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P37300

- CO7C_CONMA

UniProt

P37300 - CO7C_CONMA

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Protein

Omega-conotoxin MVIIC

Gene
N/A
Organism
Conus magus (Magus cone) (Magician's cone snail)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei15 – 151Important for calcium channel binding

GO - Molecular functioni

  1. ion channel inhibitor activity Source: InterPro

GO - Biological processi

  1. pathogenesis Source: InterPro
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 MVIIC
Alternative name(s):
SNX-230
OrganismiConus magus (Magus cone) (Magician's cone snail)
Taxonomic identifieri6492 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Organism-specific databases

ConoServeri822. MVIIC precursor.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi15 – 151Y → A: High decrease in binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei‹1 – 2›2PRO_0000034916
Peptidei3 – 2826Omega-conotoxin MVIICPRO_0000034917Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi3 ↔ 18
Disulfide bondi10 ↔ 22
Disulfide bondi17 ↔ 28
Modified residuei28 – 281Cysteine amide

Post-translational modificationi

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

Keywords - PTMi

Amidation, Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom duct.

Structurei

Secondary structure

1
29
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni12 – 154Combined sources
Beta strandi17 – 204Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CNNNMR-A3-28[»]
1OMNNMR-A3-28[»]
1V4QNMR-A3-26[»]
ProteinModelPortaliP37300.
SMRiP37300. Positions 3-28.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37300.

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

Family and domain databases

InterProiIPR012321. Conotoxin_omega-typ_CS.
[Graphical view]
PROSITEiPS60004. OMEGA_CONOTOXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

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

P37300-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20 
TRCKGKGAPC RKTMYDCCSG SCGRRGKCG
Length:29
Mass (Da):3,071
Last modified:October 1, 1994 - v1
Checksum:iAC7A68948474728A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S40826 mRNA. Translation: AAB22674.1.
PIRiJH0699.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S40826 mRNA. Translation: AAB22674.1 .
PIRi JH0699.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CNN NMR - A 3-28 [» ]
1OMN NMR - A 3-28 [» ]
1V4Q NMR - A 3-26 [» ]
ProteinModelPortali P37300.
SMRi P37300. Positions 3-28.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

ConoServeri 822. MVIIC precursor.

Miscellaneous databases

EvolutionaryTracei P37300.

Family and domain databases

InterProi IPR012321. Conotoxin_omega-typ_CS.
[Graphical view ]
PROSITEi PS60004. OMEGA_CONOTOXIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. 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.

Entry informationi

Entry nameiCO7C_CONMA
AccessioniPrimary (citable) accession number: P37300
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: November 26, 2014
This is version 89 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

3D-structure

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