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P37300

- CO7C_CONMA

UniProt

P37300 - CO7C_CONMA

Protein

Omega-conotoxin MVIIC

Gene
N/A
Organism
Conus magus (Magus cone) (Magician's cone snail)
Status
Reviewed - Annotation score: 4 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). This toxin preferentially blocks P/Q-type calcium channels (Cav2.1/CACNA1A).1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei15 – 151Important for calcium channel binding

    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 MVIIC
    Alternative name(s):
    SNX-230
    OrganismiConus magus (Magus cone) (Magician's cone snail)
    Taxonomic identifieri6492 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

    Organism-specific databases

    ConoServeri822. MVIIC 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
    Mutagenesisi15 – 151Y → A: High decrease in binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei‹1 – 2›2PRO_0000034916
    Peptidei3 – 2826Omega-conotoxin MVIICPRO_0000034917Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi3 ↔ 18
    Disulfide bondi10 ↔ 22
    Disulfide bondi17 ↔ 28
    Modified residuei28 – 281Cysteine amide

    Post-translational modificationi

    Not hydroxylated; hydroxylation, on a synthetic hydroxylated MVIIC, has a significant impact on the oxidative folding but not on the biological activity.

    Keywords - PTMi

    Amidation, Disulfide bond

    Expressioni

    Tissue specificityi

    Expressed by the venom duct.

    Structurei

    Secondary structure

    1
    29
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni12 – 154
    Beta strandi17 – 204

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CNNNMR-A3-28[»]
    1OMNNMR-A3-28[»]
    1V4QNMR-A3-26[»]
    ProteinModelPortaliP37300.
    SMRiP37300. Positions 3-28.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP37300.

    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

    Family and domain databases

    InterProiIPR012321. Conotoxin_omega-typ_CS.
    [Graphical view]
    PROSITEiPS60004. OMEGA_CONOTOXIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

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

    P37300-1 [UniParc]FASTAAdd to Basket

    « Hide

    TRCKGKGAPC RKTMYDCCSG SCGRRGKCG                          29
    Length:29
    Mass (Da):3,071
    Last modified:October 1, 1994 - v1
    Checksum:iAC7A68948474728A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S40826 mRNA. Translation: AAB22674.1.
    PIRiJH0699.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S40826 mRNA. Translation: AAB22674.1 .
    PIRi JH0699.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CNN NMR - A 3-28 [» ]
    1OMN NMR - A 3-28 [» ]
    1V4Q NMR - A 3-26 [» ]
    ProteinModelPortali P37300.
    SMRi P37300. Positions 3-28.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    ConoServeri 822. MVIIC precursor.

    Miscellaneous databases

    EvolutionaryTracei P37300.

    Family and domain databases

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

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 3-28, FUNCTION.
    2. "Tyr13 is essential for the binding of omega-conotoxin MVIIC to the P/Q-type calcium channel."
      Kim J.-I., Takahashi M., Martin-Moutot N., Seagar M.J., Ohtake A., Sato K.
      Biochem. Biophys. Res. Commun. 214:305-309(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-15.
    3. "Role of hydroxyprolines in the in vitro oxidative folding and biological activity of conotoxins."
      Lopez-Vera E., Walewska A., Skalicky J.J., Olivera B.M., Bulaj G.
      Biochemistry 47:1741-1751(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SYNTHESIS OF 3-28, ROLE OF HYDROXYLATION.
    4. "Solution structure of omega-conotoxin MVIIC, a high affinity ligand of P-type calcium channels, using 1H NMR spectroscopy and complete relaxation matrix analysis."
      Farr-Jones S., Miljanich G.P., Nadasdi L., Ramachandran J., Basus V.J.
      J. Mol. Biol. 248:106-124(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 3-28, DISULFIDE BONDS.
    5. "Structure-activity relationships of omega-conotoxins MVIIA, MVIIC and 14 loop splice hybrids at N and P/Q-type calcium channels."
      Nielsen K.J., Adams D., Thomas L., Bond T., Alewood P.F., Craik D.J., Lewis R.J.
      J. Mol. Biol. 289:1405-1421(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 3-28, DISULFIDE BONDS.

    Entry informationi

    Entry nameiCO7C_CONMA
    AccessioniPrimary (citable) accession number: P37300
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 88 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programAnimal Toxin Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    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