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Record Information
Version2.0
Creation Date2009-07-03 21:46:55 UTC
Update Date2014-12-24 20:25:33 UTC
Accession NumberT3D2467
Identification
Common NamePhalloidin
ClassProtein
DescriptionPhalloidin is one of a group of toxins from the death cap (Amanita phalloides) known as phallotoxins. The phallotoxins consist of at least seven compounds, all of which have seven similar peptide rings, isolated from the death cap (Amanita phalloides). Though highly toxic to liver cells, it has since been found to have little input into the death cap's toxicity as it is not absorbed through the gut. Furthermore, it is also found in the edible (and sought after) Blusher (Amanita rubescens). (7)
Compound Type
  • Amide
  • Amine
  • Fungal Toxin
  • Mycotoxin
  • Natural Compound
  • Organic Compound
  • Phallotoxin
  • Protein
Protein StructureT3d2467
Synonyms
Synonym
Phalloidine
Chemical FormulaNot Available
Average Molecular Mass3301.700 g/mol
CAS Registry Number17466-45-4
SequenceNot Available
Chemical Taxonomy
DescriptionNot Available
KingdomOrganic Compounds
Super ClassOrganic Acids
ClassCarboxylic Acids and Derivatives
Sub ClassAmino Acids, Peptides, and Analogues
Direct ParentPeptides
Alternative ParentsNot Available
SubstituentsNot Available
Molecular FrameworkNot Available
External DescriptorsNot Available
Biological Properties
StatusDetected and Not Quantified
OriginExogenous
Cellular Locations
  • Acrosome
  • Actin Cytoskeleton
  • Actin Filament
  • Apical Membrane
  • Axoneme
  • Basolateral Membrane
  • Caveolae
  • Cell junction
  • Cell projection
  • Cell surface
  • Centrosome
  • Clathrin Coated Vesicle
  • Cytoplasmic vesicle
  • Cytoskeleton
  • Cytosol
  • Endocytic Vesicle
  • Endoplasmic reticulum
  • Endosome
  • Extracellular
  • Extracellular matrix
  • Focal adhesion
  • Golgi apparatus
  • Intermediate Filament
  • Intracellular Vesicle
  • Kinetochore
  • Lysosome
  • Membrane Fraction
  • Microsome
  • Microtubule
  • Mitochondrial Membrane
  • Mitochondrion
  • Nerve Fiber
  • Nuclear Matrix
  • Nuclear Membrane
  • Nucleolus
  • Nucleoplasm
  • Perinuclear region
  • Plasma Membrane
  • Ribosome
  • Sarcoplasmic Reticulum
  • Secretory Granule
  • Secretory vesicle
  • Soluble Fraction
  • Synaptic Vesicle
  • Tubulin
  • Zymogen Granule
Biofluid LocationsNot Available
Tissue LocationsNot Available
Pathways
NameSMPDB LinkKEGG Link
ApoptosisNot Availablemap04210
EndocytosisNot Availablemap04144
Cell cycleNot Availablemap04110
Bile secretionNot Availablemap04976
PhagosomeNot Availablemap04145
Insulin secretionNot Availablemap04911
AminoglycosidesNot AvailableNot Available
Salivary secretionNot Availablemap04970
Regulation of actin cytoskeletonNot Availablemap04810
Long-term potentiationNot Availablemap04720
TetracyclinesNot AvailableNot Available
Synaptic vesicle cycleNot Availablemap04721
Oxidative phosphorylationNot Availablemap00190
Homologous recombinationNot Availablemap03440
Glutamatergic synapseNot Availablemap04724
Dna replicationNot Availablemap03030
Arachidonic Acid MetabolismSMP00075 map00590
ApplicationsNot Available
Biological RolesNot Available
Chemical RolesNot Available
Physical Properties
StateLiquid
AppearanceClear solution.
Experimental Properties
PropertyValue
Melting PointNot Available
Boiling PointNot Available
Solubility5 mg/mL at 0°C [MERCK INDEX (1996)]
LogPNot Available
Predicted PropertiesNot Available
Spectra
SpectraNot Available
Toxicity Profile
Route of ExposureOral, dermal, inhalation, and parenteral (contaminated drugs). (1)
Mechanism of ToxicityIt binds actin, preventing its depolymerization and poisoning the cell. Phalloidin binds specifically at the interface between F-actin subunits, locking adjacent subunits together. Phalloidin, a bicyclic heptapeptide, binds to actin filaments much more tightly than to actin monomers, leading to a decrease in the rate constant for the dissociation of actin subunits from filament ends, which essentially stabilizes actin filaments through the prevention of filament depolymerization. Moreover, phalloidin is found to inhibit the ATP hydrolysis activity of F-actin (9).
MetabolismPhalloidin was suggested to undergo bioactivation in the liver (2). 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 ValuesLD50: 2 mg/kg (Mouse) (6)
Lethal DoseNot Available
Carcinogenicity (IARC Classification)No indication of carcinogenicity (not listed by IARC). (10)
Uses/SourcesThe property of phalloidin is a useful tool for investigating the distribution of F-actin in cells by labeling phalloidin with fluorescent analogs and using them to stain actin filaments for light microscopy (7).
Minimum Risk LevelNot Available
Health EffectsLiver lesions, tachycardia, hypoglycemia, hypotension and electrolyte imbalance with acid- base disturbance (8).
