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Protein

Alpha-conotoxin GIA

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

Functioni

Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. The higher affinity site for alpha-conotoxin GI is the alpha/delta site on mouse muscle-derived BC3H-1 receptor, and the other site (alpha/gamma site) on nicotinic receptors from Torpedo californica electric organ.

Miscellaneous

This toxin is a substrate for a cone snail multienzyme complex that regulates its folding and assembly. This complex is composed of protein-disulfide isomerase (PDI), peptidyl-prolyl cis-trans isomerase (PPI) and immunoglobulin-binding protein (BiP). PDI catalyzes the oxidation and reduction of disulfide bonds. Oxidative folding rates are further increased in the presence of PPI with the maximum effect observed in the presence of both enzymes. In contrast, BiP is only observed to assist folding in the presence of microsomes, suggesting that additional cofactors are involved. This toxin has been only observed in the globular form (disulfide pattern C1-C3 and C2-C4).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 GIA
Cleaved into the following chain:
Alternative name(s):
G1
OrganismiConus geographus (Geography cone) (Nubecula geographus)
Taxonomic identifieri6491 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaNeogastropodaConoideaConidaeConusGastridium

Organism-specific databases

ConoServeri74 GI
22 GIA

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
Mutagenesisi9R → A: Reduction in affinity for both alpha/delta and alpha/gamma sites on BC3H-1 receptors and loss of affinity for both alpha/delta and alpha/gamma sites on Torpedo receptors (in GI). 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PeptideiPRO_00000348731 – 15Alpha-conotoxin GIAAdd BLAST15
PeptideiPRO_00000348741 – 13Alpha-conotoxin GIAdd BLAST13

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi2 ↔ 79 Publications
Disulfide bondi3 ↔ 139 Publications
Modified residuei13Cysteine amide; in alpha-conotoxin GI1 Publication1
Modified residuei15Lysine amide; in form alpha-conotoxin GIA1 Publication1

Post-translational modificationi

Not hydroxylated; hydroxylation, on a synthetic hydroxylated GI, improves its folding but impairs its activity against target receptors.

Keywords - PTMi

Amidation, Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom duct.Curated

Structurei

Secondary structure

115
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SMRiP01519
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01519

Family & Domainsi

Domaini

The cysteine framework is I (CC-C-C). Alpha3/5 pattern.Curated

Sequence similaritiesi

Belongs to the conotoxin A superfamily.Curated

Family and domain databases

InterProiView protein in InterPro
IPR018072 Conotoxin_a-typ_CS
PROSITEiView protein in PROSITE
PS60014 ALPHA_CONOTOXIN, 1 hit

Sequencei

Sequence statusi: Complete.

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

Length:15
Mass (Da):1,628
Last modified:July 21, 1986 - v1
Checksum:i2AE73EE90F8C2E19
GO

Sequence databases

PIRiA01782 NTKNAG

Similar proteinsi

Cross-referencesi

Sequence databases

PIRiA01782 NTKNAG

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NOTX-ray1.20A1-13[»]
1QS3NMR-A2-12[»]
1XGANMR-A1-13[»]
1XGBNMR-A1-13[»]
1XGCNMR-A1-13[»]
2FR9NMR-A1-11[»]
2FRBNMR-A1-13[»]
SMRiP01519
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ConoServeri74 GI
22 GIA

Miscellaneous databases

EvolutionaryTraceiP01519

Family and domain databases

InterProiView protein in InterPro
IPR018072 Conotoxin_a-typ_CS
PROSITEiView protein in PROSITE
PS60014 ALPHA_CONOTOXIN, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCA1A_CONGE
AccessioniPrimary (citable) accession number: P01519
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 12, 2018
This is version 101 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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Main funding by: National Institutes of Health

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