Peptide Information

General Information of This Peptide
Peptide ID
BTDP004162
Peptide Name
Mu-conotoxin TIIIA
Species
Conus tulipa (Fish-hunting cone snail) (Tulip cone)
Uniprot Name
CM3A_CONTU
Alphafold ID
P0C350
3D Structure
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2D Sequence
3D Structure
Source
Alphafold db: P0C350
Sequence
RHGCCKGPKGCSSRECRPQHCC
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Sequence Length
22
Mass (Da)
2433
Sequence Removed Signal Peptide
RHGCCKGPKGCSSRECRPQHCC
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Disulfide Bond
4-16;5-21;11-22
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Kingdom: Metazoa
Phylum: Mollusca
Class: Gastropoda
Order: Neogastropoda
Family: Conidae
Genus: Conus
Species: Conus tulipa
Full List of Activity Data of This Peptide Toxin
                        Target Name Activity Data Type Activity Data Concentration Note Reference
 Target Info    Nav1.4 IC50
9 nM
 . . [1- 5]
 Target Info    Nav1.2 IC50
40 nM
 . . [1- 5]
References
Ref 1 Isolation and structure-activity of mu-conotoxin TIIIA, a potent inhibitor of tetrodotoxin-sensitive voltage-gated sodium channels. Mol Pharmacol. 2007 Mar;71(3):676-85. doi: 10.1124/mol.106.028225. Epub 2006 Dec 1.
Ref 2 -Conotoxins that differentially block sodium channels NaV1.1 through 1.8 identify those responsible for action potentials in sciatic nerve. Proc Natl Acad Sci U S A. 2011 Jun 21;108(25):10302-7. doi: 10.1073/pnas.1107027108. Epub 2011 Jun 7.
Ref 3 A novel -conopeptide, CnIIIC, exerts potent and preferential inhibition of NaV1.2/1.4 channels and blocks neuronal nicotinic acetylcholine receptors. Br J Pharmacol. 2012 Jul;166(5):1654-68. doi: 10.1111/j.1476-5381.2012.01837.x.
Ref 4 N- and C-terminal extensions of -conotoxins increase potency and selectivity for neuronal sodium channels. Biopolymers. 2012;98(2):161-5. doi: 10.1002/bip.22032. Epub 2012 Feb 10.
Ref 5 Co-expression of Na(V) subunits alters the kinetics of inhibition of voltage-gated sodium channels by pore-blocking -conotoxins. Br J Pharmacol. 2013 Apr;168(7):1597-610. doi: 10.1111/bph.12051.
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