H2E7Q6 · AAMA2_GALM3
- ProteinAlpha-amanitin proprotein 2
- GeneAMA1-2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Major toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters (PubMed:22202811, PubMed:7642577, PubMed:8702941).
Miscellaneous
The typical symptoms of amatoxin poisoning are gastro-intestinal distress beginning 6-12 hours after ingestion, a remission phase lasting 12-24 hours, and progressive loss of liver function culminating in death within 3-5 days (PubMed:12475187).
One of the few effective treatments is liver transplantation (PubMed:12475187).
One of the few effective treatments is liver transplantation (PubMed:12475187).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Molecular Function | toxin activity |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameAlpha-amanitin proprotein 2
- Cleaved into 1 chains
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Agaricales > Agaricineae > Strophariaceae > Galerina
Accessions
- Primary accessionH2E7Q6
- Secondary accessions
Proteomes
PTM/Processing
Features
Showing features for propeptide, modified residue, peptide, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Propeptide | PRO_0000443567 | 1-10 | ||||
Sequence: MFDTNSTRLP | ||||||
Modified residue | 11 | (3R,4R)-4,5-dihydroxyisoleucine; in form alpha-amanitin | ||||
Sequence: I | ||||||
Modified residue | 11 | (3R,4S)-4-hydroxyisoleucine; in form gamma-amanitin | ||||
Sequence: I | ||||||
Peptide | PRO_0000443568 | 11-18 | Alpha-amanitin | |||
Sequence: IWGIGCNP | ||||||
Cross-link | 11↔18 | Cyclopeptide (Ile-Pro) | ||||
Sequence: IWGIGCNP | ||||||
Cross-link | 12↔16 | 2'-cysteinyl-6'-hydroxytryptophan sulfoxide (Trp-Cys) | ||||
Sequence: WGIGC | ||||||
Modified residue | 18 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Propeptide | PRO_0000443569 | 19-35 | ||||
Sequence: WTAEHVDQTLVSGNDIC |
Post-translational modification
Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic bicyclic octapeptide (By similarity).
POPB first removes 10 residues from the N-terminus (By similarity).
Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By similarity).
The enzyme rebinds the remaining peptide in a different conformation and catalyzes macrocyclization of the N-terminal 8 residues (By similarity).
POPB first removes 10 residues from the N-terminus (By similarity).
Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By similarity).
The enzyme rebinds the remaining peptide in a different conformation and catalyzes macrocyclization of the N-terminal 8 residues (By similarity).
Keywords
- PTM
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length35
- Mass (Da)3,892
- Last updated2012-03-21 v1
- ChecksumA49ED273AEFC7716
Sequence caution
Keywords
- Technical term