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P50983

- CA1_CONIM

UniProt

P50983 - CA1_CONIM

Protein

Alpha-conotoxin ImI

Gene
N/A
Organism
Conus imperialis (Imperial cone)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin blocks mammalian neuronal nAChRs (alpha-3/beta-2 > alpha-7 > alpha-3/beta-4). Acts voltage-independently. Is highly active against the neuromuscular receptor in frog.1 Publication

    Keywords - Molecular functioni

    Acetylcholine receptor inhibiting toxin, Ion channel impairing toxin, Neurotoxin, Postsynaptic neurotoxin, Toxin

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-conotoxin ImI
    Short name:
    Alpha-CTx ImI
    OrganismiConus imperialis (Imperial cone)
    Taxonomic identifieri35631 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

    Organism-specific databases

    ConoServeri93. ImI precursor.

    Subcellular locationi

    GO - Cellular componenti

    1. other organism postsynaptic membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi9 – 91D → L: Reduction of toxicity. 1 Publication
    Mutagenesisi11 – 111R → L: Reduction of toxicity. 1 Publication
    Mutagenesisi15 – 151R → E: No loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei‹1 – 4›41 PublicationPRO_0000273426
    Peptidei5 – 1612Alpha-conotoxin ImIPRO_0000034877Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi6 ↔ 12
    Disulfide bondi7 ↔ 16
    Modified residuei16 – 161Cysteine amide

    Post-translational modificationi

    Not hydroxylated; hydroxylation, on a synthetic hydroxylated ImI, improves its folding but impairs its activity against target receptors.

    Keywords - PTMi

    Amidation, Cleavage on pair of basic residues, Disulfide bond

    Expressioni

    Tissue specificityi

    Expressed by the venom duct.

    Structurei

    Secondary structure

    1
    17
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 83
    Turni10 – 123
    Helixi13 – 153

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CNLNMR-A5-16[»]
    1E74NMR-A5-14[»]
    1E75NMR-A5-16[»]
    1E76NMR-A5-16[»]
    1G2GNMR-A5-16[»]
    1IM1NMR-A5-16[»]
    1IMINMR-A5-16[»]
    2BC7NMR-A5-16[»]
    2BC8NMR-A5-16[»]
    2BYPX-ray2.07F/G/H/I/J5-16[»]
    2C9TX-ray2.25K/M/O/P/Q/R/S/T5-16[»]
    2IGUNMR-A5-16[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP50983.

    Family & Domainsi

    Domaini

    The cysteine framework is I (CC-C-C). Alpha4/3 pattern.

    Sequence similaritiesi

    Belongs to the conotoxin A superfamily.Curated

    Family and domain databases

    InterProiIPR018072. Conotoxin_a-typ_CS.
    [Graphical view]
    PROSITEiPS60014. ALPHA_CONOTOXIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

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

    P50983-1 [UniParc]FASTAAdd to Basket

    « Hide

    IVRRGCCSDP RCAWRCG                                       17
    Length:17
    Mass (Da):1,938
    Last modified:January 16, 2004 - v2
    Checksum:i9590D9CEA50279CF
    GO

    Experimental Info

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY159318 Genomic DNA. Translation: AAN78128.1.
    PIRiA53709.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY159318 Genomic DNA. Translation: AAN78128.1 .
    PIRi A53709.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CNL NMR - A 5-16 [» ]
    1E74 NMR - A 5-14 [» ]
    1E75 NMR - A 5-16 [» ]
    1E76 NMR - A 5-16 [» ]
    1G2G NMR - A 5-16 [» ]
    1IM1 NMR - A 5-16 [» ]
    1IMI NMR - A 5-16 [» ]
    2BC7 NMR - A 5-16 [» ]
    2BC8 NMR - A 5-16 [» ]
    2BYP X-ray 2.07 F/G/H/I/J 5-16 [» ]
    2C9T X-ray 2.25 K/M/O/P/Q/R/S/T 5-16 [» ]
    2IGU NMR - A 5-16 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    ConoServeri 93. ImI precursor.

