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Protein

Alpha-conotoxin AusIA

Gene
N/A
Organism
Conus australis (Cone snail) (Asprella australis)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This peptide has been experimentally synthesized as AusIA-globular and AusIA-ribbon. Both forms are active on neuronal nAChRs alpha-7/CHRNA7 (IC50=11.68 µM for AusIA-globular and 9.67 µM for AusIA-ribbon).1 Publication

Miscellaneous

Neither AusIA-globular nor AusIA-ribbon shows effect on muscle nAChRs alpha-1-beta-1-epsilon-delta/CHRNA1-CHRNB1-CHRNE-CHRND (adult subtype) and alpha-1-beta-1-gamma-delta/CHRNA1-CHRNB1-CHRNG-CHRND (fetal subtype) and on neuronal nAChRs alpha-3-beta-4/CHRNA3-CHRNB4, alpha-4-beta-4/CHRNA4-CHRNB4 and alpha-4-beta-2/CHRNA4-CHRNB2.1 Publication

GO - Molecular functioni

Keywordsi

Molecular functionAcetylcholine receptor inhibiting toxin, Ion channel impairing toxin, Neurotoxin, Postsynaptic neurotoxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-conotoxin AusIA
OrganismiConus australis (Cone snail) (Asprella australis)
Taxonomic identifieri1519798 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaNeogastropodaConoideaConidaeConusPhasmoconus

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

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PeptideiPRO_00004317361 – 16Alpha-conotoxin AusIAAdd BLAST16

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi2 ↔ 15In AusIA-ribbon form; alternate1 Publication
Disulfide bondi2 ↔ 9In AusIA-globular form; alternateBy similarity
Disulfide bondi3 ↔ 15In AusIA-globular form; alternateBy similarity
Disulfide bondi3 ↔ 9In AusIA-ribbon form; alternate1 Publication

Post-translational modificationi

Two isomers (with different disulfide connectivity) have been synthesized (AusIA-globular (C1-C3, C2-C4) and AusIA-ribbon (C1-C4, C2-C3)). Only AusIA-globular contains the cysteine connectivity described as typical for native alpha-conotoxins. However, AusIA-ribbon is more potent than AusIA-globular, suggesting that another disulfide connectivity may exist in nature. Both isomers adopt very flexible structures without having a unique folded structure, lacking any stable alpha-helical and/or beta-turn units.1 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom duct.1 Publication

Family & Domainsi

Domaini

The cysteine framework is I (CC-C-C). Alpha5/5 pattern.Curated

Sequence similaritiesi

Belongs to the conotoxin A superfamily.Curated

Sequencei

Sequence statusi: Complete.

Length:16
Mass (Da):1,768
Last modified:February 4, 2015 - v1
Checksum:i2B1EEBD02E1629C7
GO

Mass spectrometryi

Molecular mass is 1763.90 Da from positions 1 - 16. Determined by MALDI. 1 Publication

Similar proteinsi

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Entry informationi

Entry nameiCA1A_CONAV
AccessioniPrimary (citable) accession number: P0DL39
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 4, 2015
Last sequence update: February 4, 2015
Last modified: September 12, 2018
This is version 6 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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Main funding by: National Institutes of Health

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