Target Information

General Information of This Target
Target ID
BTDT00192
Target Name
Potassium voltage-gated channel subfamily H member 7 (KCNH7)
Target Bioclass
Transporter and channel
Uniprot ID
Q9NS40
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
KCNH7
Gene ID
90134
Synonym
ERG3; Ether-a-go-go-related gene potassium channel 3; Voltage-gated potassium channel subunit Kv11.3
Sequence
MPVRRGHVAPQNTFLGTIIRKFEGQNKKFIIANARVQNCAIIYCNDGFCEMTGFSRPDVM
QKPCTCDFLHGPETKRHDIAQIAQALLGSEERKVEVTYYHKNGSTFICNTHIIPVKNQEG
VAMMFIINFEYVTDNENAATPERVNPILPIKTVNRKFFGFKFPGLRVLTYRKQSLPQEDP
DVVVIDSSKHSDDSVAMKHFKSPTKESCSPSEADDTKALIQPSKCSPLVNISGPLDHSSP
KRQWDRLYPDMLQSSSQLSHSRSRESLCSIRRASSVHDIEGFGVHPKNIFRDRHASEDNG
RNVKGPFNHIKSSLLGSTSDSNLNKYSTINKIPQLTLNFSEVKTEKKNSSPPSSDKTIIA
PKVKDRTHNVTEKVTQVLSLGADVLPEYKLQTPRINKFTILHYSPFKAVWDWLILLLVIY
TAIFTPYSAAFLLNDREEQKRRECGYSCSPLNVVDLIVDIMFIIDILINFRTTYVNQNEE
VVSDPAKIAIHYFKGWFLIDMVAAIPFDLLIFGSGSDETTTLIGLLKTARLLRLVRVARK
LDRYSEYGAAVLMLLMCIFALIAHWLACIWYAIGNVERPYLTDKIGWLDSLGQQIGKRYN
DSDSSSGPSIKDKYVTALYFTFSSLTSVGFGNVSPNTNSEKIFSICVMLIGSLMYASIFG
NVSAIIQRLYSGTARYHMQMLRVKEFIRFHQIPNPLRQRLEEYFQHAWTYTNGIDMNMVL
KGFPECLQADICLHLNQTLLQNCKAFRGASKGCLRALAMKFKTTHAPPGDTLVHCGDVLT
ALYFLSRGSIEILKDDIVVAILGKNDIFGEMVHLYAKPGKSNADVRALTYCDLHKIQRED
LLEVLDMYPEFSDHFLTNLELTFNLRHESAKADLLRSQSMNDSEGDNCKLRRRKLSFESE
GEKENSTNDPEDSADTIRHYQSSKRHFEEKKSRSSSFISSIDDEQKPLFSGIVDSSPGIG
KASGLDFEETVPTSGRMHIDKRSHSCKDITDMRSWERENAHPQPEDSSPSALQRAAWGIS
ETESDLTYGEVEQRLDLLQEQLNRLESQMTTDIQTILQLLQKQTTVVPPAYSMVTAGSEY
QRPIIQLMRTSQPEASIKTDRSFSPSSQCPEFLDLEKSKLKSKESLSSGVHLNTASEDNL
TSLLKQDSDLSLELHLRQRKTYVHPIRHPSLPDSSLSTVGIVGLHRHVSDPGLPGK

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Family
the potassium channel family
Function
Pore-forming (alpha) subunit of voltage-gated potassium channel. Channel properties may be modulated by cAMP and subunit assembly.

