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Protein

Alpha-D-conotoxin GeXXA

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

Functioni

Alpha-D-conopeptides act as non-competitive inhibitors of nicotinic acetylcholine receptors (nAChR). This toxin has strong inhibitory activity on rat alpha-9-alpha-10 (CHRNA9/CHRNA10) (IC50=1.2 nM) and a moderate inhibitory activity on human alpha-7 (CHRNA7) (IC50=210 nM), rat alpha-3-beta-2 (CHRNA3/CHRNB2) (IC50=498 nM), rat alpha-3-beta-4 (CHRNA3/CHRNB4) (IC50=614 nM) and rat alpha-1-beta-1-delta-epsilon (CHRNA1/CHRNB1/CHRNE/CHRND) (IC50=743 nM) subtypes. Shows a weaker inhibitory activity on human alpha-9-alpha-10 (IC50=28 nM) than on the rat channel. This is explained by a different residue in the probable binding site (His-31 in rat alpha-10 and Leu-31 in human).1 Publication

Miscellaneous

Shows a very weak activity on alpha-4-beta-2 and alpha-4-beta-4 nAChR subtypes.1 Publication

GO - Molecular functioni

Keywordsi

Molecular functionAcetylcholine receptor inhibiting toxin, Neurotoxin, Postsynaptic neurotoxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-D-conotoxin GeXXA1 Publication
OrganismiConus generalis (General cone)
Taxonomic identifieri101304 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaNeogastropodaConoideaConidaeConusStrategoconus

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
Mutagenesisi46 – 65Missing : 70-fold decrease in inhibition of alpha-9-alpha-10 nAChR and loss of inhibition of all other nAChR subunits; when associated with S-73 (GeXXA-CTD, monomeric form). Add BLAST20
Mutagenesisi73C → S: 70-fold decrease in inhibition of alpha-9-alpha-10 nAChR and loss of inhibition of all other nAChR subunits; when associated with 46-D--L-65 (GeXXA-CTD, monomeric form). 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
PropeptideiPRO_000043896822 – 451 PublicationAdd BLAST24
ChainiPRO_500197084046 – 95Alpha-D-conotoxin GeXXAAdd BLAST50

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi51Interchain (with C-63)Combined sources1 Publication
Disulfide bondi63Interchain (with C-51)Combined sources1 Publication
Disulfide bondi64 ↔ 73Combined sources1 Publication
Disulfide bondi69 ↔ 81Combined sources1 Publication
Disulfide bondi74 ↔ 91Combined sources1 Publication
Disulfide bondi79 ↔ 93Combined sources1 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom duct.1 Publication

Structurei

Secondary structure

195
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SMRiA0A0A0VBX4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. This structure is present in the C-terminal domain.1 Publication
The cysteine framework is XX (C-CC-C-CC-C-C-C-C).Curated

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.

A0A0A0VBX4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPKQEKMMLV LLILPLPYCN AAGVTTVQWG GHGDGLDRYL QRGVRDIHRP
60 70 80 90
CQSVRPGRVW GKCCLTRLCS TMCCARADCT CVYHTWRGHG CSCVM
Length:95
Mass (Da):10,658
Last modified:February 4, 2015 - v1
Checksum:iBF5C1F8AD3507FDD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti47I → V AA sequence (PubMed:26395518).1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KM373785 mRNA Translation: AIW67484.1

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KM373785 mRNA Translation: AIW67484.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4X9ZX-ray1.50A/B46-95[»]
SMRiA0A0A0VBX4
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Entry informationi

Entry nameiCDKA_CONGR
AccessioniPrimary (citable) accession number: A0A0A0VBX4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 15, 2017
Last sequence update: February 4, 2015
Last modified: September 12, 2018
This is version 13 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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