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P01522 (CO16A_CONGE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 101. 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:
Omega-conotoxin GVIA
Alternative name(s):
SNX-124
Shaker peptide

Cleaved into the following 2 chains:

  1. Omega-conotoxin GVIB
  2. Omega-conotoxin GVIC
OrganismConus geographus (Geography cone) (Nubecula geographus)
Taxonomic identifier6491 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Protein attributes

Sequence length73 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav).

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom duct.

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).

Sequence similarities

Belongs to the conotoxin O1 superfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 4523
PRO_0000034906
Peptide46 – 7328Omega-conotoxin GVIB Ref.3
PRO_0000034907
Peptide46 – 7227Omega-conotoxin GVIA Ref.2
PRO_0000034908
Peptide46 – 7126Omega-conotoxin GVIC
PRO_0000034909

Amino acid modifications

Modified residue4914-hydroxyproline Ref.2
Modified residue5514-hydroxyproline Ref.2
Modified residue6614-hydroxyproline Ref.2
Modified residue721Tyrosine amide; in form omega-conotoxin GVIA
Disulfide bond46 ↔ 61 Ref.4 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12
Disulfide bond53 ↔ 64 Ref.4 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12
Disulfide bond60 ↔ 71 Ref.4 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Experimental info

Mutagenesis471K → A: Strong decrease in activity. Ref.5 Ref.7
Mutagenesis581Y → A: Strong decrease in activity. Ref.6 Ref.7
Mutagenesis581Y → F: Decrease in affinity. Ref.6 Ref.7
Mutagenesis621R → A: Decrease in potency, but not in affinity. Ref.5 Ref.7
Mutagenesis671Y → A: Decrease in potency, but not in affinity. Ref.7
Mutagenesis691K → A: Decrease in potency, but not in affinity. Ref.5 Ref.7
Mutagenesis701R → A: No change in activity. Ref.5

Secondary structure

........ 73
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01522 [UniParc].

Last modified February 1, 1994. Version 2.
Checksum: 51A8C8FA630F7175

FASTA737,851
        10         20         30         40         50         60 
MKLTCVVIVA VLLLTACQLI TADDSRGTQK HRALGSTTEL SLSTRCKSPG SSCSPTSYNC 

        70 
CRSCNPYTKR CYG 

« Hide

References

[1]"Precursor structure of omega-conotoxin GVIA determined from a cDNA clone."
Colledge C.J., Hunsperger J.P., Imperial J.S., Hillyard D.R.
Toxicon 30:1111-1116(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Purification and sequence of a presynaptic peptide toxin from Conus geographus venom."
Olivera B.M., McIntosh J.M., Cruz L.J., Luque F.A., Gray W.R.
Biochemistry 23:5087-5090(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 46-72 (GVIA).
[3]"Peptide neurotoxins from fish-hunting cone snails."
Olivera B.M., Gray W.R., Zeikus R.D., McIntosh J.M., Varga J., Rivier J.E., de Santos V., Cruz L.J.
Science 230:1338-1343(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 46-73 (GVIB AND GVIC).
[4]"Synthesis and secondary-structure determination of omega-conotoxin GVIA: a 27-peptide with three intramolecular disulfide bonds."
Nishiuchi Y., Kumagaye K., Noda Y., Watanabe T.X., Sakakibara S.
Biopolymers 25:S61-S68(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS OF 46-72 (GVIA), DISULFIDE BONDS.
[5]"Role of basic residues for the binding of omega-conotoxin GVIA to N-type calcium channels."
Sato K., Park N.G., Kohno T., Maeda T., Kim J.-I., Kato R., Takahashi M.
Biochem. Biophys. Res. Commun. 194:1292-1296(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LYS-47; ARG-62; LYS-69 AND ARG-70.
[6]"Hydroxyl group of Tyr13 is essential for the activity of omega-conotoxin GVIA, a peptide toxin for N-type calcium channel."
Kim J.-I., Takahashi M., Ogura A., Kohno T., Kudo Y., Sato K.
J. Biol. Chem. 269:23876-23878(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TYR-58.
[7]"Structure-function relationships of omega-conotoxin GVIA. Synthesis, structure, calcium channel binding, and functional assay of alanine-substituted analogues."
Lew M.J., Flinn J.P., Pallaghy P.K., Murphy R., Whorlow S.L., Wright C.E., Norton R.S., Angus J.A.
J. Biol. Chem. 272:12014-12023(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS OF 46-72 (GVIA), MUTAGENESIS OF LYS-47; TYR-58; ARG-62; TYR-67 AND LYS-69, STRUCTURE BY NMR OF 46-72 (GVIA).
[8]"Three-dimensional structure of omega-conotoxin GVIA determined by 1H NMR."
Sevilla P., Bruix M., Santoro J., Gago F., Garcia A.G., Rico M.
Biochem. Biophys. Res. Commun. 192:1238-1244(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 46-72 (GVIA), DISULFIDE BONDS.
[9]"Solution structure of omega-conotoxin GVIA using 2-D NMR spectroscopy and relaxation matrix analysis."
Davis J.H., Bradley E.K., Miljanich G.P., Nadasdi L., Ramachandran J., Basus V.J.
Biochemistry 32:7396-7405(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 46-72 (GVIA), DISULFIDE BONDS.
[10]"Three-dimensional structure in solution of the calcium channel blocker omega-conotoxin."
Pallaghy P.K., Duggan B.M., Pennington M.W., Norton R.S.
J. Mol. Biol. 234:405-420(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 46-72 (GVIA), DISULFIDE BONDS.
[11]"Solution structure of the calcium channel antagonist omega-conotoxin GVIA."
Skalicky J.J., Metzler W.J., Ciesla D.J., Galdes A., Pardi A.
Protein Sci. 2:1591-1603(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 46-72 (GVIA), DISULFIDE BONDS.
[12]"Refined solution structure of omega-conotoxin GVIA: implications for calcium channel binding."
Pallaghy P.K., Norton R.S.
J. Pept. Res. 53:343-351(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 46-72 (GVIA), DISULFIDE BONDS.
[13]"Structure-activity relationships of omega-conotoxins at N-type voltage-sensitive calcium channels."
Nielsen K.J., Schroeder T., Lewis R.J.
J. Mol. Recognit. 13:55-70(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M84612 mRNA. Translation: AAA81590.1.
PIRNTKN6G. A44006.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OMCNMR-A46-72[»]
1TR6NMR-A46-72[»]
1TTLNMR-A46-72[»]
2CCONMR-A46-72[»]
ProteinModelPortalP01522.
SMRP01522. Positions 46-72.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP01522. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

ConoServer820. GVIA precursor.

Family and domain databases

InterProIPR004214. Conotoxin.
IPR012321. Conotoxin_omega-typ_CS.
[Graphical view]
PfamPF02950. Conotoxin. 1 hit.
[Graphical view]
PROSITEPS60004. OMEGA_CONOTOXIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP01522.

Entry information

Entry nameCO16A_CONGE
AccessionPrimary (citable) accession number: P01522
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1994
Last modified: October 16, 2013
This is version 101 of the entry and version 2 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