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P37300 (CO7C_CONMA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Omega-conotoxin MVIIC
Alternative name(s):
SNX-230
OrganismConus magus (Magus cone) (Magician's cone snail)
Taxonomic identifier6492 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Protein attributes

Sequence length29 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav). This toxin preferentially blocks P/Q-type calcium channels (Cav2.1/CACNA1A). Ref.1

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom duct.

Domain

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).

Post-translational modification

Not hydroxylated; hydroxylation, on a synthetic hydroxylated MVIIC, has a significant impact on the oxidative folding but not on the biological activity.

Sequence similarities

Belongs to the conotoxin O1 superfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide‹1 – 2›2
PRO_0000034916
Peptide3 – 2826Omega-conotoxin MVIIC
PRO_0000034917

Sites

Site151Important for calcium channel binding

Amino acid modifications

Modified residue281Cysteine amide
Disulfide bond3 ↔ 18 Ref.4 Ref.5
Disulfide bond10 ↔ 22 Ref.4 Ref.5
Disulfide bond17 ↔ 28 Ref.4 Ref.5

Experimental info

Mutagenesis151Y → A: High decrease in binding. Ref.2
Non-terminal residue11

Secondary structure

..... 29
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P37300 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: AC7A68948474728A

FASTA293,071
        10         20 
TRCKGKGAPC RKTMYDCCSG SCGRRGKCG 

« Hide

References

[1]"A new Conus peptide ligand for mammalian presynaptic Ca2+ channels."
Hillyard D.R., Monje V.D., Mintz I.M., Bean B.P., Nadasdi L., Ramachandran J., Miljanich G.P., Azimi-Zoonooz A., McIntosh J.M., Cruz L.J., Imperial J.S., Olivera B.M.
Neuron 9:69-77(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 3-28, FUNCTION.
[2]"Tyr13 is essential for the binding of omega-conotoxin MVIIC to the P/Q-type calcium channel."
Kim J.-I., Takahashi M., Martin-Moutot N., Seagar M.J., Ohtake A., Sato K.
Biochem. Biophys. Res. Commun. 214:305-309(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TYR-15.
[3]"Role of hydroxyprolines in the in vitro oxidative folding and biological activity of conotoxins."
Lopez-Vera E., Walewska A., Skalicky J.J., Olivera B.M., Bulaj G.
Biochemistry 47:1741-1751(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS OF 3-28, ROLE OF HYDROXYLATION.
[4]"Solution structure of omega-conotoxin MVIIC, a high affinity ligand of P-type calcium channels, using 1H NMR spectroscopy and complete relaxation matrix analysis."
Farr-Jones S., Miljanich G.P., Nadasdi L., Ramachandran J., Basus V.J.
J. Mol. Biol. 248:106-124(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 3-28, DISULFIDE BONDS.
[5]"Structure-activity relationships of omega-conotoxins MVIIA, MVIIC and 14 loop splice hybrids at N and P/Q-type calcium channels."
Nielsen K.J., Adams D., Thomas L., Bond T., Alewood P.F., Craik D.J., Lewis R.J.
J. Mol. Biol. 289:1405-1421(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 3-28, DISULFIDE BONDS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S40826 mRNA. Translation: AAB22674.1.
PIRJH0699.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CNNNMR-A3-28[»]
1OMNNMR-A3-28[»]
1V4QNMR-A3-26[»]
ProteinModelPortalP37300.
SMRP37300. Positions 3-28.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

ConoServer822. MVIIC precursor.

Family and domain databases

InterProIPR012321. Conotoxin_omega-typ_CS.
[Graphical view]
PROSITEPS60004. OMEGA_CONOTOXIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP37300.

Entry information

Entry nameCO7C_CONMA
AccessionPrimary (citable) accession number: P37300
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: October 16, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references