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P07231

- CKG_CONGE

UniProt

P07231 - CKG_CONGE

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Protein

Conantokin-G

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

Functioni

Conantokins inhibit N-methyl-D-aspartate (NMDA) receptors. This toxin is selective for the NR2B/GRIN2B subunit. Induces sleep-like symptoms in young mice and hyperactivity in older mice.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei85 – 851Important for selectivity
Metal bindingi90 – 901Divalent metal cation; via 4-carboxyglutamate
Metal bindingi94 – 941Divalent metal cation; via 4-carboxyglutamate

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. pathogenesis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ion channel impairing toxin, Ionotropic glutamate receptor inhibitor, Neurotoxin, Postsynaptic neurotoxin, Toxin

Keywords - Ligandi

Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Conantokin-G
Short name:
Con-G
Alternative name(s):
CGX-1007
Conotoxin GV
Sleeper peptide
OrganismiConus geographus (Geography cone) (Nubecula geographus)
Taxonomic identifieri6491 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Organism-specific databases

ConoServeri1373. Conantokin-G precursor.
1353. Conantokin-G precursor (variant).

Subcellular locationi

GO - Cellular componenti

  1. other organism postsynaptic membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Pharmaceutical usei

Failed in phase II clinical trial. Was tested under the name CGX-1007 by Cognetix Inc. to treat convulsion and epilepsy.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi85 – 851L → I: No loss of inhibition of NR1a/NR2B receptor; no inhibition of NR1a/NR2A receptor (as for the wild-type). 1 Publication
Mutagenesisi85 – 851L → V: No loss of inhibition of NR1a/NR2B receptor; no inhibition of NR1a/NR2A receptor (as for the wild-type). 1 Publication
Mutagenesisi85 – 851L → Y: Little loss of inhibition of NR1a/NR2B receptor; 70% of inhibition of NR1a/NR2A receptor. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Add
BLAST
Propeptidei22 – 8059PRO_0000035060Add
BLAST
Peptidei81 – 9717Conantokin-GPRO_0000035061Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei83 – 8314-carboxyglutamate1 Publication
Modified residuei84 – 8414-carboxyglutamate1 Publication
Modified residuei87 – 8714-carboxyglutamate1 Publication
Modified residuei90 – 9014-carboxyglutamate1 Publication
Modified residuei94 – 9414-carboxyglutamate1 Publication
Modified residuei97 – 971Asparagine amide1 Publication

Keywords - PTMi

Amidation, Cleavage on pair of basic residues, Gamma-carboxyglutamic acid

Expressioni

Tissue specificityi

Expressed by the venom duct.

Structurei

Secondary structure

1
100
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi82 – 9615Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AD7NMR-A81-97[»]
1AWYNMR-A81-97[»]
1ONUNMR-A81-97[»]
2DPQX-ray1.25A81-97[»]
ProteinModelPortaliP07231.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07231.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni61 – 8020Gamma-carboxylation recognition sequence that plays a role in the conversion of Glu to carboxy-Glu (Gla)CuratedAdd
BLAST

Sequence similaritiesi

Belongs to the conotoxin B superfamily.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR005918. Conantokin_CS.
[Graphical view]
PROSITEiPS60025. CONANTOKIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P07231-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHLYTYLYLL VPLVTFHLIL GTGTLDDGGA LTERRSADAT ALKAEPVLLQ
60 70 80 90 100
KSAARSTDDN GKDRLTQMKR ILKQRGNKAR GEEELQENQE LIREKSNGKR
Length:100
Mass (Da):11,267
Last modified:December 15, 1998 - v2
Checksum:i3B0050FDFF2B9DFB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti85 – 851L → V.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043141 mRNA. Translation: AAC15669.1.
PIRiA05168.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043141 mRNA. Translation: AAC15669.1 .
PIRi A05168.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AD7 NMR - A 81-97 [» ]
1AWY NMR - A 81-97 [» ]
1ONU NMR - A 81-97 [» ]
2DPQ X-ray 1.25 A 81-97 [» ]
ProteinModelPortali P07231.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

ConoServeri 1373. Conantokin-G precursor.
1353. Conantokin-G precursor (variant).

Miscellaneous databases

EvolutionaryTracei P07231.

Family and domain databases

InterProi IPR005918. Conantokin_CS.
[Graphical view ]
PROSITEi PS60025. CONANTOKIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Conantokin-G precursor and its role in gamma-carboxylation by a vitamin K-dependent carboxylase from a Conus snail."
    Bandyopadhyay P.K., Colledge C.J., Walker C.S., Zhou L.-M., Hillyard D.R., Olivera B.M.
    J. Biol. Chem. 273:5447-5450(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-85.
    Tissue: Venom duct.
  2. "Gamma-carboxyglutamate in a neuroactive toxin."
    McIntosh J.M., Olivera B.M., Cruz L.J., Gray W.R.
    J. Biol. Chem. 259:14343-14346(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 81-97, AMIDATION AT ASN-97, GAMMA-CARBOXYGLUTAMATION AT GLU-83; GLU-84; GLU-87; GLU-90 AND GLU-94.
  3. Cited for: FUNCTION.
  4. "The amino acid residue at sequence position 5 in the conantokin peptides partially governs subunit-selective antagonism of recombinant N-methyl-D-aspartate receptors."
    Klein R.C., Prorok M., Galdzicki Z., Castellino F.J.
    J. Biol. Chem. 276:26860-26867(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LEU-85, SITE.
  5. "Binding of cations to individual gamma-carboxyglutamate residues of conantokin-G and conantokin-T."
    Blandl T., Warder S.E., Prorok M., Castellino F.J.
    J. Pept. Res. 53:453-464(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: METAL-BINDING.
  6. "Powerful antinociceptive effects of the cone snail venom-derived subtype-selective NMDA receptor antagonists conantokins G and T."
    Malmberg A.B., Gilbert H., McCabe R.T., Basbaum A.I.
    Pain 101:109-116(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: THERAPEUTIC USAGE.
  7. "Three-dimensional structure of a gamma-carboxyglutamic acid-containing conotoxin, conantokin G, from the marine snail Conus geographus: the metal-free conformer."
    Rigby A.C., Baleja J.D., Furie B.C., Furie B.
    Biochemistry 36:6906-6914(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 81-97.
  8. "Role of gamma-carboxyglutamic acid in the calcium-induced structural transition of conantokin G, a conotoxin from the marine snail Conus geographus."
    Rigby A.C., Baleja J.D., Li L., Pedersen L.G., Furie B.C., Furie B.
    Biochemistry 36:15677-15684(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 81-97.
  9. "Determination of the solution structures of conantokin-G and conantokin-T by CD and NMR spectroscopy."
    Skjaerbaek N., Nielsen K.J., Lewis R.J., Alewood P.F., Craik D.J.
    J. Biol. Chem. 272:2291-2299(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 81-97.

Entry informationi

Entry nameiCKG_CONGE
AccessioniPrimary (citable) accession number: P07231
Secondary accession number(s): O61475
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: December 15, 1998
Last modified: November 26, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Miscellaneous

The mature peptide does not contain cysteine residue.

Keywords - Technical termi

3D-structure, Pharmaceutical

Documents

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

External Data

Dasty 3