AAMA1_AMAFL
ID AAMA1_AMAFL Reviewed; 33 AA.
AC A0A023IWE3; S4WL84;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 25-MAY-2022, entry version 11.
DE RecName: Full=Alpha-amanitin proprotein {ECO:0000303|PubMed:24613547};
DE Contains:
DE RecName: Full=Alpha-amanitin {ECO:0000303|PubMed:24613547};
DE AltName: Full=Amatoxin {ECO:0000303|PubMed:24613547};
DE AltName: Full=Gamma-amanitin {ECO:0000250|UniProtKB:P85421};
DE Flags: Precursor;
GN Name=AMA {ECO:0000303|PubMed:24613547};
OS Amanita fuligineoides.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Amanitaceae; Amanita.
OX NCBI_TaxID=580329;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=24613547; DOI=10.1016/j.toxicon.2014.02.020;
RA Li P., Deng W., Li T.;
RT "The molecular diversity of toxin gene families in lethal Amanita
RT mushrooms.";
RL Toxicon 83:59-68(2014).
RN [2]
RP REVIEW ON TOXICITY.
RX PubMed=12475187; DOI=10.1081/clt-120014646;
RA Enjalbert F., Rapior S., Nouguier-Soule J., Guillon S., Amouroux N.,
RA Cabot C.;
RT "Treatment of amatoxin poisoning: 20-year retrospective analysis.";
RL J. Toxicol. Clin. Toxicol. 40:715-757(2002).
CC -!- FUNCTION: Major toxin belonging to the bicyclic octapeptides amatoxins
CC that acts by binding non-competitively to RNA polymerase II and greatly
CC slowing the elongation of transcripts from target promoters
CC (PubMed:24613547). {ECO:0000305|PubMed:24613547}.
CC -!- PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a
CC toxic cyclic decapeptide (PubMed:24613547). POPB first removes 10
CC residues from the N-terminus (By similarity). Conformational trapping
CC of the remaining peptide forces the enzyme to release this intermediate
CC rather than proceed to macrocyclization (By similarity). The enzyme
CC rebinds the remaining peptide in a different conformation and catalyzes
CC macrocyclization of the N-terminal 8 residues (By similarity).
CC {ECO:0000250|UniProtKB:A0A067SLB9, ECO:0000305|PubMed:24613547}.
CC -!- SIMILARITY: Belongs to the MSDIN fungal toxin family. {ECO:0000305}.
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DR EMBL; KF552095; AHB18723.1; -; Genomic_DNA.
DR EMBL; KF156783; AGO98242.1; -; Genomic_DNA.
DR EMBL; KF546283; AHX98307.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A023IWE3; -.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR027582; Amanitin/phalloidin.
DR TIGRFAMs; TIGR04309; amanitin; 1.
PE 3: Inferred from homology;
KW Hydroxylation; Thioether bond; Toxin.
FT PROPEP 1..10
FT /evidence="ECO:0000250|UniProtKB:A8W7M4"
FT /id="PRO_0000443573"
FT PEPTIDE 11..18
FT /note="Alpha-amanitin"
FT /evidence="ECO:0000250|UniProtKB:A8W7M4"
FT /id="PRO_0000443574"
FT PROPEP 19..33
FT /evidence="ECO:0000250|UniProtKB:A8W7M4"
FT /id="PRO_0000443575"
FT MOD_RES 11
FT /note="(3R,4R)-4,5-dihydroxyisoleucine; in form alpha-
FT amanitin"
FT /evidence="ECO:0000250|UniProtKB:P85421"
FT MOD_RES 11
FT /note="(3R,4S)-4-hydroxyisoleucine; in form gamma-amanitin"
FT /evidence="ECO:0000250|UniProtKB:P85421"
FT MOD_RES 18
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P85421"
FT CROSSLNK 11..18
FT /note="Cyclopeptide (Ile-Pro)"
FT /evidence="ECO:0000250|UniProtKB:A8W7M4"
FT CROSSLNK 12..16
FT /note="2'-cysteinyl-6'-hydroxytryptophan sulfoxide (Trp-
FT Cys)"
FT /evidence="ECO:0000250|UniProtKB:P85421"
SQ SEQUENCE 33 AA; 3474 MW; 77878096A7C4C3CB CRC64;
MSDINATRLP IWGIGCNPCV GDEVTALLTR GEA
