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Protein

Amatoxin

Gene
N/A
Organism
Amanita phalloides (Death cap)
Status
Reviewed-Annotation score: 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:
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)DescriptionActionsGraphical viewLength
PeptideiPRO_00003491371 – 8Amatoxin2 Publications8

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki1 ↔ 8Cyclopeptide (Ile-Pro)3 Publications
Modified residuei1(3R,4R)-4,5-dihydroxyisoleucine; in form alpha-amanitin1 Publication1
Modified residuei1(3R,4S)-4-hydroxyisoleucine; in form gamma-amanitin1 Publication1
Cross-linki2 ↔ 62'-cysteinyl-6'-hydroxytryptophan sulfoxide (Trp-Cys)
Modified residuei84-hydroxyproline3 Publications1

Keywords - PTMi

Hydroxylation, Thioether bond

Interactioni

Protein-protein interaction databases

DIPiDIP-46365N.

Structurei

Secondary structure

18
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni4 – 6Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K83X-ray2.80M1-8[»]
2VUMX-ray3.40M1-8[»]
3CQZX-ray2.80M1-8[»]
SMRiP85421.
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:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K83X-ray2.80M1-8[»]
2VUMX-ray3.40M1-8[»]
3CQZX-ray2.80M1-8[»]
SMRiP85421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46365N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP85421.

Family and domain databases

ProtoNetiSearch...

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: November 2, 2016
This is version 17 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.