Phoneutriatoxin (T3D2503)
Record Information | |||||||||||
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Version | 2.0 | ||||||||||
Creation Date | 2009-07-03 22:19:02 UTC | ||||||||||
Update Date | 2014-12-24 20:25:37 UTC | ||||||||||
Accession Number | T3D2503 | ||||||||||
Identification | |||||||||||
Common Name | Phoneutriatoxin | ||||||||||
Class | Protein | ||||||||||
Description | Phoneutriatoxin is a peptide toxin produced by the Banana spider (Phoneutria nigriventer). It acts as an antagonist at certain calcium channels, causing rapid paralysis leading to death. (1) | ||||||||||
Compound Type |
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Protein Structure | |||||||||||
Synonyms |
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Chemical Formula | Not Available | ||||||||||
Average Molecular Mass | 12677.715 g/mol | ||||||||||
CAS Registry Number | Not Available | ||||||||||
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 | Phoneutriatoxin acts as an antagonist at certain calcium channels. (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 | Not Available | ||||||||||
Lethal Dose | Not Available | ||||||||||
Carcinogenicity (IARC Classification) | No indication of carcinogenicity to humans (not listed by IARC). | ||||||||||
Uses/Sources | Phoneutriatoxin is a peptide toxin produced by the Banana spider (Phoneutria nigriventer). (1) | ||||||||||
Minimum Risk Level | Not Available | ||||||||||
Health Effects | Phoneutriatoxin is neurotoxic. (1) | ||||||||||
Symptoms | Phoneutriatoxin is a peptide toxin produced by the Banana spider (Phoneutria nigriventer). (1) | ||||||||||
Treatment | An antivenom exists for Phoneutria nigriventer stings. (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 | P81790 | ||||||||||
OMIM ID | |||||||||||
ChEBI ID | Not Available | ||||||||||
BioCyc ID | Not Available | ||||||||||
CTD ID | Not Available | ||||||||||
Stitch ID | Not Available | ||||||||||
PDB ID | Not Available | ||||||||||
ACToR ID | Not Available | ||||||||||
Wikipedia Link | Not Available | ||||||||||
References | |||||||||||
Synthesis Reference | Not Available | ||||||||||
MSDS | Not Available | ||||||||||
General References | |||||||||||
Gene Regulation | |||||||||||
Up-Regulated Genes | Not Available | ||||||||||
Down-Regulated Genes | Not Available |
Targets
- General Function:
- Voltage-gated calcium channel activity
- Specific Function:
- Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1C gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing the alpha-1C subunit play an important role in excitation-contraction coupling in the heart. The various isoforms display marked differences in the sensitivity to DHP compounds. Binding of calmodulin or CABP1 at the same regulatory sites results in an opposit effects on the channel function.
- Gene Name:
- CACNA1C
- Uniprot ID:
- Q13936
- Molecular Weight:
- 248974.1 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:
- Voltage-gated calcium channel activity
- Specific Function:
- Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1B gives rise to N-type calcium currents. N-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by omega-conotoxin-GVIA (omega-CTx-GVIA) and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to dihydropyridines (DHP), and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing alpha-1B subunit may play a role in directed migration of immature neurons.
- Gene Name:
- CACNA1B
- Uniprot ID:
- Q00975
- Molecular Weight:
- 262493.84 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:
- Voltage-gated calcium channel activity
- Specific Function:
- Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1A gives rise to P and/or Q-type calcium currents. P/Q-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by the funnel toxin (Ftx) and by the omega-agatoxin-IVA (omega-Aga-IVA). They are however insensitive to dihydropyridines (DHP), and omega-conotoxin-GVIA (omega-CTx-GVIA).
- Gene Name:
- CACNA1A
- Uniprot ID:
- O00555
- Molecular Weight:
- 282362.39 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.