Phrixotoxin (T3D2501)
Record Information | |||||||||||
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Version | 2.0 | ||||||||||
Creation Date | 2009-07-03 22:19:01 UTC | ||||||||||
Update Date | 2014-12-24 20:25:37 UTC | ||||||||||
Accession Number | T3D2501 | ||||||||||
Identification | |||||||||||
Common Name | Phrixotoxin | ||||||||||
Class | Protein | ||||||||||
Description | Phrixotoxin is a peptide toxin produced by the Chilean copper tarantula (Paraphysa scrofa). It blocks A-type potassium channels. (1) | ||||||||||
Compound Type |
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Protein Structure | |||||||||||
Synonyms |
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Chemical Formula | Not Available | ||||||||||
Average Molecular Mass | 3555.310 g/mol | ||||||||||
CAS Registry Number | 880886-00-0 or 221872-97-5 | ||||||||||
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) (2) | ||||||||||
Mechanism of Toxicity | Phrixotoxin blocks A-type potassium channels by altering the gating properties of these 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 | Phrixotoxin is a peptide toxin produced by the Chilean copper tarantula (Paraphysa scrofa). (1) | ||||||||||
Minimum Risk Level | Not Available | ||||||||||
Health Effects | Phrixotoxin is neurotoxic. (1) | ||||||||||
Symptoms | Phrixotoxin is a peptide toxin produced by the Chilean copper tarantula (Paraphysa scrofa). (1) | ||||||||||
Treatment | Not Available | ||||||||||
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 | P61230 | ||||||||||
OMIM ID | |||||||||||
ChEBI ID | Not Available | ||||||||||
BioCyc ID | Not Available | ||||||||||
CTD ID | Not Available | ||||||||||
Stitch ID | Not Available | ||||||||||
PDB ID | 1V7F | ||||||||||
ACToR ID | Not Available | ||||||||||
Wikipedia Link | Not Available | ||||||||||
References | |||||||||||
Synthesis Reference | Not Available | ||||||||||
MSDS | T3D2501.pdf | ||||||||||
General References |
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Gene Regulation | |||||||||||
Up-Regulated Genes | Not Available | ||||||||||
Down-Regulated Genes | Not Available |
Targets
- General Function:
- Voltage-gated potassium channel activity
- Specific Function:
- Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain. Mediates the major part of the dendritic A-type current I(SA) in brain neurons (By similarity). This current is activated at membrane potentials that are below the threshold for action potentials. It regulates neuronal excitability, prolongs the latency before the first spike in a series of action potentials, regulates the frequency of repetitive action potential firing, shortens the duration of action potentials and regulates the back-propagation of action potentials from the neuronal cell body to the dendrites. Contributes to the regulation of the circadian rhytm of action potential firing in suprachiasmatic nucleus neurons, which regulates the circadian rhythm of locomotor activity (By similarity). Functions downstream of the metabotropic glutamate receptor GRM5 and plays a role in neuronal excitability and in nociception mediated by activation of GRM5 (By similarity). Mediates the transient outward current I(to) in rodent heart left ventricle apex cells, but not in human heart, where this current is mediated by another family member. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient (PubMed:10551270, PubMed:15454437, PubMed:14695263, PubMed:14623880, PubMed:14980201, PubMed:16934482, PubMed:24811166, PubMed:24501278). The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:11507158). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCND2 and KCND3; channel properties depend on the type of pore-forming alpha subunits that are part of the channel. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes. Interaction with specific isoforms of the regulatory subunits KCNIP1, KCNIP2, KCNIP3 or KCNIP4 strongly increases expression at the cell surface and thereby increases channel activity; it modulates the kinetics of channel activation and inactivation, shifts the threshold for channel activation to more negative voltage values, shifts the threshold for inactivation to less negative voltages and accelerates recovery after inactivation (PubMed:15454437, PubMed:14623880, PubMed:14980201, PubMed:19171772, PubMed:24501278, PubMed:24811166). Likewise, interaction with DPP6 or DPP10 promotes expression at the cell membrane and regulates both channel characteristics and activity (By similarity).
- Gene Name:
- KCND2
- Uniprot ID:
- Q9NZV8
- Molecular Weight:
- 70535.825 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:
- Metal ion binding
- Specific Function:
- Pore-forming (alpha) subunit of voltage-gated rapidly inactivating A-type potassium channels. May contribute to I(To) current in heart and I(Sa) current in neurons. Channel properties are modulated by interactions with other alpha subunits and with regulatory subunits.
- Gene Name:
- KCND3
- Uniprot ID:
- Q9UK17
- Molecular Weight:
- 73450.53 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.