Target Information

General Information of This Target
Target ID
BTDT00186
Target Name
Small conductance calcium-activated potassium channel protein 2 (KCNN2)
Target Bioclass
Transporter and channel
Uniprot ID
Q9H2S1
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
KCNN2
Gene ID
3781
Synonym
KCa2.2
Sequence
MSSCRYNGGVMRPLSNLSASRRNLHEMDSEAQPLQPPASVGGGGGASSPSAAAAAAAAVS
SSAPEIVVSKPEHNNSNNLALYGTGGGGSTGGGGGGGGSGHGSSSGTKSSKKKNQNIGYK
LGHRRALFEKRKRLSDYALIFGMFGIVVMVIETELSWGAYDKASLYSLALKCLISLSTII
LLGLIIVYHAREIQLFMVDNGADDWRIAMTYERIFFICLEILVCAIHPIPGNYTFTWTAR
LAFSYAPSTTTADVDIILSIPMFLRLYLIARVMLLHSKLFTDASSRSIGALNKINFNTRF
VMKTLMTICPGTVLLVFSISLWIIAAWTVRACERYHDQQDVTSNFLGAMWLISITFLSIG
YGDMVPNTYCGKGVCLLTGIMGAGCTALVVAVVARKLELTKAEKHVHNFMMDTQLTKRVK
NAAANVLRETWLIYKNTKLVKKIDHAKVRKHQRKFLQAIHQLRSVKMEQRKLNDQANTLV
DLAKTQNIMYDMISDLNERSEDFEKRIVTLETKLETLIGSIHALPGLISQTIRQQQRDFI
EAQMESYDKHVTYNAERSRSSSRRRRSSSTAPPTSSESS

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Family
the potassium channel KCNN family
Function
Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization.

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Taxonomy ID
9606
TCDB ID
1.A.1.16.1
        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 alpha-KTx 5.1 Dissociation constant
0.2 nM
 [1]
 Toxin Info    ScyTx (F2V,M7R,D24V) Dissociation constant
0.45 nM
 [1]
 Toxin Info    ScyTx (A1T,M7R,D24V) Dissociation constant
0.45 nM
 [1]
 Toxin Info    ScyTx (M7L) Dissociation constant
0.55 nM
 [1]
 Toxin Info    ScyTx (V1T,F2V) Dissociation constant
0.6 nM
 [1]
 Toxin Info    ScyTx (M7K) Dissociation constant
3 nM
 [1]
 Toxin Info    ScyTx (M7[Dab]) Dissociation constant
3.8 nM
 [1]
 Toxin Info    ScyTx (R6K) Dissociation constant
4.5 nM
 [1]
 Toxin Info    ScyTx (M7[DaP]) Dissociation constant
5.5 nM
 [1]
 Toxin Info    ScyTx (R6M,M7R) Dissociation constant
9.5 nM
 [1]
 Toxin Info    ScyTx (R6L) Dissociation constant
15 nM
 [1]
 Toxin Info    ScyTx (V1T,F2V,M7R) Dissociation constant
20 nM
 [1]
 Toxin Info    Potassium channel toxin alpha-KTx 5.2 Dissociation constant
22 nM
 [1]
 Toxin Info    Potassium channel toxin alpha-KTx 4.2 Dissociation constant
80 nM
 [1]
 Toxin Info    Pi1 Dissociation constant
100 nM
 [1]
 Toxin Info    Potassium channel toxin alpha-KTx 4.8 Dissociation constant
502 nM
 [2]
 Toxin Info    ScyTx (R6[Har]) Dissociation constant
540 nM
 [1]
 Toxin Info    Potassium channel toxin alpha-KTx 6.2 Dissociation constant
1 μM
 [1]
 Toxin Info    Toxin MeKTx13-3 (D19K) Inhibition rate . [3]
 Toxin Info    Toxin MeKTx13-3 (K6D,D19K) Inhibition rate . [3]
 Toxin Info    MTX (C19[Abu],C34[Abu]) Inhibition rate . [4]
 Toxin Info    MTX (G33A) Inhibition rate . [4]
 Toxin Info    MTX (K15Q) Inhibition rate . [4]
 Toxin Info    MTX (K23A) Inhibition rate . [4]
 Toxin Info    MTX (K7A) Inhibition rate . [4]
 Toxin Info    MTX (S2A) Inhibition rate . [4]
 Toxin Info    MTX (S6A) Inhibition rate . [4]