SymptomsHypovolemic shock; Gastrointestinal symptoms occur after a latent period and include abdominal pain, vomiting, and watery diarrhea. Neurologic symptoms are related to hepatic failure and may include encephalopathy, somnolence, confusion, coma and seizures (8).
TreatmentConsider gastric lavage and activated charcoal. (3)
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
DrugBank IDNot Available
HMDB IDNot Available
PubChem Compound ID4752
ChEMBL IDCHEMBL502682
ChemSpider ID23340042
KEGG IDC08439
UniProt IDA8W7P3
OMIM ID
ChEBI ID8040
BioCyc IDNot Available
CTD IDD010590
Stitch IDPhalloidin
PDB IDNot Available
ACToR IDNot Available
Wikipedia LinkPhalloidin
References
Synthesis ReferenceNot Available
MSDST3D2467.pdf
General References
  1. Peraica M, Domijan AM: Contamination of food with mycotoxins and human health. Arh Hig Rada Toksikol. 2001 Mar;52(1):23-35. [11370295 ]
  2. Oliveira VX Jr, Fazio MA, Miranda MT, da Silva JM, Bittencourt JC, Elias CF, Miranda A: Leptin fragments induce Fos immunoreactivity in rat hypothalamus. Regul Pept. 2005 Apr 15;127(1-3):123-32. [15680478 ]
  3. Uusi-Oukari M, Korpi ER: Specific alterations in the cerebellar GABA(A) receptors of an alcohol-sensitive ANT rat line. Alcohol Clin Exp Res. 1991 Mar;15(2):241-8. [1647706 ]
  4. The Chemical Society (1972). Foreign Compound Metabolism in Mammals. Volume 2: A Review of the Literature Published Between 1970 and 1971. London: The Chemical Society.
  5. Rumack BH (2009). POISINDEX(R) Information System. Englewood, CO: Micromedex, Inc. CCIS Volume 142, edition expires Nov, 2009.
  6. Deshpande SS (2002). Handbook of food toxicology. New York, NY: Marcel Dekker Inc.
  7. Wikipedia. Phallotoxin. Last Updated 5 July 2009. [Link]
  8. Wikipedia. Tramadol. Last Updated 8 August 2009. [Link]
  9. Wikipedia. Phalloidin. Last Updated 17 July 2009. [Link]
  10. International Agency for Research on Cancer (2014). IARC Monographs on the Evaluation of Carcinogenic Risks to Humans. [Link]
Gene Regulation
Up-Regulated GenesNot Available
Down-Regulated GenesNot Available

Targets

General Function:
Myosin binding
Specific Function:
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Gene Name:
ACTC1
Uniprot ID:
P68032
Molecular Weight:
42018.6 Da
References
  1. Huang ZJ, Haugland RP, You WM, Haugland RP: Phallotoxin and actin binding assay by fluorescence enhancement. Anal Biochem. 1992 Jan;200(1):199-204. [1595896 ]
  2. Wikipedia. Phalloidin. Last Updated 17 July 2009. [Link]
General Function:
Structural constituent of cytoskeleton
Specific Function:
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Gene Name:
ACTA1
Uniprot ID:
P68133
Molecular Weight:
42050.67 Da
References
  1. Huang ZJ, Haugland RP, You WM, Haugland RP: Phallotoxin and actin binding assay by fluorescence enhancement. Anal Biochem. 1992 Jan;200(1):199-204. [1595896 ]
  2. Wikipedia. Phalloidin. Last Updated 17 July 2009. [Link]
General Function:
Protein kinase binding
Specific Function:
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Gene Name:
ACTA2
Uniprot ID:
P62736
Molecular Weight:
42008.57 Da
References
  1. Huang ZJ, Haugland RP, You WM, Haugland RP: Phallotoxin and actin binding assay by fluorescence enhancement. Anal Biochem. 1992 Jan;200(1):199-204. [1595896 ]
  2. Wikipedia. Phalloidin. Last Updated 17 July 2009. [Link]
General Function:
Tat protein binding
Specific Function:
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Gene Name:
ACTB
Uniprot ID:
P60709
Molecular Weight:
41736.37 Da
References
  1. Huang ZJ, Haugland RP, You WM, Haugland RP: Phallotoxin and actin binding assay by fluorescence enhancement. Anal Biochem. 1992 Jan;200(1):199-204. [1595896 ]
  2. Wikipedia. Phalloidin. Last Updated 17 July 2009. [Link]
General Function:
Ubiquitin protein ligase binding
Specific Function:
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Gene Name:
ACTG1
Uniprot ID:
P63261
Molecular Weight:
41792.48 Da
References
  1. Huang ZJ, Haugland RP, You WM, Haugland RP: Phallotoxin and actin binding assay by fluorescence enhancement. Anal Biochem. 1992 Jan;200(1):199-204. [1595896 ]
  2. Wikipedia. Phalloidin. Last Updated 17 July 2009. [Link]
General Function:
Atp binding
Specific Function:
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Gene Name:
ACTG2
Uniprot ID:
P63267
Molecular Weight:
41876.495 Da
References
  1. Huang ZJ, Haugland RP, You WM, Haugland RP: Phallotoxin and actin binding assay by fluorescence enhancement. Anal Biochem. 1992 Jan;200(1):199-204. [1595896 ]
  2. Wikipedia. Phalloidin. Last Updated 17 July 2009. [Link]