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Protein

Alpha-conotoxin ImII

Gene
N/A
Organism
Conus imperialis (Imperial cone)
Status
Reviewed-Annotation score: Annotation score: 3 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 neuronal mammalian alpha-7 (human and rat) and alpha-3/beta-2 (human) and muscle alpha-1-beta-1-delta-epsilon (human) nAChRs (PubMed:12384509, PubMed:15609996). Acts voltage-independently (PubMed:12384509). Does not competes with alpha-bungarotoxin for binding to the receptor (PubMed:12384509, PubMed:15609996). Binds to a different site than alpha-conotoxin ImI (PubMed:15609996).2 Publications

Miscellaneous

Does not inhibit alpha-2-beta-2, alpha-2-beta-4, alpha-3-beta-4, alpha-4-beta-2, alpha-4-beta-2 nAChRs.1 Publication

GO - Molecular functioni

Keywordsi

Molecular functionAcetylcholine receptor inhibiting toxin, Ion channel impairing toxin, Neurotoxin, Postsynaptic neurotoxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-conotoxin ImII1 Publication
Short name:
Alpha-CTx ImII1 Publication
OrganismiConus imperialis (Imperial cone)
Taxonomic identifieri35631 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Organism-specific databases

ConoServeri92. ImII precursor.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi10R → P: Gain of ability to compete with alpha-bungarotoxin. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_0000388685‹1 – 41 Publication›4
PeptideiPRO_00000348785 – 16Alpha-conotoxin ImII1 PublicationAdd BLAST12

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi6 ↔ 121 Publication
Disulfide bondi7 ↔ 161 Publication
Modified residuei16Cysteine amide1 Publication1

Keywords - PTMi

Amidation, Cleavage on pair of basic residues, Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom duct.Curated

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the conotoxin A superfamily.Curated

Family and domain databases

PROSITEiView protein in PROSITE
PS60014. ALPHA_CONOTOXIN. 1 hit.

Sequencei

Sequence statusi: Fragment.

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

Q8I6R5-1 [UniParc]FASTAAdd to basket

« Hide

        10 
IVRRACCSDR RCRWRCG
Length:17
Mass (Da):2,096
Last modified:March 1, 2003 - v1
Checksum:iCF90D9CEBB4C79CC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY159317 Genomic DNA. Translation: AAN78127.1.

Similar proteinsi

Entry informationi

Entry nameiCA2_CONIM
AccessioniPrimary (citable) accession number: Q8I6R5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: March 1, 2003
Last modified: November 22, 2017
This is version 55 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families