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C1J5M6

- CM3B_CONBU

UniProt

C1J5M6 - CM3B_CONBU

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Protein

Mu-conotoxin BuIIIB

Gene
N/A
Organism
Conus bullatus (Bubble cone)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Mu-conotoxins block voltage-gated sodium channels (Nav). This synthetic toxin potently blocks rNav1.2/SCN2A, and rNav1.4/SCN4A. It also moderately blocks rNav1.1/SCN1A, rNav1.3/SCN3A, rNav1.5/SCN5, and mNav1.6/SCN8A. The block of SCN4A is very slowly reversible.3 Publications

GO - Molecular functioni

  1. ion channel inhibitor activity Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Ion channel impairing toxin, Neurotoxin, Toxin, Voltage-gated sodium channel impairing toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Mu-conotoxin BuIIIB
Alternative name(s):
Conotoxin Bu16
OrganismiConus bullatus (Bubble cone)
Taxonomic identifieri89438 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Organism-specific databases

ConoServeri3715. BuIIIB precursor.

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi52 – 554Missing: 4-fold increase in blocking SCN3A (K(d) is 53 nM). 1 Publication
Mutagenesisi52 – 521V → A: 3.5-decrease in blocking SCN3A (K(d) is 710 nM). 1 Publication
Mutagenesisi53 – 531G → A: 5-fold increase in blocking SCN3A (K(d) is 36 nM). 1 Publication
Mutagenesisi53 – 531G → A: Mutated into D-Ala. 40-fold increase in blocking SCN3A (K(d) is 4.8 nM). 1 Publication
Mutagenesisi54 – 541E → A: 13-fold increase in blocking SCN3A (K(d) is 15 nM). 1 Publication
Mutagenesisi55 – 551R → A: No change in blocking SCN3A (K(d) is 118 nM). 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Propeptidei23 – 5129By similarityPRO_0000384433Add
BLAST
Peptidei52 – 7524Mu-conotoxin BuIIIBPRO_0000384434Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi56 ↔ 681 Publication
Disulfide bondi57 ↔ 741 Publication
Disulfide bondi64 ↔ 751 Publication
Modified residuei75 – 751Cysteine amideBy similarity

Keywords - PTMi

Amidation, Cleavage on pair of basic residues, Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom duct.

Structurei

Secondary structure

1
78
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi54 – 574Combined sources
Helixi60 – 623Combined sources
Turni63 – 653Combined sources
Helixi66 – 716Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LO9NMR-A52-75[»]
2LOCNMR-A52-75[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The cysteine framework is III (CC-C-C-CC). Classified in the M-5 branch, since 5 residues stand between the fourth and the fifth cysteine residues.

Sequence similaritiesi

Belongs to the conotoxin M superfamily.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR004214. Conotoxin.
[Graphical view]
PfamiPF02950. Conotoxin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

C1J5M6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMSKLGVLLT ICLLLFPLFA LPQDGDQPAD RPAERMQDDI SSEQNPLLEK
60 70
RVGERCCKNG KRGCGRWCRD HSRCCGRR
Length:78
Mass (Da):8,877
Last modified:May 26, 2009 - v1
Checksum:i907D09C9B4DE3164
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FJ240166 mRNA. Translation: ACO50771.1.

Cross-referencesi

Web resourcesi

Biological Magnetic Resonance Data Bank

synthetic mu-BuIIIB

Biological Magnetic Resonance Data Bank

synthetic mutagen mu-[D-Ala2]BuIIIB

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FJ240166 mRNA. Translation: ACO50771.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LO9 NMR - A 52-75 [» ]
2LOC NMR - A 52-75 [» ]
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

ConoServeri 3715. BuIIIB precursor.

Family and domain databases

InterProi IPR004214. Conotoxin.
[Graphical view ]
Pfami PF02950. Conotoxin. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Pruning nature: biodiversity-derived discovery of novel sodium channel blocking conotoxins from Conus bullatus."
    Holford M., Zhang M.-M., Gowd K.H., Azam L., Green B.R., Watkins M., Ownby J.-P., Yoshikami D., Bulaj G., Olivera B.M.
    Toxicon 53:90-98(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 51-75, FUNCTION ON SCN4A.
  2. "Characterization of the Conus bullatus genome and its venom-duct transcriptome."
    Hu H., Bandyopadhyay P.K., Olivera B.M., Yandell M.
    BMC Genomics 12:60-60(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-78.
    Tissue: Venom duct.
  3. "mu-Conotoxins that differentially block sodium channels Nav1.1 through 1.8 identify those responsible for action potentials in sciatic nerve."
    Wilson M.J., Yoshikami D., Azam L., Gajewiak J., Olivera B.M., Bulaj G., Zhang M.M.
    Proc. Natl. Acad. Sci. U.S.A. 108:10302-10307(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION ON SODIUM CHANNELS, SYNTHESIS OF 52-75.
  4. "Mammalian neuronal sodium channel blocker mu-conotoxin BuIIIB has a structured N-terminus that influences potency."
    Kuang Z., Zhang M.-M., Gupta K., Gajewiak J., Gulyas J., Balaram P., Rivier J.E., Olivera B.M., Yoshikami D., Bulaj G., Norton R.S.
    ACS Chem. Biol. 8:1344-1351(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 52-75, SYNTHESIS OF 52-75, MUTAGENESIS OF VAL-52; GLY-53; GLU-54; ARG-55 AND 52-VAL--ARG-55, FUNCTION ON SCN3A, DISULFIDE BONDS.

Entry informationi

Entry nameiCM3B_CONBU
AccessioniPrimary (citable) accession number: C1J5M6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 26, 2009
Last modified: October 29, 2014
This is version 25 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