ID   MSD1_AMAEX              Reviewed;          32 AA.
AC   U5L3X0;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=MSDIN-like toxin proprotein 1 {ECO:0000303|PubMed:24050899};
DE   Contains:
DE     RecName: Full=Toxin MSD1 {ECO:0000303|PubMed:24050899};
DE   Flags: Precursor;
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: Probable toxin that belongs to the MSDIN-like toxin family
CC       responsible for a large number of food poisoning cases and deaths
CC       (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 octapeptide (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 8 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; KF387480; AGW83704.1; -; mRNA.
DR   EMBL; KF387490; AGW83714.1; -; mRNA.
DR   AlphaFoldDB; U5L3X0; -.
DR   SMR; U5L3X0; -.
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   Toxin.
FT   PROPEP          1..10
FT                   /evidence="ECO:0000305|PubMed:24050899"
FT                   /id="PRO_0000443755"
FT   PEPTIDE         11..18
FT                   /note="Toxin MSD1"
FT                   /evidence="ECO:0000305|PubMed:24050899"
FT                   /id="PRO_0000443756"
FT   PROPEP          19..32
FT                   /evidence="ECO:0000305|PubMed:24050899"
FT                   /id="PRO_0000443757"
FT   CROSSLNK        11..18
FT                   /note="Cyclopeptide (Ile-Pro)"
FT                   /evidence="ECO:0000305|PubMed:24050899"
SQ   SEQUENCE   32 AA;  3751 MW;  BE0E1EA54D2FA76F CRC64;
     MSDINATRLP IFWFIYFPCV SDVDSTLTRG ER