 Toxin Info    MTX (T4A) Inhibition rate . [4]
 Toxin Info    MTX (Y10A) Inhibition rate . [4]
 Toxin Info    MTX (Y32A) Inhibition rate . [4]
 Toxin Info    Potassium channel toxin alpha-KTx 8.1 Inhibition rate . [1]
 Toxin Info    Potassium channel toxin alpha-KTx 6.1 Inhibition rate . [1]
 Toxin Info    Potassium channel toxin alpha-KTx J123 Inhibition rate
24 %
 [5]
 Toxin Info    Apamin IC50
27 - 140 pM
 [6- 25]
 Toxin Info    Toxin (KJ6) IC50
15.5 nM
 [26]
 Toxin Info    Tamapin (R6A) IC50
18.2 nM
 [26]
 Toxin Info    Tamapin (R13A) IC50
19.7 nM
 [26]
 Toxin Info    Tamapin (R6A,R7A) IC50
23.6 nM
 [26]
 Toxin Info    Leiurotoxin I-like toxin P05 (R5K,Q8E,E26K) IC50
100 nM
 [27]
References
Ref 1 Design and characterization of a highly selective peptide inhibitor of the small conductance calcium-activated K+ channel, SkCa2. J Biol Chem. 2001 Nov 16;276(46):43145-51. doi: 10.1074/jbc.M106981200. Epub 2001 Aug 29.
Ref 2 Characterization and Chemical Synthesis of Cm39 (-KTx 4.8): A Scorpion Toxin That Inhibits Voltage-Gated K(+) Channel K(V)1.2 and Small- and Intermediate-Conductance Ca(2+)-Activated K(+) Channels K(Ca)2.2 and K(Ca)3.1. Toxins (Basel). 2023 Jan 5;15(1):41. doi: 10.3390/toxins15010041.
Ref 3 Toxin acidic residue evolutionary function-guided design of de novo peptide drugs for the immunotherapeutic target, the Kv1.3 channel. Sci Rep. 2015 May 8;5:9881. doi: 10.1038/srep09881.
Ref 4 Maurotoxin: a potent inhibitor of intermediate conductance Ca2+-activated potassium channels. Mol Pharmacol. 2003 Feb;63(2):409-18. doi: 10.1124/mol.63.2.409.
Ref 5 Characterization of a new Kv1.3 channel-specific blocker, J123, from the scorpion Buthus martensii Karsch. Peptides. 2008 Sep;29(9):1514-20. doi: 10.1016/j.peptides.2008.04.021. Epub 2008 May 13.
Ref 6 The precursors of the bee venom constituents apamin and MCD peptide are encoded by two genes in tandem which share the same 3'-exon. J Biol Chem. 1995 May 26;270(21):12704-8. doi: 10.1074/jbc.270.21.12704.
Ref 7 [Sequence analysis of bee venom neurotoxin (apamine) from its tryptic and chymotryptic cleavage products]. Hoppe Seylers Z Physiol Chem. 1967 Jun;348(6):737-8.
Ref 8 The peptide components of bee venom. Eur J Biochem. 1976 Jan 15;61(2):369-76. doi: 10.1111/j.1432-1033.1976.tb10030.x.
Ref 9 Apamin as a selective blocker of the calcium-dependent potassium channel in neuroblastoma cells: voltage-clamp and biochemical characterization of the toxin receptor. Proc Natl Acad Sci U S A. 1982 Feb;79(4):1308-12. doi: 10.1073/pnas.79.4.1308.
Ref 10 Apamin, a blocker of the calcium-activated potassium channel, induces neurodegeneration of Purkinje cells exclusively. Brain Res. 1997 Dec 19;778(2):405-8. doi: 10.1016/s0006-8993(97)01165-7.
Ref 11 Determinants of apamin and d-tubocurarine block in SK potassium channels. J Biol Chem. 1997 Sep 12;272(37):23195-200. doi: 10.1074/jbc.272.37.23195.
