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Protein

Conotoxin CcTx

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

Functioni

May specifically activate neuronal voltage-gated sodium channels (Nav) at the resting membrane potential. Causes a marked contraction and extension of the caudal and dorsal fins in fish and noticeable spontaneous contractions of isolated frog neuromuscular preparations.

Keywords - Molecular functioni

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

Names & Taxonomyi

Protein namesi
Recommended name:
Conotoxin CcTx
Alternative name(s):
Excitotoxin CcTx
OrganismiConus consors (Singed cone)
Taxonomic identifieri101297 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Organism-specific databases

ConoServeri1510. CcTx.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Peptidei1 – 3030Conotoxin CcTxPRO_0000044514Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 214-hydroxyproline1 Publication
Glycosylationi7 – 71O-linked (HexNAc...)1 Publication
Modified residuei17 – 1714-hydroxyproline1 Publication
Modified residuei22 – 2214-hydroxyproline1 Publication

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Expressioni

Tissue specificityi

Expressed by the venom duct.

Structurei

Secondary structure

1
30
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi23 – 264Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B1QNMR-P1-30[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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

Sequencei

Sequence statusi: Complete.

P58928-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30
APWLVPSQIT TCCGYNPGTM CPSCMCTNTC
Length:30
Mass (Da):3,184
Last modified:March 23, 2010 - v2
Checksum:iAD8E9CC5ABB0E065
GO

Mass spectrometryi

Molecular mass is 4156 Da from positions 1 - 30. Determined by ESI. 1 Publication

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B1QNMR-P1-30[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ConoServeri1510. CcTx.

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "A new conotoxin isolated from Conus consors venom acting selectively on axons and motor nerve terminals through a Na+-dependent mechanism."
    Le Gall F., Favreau P., Benoit E., Mattei C., Bouet F., Menou J.-L., Menez A., Letourneux Y., Molgo J.
    Eur. J. Neurosci. 11:3134-3142(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, HYDROXYLATION AT PRO-2; PRO-17 AND PRO-22, MASS SPECTROMETRY.
    Tissue: Venom.
  2. "Comparative proteomic study of the venom of the piscivorous cone snail Conus consors."
    Biass D., Dutertre S., Gerbault A., Menou J.L., Offord R., Favreau P., Stocklin R.
    J. Proteomics 72:210-218(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 7, GLYCOSYLATION AT SER-7.
  3. "Large-scale discovery of conopeptides and conoproteins in the injectable venom of a fish-hunting cone snail using a combined proteomic and transcriptomic approach."
    Violette A., Biass D., Dutertre S., Koua D., Piquemal D., Pierrat F., Stocklin R., Favreau P.
    J. Proteomics 75:5215-5225(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY OF GLYCOSYLATED AND NON-GLYCOSYLATED FORMS.
    Tissue: Venom.

Entry informationi

Entry nameiCEX_CONCN
AccessioniPrimary (citable) accession number: P58928
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: March 23, 2010
Last modified: July 22, 2015
This is version 47 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Miscellaneous

Found in both injectable (milked) (IV) and dissected venom (DV).1 Publication

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

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 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.