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P58928

- CEX_CONCN

UniProt

P58928 - CEX_CONCN

Protein

Conotoxin CcTx

Gene
N/A
Organism
Conus consors (Singed cone)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. 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

    1. other organism presynaptic membrane Source: UniProtKB-KW

    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 – 264

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    APWLVPSQIT TCCGYNPGTM CPSCMCTNTC                         30
    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:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4B1Q NMR - P 1-30 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    ConoServeri 1510. CcTx.

    Family and domain databases

    ProtoNeti Search...

    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: October 1, 2014
    This is version 45 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