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Protein

Kappa-conotoxin PVIIA

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

Functioni

Kappa-conotoxins bind and inhibit voltage-gated potassium channels (Kv). This toxin inhibits the Shaker channel from insects. The interaction site between the Shaker channel and this toxin is within the S5-S6 loop of the Shaker channel. In fish, this toxin induces hyperactivity, followed by continuous contraction and extension of major fins, without immobilization or death. Injection of this peptide together with the delta-conotoxin PVIA causes the sudden tetanus of prey (STOP) syndrome, which is a single, lethal "fin-pop" in envenomed fish. In mice, induces hyperactivity.4 Publications

Miscellaneous

This toxin has no effect on the rat Kv1.1/KCNA1 channel.1 Publication

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIon channel impairing toxin, Neurotoxin, Potassium channel impairing toxin, Toxin, Voltage-gated potassium channel impairing toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Kappa-conotoxin PVIIA
Alternative name(s):
CGX-1051
Fin-popping peptide
OrganismiConus purpurascens (Purple cone)
Taxonomic identifieri41690 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Organism-specific databases

ConoServeri1331. PVIIA precursor.

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Pharmaceutical usei

Is under preclinical trial by Cognetix Inc under the name CGX-1051. Used as a cardioprotective agent.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi47R → A, K or Q: 100% reduction of toxicity. 1 Publication1
Mutagenesisi48I → A: 3-fold decrease of toxicity. 1 Publication1
Mutagenesisi49P → A: 100% reduction of toxicity. 1 Publication1
Mutagenesisi50N → A: 100% reduction of toxicity. 1 Publication1
Mutagenesisi51Q → A: 13-fold decrease of toxicity. 1 Publication1
Mutagenesisi52K → A or R: 100% reduction of toxicity. 1 Publication1
Mutagenesisi54F → A or M: 100% reduction of toxicity. 1 Publication1
Mutagenesisi54F → Y: 11-fold decrease of toxicity. 1 Publication1
Mutagenesisi55Q → A: 3-fold decrease of toxicity. 1 Publication1
Mutagenesisi56H → A: 3-fold decrease of toxicity. 1 Publication1
Mutagenesisi57L → A: 100% reduction of toxicity. 1 Publication1
Mutagenesisi58D → A: 1.5-fold decrease of toxicity. 1 Publication1
Mutagenesisi59D → A: 100% reduction of toxicity. 1 Publication1
Mutagenesisi62S → A: 1.5-fold decrease of toxicity. 1 Publication1
Mutagenesisi63R → A: 3.5-fold decrease of toxicity. 1 Publication1
Mutagenesisi64K → A: 1.2-fold decrease of toxicity. 1 Publication1
Mutagenesisi67R → A: 5-fold decrease of toxicity. 1 Publication1
Mutagenesisi68F → A: 17-fold decrease of toxicity. 1 Publication1
Mutagenesisi69N → A: 19-fold decrease of toxicity. 1 Publication1
Mutagenesisi70K → A: 117-fold decrease of toxicity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
PropeptideiPRO_000003498123 – 451 PublicationAdd BLAST23
PeptideiPRO_000003498246 – 72Kappa-conotoxin PVIIAAdd BLAST27

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi46 ↔ 61
Modified residuei494-hydroxyproline1 Publication1
Disulfide bondi53 ↔ 65
Disulfide bondi60 ↔ 71

Keywords - PTMi

Disulfide bond, Hydroxylation

Expressioni

Tissue specificityi

Expressed by the venom duct.

Structurei

Secondary structure

172
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi55 – 57Combined sources3
Beta strandi60 – 62Combined sources3
Beta strandi69 – 71Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AV3NMR-A46-72[»]
1KCPNMR-A46-72[»]
2N8ENMR-A46-72[»]
ProteinModelPortaliP56633.
SMRiP56633.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56633.

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

Family and domain databases

InterProiView protein in InterPro
IPR004214. Conotoxin.
PfamiView protein in Pfam
PF02950. Conotoxin. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P56633-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLTCVVIVV VLFLTACQLI TADDSRRTQK HRALRSTTKL SLSTRCRIPN
60 70
QKCFQHLDDC CSRKCNRFNK CV
Length:72
Mass (Da):8,317
Last modified:July 26, 2002 - v2
Checksum:i53BFAF79EE751C16
GO

Mass spectrometryi

Molecular mass is 3268.4 Da from positions 46 - 72. Determined by FAB. 1 Publication

Sequence databases

PIRiA58997.

Similar proteinsi

Entry informationi

Entry nameiCO17A_CONPU
AccessioniPrimary (citable) accession number: P56633
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 26, 2002
Last modified: November 2, 2016
This is version 92 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Caution

Because analogs resulting of mutagenesis of Hyp-49, Asn-50, Leu-57 and Asp-59 gave very low yields upon folding, the results of mutagenesis on these residues should be interpreted with caution.Curated

Keywords - Technical termi

3D-structure, Direct protein sequencing, Pharmaceutical

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families