
Erabutoxin (T3D2635)
| Record Information | |||||||||||
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| Version | 2.0 | ||||||||||
| Creation Date | 2009-07-06 21:35:44 UTC | ||||||||||
| Update Date | 2014-12-24 20:25:47 UTC | ||||||||||
| Accession Number | T3D2635 | ||||||||||
| Identification | |||||||||||
| Common Name | Erabutoxin | ||||||||||
| Class | Protein | ||||||||||
| Description | Erabutoxin is a peptide toxin produced by the Broad-banded blue sea snake (Laticauda semifasciata). It binds to muscular and neuronal nicotinic acetylcholine receptors (nAChRs), produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site. (1) | ||||||||||
| Compound Type |
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| Protein Structure | |||||||||||
| Synonyms |
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| Chemical Formula | Not Available | ||||||||||
| Average Molecular Mass | 9136.510 g/mol | ||||||||||
| CAS Registry Number | 59536-69-5 | ||||||||||
| Sequence | Not Available | ||||||||||
| Chemical Taxonomy | |||||||||||
| Description | Not Available | ||||||||||
| Kingdom | Organic Compounds | ||||||||||
| Super Class | Organic Acids | ||||||||||
| Class | Carboxylic Acids and Derivatives | ||||||||||
| Sub Class | Amino Acids, Peptides, and Analogues | ||||||||||
| Direct Parent | Peptides | ||||||||||
| Alternative Parents | Not Available | ||||||||||
| Substituents | Not Available | ||||||||||
| Molecular Framework | Not Available | ||||||||||
| External Descriptors | Not Available | ||||||||||
| Biological Properties | |||||||||||
| Status | Detected and Not Quantified | ||||||||||
| Origin | Exogenous | ||||||||||
| Cellular Locations | Not Available | ||||||||||
| Biofluid Locations | Not Available | ||||||||||
| Tissue Locations | Not Available | ||||||||||
| Pathways | Not Available | ||||||||||
| Applications | Not Available | ||||||||||
| Biological Roles | Not Available | ||||||||||
| Chemical Roles | Not Available | ||||||||||
| Physical Properties | |||||||||||
| State | Liquid | ||||||||||
| Appearance | Clear solution. | ||||||||||
| Experimental Properties |
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| Predicted Properties | Not Available | ||||||||||
| Spectra | |||||||||||
| Spectra |
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| Toxicity Profile | |||||||||||
| Route of Exposure | Injection (sting/bite) (3) | ||||||||||
| Mechanism of Toxicity | Erabutoxin binds with high affinity to muscular nicotinic acetylcholine receptors (nAChRs), and with low affinity to neuronal alpha-7 nAChRs. This produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site. (1) | ||||||||||
| Metabolism | Free toxin may be removed by opsonization via the reticuloendothelial system (primarily the liver and kidneys) or it may be degraded through cellular internalization via the lysosomes. Lysosomes are membrane-enclosed organelles that contain an array of digestive enzymes, including several proteases. | ||||||||||
| Toxicity Values | LD50: 0.273 mg/kg (Subcutaneous, Mouse) (4) LD50: 0.34 mg/kg (Intravenous, Mouse) (4) | ||||||||||
| Lethal Dose | Not Available | ||||||||||
| Carcinogenicity (IARC Classification) | No indication of carcinogenicity to humans (not listed by IARC). | ||||||||||
| Uses/Sources | Erabutoxin is a peptide toxin produced by the Broad-banded blue sea snake (Laticauda semifasciata). (1) | ||||||||||
| Minimum Risk Level | Not Available | ||||||||||
| Health Effects | Erabutoxin is neurotoxic and causes peripheral paralysis. (1) | ||||||||||
| Symptoms | Erabutoxin causes peripheral paralysis. (1) | ||||||||||
| Treatment | An antivenom exists for Broad-banded blue sea snake venom. (2) | ||||||||||
| Normal Concentrations | |||||||||||
| Not Available | |||||||||||
| Abnormal Concentrations | |||||||||||
| Not Available | |||||||||||
