Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Alpha-conotoxin LsIA

Conus limpusi (Cone snail)
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli


Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin inhibits human alpha-7 (IC50=10.1 nM), rat alpha-3-beta-2 (IC50=10.3 nM) and rat alpha-3-alpha-5-beta-2 (IC50=31.2 nM).1 Publication


Shows a weak inhibition of alpha-3-beta-4 nAChR and does not inhibit alpha-9 alpha-10, alpha-4-beta-2 and alpha-4-beta-4 nAChR.1 Publication

GO - Molecular functioni


Molecular functionAcetylcholine receptor inhibiting toxin, Neurotoxin, Postsynaptic neurotoxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-conotoxin LsIA1 Publication
OrganismiConus limpusi (Cone snail)
Taxonomic identifieri1967283 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConusEremiconus

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti


Pathology & Biotechi


Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1 – 2Missing : 9-fold and 4.4-fold decrease in potency at alpha-3-beta-2 and alpha-7 nAChR subunits, respectively. 1 Publication2
Mutagenesisi1Missing : 5.5-fold and 2.3-fold decrease in potency at alpha-3-beta-2 and alpha-7 nAChR subunits, respectively. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PeptideiPRO_00004398311 – 17Alpha-conotoxin LsIA1 PublicationAdd BLAST17

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi3 ↔ 91 Publication
Disulfide bondi4 ↔ 171 Publication
Modified residuei17Cysteine amide1 Publication1

Post-translational modificationi

Amidation at Cys-17 plays a critical role, since a C-terminally carboxylated analog of this toxin is 3-fold less porent at the alpha-7 subtype and 3-fold more potent at the alpha-3-beta-2 subtype.1 Publication

Keywords - PTMi

Amidation, Disulfide bond


Tissue specificityi

Expressed by the venom duct.1 Publication

Family & Domainsi


The cysteine framework is I (CC-C-C). Alpha4/7 pattern.Curated

Sequence similaritiesi

Belongs to the conotoxin A superfamily.Curated

Family and domain databases

InterProiView protein in InterPro
IPR009958. Conotoxin_a-typ.
IPR018072. Conotoxin_a-typ_CS.
PfamiView protein in Pfam
PF07365. Toxin_8. 1 hit.


Sequence statusi: Complete.

P0DL68-1 [UniParc]FASTAAdd to basket

« Hide

Mass (Da):1,752
Last modified:May 10, 2017 - v1

Mass spectrometryi

Molecular mass is 1746.6 Da from positions 1 - 17. Determined by MALDI. 1 Publication

Similar proteinsi

Entry informationi

Entry nameiCA1A_CONLM
AccessioniPrimary (citable) accession number: P0DL68
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2017
Last sequence update: May 10, 2017
Last modified: February 28, 2018
This is version 5 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program


Keywords - Technical termi

Direct protein sequencing