    Miscellaneous databases

    EvolutionaryTracei P50983.

    Family and domain databases

    InterProi IPR018072. Conotoxin_a-typ_CS.
    [Graphical view ]
    PROSITEi PS60014. ALPHA_CONOTOXIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Alpha-conotoxins ImI and ImII: similar alpha 7 nicotinic receptor antagonists act at different sites."
      Ellison M.A., McIntosh J.M., Olivera B.M.
      J. Biol. Chem. 278:757-764(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SYNTHESIS OF 5-16.
      Tissue: Venom duct.
    2. "A nicotinic acetylcholine receptor ligand of unique specificity, alpha-conotoxin ImI."
      McIntosh J.M., Yoshikami D., Mahe E., Nielsen D.B., Rivier J.E., Gray W.R., Olivera B.M.
      J. Biol. Chem. 269:16733-16739(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 5-16, FUNCTION, SYNTHESIS OF 5-16, DISULFIDE BONDS.
      Tissue: Venom.
    3. "Alpha-conotoxin ImI exhibits subtype-specific nicotinic acetylcholine receptor blockade: preferential inhibition of homomeric alpha 7 and alpha 9 receptors."
      Johnson D.S., Martinez J., Elgoyhen A.B., Heinemann S.F., McIntosh J.M.
      Mol. Pharmacol. 48:194-199(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    4. "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 5-16, ROLE OF HYDROXYLATION.
    5. "NMR solution structure of alpha-conotoxin ImI and comparison to other conotoxins specific for neuronal nicotinic acetylcholine receptors."
      Rogers J.P., Luginbuehl P., Shen G.S., McCabe R.T., Stevens R.C., Wemmer D.E.
      Biochemistry 38:3874-3882(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 5-16, DISULFIDE BONDS.
    6. "Solution structure of alpha-conotoxin ImI determined by two-dimensional NMR spectroscopy."
      Gouda H., Hirono S.
      Biochim. Biophys. Acta 1431:384-394(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 5-16, DISULFIDE BONDS.
    7. "NMR spatial structure of alpha-conotoxin ImI reveals a common scaffold in snail and snake toxins recognizing neuronal nicotinic acetylcholine receptors."
      Maslennikov I.V., Shenkarev Z.O., Zhmak M.N., Ivanov V.T., Methfessel C., Tsetlin V.I., Arseniev A.S.
      FEBS Lett. 444:275-280(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 5-16, DISULFIDE BONDS.
    8. "Minimal conformation of the alpha-conotoxin ImI for the alpha7 neuronal nicotinic acetylcholine receptor recognition: correlated CD, NMR and binding studies."
      Lamthanh H., Jegou-Matheron C., Servent D., Menez A., Lancelin J.-M.
      FEBS Lett. 454:293-298(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 5-16, DISULFIDE BONDS.
    9. "Solution structure of alpha-conotoxin ImI by 1H nuclear magnetic resonance."
      Gehrmann J., Daly N.L., Alewood P.F., Craik D.J.
      J. Med. Chem. 42:2364-2372(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 5-16, DISULFIDE BONDS.
    10. "Structure-activity relationships in a peptidic alpha7 nicotinic acetylcholine receptor antagonist."
      Rogers J.P., Luginbuhl P., Pemberton K., Harty P., Wemmer D.E., Stevens R.C.
      J. Mol. Biol. 304:911-926(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-9; ARG-11 AND ARG-15, STRUCTURE BY NMR OF 5-16 OF THESE THREE MUTANTS, DISULFIDE BONDS.

    Entry informationi

    Entry nameiCA1_CONIM
    AccessioniPrimary (citable) accession number: P50983
    Secondary accession number(s): Q8I6R4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 16, 2004
    Last modified: October 1, 2014
    This is version 87 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programAnimal Toxin Annotation Program

    Miscellaneousi

    Miscellaneous

    Has no effect on nAChRs composed of alpha-2/beta-2, alpha-3/beta-2, alpha-4/beta-2, alpha-2/beta-4, alpha-3/beta-4, or alpha-4/beta-4 subunits.

    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