Peptide Information

General Information of This Peptide
Peptide ID
BTDP008421
Peptide Name
Lambda-hexatoxin-Hv1c
Symonym
Janus-atracotoxin-Hv1c; Kappa-atracotoxin-Hv1c; Kappa-hexatoxin-Hv1c
Species
Hadronyche versuta (Blue mountains funnel-web spider) (Atrax versutus)
Uniprot Name
TK1C_HADVE
Alphafold ID
P82228
3D Structure
Download
2D Sequence
3D Structure
Source
RSCB PDB: 1DL0
Sequence
AICTGADRPCAACCPCCPGTSCKAESNGVSYCRKDEP
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Sequence Length
37
Mass (Da)
3768
Sequence Removed Signal Peptide
AICTGADRPCAACCPCCPGTSCKAESNGVSYCRKDEP
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Disulfide Bond
3-17;10-22;13-14;16-32
PDB ID
1DL0
        Click to Show/Hide the Complete Species Lineage
Kingdom: Metazoa
Phylum: Arthropoda
Class: Arachnida
Order: Araneae
Family: Hexathelidae
Genus: Hadronyche
Species: Hadronyche versuta
Full List of Activity Data of This Peptide Toxin
                        Target Name Activity Data Type Activity Data Concentration Note Reference
 Target Info    KCa1.1 IC50
2.3 nM
 .
Blocker
 [6]
 Target Info    KCa1.1 IC50
240 nM
 .
Blocker
 [6]
 Target Info    KCa1.1 IC50
9.776 μM
 .
Blocker
 [6]
References
Ref 1 Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge. Nat Struct Biol. 2000 Jun;7(6):505-13. doi: 10.1038/75921.
Ref 2 Scanning mutagenesis of a Janus-faced atracotoxin reveals a bipartite surface patch that is essential for neurotoxic function. J Biol Chem. 2002 Jun 21;277(25):22806-13. doi: 10.1074/jbc.M202297200. Epub 2002 Apr 5.
Ref 3 Role of the structurally disordered N- and C-terminal residues in the Janus-faced atracotoxins. Toxicon. 2002 Sep;40(9):1355-61. doi: 10.1016/s0041-0101(02)00154-x.
Ref 4 A model genetic system for testing the in vivo function of peptide toxins. Peptides. 2007 Jan;28(1):51-6. doi: 10.1016/j.peptides.2006.08.026. Epub 2006 Dec 1.
Ref 5 Phase coupling of a circadian neuropeptide with rest/activity rhythms detected using a membrane-tethered spider toxin. PLoS Biol. 2008 Nov 4;6(11):e273. doi: 10.1371/journal.pbio.0060273.
Ref 6 The Janus-faced atracotoxins are specific blockers of invertebrate K(Ca) channels. FEBS J. 2008 Aug;275(16):4045-59. doi: 10.1111/j.1742-4658.2008.06545.x. Epub 2008 Jul 9.
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