| External Links | |||||||||||
| DrugBank ID | Not Available | ||||||||||
| HMDB ID | Not Available | ||||||||||
| PubChem Compound ID | Not Available | ||||||||||
| ChEMBL ID | Not Available | ||||||||||
| ChemSpider ID | Not Available | ||||||||||
| KEGG ID | Not Available | ||||||||||
| UniProt ID | P60775 | ||||||||||
| OMIM ID | |||||||||||
| ChEBI ID | Not Available | ||||||||||
| BioCyc ID | Not Available | ||||||||||
| CTD ID | Not Available | ||||||||||
| Stitch ID | Not Available | ||||||||||
| PDB ID | 1QKD | ||||||||||
| ACToR ID | Not Available | ||||||||||
| Wikipedia Link | Not Available | ||||||||||
| References | |||||||||||
| Synthesis Reference | Not Available | ||||||||||
| MSDS | T3D2635.pdf | ||||||||||
| General References | |||||||||||
| Gene Regulation | |||||||||||
| Up-Regulated Genes | Not Available | ||||||||||
| Down-Regulated Genes | Not Available | ||||||||||
Targets
- General Function:
- Ion channel activity
- Specific Function:
- After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
- Gene Name:
- CHRNA1
- Uniprot ID:
- P02708
- Molecular Weight:
- 54545.235 Da
References
- Armas LA, Hollis BW, Heaney RP: Vitamin D2 is much less effective than vitamin D3 in humans. J Clin Endocrinol Metab. 2004 Nov;89(11):5387-91. [15531486 ]
- The UniProt Consortium. The Universal Protein Resource (UniProt) Nucleic Acids Res. 2008;36:D190-D195.
- General Function:
- Ligand-gated ion channel activity
- Specific Function:
- After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
- Gene Name:
- CHRNB1
- Uniprot ID:
- P11230
- Molecular Weight:
- 56697.9 Da
References
- Armas LA, Hollis BW, Heaney RP: Vitamin D2 is much less effective than vitamin D3 in humans. J Clin Endocrinol Metab. 2004 Nov;89(11):5387-91. [15531486 ]
- The UniProt Consortium. The Universal Protein Resource (UniProt) Nucleic Acids Res. 2008;36:D190-D195.
- General Function:
- Acetylcholine-activated cation-selective channel activity
- Specific Function:
- After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
- Gene Name:
- CHRND
- Uniprot ID:
- Q07001
- Molecular Weight:
- 58894.55 Da
References
- Armas LA, Hollis BW, Heaney RP: Vitamin D2 is much less effective than vitamin D3 in humans. J Clin Endocrinol Metab. 2004 Nov;89(11):5387-91. [15531486 ]
- The UniProt Consortium. The Universal Protein Resource (UniProt) Nucleic Acids Res. 2008;36:D190-D195.
- General Function:
- Cation transmembrane transporter activity
- Specific Function:
- After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
- Gene Name:
- CHRNE
- Uniprot ID:
- Q04844
- Molecular Weight:
- 54696.54 Da
References
- Armas LA, Hollis BW, Heaney RP: Vitamin D2 is much less effective than vitamin D3 in humans. J Clin Endocrinol Metab. 2004 Nov;89(11):5387-91. [15531486 ]
- The UniProt Consortium. The Universal Protein Resource (UniProt) Nucleic Acids Res. 2008;36:D190-D195.
- General Function:
- Channel activity
- Specific Function:
- After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
- Gene Name:
- CHRNG
- Uniprot ID:
- P07510
- Molecular Weight:
- 57882.8 Da
References
- Armas LA, Hollis BW, Heaney RP: Vitamin D2 is much less effective than vitamin D3 in humans. J Clin Endocrinol Metab. 2004 Nov;89(11):5387-91. [15531486 ]
- The UniProt Consortium. The Universal Protein Resource (UniProt) Nucleic Acids Res. 2008;36:D190-D195.
- General Function:
- Toxic substance binding
- Specific Function:
- After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. The channel is blocked by alpha-bungarotoxin.
- Gene Name:
- CHRNA7
- Uniprot ID:
- P36544
- Molecular Weight:
- 56448.925 Da
References
- Armas LA, Hollis BW, Heaney RP: Vitamin D2 is much less effective than vitamin D3 in humans. J Clin Endocrinol Metab. 2004 Nov;89(11):5387-91. [15531486 ]
- The UniProt Consortium. The Universal Protein Resource (UniProt) Nucleic Acids Res. 2008;36:D190-D195.