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Protein

Delta-conotoxin TxVIA

Gene
N/A
Organism
Conus textile (Cloth-of-gold 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 (Nav) and inhibit the inactivation process. Binding of this toxin is strongly calcium-dependent but not voltage-dependent. The binding site is most likely on the extracellular side of the sodium channel. Binds receptor sites on both mollusk and rat central nervous system, but despite its high affinity binding to rat sodium channel, it has no functional effect in vivo and in vitro on it. Has also no effect on Gambusia fish. Is important in mollusk for the paralysis of the prey. Upon injection of the peptide, a subordinate lobster assumes an exaggerated dominant posture (of a 'King-Kong' lobster!).

GO - Molecular functioni

  1. sodium channel inhibitor activity Source: InterPro

GO - Biological processi

  1. pathogenesis Source: InterPro
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 TxVIA
Short name:
TxIA
Alternative name(s):
Conotoxin King-Kong 0
Short name:
KK-0
OrganismiConus textile (Cloth-of-gold cone)
Taxonomic identifieri6494 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Organism-specific databases

ConoServeri598. TxVIA precursor.

Subcellular locationi

  1. Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Propeptidei23 – 4927PRO_0000034900Add
BLAST
Peptidei52 – 7827Delta-conotoxin TxVIAPRO_0000034901Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi53 ↔ 68
Modified residuei59 – 591Methionine sulfoxide1 Publication
Disulfide bondi60 ↔ 72
Disulfide bondi67 ↔ 77

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Oxidation

Expressioni

Tissue specificityi

Expressed by the venom duct.1 Publication

Structurei

Secondary structure

1
78
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi62 – 643Combined sources
Beta strandi67 – 704Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FU3NMR-A52-78[»]
SMRiP18511. Positions 52-78.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18511.

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, Signal

Family and domain databases

InterProiIPR004214. Conotoxin.
IPR012322. Conotoxin_d-typ_CS.
[Graphical view]
PfamiPF02950. Conotoxin. 1 hit.
[Graphical view]
PROSITEiPS60005. DELTA_CONOTOXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P18511-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLTCMMIVA VLFLTAWTFA TADDPRNGLG NLFSNAHHEM KNPEASKLNK
60 70
RWCKQSGEMC NLLDQNCCDG YCIVLVCT
Length:78
Mass (Da):8,760
Last modified:November 1, 1990 - v1
Checksum:iC5CBFD462AD40A35
GO

Mass spectrometryi

Molecular mass is 3034.2±0.05 Da from positions 52 - 78. Determined by ESI. Without oxidation at Met-59.1 Publication
Molecular mass is 3050.189±0.05 Da from positions 52 - 78. Determined by ESI. With oxidation at Met-59.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53283 mRNA. Translation: CAA37377.1.
PIRiS12513.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53283 mRNA. Translation: CAA37377.1.
PIRiS12513.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FU3NMR-A52-78[»]
SMRiP18511. Positions 52-78.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ConoServeri598. TxVIA precursor.

Miscellaneous databases

EvolutionaryTraceiP18511.

Family and domain databases

InterProiIPR004214. Conotoxin.
IPR012322. Conotoxin_d-typ_CS.
[Graphical view]
PfamiPF02950. Conotoxin. 1 hit.
[Graphical view]
PROSITEiPS60005. DELTA_CONOTOXIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Constant and hypervariable regions in conotoxin propeptides."
    Woodward S.R., Cruz L.J., Olivera B.M., Hillyard D.R.
    EMBO J. 9:1015-1020(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "A molluscivorous Conus toxin: conserved frameworks in conotoxins."
    Hillyard D.R., Olivera B.M., Woodward S.R., Corpuz G.P., Gray W.R., Ramilo C.A., Cruz L.J.
    Biochemistry 28:358-361(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 52-78.
  3. "Mollusc-specific toxins from the venom of Conus textile neovicarius."
    Fainzilber M., Gordon D., Hasson A., Spira M.E., Zlotkin E.
    Eur. J. Biochem. 202:589-595(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 52-78.
    Strain: Neovicarius.
  4. "Rapid sensitive analysis of cysteine rich peptide venom components."
    Ueberheide B.M., Fenyo D., Alewood P.F., Chait B.T.
    Proc. Natl. Acad. Sci. U.S.A. 106:6910-6915(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 52-78, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, DISULFIDE BONDS, OXIDATION AT MET-59.
    Tissue: Venom.
  5. "Alteration of sodium currents by new peptide toxins from the venom of a molluscivorous Conus snail."
    Hasson A., Fainzilber M., Gordon D., Zlotkin E., Spira M.E.
    Eur. J. Neurosci. 5:56-64(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "A new neurotoxin receptor site on sodium channels is identified by a conotoxin that affects sodium channel inactivation in molluscs and acts as an antagonist in rat brain."
    Fainzilber M., Kofman O., Zlotkin E., Gordon D.
    J. Biol. Chem. 269:2574-2580(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "Delta-conotoxin GmVIA, a novel peptide from the venom of Conus gloriamaris."
    Shon K.-J., Hasson A., Spira M.E., Cruz L.J., Gray W.R., Olivera B.M.
    Biochemistry 33:11420-11425(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
    Tissue: Venom.
  8. "Three-dimensional solution structure of the sodium channel agonist/antagonist delta-conotoxin TxVIA."
    Kohno T., Sasaki T., Kobayashi K., Fainzilber M., Sato K.
    J. Biol. Chem. 277:36387-36391(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, DISULFIDE BONDS.

Entry informationi

Entry nameiCO16A_CONTE
AccessioniPrimary (citable) accession number: P18511
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: April 1, 2015
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Miscellaneous

Veratridine increases the rate of dissociation in a dose-dependent manner.

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

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.