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P01523

- CM3A_CONGE

UniProt

P01523 - CM3A_CONGE

Protein

Mu-conotoxin GIIIA

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

    Mu-conotoxins block voltage-gated sodium channels (Nav). This toxin potently blocks Nav1.4/SCN4A. It also moderately blocks rNav1.1/SCN1A, rNav1.2/SCN2A, and mNav1.6/SCN8A. The inhibition is reversible. Induces paralysis in vertebrates.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei63 – 631Important for binding sodium channel

    GO - Molecular functioni

    1. sodium channel inhibitor activity Source: InterPro

    GO - Biological processi

    1. pathogenesis Source: InterPro

    Keywords - Molecular functioni

    Ion channel impairing toxin, Neurotoxin, Toxin, Voltage-gated sodium channel impairing toxin

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mu-conotoxin GIIIA
    Alternative name(s):
    G3.9
    Geographutoxin I
    Short name:
    GTx-I
    Myotoxin I
    OrganismiConus geographus (Geography cone) (Nubecula geographus)
    Taxonomic identifieri6491 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

    Organism-specific databases

    ConoServeri1570. GIIIA [R13A].
    1464. GIIIA precursor.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi63 – 631R → A: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Propeptidei20 – 50312 PublicationsPRO_0000246004Add
    BLAST
    Peptidei51 – 7222Mu-conotoxin GIIIAPRO_0000044493Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi53 ↔ 651 Publication
    Disulfide bondi54 ↔ 701 Publication
    Modified residuei56 – 5614-hydroxyproline; partial3 Publications
    Modified residuei57 – 5714-hydroxyproline; partial3 Publications
    Disulfide bondi60 ↔ 711 Publication
    Modified residuei67 – 6714-hydroxyproline3 Publications
    Modified residuei72 – 721Alanine amide3 Publications

    Post-translational modificationi

    Hydroxylated; hydroxylations improve the ability to block.2 Publications

    Keywords - PTMi

    Amidation, Cleavage on pair of basic residues, Disulfide bond, Hydroxylation

    Expressioni

    Tissue specificityi

    Expressed by the venom duct.

    Structurei

    Secondary structure

    1
    74
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi53 – 575
    Helixi63 – 653
    Turni69 – 713

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TCGNMR-A51-72[»]
    1TCHNMR-A51-72[»]
    1TCJNMR-A51-72[»]
    1TCKNMR-A51-72[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01523.

    Family & Domainsi

    Domaini

    The cysteine framework is III (CC-C-C-CC). Classified in the M-4 branch, since 4 residues stand between the fourth and the fifth cysteine residues.

    Sequence similaritiesi

    Belongs to the conotoxin M superfamily.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR008036. Conotoxin_mu-typ.
    [Graphical view]
    PfamiPF05374. Mu-conotoxin. 1 hit.
    [Graphical view]
    PROSITEiPS60013. MU_CONOTOXIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P01523-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKLGVLLTI CLLLFPLTAL PMDGDEPANR PVERMQDNIS SEQYPLFEKR   50
    RDCCTPPKKC KDRQCKPQRC CAGR 74
    Length:74
    Mass (Da):8,455
    Last modified:July 11, 2006 - v2
    Checksum:i94CC38599C8374BA
    GO

    Sequence databases

    PIRiA01786. MXKN1.

    Cross-referencesi

    Sequence databases

    PIRi A01786. MXKN1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TCG NMR - A 51-72 [» ]
    1TCH NMR - A 51-72 [» ]
    1TCJ NMR - A 51-72 [» ]
    1TCK NMR - A 51-72 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    ConoServeri 1570. GIIIA [R13A].
    1464. GIIIA precursor.

    Miscellaneous databases

    EvolutionaryTracei P01523.

