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Protein

Alpha-conotoxin MII

Gene
N/A
Organism
Conus magus (Magus cone) (Magician's cone snail)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Alpha-conotoxins bind to the nicotinic acetylcholine receptors (nAChR) and inhibit them. This toxin blocks neuronal mammalian nAChRs (alpha-6 or -3/beta-2 or -3 > alpha-3/beta-2 > alpha-3/beta-4 = alpha-4/beta-2).2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

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

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-conotoxin MII
Short name:
Alpha-MII
Short name:
CtxMII
Alternative name(s):
Alpha-conotoxin M2
OrganismiConus magus (Magus cone) (Magician's cone snail)
Taxonomic identifieri6492 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Organism-specific databases

ConoServeri8. MII precursor.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi53N → A: Causes a >2700-fold reduction in activity at the alpha-3/beta-2 nAChR. 1 Publication1
Mutagenesisi54P → A: Causes a 700-fold reduction in activity at the alpha-3/beta-2 nAChR. 1 Publication1
Mutagenesisi57H → A: Causes a 17-fold reduction in activity at the alpha-3/beta-2 nAChR. 1 Publication1
Mutagenesisi60H → A: Causes a 2700-fold reduction in activity at the alpha-3/beta-2 nAChR. 1 Publication1
Mutagenesisi63L → A: Causes a 15-fold reduction in activity at the alpha-3/beta-2 nAChR. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
PropeptideiPRO_000003488122 – 481 PublicationAdd BLAST27
PeptideiPRO_000003488249 – 64Alpha-conotoxin MIIAdd BLAST16

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi50 ↔ 56
Disulfide bondi51 ↔ 64
Modified residuei64Cysteine amide2 Publications1

Keywords - PTMi

Amidation, Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom duct.

Structurei

Secondary structure

168
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni50 – 52Combined sources3
Helixi54 – 59Combined sources6
Helixi61 – 63Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M2CNMR-A49-64[»]
1MIINMR-A49-64[»]
2AJWNMR-A49-64[»]
2AK0NMR-A49-64[»]
ProteinModelPortaliP56636.
SMRiP56636.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56636.

Family & Domainsi

Domaini

The cysteine framework is I (CC-C-C). Alpha4/7 pattern.

Sequence similaritiesi

Belongs to the conotoxin A superfamily.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR009958. Conotoxin_a-typ.
IPR018072. Conotoxin_a-typ_CS.
[Graphical view]
PfamiPF07365. Toxin_8. 1 hit.
[Graphical view]
PROSITEiPS60014. ALPHA_CONOTOXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P56636-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGMRMMFTVF LLVVLATTVV SFPSDRASDG RNAAANDKAS DVITLALKGC
60
CSNPVCHLEH SNLCGRRR
Length:68
Mass (Da):7,357
Last modified:September 5, 2006 - v3
Checksum:iFBD9AB40E6F277DF
GO

Mass spectrometryi

Molecular mass is 1710.6 Da from positions 49 - 64. Determined by LSI. 1 Publication

Sequence databases

PIRiA59046.

Cross-referencesi

Sequence databases

PIRiA59046.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M2CNMR-A49-64[»]
1MIINMR-A49-64[»]
2AJWNMR-A49-64[»]
2AK0NMR-A49-64[»]
ProteinModelPortaliP56636.
SMRiP56636.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ConoServeri8. MII precursor.

Miscellaneous databases

EvolutionaryTraceiP56636.

Family and domain databases

InterProiIPR009958. Conotoxin_a-typ.
IPR018072. Conotoxin_a-typ_CS.
[Graphical view]
PfamiPF07365. Toxin_8. 1 hit.
[Graphical view]
PROSITEiPS60014. ALPHA_CONOTOXIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCA2_CONMA
AccessioniPrimary (citable) accession number: P56636
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: September 5, 2006
Last modified: November 2, 2016
This is version 88 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Miscellaneous

There are currently a number of patents describing the use of this peptide in therapeutic applications.

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.