Skip Header

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

Alpha-conotoxin EIVA

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

Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin binds with high affinity to both fetal (alpha-1/beta-1/epsilon/delta subunits) and adult (alpha-1/beta-1/gamma/delta subunits) mammalian muscle nicotinic acetylcholine receptors (nAChR).

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 EIVA
OrganismiConus ermineus (Atlantic fish-hunting cone)
Taxonomic identifieri55423 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Organism-specific databases

ConoServeri1635. EIVA.

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_00000444641 – 30Alpha-conotoxin EIVAAdd BLAST30

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi2 ↔ 161 Publication
Disulfide bondi3 ↔ 111 Publication
Modified residuei74-hydroxyproline1 Publication1
Modified residuei134-hydroxyproline1 Publication1
Disulfide bondi14 ↔ 241 Publication
Modified residuei214-hydroxyproline1 Publication1
Modified residuei224-hydroxyproline1 Publication1
Modified residuei274-hydroxyproline1 Publication1
Modified residuei30Glycine amide1 Publication1

Keywords - PTMi

Amidation, Disulfide bond, Hydroxylation

Expressioni

Tissue specificityi

Expressed by the venom duct.

Structurei

Secondary structure

130
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 10Combined sources6
Beta strandi16 – 19Combined sources4
Helixi22 – 25Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PQRNMR-A1-30[»]
ProteinModelPortaliP58782.
SMRiP58782.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP58782.

Family & Domainsi

Domaini

The cysteine framework is IV (CC-C-C-C-C).

Sequence similaritiesi

Belongs to the conotoxin A superfamily.Curated

Family and domain databases

InterProiView protein in InterPro
IPR012498. Toxin_14.
PfamiView protein in Pfam
PF07829. Toxin_14. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD045217. Toxin_14. 1 hit.

Sequencei

Sequence statusi: Complete.

P58782-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30
GCCGPYPNAA CHPCGCKVGR PPYCDRPSGG
Length:30
Mass (Da):3,023
Last modified:April 16, 2002 - v1
Checksum:i5F373E7AAF385783
GO

Mass spectrometryi

Molecular mass is 3095.2 Da from positions 1 - 30. Determined by ESI. 1 Publication

Similar proteinsi

Entry informationi

Entry nameiCA4A_CONER
AccessioniPrimary (citable) accession number: P58782
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: April 16, 2002
Last modified: November 22, 2017
This is version 74 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families