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Protein

Alpha-conotoxin PnIA

Gene
N/A
Organism
Conus pennaceus (Feathered cone) (Conus episcopus)
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 toxin blocks mammalian alpha-3-beta-2/CHRNA3-CHRNB2 (IC50=7-68 nM) and alpha-7/CHRNA7 (IC50=253 nM) nAChRs (PubMed:8068627, PubMed:10545176, PubMed:15929983, PubMed:22024738, PubMed:25101833). It also shows a high inhibition on alpha-6/alpha-3-beta-2-beta-3 (CHRNA6/CHRNA3-CHRNB2-CHRNB3) (IC50=11 nM) and a low inhibition on alpha-6-beta-4/CHRNA4-CHRNB4 (IC50>500 nM) (PubMed:22024738).6 Publications

Miscellaneous

The replacement of Ala-10 by a norleucine (A10Nle) produces the more potent analog on alpha-7/CHRNA7 (IC50=4.3 nM) and on alpha-3-beta-2/CHRNA3-CHRNB2 (IC50=0.7 nM) (PubMed:25101833).1 Publication
This toxin shows no or very weak inhibition on alpha-2-beta-2/CHRNA2-CHRNB2, alpha-3-beta-4/CHRNA3-CHRNB4, alpha-4-beta-2/CHRNA4-CHRNB2 and alpha-6/alpha-3-beta-4 nAChRs.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei10Important for inhibitory potency on alpha-3-beta-2/CHRNA3-CHRNB2 nAChR; interacts with a hydrophobic pocket between the two alpha-7/CHRNA7 subunits or between the alpha-3 and the beta-2 subunits of alpha-3-beta-2/CHRNA3-CHRNB2 nAChR2 Publications1
Sitei11Important for inhibitory potency on alpha-3-beta-2/CHRNA3-CHRNB2 and alpha-7/CHRNA7 nAChR1 Publication1

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 PnIA2 Publications
Short name:
Alpha-PnIA2 Publications
OrganismiConus pennaceus (Feathered cone) (Conus episcopus)
Taxonomic identifieri37335 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaNeogastropodaConoideaConidaeConusDarioconus

Organism-specific databases

ConoServeri75 Pni1
51 PnIA

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi5L → R in PnIA(L5R-A10L); 25-fold increase in inhibitory potency on alpha-7/CHRNA7 and small increase in inhibitory potency on alpha-3-beta-2/CHRNA3-CHRNB2. 1 Publication1
Mutagenesisi10A → L: Selectivity change from alpha-3-beta-2/CHRNA3-CHRNB2 to alpha-7/CHRNA7. 20-fold increase in inhibitory potency on alpha-7/CHRNA7, 7-10-fold decrease in inhibitory potency on alpha-3-beta-2/CHRNA3-CHRNB2, and no change in inhibitory potency on alpha-4-beta-2/CHRNA4-CHRNB2 nAChRs. In PnIA(L5R-A10L); 25-fold increase in inhibitory potency on alpha-7/CHRNA7 and small increase in inhibitory potency on alpha-3-beta-2/CHRNA3-CHRNB2. 4 Publications1
Mutagenesisi11N → S: 7-fold decrease in inhibitory potency on alpha-7/CHRNA7 and 25-fold decrease in inhibitory potency on alpha-3-beta-2/CHRNA3-CHRNB2 nAChRs. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PeptideiPRO_00000444621 – 16Alpha-conotoxin PnIA1 PublicationAdd BLAST16

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi2 ↔ 82 PublicationsImported
Disulfide bondi3 ↔ 162 PublicationsImported
Modified residuei15Sulfotyrosine1 Publication1
Modified residuei16Cysteine amide1 Publication1

Keywords - PTMi

Amidation, Disulfide bond, Sulfation

Expressioni

Tissue specificityi

Expressed by the venom duct.1 Publication

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Q8WSF82EBI-15553601,EBI-7179765From Aplysia californica.

Protein-protein interaction databases

DIPiDIP-60493N
IntActiP50984, 2 interactors

Structurei

Secondary structure

116
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SMRiP50984
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50984

Family & Domainsi

Domaini

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
IPR018072 Conotoxin_a-typ_CS
PROSITEiView protein in PROSITE
PS60014 ALPHA_CONOTOXIN, 1 hit

Sequencei

Sequence statusi: Complete.

Length:16
Mass (Da):1,628
Last modified:October 1, 1996 - v1
Checksum:i05310FF95EC99005
GO

Sequence databases

PIRiA54877

Similar proteinsi

Cross-referencesi

Sequence databases

PIRiA54877

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PENX-ray1.10A1-16[»]
2BR8X-ray2.40F/G/H/I/J1-16[»]
SMRiP50984
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60493N
IntActiP50984, 2 interactors

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ConoServeri75 Pni1
51 PnIA

Miscellaneous databases

EvolutionaryTraceiP50984

Family and domain databases

InterProiView protein in InterPro
IPR018072 Conotoxin_a-typ_CS
PROSITEiView protein in PROSITE
PS60014 ALPHA_CONOTOXIN, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCA1A_CONPE
AccessioniPrimary (citable) accession number: P50984
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 12, 2018
This is version 86 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

3D-structure, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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