Peptide Information

General Information of This Peptide
Peptide ID
BTDP008468
Peptide Name
Potassium channel toxin alpha-KTx 15.6
Symonym
Discrepin
Species
Tityus discrepans (Venezuelan scorpion)
Uniprot Name
KA156_TITDI
Alphafold ID
P84777
3D Structure
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2D Sequence
3D Structure
Source
RSCB PDB: 2AXK
Sequence
MKAFYGMLVIFILCSTCYISVDSQIDTNVKCSGSSKCVKICIDRYNTRGAKCINGRCTCY
P
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Sequence Length
61
Mass (Da)
6787
Signal Sequence
MKAFYGMLVIFILCSTCYISVDS
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Sequence Removed Signal Peptide
QIDTNVKCSGSSKCVKICIDRYNTRGAKCINGRCTCYP
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Disulfide Bond
31-52;37-57;41-59
PDB ID
2AXK
        Click to Show/Hide the Complete Species Lineage
Kingdom: Metazoa
Phylum: Arthropoda
Class: Arachnida
Order: Scorpiones
Family: Buthidae
Genus: Tityus
Species: Tityus discrepans
Full List of Activity Data of This Peptide Toxin
                        Target Name Activity Data Type Activity Data Concentration Note Reference
 Target Info    Kv11 Inhibition rate .
3 μM
Blocker
 [1]
 Target Info    A-type voltage-gated potassium channel Inhibition rate
50 %
190 nM
Cerebellum granular cells
 [1- 7]
 Target Info    A-type voltage-gated potassium channel IC50
190 nM
 .
Cerebellum granular cells
 [1- 7]
References
Ref 1 A common "hot spot" confers hERG blockade activity to alpha-scorpion toxins affecting K+ channels. Biochem Pharmacol. 2008 Sep 15;76(6):805-15. doi: 10.1016/j.bcp.2008.07.008. Epub 2008 Jul 18.
Ref 2 Molecular cloning and nucleotide sequence analysis of genes from a cDNA library of the scorpion Tityus discrepans. Biochimie. 2009 Aug;91(8):1010-9. doi: 10.1016/j.biochi.2009.05.005. Epub 2009 May 24.
Ref 3 Discrepin, a new peptide of the sub-family alpha-ktx15, isolated from the scorpion Tityus discrepans irreversibly blocks K+ -channels (IA currents) of cerebellum granular cells. Arch Biochem Biophys. 2004 Oct 15;430(2):256-63. doi: 10.1016/j.abb.2004.07.010.
Ref 4 Proteomic analysis of Tityus discrepans scorpion venom and amino acid sequence of novel toxins. Proteomics. 2006 Jun;6(12):3718-27. doi: 10.1002/pmic.200500525.
Ref 5 A positive charge at the N-terminal segment of Discrepin increases the blocking effect of K+ channels responsible for the IA currents in cerebellum granular cells. Biochim Biophys Acta. 2008 Apr;1780(4):750-5. doi: 10.1016/j.bbagen.2008.01.012. Epub 2008 Jan 30.
Ref 6 Screening, large-scale production and structure-based classification of cystine-dense peptides. Nat Struct Mol Biol. 2018 Mar;25(3):270-278. doi: 10.1038/s41594-018-0033-9. Epub 2018 Feb 26.
Ref 7 Solution structure of discrepin, a new K+-channel blocking peptide from the alpha-KTx15 subfamily. Biochemistry. 2006 Feb 14;45(6):1795-804. doi: 10.1021/bi0519248.
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