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Protein

Erabutoxin b

Gene
N/A
Organism
Laticauda semifasciata (Black-banded sea krait) (Pseudolaticauda semifasciata)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Binds with high affinity to muscular nicotinic acetylcholine receptors (nAChRs), and with low affinity to neuronal alpha-7 nAChRs and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acetylcholine receptor inhibiting toxin, Ion channel impairing toxin, Neurotoxin, Postsynaptic neurotoxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Erabutoxin b
Short name:
ETXB
Alternative name(s):
Short neurotoxin 1b
OrganismiLaticauda semifasciata (Black-banded sea krait) (Pseudolaticauda semifasciata)
Taxonomic identifieri8631 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeLaticaudinaeLaticauda

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

LD50 is 0.15 mg/kg by intramuscular injection.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21211 PublicationAdd
BLAST
Chaini22 – 8362Erabutoxin bPRO_0000035447Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 45
Disulfide bondi38 ↔ 62
Disulfide bondi64 ↔ 75
Disulfide bondi76 ↔ 81

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.Curated

Structurei

Secondary structure

1
83
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 253Combined sources
Beta strandi29 – 313Combined sources
Beta strandi35 – 373Combined sources
Beta strandi45 – 528Combined sources
Beta strandi55 – 639Combined sources
Beta strandi73 – 764Combined sources
Turni79 – 824Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ERANMR-A22-83[»]
1FRANMR-A22-83[»]
1NXBX-ray1.38A22-83[»]
3EBXX-ray1.40A22-83[»]
6EBXX-ray1.70A/B22-83[»]
ProteinModelPortaliQ90VW1.
SMRiQ90VW1. Positions 22-83.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ90VW1.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG006553.

Family and domain databases

InterProiIPR003571. Snake_3FTx.
IPR018354. Snake_toxin_con_site.
[Graphical view]
PfamiPF00087. Toxin_1. 1 hit.
[Graphical view]
PROSITEiPS00272. SNAKE_TOXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q90VW1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTLLLTLVV VTIVCLDLGY TRICFNHQSS QPQTTKTCSP GESSCYHKQW
60 70 80
SDFRGTIIER GCGCPTVKPG IKLSCCESEV CNN
Length:83
Mass (Da):9,160
Last modified:December 1, 2001 - v1
Checksum:iBBB499DA36BE50E4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti80 – 801V → R May be a real difference between the Philippine and Japanese populations. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16950 mRNA. Translation: CAA34824.1.
AB017929 mRNA. Translation: BAA75749.1.
AB017930 mRNA. Translation: BAA75750.1.
AB017931 mRNA. Translation: BAA75751.1.
AB098528 Genomic DNA. Translation: BAC78201.1.
AB098529 Genomic DNA. Translation: BAC78202.1.
PIRiS06931.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16950 mRNA. Translation: CAA34824.1.
AB017929 mRNA. Translation: BAA75749.1.
AB017930 mRNA. Translation: BAA75750.1.
AB017931 mRNA. Translation: BAA75751.1.
AB098528 Genomic DNA. Translation: BAC78201.1.
AB098529 Genomic DNA. Translation: BAC78202.1.
PIRiS06931.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ERANMR-A22-83[»]
1FRANMR-A22-83[»]
1NXBX-ray1.38A22-83[»]
3EBXX-ray1.40A22-83[»]
6EBXX-ray1.70A/B22-83[»]
ProteinModelPortaliQ90VW1.
SMRiQ90VW1. Positions 22-83.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG006553.

Miscellaneous databases

EvolutionaryTraceiQ90VW1.

Family and domain databases

InterProiIPR003571. Snake_3FTx.
IPR018354. Snake_toxin_con_site.
[Graphical view]
PfamiPF00087. Toxin_1. 1 hit.
[Graphical view]
PROSITEiPS00272. SNAKE_TOXIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Sequence analysis of a cDNA encoding a erabutoxin b from the sea-snake Laticauda semifasciata."
    Obara K., Fuse N., Tsuchiya T., Nonomura Y., Menez A., Tamiya T.
    Nucleic Acids Res. 17:10490-10490(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Venom gland.
  2. "Classification of sea snakes in genus Laticauda by nucleotide sequences encoding short chain neurotoxins."
    Kariya Y., Araki S., Agu H., Tamiya T., Tsuchiya T.
    Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Venom gland.
  3. "Molecular evolution and diversification of snake toxin genes, revealed by analysis of intron sequences."
    Fujimi T.J., Nakajyo T., Nishimura E., Ogura E., Tsuchiya T., Tamiya T.
    Gene 313:111-118(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Liver.
  4. "The amino acid sequences of erabutoxins, neurotoxic proteins of sea-snake (Laticauda semifasciata) venom."
    Sato S., Tamiya N.
    Biochem. J. 122:453-461(1971) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-83, SUBCELLULAR LOCATION.
  5. "The disulphide bonds of erabutoxin a, a neurotoxic protein of a sea-snake (Laticauda semifasciata) venom."
    Endo Y., Sato S., Ishii S., Tamiya N.
    Biochem. J. 122:463-467(1971) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  6. "Correction of partial amino acid sequence of erabutoxins."
    Maeda N., Tamiya N.
    Biochem. J. 167:289-291(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION, VARIANT ARG-80.
  7. Cited for: PRELIMINARY PROTEIN SEQUENCE OF 22-83.
  8. "Only snake curaremimetic toxins with a fifth disulfide bond have high affinity for the neuronal alpha7 nicotinic receptor."
    Servent D., Winckler-Dietrich V., Hu H.-Y., Kessler P., Drevet P., Bertrand D., Menez A.
    J. Biol. Chem. 272:24279-24286(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Tissue: Venom.
  9. "The crystal structure of a post-synaptic neurotoxin from sea snake at 2.2-A resolution."
    Tsernoglou D., Petsko G.A.
    FEBS Lett. 68:1-4(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 22-83, DISULFIDE BONDS.
  10. "Structure and function of snake venom curarimimetic neurotoxins."
    Tsernoglou D., Petsko G.A., Hudson R.A.
    Mol. Pharmacol. 14:710-716(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 22-83, DISULFIDE BONDS.
  11. "Molecular conformation of erabutoxin b; atomic coordinates at 2.5-A resolution."
    Kimball M.R., Sato A., Richardson J.S., Rosen L.S., Low B.W.
    Biochem. Biophys. Res. Commun. 88:950-959(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-83, DISULFIDE BONDS.
  12. "Erabutoxin b. Structure/function relationships following initial protein refinement at 0.140-nm resolution."
    Low B.W., Corfield P.W.
    Eur. J. Biochem. 161:579-587(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 22-83, DISULFIDE BONDS.
  13. "Structure determination of a dimeric form of erabutoxin-b, crystallized from a thiocyanate solution."
    Saludjian P., Prange T., Navaza J., Menez R., Guilloteau J.P., Ries-Kautt M., Ducruix A.
    Acta Crystallogr. B 48:520-531(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 22-83, DISULFIDE BONDS.
  14. "Tertiary structure of erabutoxin b in aqueous solution as elucidated by two-dimensional nuclear magnetic resonance."
    Hatanaka H., Oka M., Kohda D., Tate S., Suda A., Tamiya N., Inagaki F.
    J. Mol. Biol. 240:155-166(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 22-83, DISULFIDE BONDS.

Entry informationi

Entry namei3S1EB_LATSE
AccessioniPrimary (citable) accession number: Q90VW1
Secondary accession number(s): P01435
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 1, 2001
Last modified: October 14, 2015
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.