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P01525

- NXB4_CERLA

UniProt

P01525 - NXB4_CERLA

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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

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
Complete GO annotation...

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-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi9 – 91Y → F: 5-fold decrease in toxicity. 1 Publication
Mutagenesisi13 – 131E → A: No change in toxicity. 1 Publication
Mutagenesisi13 – 131E → Q: No change in toxicity. 1 Publication
Mutagenesisi17 – 171R → A: Complete loss of toxicity. 1 Publication
Mutagenesisi17 – 171R → K: Complete loss of toxicity. 1 Publication
Mutagenesisi17 – 171R → Q: Complete loss of toxicity. 1 Publication
Mutagenesisi18 – 192KK → QQ: Very low decrease in toxicity. 1 Publication
Mutagenesisi18 – 181K → Q: No change in toxicity. 1 Publication
Mutagenesisi21 – 211D → A: No change in toxicity. 1 Publication
Mutagenesisi21 – 211D → N: No change in toxicity. 1 Publication
Mutagenesisi21 – 211D → P: 10-fold decrease in toxicity. 1 Publication
Mutagenesisi22 – 221L → D: No change in toxicity. 1 Publication
Mutagenesisi25 – 251R → K: No change in toxicity. 1 Publication
Mutagenesisi25 – 251R → Q: 400-fold decrease in toxicity. 1 Publication
Mutagenesisi29 – 291K → N: No change in toxicity. 1 Publication
Mutagenesisi30 – 301W → F: No change in toxicity. 1 Publication
Mutagenesisi30 – 301W → S: 41-fold decrease in toxicity. 1 Publication
Mutagenesisi30 – 301W → Y: 5-fold decrease in toxicity. 1 Publication
Mutagenesisi33 – 331K → N: No decrease in toxicity. 1 Publication
Mutagenesisi34 – 341R → A: 80-fold decrease in toxicity. 1 Publication
Mutagenesisi34 – 341R → K: 8-fold decrease in toxicity. 1 Publication
Mutagenesisi34 – 341R → Q: 20-fold decrease in toxicity. 1 Publication

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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
ASATWGAAYP ACENNCRKKY DLCIRCQGKW AGKRGKCAAH CIIQKNNCKG

KCKKE
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 29, 2014
This is version 80 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