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Protein

Mu-conotoxin GIIIA

Gene
N/A
Organism
Conus geographus (Geography cone) (Nubecula geographus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mu-conotoxins block voltage-gated sodium channels (Nav). This toxin potently blocks Nav1.4/SCN4A. It also moderately blocks rNav1.1/SCN1A, rNav1.2/SCN2A, and mNav1.6/SCN8A. The inhibition is reversible. Induces paralysis in vertebrates.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei63Important for binding sodium channel1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel impairing toxin, Neurotoxin, Toxin, Voltage-gated sodium channel impairing toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Mu-conotoxin GIIIA
Alternative name(s):
G3.9
Geographutoxin I
Short name:
GTx-I
Myotoxin I
OrganismiConus geographus (Geography cone) (Nubecula geographus)
Taxonomic identifieri6491 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Organism-specific databases

ConoServeri1570. GIIIA [R13A].
1464. GIIIA precursor.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi63R → A: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
PropeptideiPRO_000024600420 – 502 PublicationsAdd BLAST31
PeptideiPRO_000004449351 – 72Mu-conotoxin GIIIAAdd BLAST22

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi53 ↔ 651 Publication
Disulfide bondi54 ↔ 701 Publication
Modified residuei564-hydroxyproline; partial3 Publications1
Modified residuei574-hydroxyproline; partial3 Publications1
Disulfide bondi60 ↔ 711 Publication
Modified residuei674-hydroxyproline3 Publications1
Modified residuei72Alanine amide3 Publications1

Post-translational modificationi

Hydroxylated; hydroxylations improve the ability to block.2 Publications

Keywords - PTMi

Amidation, Cleavage on pair of basic residues, Disulfide bond, Hydroxylation

Expressioni

Tissue specificityi

Expressed by the venom duct.

Structurei

Secondary structure

174
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi53 – 57Combined sources5
Helixi63 – 65Combined sources3
Turni69 – 71Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TCGNMR-A51-72[»]
1TCHNMR-A51-72[»]
1TCJNMR-A51-72[»]
1TCKNMR-A51-72[»]
SMRiP01523.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01523.

Family & Domainsi

Domaini

The cysteine framework is III (CC-C-C-CC). Classified in the M-4 branch, since 4 residues stand between the fourth and the fifth cysteine residues.

Sequence similaritiesi

Belongs to the conotoxin M superfamily.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR004214. Conotoxin.
IPR008036. Conotoxin_mu-typ.
[Graphical view]
PfamiPF02950. Conotoxin. 1 hit.
[Graphical view]
PROSITEiPS60013. MU_CONOTOXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P01523-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKLGVLLTI CLLLFPLTAL PMDGDEPANR PVERMQDNIS SEQYPLFEKR
60 70
RDCCTPPKKC KDRQCKPQRC CAGR
Length:74
Mass (Da):8,455
Last modified:July 11, 2006 - v2
Checksum:i94CC38599C8374BA
GO

Sequence databases

PIRiA01786. MXKN1.

Cross-referencesi

Sequence databases

PIRiA01786. MXKN1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TCGNMR-A51-72[»]
1TCHNMR-A51-72[»]
1TCJNMR-A51-72[»]
1TCKNMR-A51-72[»]
SMRiP01523.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ConoServeri1570. GIIIA [R13A].
1464. GIIIA precursor.

Miscellaneous databases

EvolutionaryTraceiP01523.

Family and domain databases

InterProiIPR004214. Conotoxin.
IPR008036. Conotoxin_mu-typ.
[Graphical view]
PfamiPF02950. Conotoxin. 1 hit.
[Graphical view]
PROSITEiPS60013. MU_CONOTOXIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCM3A_CONGE
AccessioniPrimary (citable) accession number: P01523
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 11, 2006
Last modified: November 2, 2016
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Miscellaneous

Does not block rNav1.3/SCN3A, rNav1.5/SCN5A, rNav1.7/SCN9A, and rNav1.8/SCN10A (PubMed:21652775). Nav1.4/SCN4A sodium channels but did not affect folding.1 Publication

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.