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P01522

- CO16A_CONGE

UniProt

P01522 - CO16A_CONGE

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
  1. 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

    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

    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 – 2222Sequence AnalysisAdd
    BLAST
    Propeptidei23 – 45232 PublicationsPRO_0000034906Add
    BLAST
    Peptidei46 – 7328Omega-conotoxin GVIBPRO_0000034907Add
    BLAST
    Peptidei46 – 7227Omega-conotoxin GVIAPRO_0000034908Add
    BLAST
    Peptidei46 – 7126Omega-conotoxin GVICPRO_0000034909Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi46 ↔ 611 Publication
    Modified residuei49 – 4914-hydroxyproline1 Publication
    Disulfide bondi53 ↔ 641 Publication
    Modified residuei55 – 5514-hydroxyproline1 Publication
    Disulfide bondi60 ↔ 711 Publication
    Modified residuei66 – 6614-hydroxyproline1 Publication
    Modified residuei72 – 721Tyrosine amide; in form omega-conotoxin GVIA1 Publication

    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

    1
    73
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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.Curated

    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: October 1, 2014
    This is version 104 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