SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P01522

- CO16A_CONGE

UniProt

P01522 - CO16A_CONGE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Omega-conotoxin GVIA
Gene
N/A
Organism
Conus geographus (Geography cone) (Nubecula geographus)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. ion channel inhibitor activity Source: InterPro

GO - Biological processi

  1. pathogenesis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

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

Names & Taxonomyi

Protein namesi
Recommended name:
Omega-conotoxin GVIA
Alternative name(s):
SNX-124
Shaker peptide
Cleaved into the following 2 chains:
OrganismiConus geographus (Geography cone) (Nubecula geographus)
Taxonomic identifieri6491 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Organism-specific databases

ConoServeri820. GVIA precursor.

Subcellular locationi

GO - Cellular componenti

  1. other organism presynaptic membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi47 – 471K → A: Strong decrease in activity. 2 Publications
Mutagenesisi58 – 581Y → A: Strong decrease in activity. 2 Publications
Mutagenesisi58 – 581Y → F: Decrease in affinity. 2 Publications
Mutagenesisi62 – 621R → A: Decrease in potency, but not in affinity. 2 Publications
Mutagenesisi67 – 671Y → A: Decrease in potency, but not in affinity. 1 Publication
Mutagenesisi69 – 691K → A: Decrease in potency, but not in affinity. 2 Publications
Mutagenesisi70 – 701R → A: No change in activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222 Reviewed prediction
Add
BLAST
Propeptidei23 – 4523
PRO_0000034906Add
BLAST
Peptidei46 – 7328Omega-conotoxin GVIB1 Publication
PRO_0000034907Add
BLAST
Peptidei46 – 7227Omega-conotoxin GVIA1 Publication
PRO_0000034908Add
BLAST
Peptidei46 – 7126Omega-conotoxin GVIC
PRO_0000034909Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 616 Publications
Modified residuei49 – 4914-hydroxyproline1 Publication
Disulfide bondi53 ↔ 646 Publications
Modified residuei55 – 5514-hydroxyproline1 Publication
Disulfide bondi60 ↔ 716 Publications
Modified residuei66 – 6614-hydroxyproline1 Publication
Modified residuei72 – 721Tyrosine amide; in form omega-conotoxin GVIA

Keywords - PTMi

Amidation, Disulfide bond, Hydroxylation

Expressioni

Tissue specificityi

Expressed by the venom duct.

Interactioni

Protein-protein interaction databases

IntActiP01522. 1 interaction.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni55 – 584
Beta strandi60 – 623
Turni66 – 683
Beta strandi69 – 713

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OMCNMR-A46-72[»]
1TR6NMR-A46-72[»]
1TTLNMR-A46-72[»]
2CCONMR-A46-72[»]
ProteinModelPortaliP01522.
SMRiP01522. Positions 46-72.

Miscellaneous databases

EvolutionaryTraceiP01522.

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.

Keywords - Domaini

Knottin, Signal

Family and domain databases

InterProiIPR004214. Conotoxin.
IPR012321. Conotoxin_omega-typ_CS.
[Graphical view]
PfamiPF02950. Conotoxin. 1 hit.
[Graphical view]
PROSITEiPS60004. OMEGA_CONOTOXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P01522-1 [UniParc]FASTAAdd to Basket

« Hide

MKLTCVVIVA VLLLTACQLI TADDSRGTQK HRALGSTTEL SLSTRCKSPG   50
SSCSPTSYNC CRSCNPYTKR CYG 73
Length:73
Mass (Da):7,851
Last modified:February 1, 1994 - v2
Checksum:i51A8C8FA630F7175
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M84612 mRNA. Translation: AAA81590.1.
PIRiA44006. NTKN6G.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M84612 mRNA. Translation: AAA81590.1 .
PIRi A44006. NTKN6G.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1OMC NMR - A 46-72 [» ]
1TR6 NMR - A 46-72 [» ]
1TTL NMR - A 46-72 [» ]
2CCO NMR - A 46-72 [» ]
ProteinModelPortali P01522.
SMRi P01522. Positions 46-72.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P01522. 1 interaction.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

ConoServeri 820. GVIA precursor.

Miscellaneous databases

EvolutionaryTracei P01522.

Family and domain databases

InterProi IPR004214. Conotoxin.
IPR012321. Conotoxin_omega-typ_CS.
[Graphical view ]
Pfami PF02950. Conotoxin. 1 hit.
[Graphical view ]
PROSITEi PS60004. OMEGA_CONOTOXIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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), HYDROXYLATION AT PRO-49; PRO-55 AND PRO-66, AMIDATION AT TYR-72.
  3. 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.

Entry informationi

Entry nameiCO16A_CONGE
AccessioniPrimary (citable) accession number: P01522
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1994
Last modified: September 3, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

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