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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    Potassium channel toxin gamma-KTx 1.7 Dissociation constant
0.88 nM
 [1]
 Toxin Info    Potassium channel toxin gamma-KTx 1.1 Dissociation constant
4.05 nM
 [2]
 Toxin Info    Potassium channel toxin gamma-KTx 1.1 Dissociation constant
4.05 nM
 [2- 13]
 Toxin Info    Potassium channel toxin gamma-KTx 2.1 Dissociation constant
11.5 nM
 [2- 20]
 Toxin Info    Potassium channel toxin gamma-KTx 2.1 Dissociation constant
11.5 nM
 [2]
 Toxin Info    Beta-theraphotoxin-Gr1a Inhibition rate . [21], [22], [23], [24]
 Toxin Info    Beta-theraphotoxin-Gr1b Inhibition rate . [22], [23], [24]
 Toxin Info    Kappa-theraphotoxin-Gr2c Inhibition rate . [25], [22], [23], [24]
 Toxin Info    Potassium channel toxin gamma-KTx 1.8 Inhibition rate
100 %
 [1]
 Toxin Info    M-theraphotoxin-Gr1a IC50
53 μM
 [22- 37]
 Toxin Info    Kappa-theraphotoxin-Gr3a IC50
55 μM
 [22- 41]
References
Ref 1 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 2 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 3 A large number of novel Ergtoxin-like genes and ERG K+-channels blocking peptides from scorpions of the genus Centruroides. FEBS Lett. 2002 Dec 4;532(1-2):121-6. doi: 10.1016/s0014-5793(02)03652-9.
Ref 4 A toxin to nervous, cardiac, and endocrine ERG K+ channels isolated from Centruroides noxius scorpion venom. FASEB J. 1999 May;13(8):953-62.
Ref 5 Disulfide bridges of ergtoxin, a member of a new sub-family of peptide blockers of the ether-a-go-go-related K+ channel. FEBS Lett. 2000 Aug 18;479(3):156-7. doi: 10.1016/s0014-5793(00)01891-3.
Ref 6 Mapping the receptor site for ergtoxin, a specific blocker of ERG channels. FEBS Lett. 2002 Jan 2;510(1-2):45-9. doi: 10.1016/s0014-5793(01)03218-5.
Ref 7 Mapping the binding site of a human ether-a-go-go-related gene-specific peptide toxin (ErgTx) to the channel's outer vestibule. J Biol Chem. 2002 May 10;277(19):16403-11. doi: 10.1074/jbc.M200460200. Epub 2002 Feb 25.
Ref 8 Preferential closed channel blockade of HERG potassium currents by chemically synthesised BeKm-1 scorpion toxin. FEBS Lett. 2003 Jul 17;547(1-3):20-6. doi: 10.1016/s0014-5793(03)00662-8.
Ref 9 Mechanism of block of the hERG K+ channel by the scorpion toxin CnErg1. Biophys J. 2007 Jun 1;92(11):3915-29. doi: 10.1529/biophysj.106.101956. Epub 2007 Mar 16.
Ref 10 Recombinant expression of the toxic peptide ErgTx1 and role of Met35 on its stability and function. Peptides. 2011 Mar;32(3):560-7. doi: 10.1016/j.peptides.2010.06.018. Epub 2010 Jun 30.
Ref 11 Positive selection-guided mutational analysis revealing two key functional sites of scorpion ERG K(+) channel toxins. Biochem Biophys Res Commun. 2012 Dec 7;429(1-2):111-6. doi: 10.1016/j.bbrc.2012.10.065. Epub 2012 Oct 24.
Ref 12 Solution structure of CnErg1 (Ergtoxin), a HERG specific scorpion toxin. FEBS Lett. 2003 Mar 27;539(1-3):138-42. doi: 10.1016/s0014-5793(03)00216-3.
Ref 13 Exploring structural features of the interaction between the scorpion toxinCnErg1 and ERG K+ channels. Proteins. 2004 Aug 1;56(2):367-75. doi: 10.1002/prot.20102.
Ref 14 An ERG channel inhibitor from the scorpion Buthus eupeus. J Biol Chem. 2001 Mar 30;276(13):9868-76. doi: 10.1074/jbc.M005973200. Epub 2001 Jan 2.
Ref 15 M-type K+ current inhibition by a toxin fron the scorpion Buthus eupeus. FEBS Lett. 1996 Apr 22;384(3):277-80. doi: 10.1016/0014-5793(96)00333-x.
Ref 16 BeKm-1 is a HERG-specific toxin that shares the structure with ChTx but the mechanism of action with ErgTx1. Biophys J. 2003 May;84(5):3022-36. doi: 10.1016/S0006-3495(03)70028-9.
Ref 17 Unique interaction of scorpion toxins with the hERG channel. J Mol Recognit. 2004 May-Jun;17(3):209-17. doi: 10.1002/jmr.667.
Ref 18 BeKm-1, a peptide inhibitor of human ether-a-go-go-related gene potassium currents, prolongs QTc intervals in isolated rabbit heart. J Pharmacol Exp Ther. 2011 Apr;337(1):2-8. doi: 10.1124/jpet.110.176883. Epub 2010 Dec 23.
Ref 19 Interaction simulation of hERG K+ channel with its specific BeKm-1 peptide: insights into the selectivity of molecular recognition. J Proteome Res. 2007 Feb;6(2):611-20. doi: 10.1021/pr060368g.
Ref 20 New binding site on common molecular scaffold provides HERG channel specificity of scorpion toxin BeKm-1. J Biol Chem. 2002 Nov 8;277(45):43104-9. doi: 10.1074/jbc.M204083200. Epub 2002 Jul 31.
Ref 21 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 22 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 23 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 24 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 25 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 26 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 27 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 28 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 29 Tarantula peptide inhibits atrial fibrillation. Nature. 2001 Jan 4;409(6816):35-6. doi: 10.1038/35051165.
Ref 30 Localization of the voltage-sensor toxin receptor on KvAP. Biochemistry. 2004 Aug 10;43(31):10071-9. doi: 10.1021/bi049463y.
Ref 31 Bilayer-dependent inhibition of mechanosensitive channels by neuroactive peptide enantiomers. Nature. 2004 Jul 8;430(6996):235-40. doi: 10.1038/nature02743.
Ref 32 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 33 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 34 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 35 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 36 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 37 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 38 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 39 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 40 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 41 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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