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P01525

- NXB4_CERLA

UniProt

P01525 - NXB4_CERLA

Protein

Neurotoxin B-IV

Gene
N/A
Organism
Cerebratulus lacteus (Milky ribbon worm) (Micrura lactea)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    This toxin increases the excitability of nerves by delaying the inactivation of the voltage-gated sodium channel (Nav). Only acts on some crustacean. Neurotoxin B-IV is more abundant, but 15-fold less toxic than neurotoxin B-II.

    GO - Molecular functioni

    1. sodium channel inhibitor activity Source: InterPro

    GO - Biological processi

    1. pathogenesis Source: InterPro

    Keywords - Molecular functioni

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neurotoxin B-IV
    OrganismiCerebratulus lacteus (Milky ribbon worm) (Micrura lactea)
    Taxonomic identifieri6221 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaLophotrochozoaNemerteaAnoplaHeteronemerteaCerebratulidaeCerebratulus

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi9 – 91Y → F: 5-fold decrease in toxicity. 2 Publications
    Mutagenesisi13 – 131E → A: No change in toxicity. 2 Publications
    Mutagenesisi13 – 131E → Q: No change in toxicity. 2 Publications
    Mutagenesisi17 – 171R → A: Complete loss of toxicity. 2 Publications
    Mutagenesisi17 – 171R → K: Complete loss of toxicity. 2 Publications
    Mutagenesisi17 – 171R → Q: Complete loss of toxicity. 2 Publications
    Mutagenesisi18 – 192KK → QQ: Very low decrease in toxicity. 2 Publications
    Mutagenesisi18 – 181K → Q: No change in toxicity. 2 Publications
    Mutagenesisi21 – 211D → A: No change in toxicity. 2 Publications
    Mutagenesisi21 – 211D → N: No change in toxicity. 2 Publications
    Mutagenesisi21 – 211D → P: 10-fold decrease in toxicity. 2 Publications
    Mutagenesisi22 – 221L → D: No change in toxicity. 2 Publications
    Mutagenesisi25 – 251R → K: No change in toxicity. 2 Publications
    Mutagenesisi25 – 251R → Q: 400-fold decrease in toxicity. 2 Publications
    Mutagenesisi29 – 291K → N: No change in toxicity. 2 Publications
    Mutagenesisi30 – 301W → F: No change in toxicity. 2 Publications
    Mutagenesisi30 – 301W → S: 41-fold decrease in toxicity. 2 Publications
    Mutagenesisi30 – 301W → Y: 5-fold decrease in toxicity. 2 Publications
    Mutagenesisi33 – 331K → N: No decrease in toxicity. 2 Publications
    Mutagenesisi34 – 341R → A: 80-fold decrease in toxicity. 2 Publications
    Mutagenesisi34 – 341R → K: 8-fold decrease in toxicity. 2 Publications
    Mutagenesisi34 – 341R → Q: 20-fold decrease in toxicity. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 5555Neurotoxin B-IVPRO_0000221572Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei10 – 101Hydroxyproline1 Publication
    Disulfide bondi12 ↔ 481 Publication
    Disulfide bondi16 ↔ 521 Publication
    Disulfide bondi23 ↔ 411 Publication
    Disulfide bondi26 ↔ 371 Publication

    Keywords - PTMi

    Disulfide bond, Hydroxylation

    Structurei

    Secondary structure

    1
    55
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni7 – 104
    Helixi11 – 2313
    Helixi28 – 303
    Helixi34 – 4815
    Turni49 – 513

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VIBNMR-A1-55[»]
    ProteinModelPortaliP01525.
    SMRiP01525. Positions 1-44.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01525.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the worm B-toxin family.Curated

    Family and domain databases

    Gene3Di1.10.287.120. 1 hit.
    InterProiIPR012497. Neurotoxin_B-IV.
    [Graphical view]
    PfamiPF07822. Toxin_13. 1 hit.
    [Graphical view]
    SUPFAMiSSF57011. SSF57011. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P01525-1 [UniParc]FASTAAdd to Basket

    « Hide

    ASATWGAAYP ACENNCRKKY DLCIRCQGKW AGKRGKCAAH CIIQKNNCKG   50
    KCKKE 55
    Length:55
    Mass (Da):6,107
    Last modified:July 21, 1986 - v1
    Checksum:iBB76B72E48DB050D
    GO

    Sequence databases

    PIRiA92340. NTHNB4.

    Cross-referencesi

    Sequence databases

    PIRi A92340. NTHNB4.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1VIB NMR - A 1-55 [» ]
    ProteinModelPortali P01525.
    SMRi P01525. Positions 1-44.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P01525.

    Family and domain databases

    Gene3Di 1.10.287.120. 1 hit.
    InterProi IPR012497. Neurotoxin_B-IV.
    [Graphical view ]
    Pfami PF07822. Toxin_13. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57011. SSF57011. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Structure and action of heteronemertine polypeptide toxins. Amino acid sequence of Cerebratulus lacteus toxin B-II and revised structure of toxin B-IV."
      Blumenthal K.M., Keim P.S., Heinrikson R.L., Kem W.R.
      J. Biol. Chem. 256:9063-9067(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, HYDROXYLATION AT PRO-10, SEQUENCE REVISION.
    2. "Structure and action of heteronemertine polypeptide toxins. Primary structure of Cerebratulus lacteus toxin B-IV."
      Blumenthal K.M., Kem W.R.
      J. Biol. Chem. 251:6025-6029(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
    3. "Mutagenesis of Cerebratulus lacteus neurotoxin B-IV identifies NH2-terminal sequences important for biological activity."
      Howell M.L., Blumenthal K.M.
      J. Biol. Chem. 266:12884-12888(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    4. "Role of electrostatic interactions in defining the potency of neurotoxin B-IV from Cerebratulus lacteus."
      Wen P.H., Blumenthal K.M.
      J. Biol. Chem. 271:29752-29758(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-9; GLU-13; ARG-17; ASP-21; ARG-25 AND ARG-34.
    5. "Structure and function of Cerebratulus lacteus neurotoxin B-IV: tryptophan-30 is critical for function while lysines-18, -19, -29, and -33 are not required."
      Wen P.H., Blumenthal K.M.
      Biochemistry 36:13435-13440(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-18; 18-LYS-LYS-19; LEU-22; LYS-29; TRP-30 AND LYS-33.
    6. "1H-NMR study of neurotoxin B-IV from the marine worm Cerebratulus lacteus. Solution properties, sequence-specific resonance assignments, secondary structure and global fold."
      Hansen P.E., Kem W.R., Bieber A.L., Norton R.S.
      Eur. J. Biochem. 210:231-240(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    7. "Structure of neurotoxin B-IV from the marine worm Cerebratulus lacteus: a helical hairpin cross-linked by disulphide bonding."
      Barnham K.J., Dyke T.R., Kem W.R., Norton R.S.
      J. Mol. Biol. 268:886-902(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.

    Entry informationi

    Entry nameiNXB4_CERLA
    AccessioniPrimary (citable) accession number: P01525
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 79 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, Direct protein sequencing

    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