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P85421

- AMATX_AMAPH

UniProt

P85421 - AMATX_AMAPH

Protein

Amatoxin

Gene
N/A
Organism
Amanita phalloides (Death cap)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. 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:
    Amatoxin1 Publication
    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)3 Publications
    Modified residuei1 – 11(3R,4R)-4,5-dihydroxyisoleucine; in form alpha-amanitin1 Publication
    Modified residuei1 – 11(3R,4S)-4-hydroxyisoleucine; in form gamma-amanitin1 Publication
    Cross-linki2 ↔ 62'-cysteinyl-6'-hydroxytryptophan sulfoxide (Trp-Cys)
    Modified residuei8 – 814-hydroxyproline3 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[»]
    ModBaseiSearch...
    MobiDBiSearch...

    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: October 1, 2014
    This is version 15 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.Curated
    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.Curated

    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