ID   PHAT2_AMAEX             Reviewed;          34 AA.
AC   U5L397;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Phallacidin proprotein 2 {ECO:0000303|PubMed:24050899};
DE   Contains:
DE     RecName: Full=Phallacidin {ECO:0000303|PubMed:24050899};
DE   Flags: Precursor;
GN   Name=PHA {ECO:0000303|PubMed:24050899};
OS   Amanita exitialis (Guangzhou destroying angel).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Amanitaceae; Amanita.
OX   NCBI_TaxID=262245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=24050899; DOI=10.1016/j.gene.2013.09.014;
RA   Li P., Deng W.Q., Li T.H., Song B., Shen Y.H.;
RT   "Illumina-based de novo transcriptome sequencing and analysis of Amanita
RT   exitialis basidiocarps.";
RL   Gene 532:63-71(2013).
CC   -!- FUNCTION: Toxin that belongs to the bicyclic heptapeptides called
CC       phallotoxins (PubMed:24050899). Although structurally related to
CC       amatoxins, phallotoxins have a different mode of action, which is the
CC       stabilization of F-actin (PubMed:24050899). Phallotoxins are poisonous
CC       when administered parenterally, but not orally because of poor
CC       absorption (PubMed:24050899). {ECO:0000305|PubMed:24050899}.
CC   -!- TISSUE SPECIFICITY: Expressed in basidiocarps (PubMed:24050899).
CC       {ECO:0000269|PubMed:24050899}.
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}.
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DR   EMBL; KF387478; AGW83702.1; -; mRNA.
DR   EMBL; KF387488; AGW83712.1; -; mRNA.
DR   EMBL; KF793337; AIS72234.1; -; mRNA.
DR   AlphaFoldDB; U5L397; -.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR027582; Amanitin/phalloidin.
DR   TIGRFAMs; TIGR04309; amanitin; 1.
PE   2: Evidence at transcript level;
KW   Thioether bond; Toxin.
FT   PROPEP          1..10
FT                   /evidence="ECO:0000305|PubMed:24050899"
FT                   /id="PRO_0000443737"
FT   PEPTIDE         11..17
FT                   /note="Phallacidin"
FT                   /evidence="ECO:0000305|PubMed:24050899"
FT                   /id="PRO_0000443738"
FT   PROPEP          18..34
FT                   /evidence="ECO:0000305|PubMed:24050899"
FT                   /id="PRO_0000443739"
FT   CROSSLNK        11..17
FT                   /note="Cyclopeptide (Ala-Pro)"
FT                   /evidence="ECO:0000305|PubMed:24050899"
FT   CROSSLNK        12..16
FT                   /note="2'-cysteinyl-6'-hydroxytryptophan sulfoxide (Trp-
FT                   Cys)"
FT                   /evidence="ECO:0000250|UniProtKB:P85421"
SQ   SEQUENCE   34 AA;  3734 MW;  6576CEEE0E21CE58 CRC64;
     MSDINATRLP AWLVDCPCVG DDVNRLLTRG ESLC