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Protein

Delta-conotoxin EVIA

Gene
N/A
Organism
Conus ermineus (Atlantic fish-hunting cone)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Delta-conotoxins bind to site 6 of voltage-gated sodium channels and inhibit the inactivation process. This toxin inhibits sodium channel inactivation in neuronal membranes from amphibians and mammals (Nav1.2a/SCN1A, Nav1.3/SCN3A and Nav1.6/SCN8A) upon binding to receptor site 6.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel impairing toxin, Neurotoxin, Toxin, Voltage-gated sodium channel impairing toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-conotoxin EVIA
Short name:
Delta-EVIA
OrganismiConus ermineus (Atlantic fish-hunting cone)
Taxonomic identifieri55423 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Organism-specific databases

ConoServeri1561. EVIA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

Dose that produces hyperactivity (ED(50)) is 1.8 pmol/g body mass (native toxin), 1.9 pmol/g body mass (synthetic toxin) and 3.9 pmol/g body mass (P13A mutant).1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi13 – 131P → A: 2-fold decrease of activity. Exists only as a trans isomer. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Peptidei1 – 3232Delta-conotoxin EVIAPRO_0000044868Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi3 ↔ 211 Publication
Modified residuei6 – 614-hydroxyproline1 Publication
Disulfide bondi10 ↔ 251 Publication
Disulfide bondi20 ↔ 291 Publication
Modified residuei32 – 321Leucine amide1 Publication

Keywords - PTMi

Amidation, Disulfide bond, Hydroxylation

Expressioni

Tissue specificityi

Expressed by the venom duct.2 Publications

Structurei

Secondary structure

1
32
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 164Combined sources
Beta strandi25 – 295Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G1PNMR-A1-32[»]
1G1ZNMR-A1-32[»]
ProteinModelPortaliP60513.
SMRiP60513. Positions 1-32.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60513.

Family & Domainsi

Domaini

The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
The cysteine framework is VI/VII (C-C-CC-C-C).

Sequence similaritiesi

Belongs to the conotoxin O1 superfamily.Curated

Keywords - Domaini

Knottin

Family and domain databases

InterProiIPR012322. Conotoxin_d-typ_CS.
[Graphical view]
PROSITEiPS60005. DELTA_CONOTOXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P60513-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30 
DDCIKPYGFC SLPILKNGLC CSGACVGVCA DL
Length:32
Mass (Da):3,279
Last modified:March 1, 2004 - v1
Checksum:i96C544273232D62D
GO

Mass spectrometryi

Molecular mass is 3288.3 Da from positions 1 - 32. Determined by ESI. 1 Publication

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G1PNMR-A1-32[»]
1G1ZNMR-A1-32[»]
ProteinModelPortaliP60513.
SMRiP60513. Positions 1-32.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ConoServeri1561. EVIA.

Miscellaneous databases

EvolutionaryTraceiP60513.

Family and domain databases

InterProiIPR012322. Conotoxin_d-typ_CS.
[Graphical view]
PROSITEiPS60005. DELTA_CONOTOXIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A delta-conotoxin from Conus ermineus venom inhibits inactivation in vertebrate neuronal Na+ channels but not in skeletal and cardiac muscles."
    Barbier J., Lamthanh H., Le Gall F., Favreau P., Benoit E., Chen H., Gilles N., Ilan N., Heinemann S.H., Gordon D., Menez A., Molgo J.
    J. Biol. Chem. 279:4680-4685(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, HYDROXYLATION AT PRO-6, AMIDATION AT LEU-32, SYNTHESIS.
    Tissue: Venom.
  2. "NMR solution structures of delta-conotoxin EVIA from Conus ermineus that selectively acts on vertebrate neuronal Na+ channels."
    Volpon L., Lamthanh H., Barbier J., Gilles N., Molgo J., Menez A., Lancelin J.-M.
    J. Biol. Chem. 279:21356-21366(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, TOXIC DOSE, DISULFIDE BONDS, SYNTHESIS, MUTAGENESIS OF PRO-13.
    Tissue: Venom.

Entry informationi

Entry nameiCO6A_CONER
AccessioniPrimary (citable) accession number: P60513
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2004
Last modified: December 9, 2015
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Miscellaneous

Does not affect rat skeletal muscle (Nav1.4/SCN4A) and human cardiac muscle (Nav1.5/SCN5A) sodium channels.1 Publication
Exists in two forms, due to cis-trans isomerization at 12-Leu-Pro-13.

Caution

Another delta-conotoxin was named EVIA in 2001, but this toxin was renamed EVIB.Curated

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.