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Protein

Omega-conotoxin CVID

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

Functioni

Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels. This toxin inhibits neurotransmitter release, it blocks N-type calcium channels, probably a N-type (Cav2.2/CACNA1B) calcium channel variant.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei58 – 581Important for calcium channel binding

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Calcium channel impairing toxin, Ion channel impairing toxin, Neurotoxin, Presynaptic neurotoxin, Toxin, Voltage-gated calcium channel impairing toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Omega-conotoxin CVID
Alternative name(s):
AM-336
Short name:
AM336
CNSB004
Leconotide
OrganismiConus catus (Cat cone)
Taxonomic identifieri101291 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Organism-specific databases

ConoServeri1569. CVID precursor.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Pharmaceutical usei

Is under phase I clinical trial under the name AM336 by Amrad Corporation Limited for treating severe morphine-resistant pain stress.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi55 – 551K → R: 20% reduction of neurotransmitter release. 1 Publication
Mutagenesisi58 – 581Y → F: No activity on neurotransmitter release. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Propeptidei23 – 45231 PublicationPRO_0000034964Add
BLAST
Peptidei46 – 7227Omega-conotoxin CVIDPRO_0000034965Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 61
Disulfide bondi53 ↔ 65
Disulfide bondi60 ↔ 72
Modified residuei72 – 721Cysteine amide

Keywords - PTMi

Amidation, Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom duct.

Family & Domainsi

Domaini

The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
The cysteine framework is VI/VII (C-C-CC-C-C).

Sequence similaritiesi

Belongs to the conotoxin O1 superfamily.Curated

Keywords - Domaini

Knottin, Signal

Phylogenomic databases

HOGENOMiHOG000091618.

Family and domain databases

InterProiIPR004214. Conotoxin.
IPR012321. Conotoxin_omega-typ_CS.
[Graphical view]
PfamiPF02950. Conotoxin. 1 hit.
[Graphical view]
PROSITEiPS60004. OMEGA_CONOTOXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P58920-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLTCVVIVA VLLLTACQLI TADDSRGTQK HRALRSDTKL SMSTRCKSKG
60 70
AKCSKLMYDC CSGSCSGTVG RCG
Length:73
Mass (Da):7,748
Last modified:July 26, 2002 - v1
Checksum:iC4CEBD30C77DAEC3
GO

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ConoServeri1569. CVID precursor.

Phylogenomic databases

HOGENOMiHOG000091618.

Family and domain databases

InterProiIPR004214. Conotoxin.
IPR012321. Conotoxin_omega-typ_CS.
[Graphical view]
PfamiPF02950. Conotoxin. 1 hit.
[Graphical view]
PROSITEiPS60004. OMEGA_CONOTOXIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 46-72, SYNTHESIS OF 46-72, STRUCTURE BY NMR OF 46-72.
    Tissue: Venom and Venom duct.
  2. "Omega-conotoxin CVID inhibits a pharmacologically distinct voltage-sensitive calcium channel associated with transmitter release from preganglionic nerve terminals."
    Adams D.J., Smith A.B., Schroeder C.I., Yasuda T., Lewis R.J.
    J. Biol. Chem. 278:4057-4062(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-55 AND TYR-58, STRUCTURE BY NMR OF 46-72.

Entry informationi

Entry nameiCO16D_CONCT
AccessioniPrimary (citable) accession number: P58920
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: July 26, 2002
Last modified: July 22, 2015
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Pharmaceutical

Documents

  1. 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.