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P18511 (CO16A_CONTE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Delta-conotoxin TxVIA

Short name=TxIA
Alternative name(s):
Conotoxin King-Kong 0
Short name=KK-0
OrganismConus textile (Cloth-of-gold cone)
Taxonomic identifier6494 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Protein attributes

Sequence length78 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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!).

Subcellular location

Secreted Ref.4.

Tissue specificity

Expressed by the venom duct. Ref.4

Domain

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).

Miscellaneous

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

Sequence similarities

Belongs to the conotoxin O1 superfamily.

Mass spectrometry

Molecular mass is 3034.2±0.05 Da from positions 52 - 78. Determined by ESI. Without oxidation at Met-59. Ref.4

Molecular mass is 3050.189±0.05 Da from positions 52 - 78. Determined by ESI. With oxidation at Met-59. Ref.4

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 4927
PRO_0000034900
Peptide52 – 7827Delta-conotoxin TxVIA Ref.2 Ref.3 Ref.4
PRO_0000034901

Sites

Site591Susceptible to oxidation

Amino acid modifications

Disulfide bond53 ↔ 68 Ref.4 Ref.7 Ref.8
Disulfide bond60 ↔ 72 Ref.4 Ref.7 Ref.8
Disulfide bond67 ↔ 77 Ref.4 Ref.7 Ref.8

Secondary structure

..... 78
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18511 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: C5CBFD462AD40A35

FASTA788,760
        10         20         30         40         50         60 
MKLTCMMIVA VLFLTAWTFA TADDPRNGLG NLFSNAHHEM KNPEASKLNK RWCKQSGEMC 

        70 
NLLDQNCCDG YCIVLVCT 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53283 mRNA. Translation: CAA37377.1.
PIRS12513.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FU3NMR-A52-78[»]
ProteinModelPortalP18511.
SMRP18511. Positions 52-78.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

ConoServer598. TxVIA precursor.

Family and domain databases

InterProIPR004214. Conotoxin.
IPR012322. Conotoxin_d-typ_CS.
[Graphical view]
PfamPF02950. Conotoxin. 1 hit.
[Graphical view]
PROSITEPS60005. DELTA_CONOTOXIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP18511.

Entry information

Entry nameCO16A_CONTE
AccessionPrimary (citable) accession number: P18511
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: October 16, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references