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P01521

- CA1_CONMA

UniProt

P01521 - CA1_CONMA

Protein

Alpha-conotoxin MI

Gene
N/A
Organism
Conus magus (Magus cone) (Magician's cone snail)
Status
Reviewed - Annotation score: 5 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. Blocks mammalian nAChR composed of alpha-1/delta subunits with high potency and alpha-1/gamma with a low potency.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 MI
    Short name:
    Alpha-MI
    Short name:
    CtxMI
    Alternative name(s):
    M1
    OrganismiConus magus (Magus cone) (Magician's cone snail)
    Taxonomic identifieri6492 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

    Organism-specific databases

    ConoServeri23. MI.

    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
    Mutagenesisi2 – 21R → A: 4-fold loss of activity. 1 Publication
    Mutagenesisi5 – 51H → A: 3-fold loss of activity. 1 Publication
    Mutagenesisi6 – 61P → A: 73-fold loss of activity. 1 Publication
    Mutagenesisi10 – 101K → A: 9-fold loss of activity. 1 Publication
    Mutagenesisi11 – 111N → A: 3-fold loss of activity. 1 Publication
    Mutagenesisi12 – 121Y → A: 8500-fold loss of activity. 1 Publication
    Mutagenesisi12 – 121Y → H: 33-fold loss of activity. 1 Publication
    Mutagenesisi12 – 121Y → M: 48-fold loss of activity. 1 Publication
    Mutagenesisi12 – 121Y → W: 5-fold loss of activity. 1 Publication
    Mutagenesisi13 – 131S → A: No loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Peptidei1 – 1414Alpha-conotoxin MIPRO_0000044461Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi3 ↔ 81 Publication
    Disulfide bondi4 ↔ 141 Publication
    Modified residuei14 – 141Cysteine amide1 Publication

    Post-translational modificationi

    Amidated; synthetic peptide with a C-terminus free is 6-fold less active than the amidated peptide.

    Keywords - PTMi

    Amidation, Disulfide bond

    Expressioni

    Tissue specificityi

    Expressed by the venom duct.

    Family & Domainsi

    Domaini

    The cysteine framework is I (CC-C-C). Alpha3/5 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: Complete.

    P01521-1 [UniParc]FASTAAdd to Basket

    « Hide

    GRCCHPACGK NYSC                                          14
    Length:14
    Mass (Da):1,499
    Last modified:July 21, 1986 - v1
    Checksum:iDEEE91898BF5E5BD
    GO

    Sequence databases

    PIRiA01784. NTKN1M.

    Cross-referencesi

    Sequence databases

    PIRi A01784. NTKN1M.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    ConoServeri 23. MI.

    Family and domain databases

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

    Publicationsi

    1. "Isolation and structure of a peptide toxin from the marine snail Conus magus."
      McIntosh J.M., Cruz L.J., Hunkapiller M.W., Gray W.R., Olivera B.M.
      Arch. Biochem. Biophys. 218:329-334(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
    2. "Conotoxin MI. Disulfide bonding and conformational states."
      Gray W.R., Rivier J.E., Galyean R., Cruz L.J., Olivera B.M.
      J. Biol. Chem. 258:12247-12251(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    3. "Critical residues influence the affinity and selectivity of alpha-conotoxin MI for nicotinic acetylcholine receptors."
      Jacobsen R.B., DelaCruz R.G., Grose J.H., McIntosh J.M., Yoshikami D., Olivera B.M.
      Biochemistry 38:13310-13315(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SYNTHESIS, MUTAGENESIS OF ARG-2; HIS-5; PRO-6; LYS-10; ASN-11; TYR-12 AND SER-13.

    Entry informationi

    Entry nameiCA1_CONMA
    AccessioniPrimary (citable) accession number: P01521
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 67 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

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3