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Protein

Erabutoxin a

Gene
N/A
Organism
Laticauda semifasciata (Black-banded sea krait) (Pseudolaticauda semifasciata)
Status
Reviewed-Annotation score: -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. Binds to T.marmorata nAChR (Kd=0.07 nM) (PubMed:7721859). Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site. Blocks the extracellular increase of dopamine evoked by nicotine at 4.2 µM concentrations.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei27Moderately important residue for binding to acetylcholine receptor1 Publication1
Sitei28Very important residue for binding to acetylcholine receptor1 Publication1
Sitei29Key residue for binding to acetylcholine receptor2 Publications1
Sitei30Moderately important residue for binding to acetylcholine receptor1 Publication1
Sitei31Key residue for binding to acetylcholine receptor2 Publications1
Sitei46Moderately important residue for binding to acetylcholine receptor1 Publication1
Sitei48Key residue for binding to acetylcholine receptor1 Publication1
Sitei50Very important residue for binding to acetylcholine receptor1 Publication1
Sitei52Very important residue for binding to acetylcholine receptor1 Publication1
Sitei53Moderately important residue for binding to acetylcholine receptor1 Publication1
Sitei54Key residue for binding to acetylcholine receptor2 Publications1
Sitei55Moderately important residue for binding to acetylcholine receptor1 Publication1
Sitei57Very important residue for binding to acetylcholine receptor1 Publication1
Sitei59Very important residue for binding to acetylcholine receptor1 Publication1
Sitei68Very important residue for binding to acetylcholine receptor1 Publication1

GO - Molecular functioni

Keywordsi

Molecular functionAcetylcholine receptor inhibiting toxin, Ion channel impairing toxin, Neurotoxin, Postsynaptic neurotoxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Erabutoxin a2 Publications
Short name:
ETXA
Short name:
Ea1 Publication
Alternative name(s):
Short neurotoxin 1a
OrganismiLaticauda semifasciata (Black-banded sea krait) (Pseudolaticauda semifasciata)
Taxonomic identifieri8631 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeLaticaudinaeLaticauda

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi25F → A: 1.2-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi26N → V: 1.4-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi27H → A: 6-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi28Q → L: 23-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi29S → G: 176-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi29S → T: 780-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi30S → G: 8.8-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi31Q → A: 210-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi32P → N: 2.2-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi33Q → A: 1.2-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi34T → V: 3-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi35T → A: 2.7-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi36K → A: No change in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi37T → A: 2-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi39Missing : No change in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi42E → A: No change in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi46Y → A: 3.7-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi47N → A: No change in potency of inhibition of T.marmorata acetylcholine receptor (identical to erabutoxin b). 1 Publication1
Mutagenesisi48K → E: 175-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi49Q → A: 1.35-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi50W → F: 67-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi50W → H: 8.6-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi51S → A: No change in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi52D → H: 46-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi52D → N: 1.5-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi53F → L: 7-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi54R → E: 187-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi54R → E: 318-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi54R → K: 25-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi55G → S: 7-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi56T → A: No change in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi57I → A: 7-fold increase in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi59E → K: 7.8-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi59E → L: 25-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi59E → Q: 1.4-fold increase in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi65P → V: 3-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi66T → A: No change in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi67V → A: 2-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi68K → A: 32-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi69P → Q: No change in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi70G → V: 2.4-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi71I → Q: 2.3-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi72K → N: 2-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor (identical to erabutoxin c). 1 Publication1
Mutagenesisi73L → A: 1.4-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1
Mutagenesisi74S → A: 2-fold decrease in potency of inhibition of T.marmorata acetylcholine receptor. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 211 PublicationAdd BLAST21
ChainiPRO_000003544622 – 83Erabutoxin a1 PublicationAdd BLAST62

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi24 ↔ 454 PublicationsImported
Disulfide bondi38 ↔ 624 PublicationsImported
Disulfide bondi64 ↔ 754 PublicationsImported
Disulfide bondi76 ↔ 814 PublicationsImported

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.Curated

Structurei

Secondary structure

183
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP60775
SMRiP60775
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60775

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni24 – 38Loop I1 PublicationAdd BLAST15
Regioni39 – 44Stretch between loop I and loop II1 Publication6
Regioni45 – 62Loop II1 PublicationAdd BLAST18
Regioni64 – 75Loop III1 PublicationAdd BLAST12

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG006553

Family and domain databases

CDDicd00206 snake_toxin, 1 hit
InterProiView protein in InterPro
IPR003571 Snake_3FTx
IPR018354 Snake_toxin_con_site
IPR035076 Toxin/TOLIP
PfamiView protein in Pfam
PF00087 Toxin_TOLIP, 1 hit
PROSITEiView protein in PROSITE
PS00272 SNAKE_TOXIN, 1 hit

Sequencei

Sequence statusi: Complete.

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

P60775-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKTLLLTLVV VTIVCLDLGY TRICFNHQSS QPQTTKTCSP GESSCYNKQW
60 70 80
SDFRGTIIER GCGCPTVKPG IKLSCCESEV CNN
Length:83
Mass (Da):9,137
Last modified:July 21, 1986 - v1
Checksum:iBBB499DA33440F44
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02533 mRNA Translation: CAA26373.1
AB017932 mRNA Translation: BAA75752.1
AB098526 Genomic DNA Translation: BAC78199.1
AB098527 Genomic DNA Translation: BAC78200.1
PIRiA01703 N1LT2E

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02533 mRNA Translation: CAA26373.1
AB017932 mRNA Translation: BAA75752.1
AB098526 Genomic DNA Translation: BAC78199.1
AB098527 Genomic DNA Translation: BAC78200.1
PIRiA01703 N1LT2E

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QKDX-ray1.49A/B22-83[»]
1QKEX-ray1.50A22-83[»]
2ERAX-ray1.81A22-83[»]
3ERAX-ray1.70A/B22-83[»]
5EBXX-ray2.00A22-83[»]
ProteinModelPortaliP60775
SMRiP60775
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG006553

Miscellaneous databases

EvolutionaryTraceiP60775

Family and domain databases

CDDicd00206 snake_toxin, 1 hit
InterProiView protein in InterPro
IPR003571 Snake_3FTx
IPR018354 Snake_toxin_con_site
IPR035076 Toxin/TOLIP
PfamiView protein in Pfam
PF00087 Toxin_TOLIP, 1 hit
PROSITEiView protein in PROSITE
PS00272 SNAKE_TOXIN, 1 hit
ProtoNetiSearch...

Entry informationi

Entry namei3S1EA_LATSE
AccessioniPrimary (citable) accession number: P60775
Secondary accession number(s): P01435
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 10, 2018
This is version 78 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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