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P50983

- CA1_CONIM

UniProt

P50983 - CA1_CONIM

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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

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
Complete GO annotation...

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 – 83Combined sources
Turni10 – 123Combined sources
Helixi13 – 153Combined sources

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

        10
IVRRGCCSDP RCAWRCG
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 29, 2014
This is version 88 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