ID   PHAT_AMAPL              Reviewed;          32 AA.
AC   A0A023IWI8; A0A023UAK0;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Phallacidin proprotein {ECO:0000303|PubMed:24613547};
DE   Contains:
DE     RecName: Full=Phallacidin {ECO:0000303|PubMed:24613547};
DE   Flags: Precursor;
GN   Name=PHA {ECO:0000303|PubMed:24613547};
OS   Amanita pallidorosea.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Amanitaceae; Amanita.
OX   NCBI_TaxID=1324310;
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).
CC   -!- FUNCTION: Major toxin that belongs to the bicyclic heptapeptides called
CC       phallotoxins (PubMed:24613547). Although structurally related to
CC       amatoxins, phallotoxins have a different mode of action, which is the
CC       stabilization of F-actin (PubMed:24613547). Phallotoxins are poisonous
CC       when administered parenterally, but not orally because of poor
CC       absorption (PubMed:24613547). {ECO:0000305|PubMed:24613547}.
CC   -!- PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a
CC       toxic cyclic heptapeptide (By similarity). 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 7 residues (By similarity).
CC       {ECO:0000250|UniProtKB:A0A067SLB9}.
CC   -!- SIMILARITY: Belongs to the MSDIN fungal toxin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KF552098; AHB18726.1; -; Genomic_DNA.
DR   EMBL; KC778571; AGO98227.1; -; Genomic_DNA.
DR   EMBL; KC778572; AGO98228.1; -; Genomic_DNA.
DR   EMBL; KC778573; AGO98229.1; -; Genomic_DNA.
DR   EMBL; KF546300; AHX98324.1; -; Genomic_DNA.
DR   EMBL; KF546301; AHX98325.1; -; Genomic_DNA.
DR   EMBL; KF546302; AHX98326.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A023IWI8; -.
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   Thioether bond; Toxin.
FT   PROPEP          1..10
FT                   /evidence="ECO:0000250|UniProtKB:A8W7M4"
FT                   /id="PRO_0000443626"
FT   PEPTIDE         11..17
FT                   /note="Phallacidin"
FT                   /evidence="ECO:0000250|UniProtKB:A8W7M4"
FT                   /id="PRO_0000443627"
FT   PROPEP          18..32
FT                   /evidence="ECO:0000250|UniProtKB:A8W7M4"
FT                   /id="PRO_0000443628"
FT   CROSSLNK        11..17
FT                   /note="Cyclopeptide (Ala-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   32 AA;  3573 MW;  F876AD21CE580CE2 CRC64;
     MSDINATRLP AWLVDCPCVG DDINRLLTRG EK