    Family and domain databases

    InterProi IPR008036. Conotoxin_mu-typ.
    [Graphical view ]
    Pfami PF05374. Mu-conotoxin. 1 hit.
    [Graphical view ]
    PROSITEi PS60013. MU_CONOTOXIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Definition of the M-conotoxin superfamily: characterization of novel peptides from molluscivorous Conus venoms."
      Corpuz G.P., Jacobsen R.B., Jimenez E.C., Watkins M., Walker C., Colledge C., Garrett J.E., McDougal O., Li W., Gray W.R., Hillyard D.R., Rivier J., McIntosh J.M., Cruz L.J., Olivera B.M.
      Biochemistry 44:8176-8186(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Venom duct.
    2. "Conus geographus toxins that discriminate between neuronal and muscle sodium channels."
      Cruz L.J., Gray W.R., Olivera B.M., Zeikus R.D., Kerr L., Yoshikami D., Moczydlowski E.
      J. Biol. Chem. 260:9280-9288(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 51-72, FUNCTION, BIOASSAY.
      Tissue: Venom.
    3. "The amino acid sequences of homologous hydroxyproline-containing myotoxins from the marine snail Conus geographus venom."
      Sato S., Nakamura H., Ohizumi Y., Kobayashi J., Hirata Y.
      FEBS Lett. 155:277-280(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 51-72.
      Tissue: Venom.
    4. "Disulfide pairings in geographutoxin I, a peptide neurotoxin from Conus geographus."
      Hidaka Y., Sato K., Nakamura H., Kobayashi J., Ohizumi Y., Simonishi Y.
      FEBS Lett. 264:29-32(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    5. "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 51-72, ROLE OF HYDROXYLATION.
    6. "Pruning nature: biodiversity-derived discovery of novel sodium channel blocking conotoxins from Conus bullatus."
      Holford M., Zhang M.-M., Gowd K.H., Azam L., Green B.R., Watkins M., Ownby J.-P., Yoshikami D., Bulaj G., Olivera B.M.
      Toxicon 53:90-98(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "mu-Conotoxins that differentially block sodium channels Nav1.1 through 1.8 identify those responsible for action potentials in sciatic nerve."
      Wilson M.J., Yoshikami D., Azam L., Gajewiak J., Olivera B.M., Bulaj G., Zhang M.M.
      Proc. Natl. Acad. Sci. U.S.A. 108:10302-10307(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION ON SODIUM CHANNELS, SYNTHESIS OF 51-72.
    8. "Solution structure of mu-conotoxin GIIIA analysed by 2D-NMR and distance geometry calculations."
      Ott K.-H., Becker S., Gordon R.D., Rueterjans H.
      FEBS Lett. 278:160-166(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 51-72, HYDROXYLATION AT PRO-56; PRO-57 AND PRO-67, AMIDATION AT ALA-72, DISULFIDE BONDS.
    9. "Tertiary structure of conotoxin GIIIA in aqueous solution."
      Lancelin J.-M., Kohda D., Tate S., Yanagawa Y., Abe T., Satake M., Inagaki F.
      Biochemistry 30:6908-6916(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 51-72, HYDROXYLATION AT PRO-56; PRO-57 AND PRO-67, AMIDATION AT ALA-72, DISULFIDE BONDS.
    10. "Structure-activity relationships of mu-conotoxin GIIIA: structure determination of active and inactive sodium channel blocker peptides by NMR and simulated annealing calculations."
      Wakamatsu K., Kohda D., Hatanaka H., Lancelin J.M., Ishida Y., Oya M., Nakamura H., Inagaki F., Sato K.
      Biochemistry 31:12577-12584(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 51-72, SYNTHESIS OF 51-72, DISULFIDE BONDS, MUTAGENESIS OF ARG-63.

    Entry informationi

    Entry nameiCM3A_CONGE
    AccessioniPrimary (citable) accession number: P01523
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 11, 2006
    Last modified: October 1, 2014
    This is version 99 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programAnimal Toxin Annotation Program

    Miscellaneousi

    Miscellaneous

    Does not block rNav1.3/SCN3A, rNav1.5/SCN5A, rNav1.7/SCN9A, and rNav1.8/SCN10A (PubMed:21652775). Nav1.4/SCN4A sodium channels but did not affect folding.1 Publication

    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