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Protein

Alpha-conotoxin Ms20.3

Gene
N/A
Organism
Conus mustelinus (Weasel cone)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Alpha-D-conopeptides act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin specifically blocks mammalian neuronal nAChR of the alpha-7/CHRNA7 (IC50=0.12 nM), alpha-3-beta-2/CHRNA3-CHRNB2 (IC50=1.08 nM), and alpha-4-beta-2/CHRNA4-CHRNB2 (IC50=4.5 nM) subtypes. Has no effect on alpha-3-beta-4/CHRNA3-CHRNB4, alpha-4-beta-4/CHRNA4-CHRNB4 and alpha-1-beta-1-epsilon-delta/CHRNA1-CHRNB1-CHRNE-CHRND subtypes of 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 Ms20.3
Alternative name(s):
Conopeptide alpha-D Ms
OrganismiConus mustelinus (Weasel cone)
Taxonomic identifieri101309 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConusRhizoconus

Organism-specific databases

ConoServeri3728 Ms20.3 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
PropeptideiPRO_000038873125 – 452 PublicationsAdd BLAST21
ChainiPRO_000038873246 – 94Alpha-conotoxin Ms20.3Add BLAST49

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei494-carboxyglutamate1 Publication1
Modified residuei554-hydroxyproline1 Publication1

Post-translational modificationi

Contains 5 disulfide bonds.Curated

Keywords - PTMi

Disulfide bond, Gamma-carboxyglutamic acid, Hydroxylation

Proteomic databases

PRIDEiC3VVN5

Expressioni

Tissue specificityi

Expressed by the venom duct.1 Publication

Interactioni

Subunit structurei

Hetero-, homo- or pseudo-homodimers (identical sequence, different post-translational modifications). Homodimer of [carboxyGlu-49, hydroxyPro-55]Ms20.3, and heterodimer of [carboxyGlu-49, hydroxyPro-55]Ms20.3 and [carboxy'Glu-50', hydroxy'Pro-56']Ms20.5 may exist.2 Publications

Structurei

3D structure databases

ProteinModelPortaliC3VVN5
SMRiC3VVN5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The cysteine framework is XX (C-CC-C-CC-C-C-C-C).

Sequence similaritiesi

Belongs to the conotoxin D superfamily.Curated

Keywords - Domaini

Signal

Sequencei

Sequence statusi: Complete.

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

C3VVN5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKLAVVLLV LLILPLSYFD AAGGQVVQGD RRGNGLARYL QRGDRDVREC
60 70 80 90
QVNTPGSSWG KCCMTRMCGT MCCARSGCTC VYHWRRGHGC SCPG
Length:94
Mass (Da):10,256
Last modified:March 2, 2010 - v2
Checksum:i571CDB3BB5CB36DB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti58S → K in ACP50600 (PubMed:19393680).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ896005 mRNA Translation: ACP50600.1

Similar proteinsi

Entry informationi

Entry nameiCDK3_CONMS
AccessioniPrimary (citable) accession number: C3VVN5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: March 2, 2010
Last modified: May 23, 2018
This is version 22 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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