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Protein

Iota-conotoxin RXIA

Gene
N/A
Organism
Conus radiatus (Rayed cone)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Iota-conotoxins bind to voltage-gated sodium channels and act as agonists by shifting the voltage-dependence of activation to more hyperpolarized levels. This toxin acts on Nav1.6/SCN8A > Nav1.2/SCN2A > Nav1.7/SCN9A sodium channels. Produces general excitatory symptoms upon intracorporeal injection and repetitive action potentials in the frog cutaneous pectoris muscle. Natural peptide (with D-Phe) is active on nerve, but not on muscle. Synthetic peptide (with L-Phe) is not active on both nerve and muscle.2 Publications

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:
Iota-conotoxin RXIA
Alternative name(s):
R11.6
r11a
OrganismiConus radiatus (Rayed cone)
Taxonomic identifieri61198 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Organism-specific databases

ConoServeri840. RXIA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4646Iota-conotoxin RXIAPRO_0000086868Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 214-hydroxyproline; partial1 Publication
Disulfide bondi5 ↔ 191 Publication
Modified residuei11 – 1114-hydroxyproline; partial1 Publication
Disulfide bondi12 ↔ 221 Publication
Disulfide bondi18 ↔ 271 Publication
Disulfide bondi21 ↔ 381 Publication
Modified residuei29 – 2914-hydroxyproline1 Publication
Modified residuei44 – 441D-phenylalanine1 Publication

Post-translational modificationi

The natural D-Phe-44 form of the peptide is more potent than the L-Phe-44 form.

Keywords - PTMi

D-amino acid, Disulfide bond, Hydroxylation

Expressioni

Tissue specificityi

Expressed by the venom duct.

Structurei

Secondary structure

1
46
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 103Combined sources
Beta strandi18 – 236Combined sources
Beta strandi26 – 294Combined sources
Beta strandi32 – 354Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JRYNMR-A1-46[»]
2JTUNMR-A1-38[»]
2P4LNMR-A1-46[»]
ProteinModelPortaliQ7Z094.
SMRiQ7Z094. Positions 1-46.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7Z094.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the conotoxin I1 superfamily.Curated

Family and domain databases

InterProiIPR013141. Conotoxin-I_CS.
IPR012624. Toxin_19.
[Graphical view]
PfamiPF08088. Toxin_19. 1 hit.
[Graphical view]
PROSITEiPS60019. I_CONOTOXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7Z094-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40 
GPSFCKADEK PCEYHADCCN CCLSGICAPS TNWILPGCST SSFFKI
Length:46
Mass (Da):4,936
Last modified:October 1, 2003 - v1
Checksum:i32C2812A24D82675
GO

Mass spectrometryi

Molecular mass is 3816.7 Da from positions 1 - 46. Determined by LSI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY208959 mRNA. Translation: AAP41541.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY208959 mRNA. Translation: AAP41541.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JRYNMR-A1-46[»]
2JTUNMR-A1-38[»]
2P4LNMR-A1-46[»]
ProteinModelPortaliQ7Z094.
SMRiQ7Z094. Positions 1-46.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ConoServeri840. RXIA.

Miscellaneous databases

EvolutionaryTraceiQ7Z094.

Family and domain databases

InterProiIPR013141. Conotoxin-I_CS.
IPR012624. Toxin_19.
[Graphical view]
PfamiPF08088. Toxin_19. 1 hit.
[Graphical view]
PROSITEiPS60019. I_CONOTOXIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Novel excitatory Conus peptides define a new conotoxin superfamily."
    Jimenez E.C., Shetty R.P., Lirazan M., Rivier J., Walker C., Abogadie F.C., Yoshikami D., Cruz L.J., Olivera B.M.
    J. Neurochem. 85:610-621(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE, HYDROXYLATION AT PRO-2; PRO-11 AND PRO-29, MASS SPECTROMETRY.
    Tissue: Venom and Venom duct.
  2. "Post-translational amino acid isomerization: a functionally important D-amino acid in an excitatory peptide."
    Buczek O., Yoshikami D., Bulaj G., Jimenez E.C., Olivera B.M.
    J. Biol. Chem. 280:4247-4253(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SYNTHESIS, D-AMINO ACID AT PHE-44.
    Tissue: Venom.
  3. "Structure and sodium channel activity of an excitatory I(1)-superfamily conotoxin."
    Buczek O., Wei D., Babon J.J., Yang X., Fiedler B., Chen P., Yoshikami D., Olivera B.M., Bulaj G., Norton R.S.
    Biochemistry 46:9929-9940(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SYNTHESIS (D-PHE AND L-PHE), STRUCTURE BY NMR, DISULFIDE BONDS.
  4. "Specificity, affinity and efficacy of iota-conotoxin RXIA, an agonist of voltage-gated sodium channels Na(V)1.2, 1.6 and 1.7."
    Fiedler B., Zhang M.M., Buczek O., Azam L., Bulaj G., Norton R.S., Olivera B.M., Yoshikami D.
    Biochem. Pharmacol. 75:2334-2344(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TOXIN TARGET.

Entry informationi

Entry nameiCI1BA_CONRA
AccessioniPrimary (citable) accession number: Q7Z094
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: October 1, 2003
Last modified: December 9, 2015
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Miscellaneous

Does not have effect on sodium channels Nav1.1/SCN1A, Nav1.3/SCN3A, Nav1.4/SCN4A, Nav1.5/SCN5A and on potassium channels Kv7.2/KCNQ2, Kv7.3/KCNQ3, Kv1.2/KCNA2, Kv1.3/KCNA3, Kv1.4/KCNA4, Kv1.5/KCNA5 and Kv1.6/KCNA6 (PubMed:18486102, PubMed:17696362).2 Publications

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.