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C1J5M6

- CM3B_CONBU

UniProt

C1J5M6 - CM3B_CONBU

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
  1. 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

    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-SubCell

    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 – 574
    Helixi60 – 623
    Turni63 – 653
    Helixi66 – 716

    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

    MMSKLGVLLT ICLLLFPLFA LPQDGDQPAD RPAERMQDDI SSEQNPLLEK   50
    RVGERCCKNG KRGCGRWCRD HSRCCGRR 78
    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 1, 2014
    This is version 24 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