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P85421 (AMATX_AMAPH) Reviewed, UniProtKB/Swiss-Prot

Last modified October 31, 2012. Version 13. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Amatoxin
Alternative name(s):
Alpha-amanitin
Gamma-amanitin
OrganismAmanita phalloides (Death cap)
Taxonomic identifier67723 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesAmanitaceaeAmanita

Protein attributes

Sequence length8 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Major toxin from Amanita phalloideae. Acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters. Ref.1 Ref.2 Ref.3 Ref.4

Toxic dose

LD50 is 0.35 mg/kg by intraperitoneal injection into mice. LD50 is 4 mg/kg by intravenous injection into rats, and 0.1 mg/kg by intravenous injection into dogs. LD50 is 2 µg/kg by intracerebroventricular injection into mice, and 10 µg/kg by intracerebroventricular injection into rats. Ref.3

Caution

This peptide is cyclic. The peptide order is assigned by homology with the gene sequence for alpha-amanitin from Amanita bisporigera. Ref.4

In peptide sequencing work prior to 1968, the residue shown in the first position was reported as a beta-methylleucine derivative that could arise by either beta-methylation of leucine or gamma-methylation of isoleucine. The correct structure has been determined to be derived from isoleucine without methylation. Ref.4

Ontologies

Keywords
   Molecular functionToxin
   PTMHydroxylation
Thioether bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Peptide1 – 88Amatoxin Ref.3 Ref.4
PRO_0000349137

Amino acid modifications

Modified residue11(3R,4R)-4,5-dihydroxyisoleucine; in form alpha-amanitin Ref.3 Ref.6
Modified residue11(3R,4S)-4-hydroxyisoleucine; in form gamma-amanitin
Modified residue814-hydroxyproline Ref.3 Ref.6
Cross-link1 ↔ 8Cyclopeptide (Ile-Pro) Ref.3 Ref.6
Cross-link2 ↔ 62'-cysteinyl-6'-hydroxytryptophan sulfoxide (Trp-Cys) Ref.3 Ref.6

Secondary structure

... 8
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P85421 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 5A644EB870586370

FASTA8859
IWGIGCNP 

« Hide

References

[1]"Poisonous principles of mushrooms of the genus Amanita. Four-carbon amines acting on the central nervous system and cell-destroying cyclic peptides are produced."
Wieland T.
Science 159:946-952(1968) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, 3D-STRUCTURE.
[2]"Amatoxins, phallotoxins, phallolysin, and antamanide: the biologically active components of poisonous Amanita mushrooms."
Wieland T., Faulstich H.
CRC Crit. Rev. Biochem. 5:185-260(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, TOXIC DOSE.
[3]"Action of alpha-amanitin during pyrophosphorolysis and elongation by RNA polymerase II."
Chafin D.R., Guo H., Price D.H.
J. Biol. Chem. 270:19114-19119(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"Amanitin greatly reduces the rate of transcription by RNA polymerase II ternary complexes but fails to inhibit some transcript cleavage modes."
Rudd M.D., Luse D.S.
J. Biol. Chem. 271:21549-21558(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Structural basis of transcription: alpha-amanitin-RNA polymerase II cocrystal at 2.8 A resolution."
Bushnell D.A., Cramer P., Kornberg R.D.
Proc. Natl. Acad. Sci. U.S.A. 99:1218-1222(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH RNA POL II CORE COMPLEX.
[6]"Structural basis of transcription inhibition by alpha-amanitin and implications for RNA polymerase II translocation."
Brueckner F., Cramer P.
Nat. Struct. Mol. Biol. 15:811-818(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) IN COMPLEX WITH RNA POL II ELONGATION COMPLEX.
+Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K83X-ray2.80M1-8[»]
2VUMX-ray3.40M1-8[»]
3CQZX-ray2.80M1-8[»]
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-46365N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Other

EvolutionaryTraceP85421.

Entry information

Entry nameAMATX_AMAPH
AccessionPrimary (citable) accession number: P85421
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 2, 2008
Last modified: October 31, 2012
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references