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P85421

- AMATX_AMAPH

UniProt

P85421 - AMATX_AMAPH

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Protein

Amatoxin

Gene
N/A
Organism
Amanita phalloides (Death cap)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

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

Keywords - Molecular functioni

Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Amatoxin
Alternative name(s):
Alpha-amanitin
Gamma-amanitin
OrganismiAmanita phalloides (Death cap)
Taxonomic identifieri67723 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesAmanitaceaeAmanita

Pathology & Biotechi

Toxic dosei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Peptidei1 – 88Amatoxin2 PublicationsPRO_0000349137

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki1 ↔ 8Cyclopeptide (Ile-Pro)2 Publications
Modified residuei1 – 11(3R,4R)-4,5-dihydroxyisoleucine; in form alpha-amanitin2 Publications
Modified residuei1 – 11(3R,4S)-4-hydroxyisoleucine; in form gamma-amanitin
Cross-linki2 ↔ 62'-cysteinyl-6'-hydroxytryptophan sulfoxide (Trp-Cys)2 Publications
Modified residuei8 – 814-hydroxyproline2 Publications

Keywords - PTMi

Hydroxylation, Thioether bond

Interactioni

Protein-protein interaction databases

DIPiDIP-46365N.

Structurei

Secondary structure

1
8
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 63

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K83X-ray2.80M1-8[»]
2VUMX-ray3.40M1-8[»]
3CQZX-ray2.80M1-8[»]

Miscellaneous databases

EvolutionaryTraceiP85421.

Sequencei

Sequence statusi: Complete.

Length:8
Mass (Da):859
Last modified:September 2, 2008 - v1
Checksum:i5A644EB870586370
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1K83 X-ray 2.80 M 1-8 [» ]
2VUM X-ray 3.40 M 1-8 [» ]
3CQZ X-ray 2.80 M 1-8 [» ]
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-46365N.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P85421.

Family and domain databases

ProtoNeti Search...

Publicationsi

  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, HYDROXYLATION AT ILE-1 AND PRO-8.
  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.

Entry informationi

Entry nameiAMATX_AMAPH
AccessioniPrimary (citable) accession number: P85421
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 2, 2008
Last modified: September 3, 2014
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

This peptide is cyclic. The peptide order is assigned by homology with the gene sequence for alpha-amanitin from Amanita bisporigera.1 Publication
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.1 Publication

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3