mol Pharmacol. 2006 May;69(5):1673-83. doi: 10.1124/mol.105.019729. Epub 2006 Feb 23.
Ref 2 Isolation and characterization of a novel toxin from the venom of the spider Grammostola rosea that blocks sodium channels. Toxicon. 2007 Jul;50(1):65-74. doi: 10.1016/j.toxicon.2007.02.015. Epub 2007 Mar 3.
Ref 3 Target promiscuity and heterogeneous effects of tarantula venom peptides affecting Na+ and K+ ion channels. J Biol Chem. 2010 Feb 5;285(6):4130-4142. doi: 10.1074/jbc.M109.054718. Epub 2009 Dec 2.
Ref 4 Structural Basis of Nav1.7 Inhibition by a Gating-Modifier Spider Toxin. Cell. 2019 Feb 7;176(4):702-715.e14. doi: 10.1016/j.cell.2018.12.018. Epub 2019 Jan 17.
Ref 5 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 6 Characterization of voltage-dependent calcium channel blocking peptides from the venom of the tarantula Grammostola rosea. Toxicon. 2011 Sep 1;58(3):265-76. doi: 10.1016/j.toxicon.2011.06.006. Epub 2011 Jun 28.
Ref 7 Two novel ergtoxins, blockers of K+-channels, purified from the Mexican scorpion Centruroides elegans elegans. Neurochem Res. 2008 Aug;33(8):1525-33. doi: 10.1007/s11064-008-9634-8. Epub 2008 Mar 13.
Ref 8 cDNA sequence and in vitro folding of GsMTx4, a specific peptide inhibitor of mechanosensitive channels. Toxicon. 2003 Sep;42(3):263-74. doi: 10.1016/s0041-0101(03)00141-7.
Ref 9 Identification of a peptide toxin from Grammostola spatulata spider venom that blocks cation-selective stretch-activated channels. J Gen Physiol. 2000 May;115(5):583-98. doi: 10.1085/jgp.115.5.583.
Ref 10 Solution structure of peptide toxins that block mechanosensitive ion channels. J Biol Chem. 2002 Sep 13;277(37):34443-50. doi: 10.1074/jbc.M202715200. Epub 2002 Jun 24.
Ref 11 Tarantula peptide inhibits atrial fibrillation. Nature. 2001 Jan 4;409(6816):35-6. doi: 10.1038/35051165.
Ref 12 Localization of the voltage-sensor toxin receptor on KvAP. Biochemistry. 2004 Aug 10;43(31):10071-9. doi: 10.1021/bi049463y.
Ref 13 Bilayer-dependent inhibition of mechanosensitive channels by neuroactive peptide enantiomers. Nature. 2004 Jul 8;430(6996):235-40. doi: 10.1038/nature02743.
Ref 14 Lipid membrane interaction and antimicrobial activity of GsMTx-4, an inhibitor of mechanosensitive channel. Biochem Biophys Res Commun. 2006 Feb 10;340(2):633-8. doi: 10.1016/j.bbrc.2005.12.046. Epub 2005 Dec 19.
Ref 15 Effects of tarantula toxin GsMTx4 on the membrane motor of outer hair cells. Neurosci Lett. 2006 Aug 14;404(1-2):213-6. doi: 10.1016/j.neulet.2006.05.059. Epub 2006 Jun 22.
Ref 16 Molecular dynamics simulations of a stretch-activated channel inhibitor GsMTx4 with lipid membranes: two binding modes and effects of lipid structure. Biophys J. 2007 Jun 15;92(12):4233-43. doi: 10.1529/biophysj.106.101071. Epub 2007 Mar 23.
Ref 17 Is lipid bilayer binding a common property of inhibitor cysteine knot ion-channel blockers?. Biophys J. 2007 Aug 15;93(4):L20-2. doi: 10.1529/biophysj.107.112375. Epub 2007 Jun 15.
Ref 18 Gating modifier toxins isolated from spider venom: Modulation of voltage-gated sodium channels and the role of lipid membranes. J Biol Chem. 2018 Jun 8;293(23):9041-9052. doi: 10.1074/jbc.RA118.002553. Epub 2018 Apr 27.
Ref 19 Fast desensitization of acetylcholine receptors induced by a spider toxin. Channels (Austin). 2021 Dec;15(1):507-515. doi: 10.1080/19336950.2021.1961459.
Ref 20 Functional analysis of an archaebacterial voltage-dependent K+ channel. Nature. 2003 Mar 13;422(6928):180-5. doi: 10.1038/nature01473. Epub 2003 Mar 2.
Ref 21 A membrane-access mechanism of ion channel inhibition by voltage sensor toxins from spider venom. Nature. 2004 Jul 8;430(6996):232-5. doi: 10.1038/nature02632.
Ref 22 Vstx1, a modifier of Kv channel gating, localizes to the interfacial region of lipid bilayers. Biochemistry. 2006 Oct 3;45(39):11844-55. doi: 10.1021/bi061111z.
Ref 23 Solution structure and lipid membrane partitioning of VSTx1, an inhibitor of the KvAP potassium channel. Biochemistry. 2005 Apr 26;44(16):6015-23. doi: 10.1021/bi0477034.
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