Ref 12 Pharmacological characterization of small-conductance Ca(2+)-activated K(+) channels stably expressed in HEK 293 cells. Br J Pharmacol. 2000 Mar;129(5):991-9. doi: 10.1038/sj.bjp.0703120.
Ref 13 SK3 is an important component of K(+) channels mediating the afterhyperpolarization in cultured rat SCG neurones. J Physiol. 2001 Sep 1;535(Pt 2):323-34. doi: 10.1111/j.1469-7793.2001.00323.x.
Ref 14 Apamin interacts with all subtypes of cloned small-conductance Ca2+-activated K+ channels. Pflugers Arch. 2001 Jan;441(4):544-50. doi: 10.1007/s004240000447.
Ref 15 An amino acid outside the pore region influences apamin sensitivity in small conductance Ca2+-activated K+ channels. J Biol Chem. 2007 Feb 9;282(6):3478-86. doi: 10.1074/jbc.M607213200. Epub 2006 Dec 1.
Ref 16 Apamin reduces neuromuscular transmission by activating inhibitory muscarinic M(2) receptors on motor nerve terminals. Eur J Pharmacol. 2010 Jan 25;626(2-3):239-43. doi: 10.1016/j.ejphar.2009.09.064. Epub 2009 Oct 8.
Ref 17 Allosteric block of KCa2 channels by apamin. J Biol Chem. 2010 Aug 27;285(35):27067-27077. doi: 10.1074/jbc.M110.110072. Epub 2010 Jun 18.
Ref 18 The small neurotoxin apamin blocks not only small conductance Ca(2+) activated K(+) channels (SK type) but also the voltage dependent Kv1.3 channel. Eur Biophys J. 2017 Sep;46(6):517-523. doi: 10.1007/s00249-016-1196-0. Epub 2017 Jan 20.
Ref 19 Apamin inhibits TNF-- and IFN--induced inflammatory cytokines and chemokines via suppressions of NF-B signaling pathway and STAT in human keratinocytes. Pharmacol Rep. 2017 Oct;69(5):1030-1035. doi: 10.1016/j.pharep.2017.04.006. Epub 2017 Apr 18.
Ref 20 Apamin Suppresses LPS-Induced Neuroinflammatory Responses by Regulating SK Channels and TLR4-Mediated Signaling Pathways. Int J Mol Sci. 2020 Jun 17;21(12):4319. doi: 10.3390/ijms21124319.
Ref 21 Apamin from bee venom suppresses inflammation in a murine model of gouty arthritis. J Ethnopharmacol. 2020 Jul 15;257:112860. doi: 10.1016/j.jep.2020.112860. Epub 2020 Apr 11.
Ref 22 Antioxidative, Antiapoptotic, and Anti-Inflammatory Effects of Apamin in a Murine Model of Lipopolysaccharide-Induced Acute Kidney Injury. Molecules. 2020 Dec 3;25(23):5717. doi: 10.3390/molecules25235717.
Ref 23 Solution structure of apamin determined by nuclear magnetic resonance and distance geometry. Biochemistry. 1988 Nov 1;27(22):8491-8. doi: 10.1021/bi00422a029.
Ref 24 [Spatial structure of apamin in solution]. Mol Biol (Mosk). 1991 Jul-Aug;25(4):937-45.
Ref 25 Binding and toxicity of apamin. Characterization of the active site. Eur J Biochem. 1991 Mar 28;196(3):639-45. doi: 10.1111/j.1432-1033.1991.tb15860.x.
Ref 26 Cytotoxicity of recombinant tamapin and related toxin-like peptides on model cell lines. Chem Res Toxicol. 2014 Jun 16;27(6):960-7. doi: 10.1021/tx4004193. Epub 2014 May 12.
Ref 27 Protein-protein recognition control by modulating electrostatic interactions. J Proteome Res. 2010 Jun 4;9(6):3118-25. doi: 10.1021/pr100027k.
Ref 28 Venom composition and pain-causing toxins of the Australian great carpenter bee Xylocopa aruana. Sci Rep. 2022 Dec 22;12(1):22168. doi: 10.1038/s41598-022-26867-8.
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