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Protein

Alpha-conotoxin EIVB

Gene
N/A
Organism
Conus ermineus (Atlantic fish-hunting cone)
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 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 EIVB
OrganismiConus ermineus (Atlantic fish-hunting cone)
Taxonomic identifieri55423 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaNeogastropodaConoideaConidaeConusChelyconus

Organism-specific databases

ConoServeri1740 EIVB

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_00000444651 – 30Alpha-conotoxin EIVBAdd BLAST30

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei74-hydroxyproline1 Publication1
Modified residuei134-hydroxyproline1 Publication1
Modified residuei214-hydroxyproline1 Publication1
Modified residuei224-hydroxyproline1 Publication1
Modified residuei274-hydroxyproline1 Publication1
Modified residuei30Glycine amide1 Publication1

Post-translational modificationi

Contains 3 disulfide bonds (By similarity). They are not added, since framework IV presents two different connectivities (I-V, II-III, IV-VI and I-III, II-V, IV-VI).By similarity

Keywords - PTMi

Amidation, Disulfide bond, Hydroxylation

Expressioni

Tissue specificityi

Expressed by the venom duct.

Structurei

3D structure databases

ProteinModelPortaliP58783
SMRiP58783
ModBaseiSearch...
MobiDBiSearch...

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.

P58783-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30
GCCGKYPNAA CHPCGCTVGR PPYCDRPSGG
Length:30
Mass (Da):3,027
Last modified:April 16, 2002 - v1
Checksum:i5F2D8FD1AF20F483
GO

Mass spectrometryi

Molecular mass is 3099.1 Da from positions 1 - 30. Determined by ESI. 1 Publication

Similar proteinsi

Cross-referencesi

3D structure databases

ProteinModelPortaliP58783
SMRiP58783
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ConoServeri1740 EIVB

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
ProtoNetiSearch...

Entry informationi

Entry nameiCA4B_CONER
AccessioniPrimary (citable) accession number: P58783
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: April 16, 2002
Last modified: September 12, 2018
This is version 65 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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