ID   MSD1_AMAPH              Reviewed;          32 AA.
AC   A8W7P2;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=MSDIN-like toxin proprotein a {ECO:0000303|PubMed:18025465};
DE   Contains:
DE     RecName: Full=Toxin MSD1 {ECO:0000305|PubMed:18025465};
DE     AltName: Full=Toxin MSDa {ECO:0000303|PubMed:18025465};
DE   Flags: Precursor; Fragment;
GN   Name=MSDa {ECO:0000303|PubMed:18025465};
OS   Amanita phalloides (Death cap).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Amanitaceae; Amanita.
OX   NCBI_TaxID=67723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=18025465; DOI=10.1073/pnas.0707340104;
RA   Hallen H.E., Luo H., Scott-Craig J.S., Walton J.D.;
RT   "Gene family encoding the major toxins of lethal Amanita mushrooms.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:19097-19101(2007).
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:18025465). {ECO:0000305|PubMed:18025465}.
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}.
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; EU196157; ABW87786.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8W7P2; -.
DR   SMR; A8W7P2; -.
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   Toxin.
FT   PROPEP          1..10
FT                   /evidence="ECO:0000305|PubMed:18025465"
FT                   /id="PRO_0000443671"
FT   PEPTIDE         11..18
FT                   /note="Toxin MSD1"
FT                   /evidence="ECO:0000305|PubMed:18025465"
FT                   /id="PRO_0000443672"
FT   PROPEP          19..32
FT                   /evidence="ECO:0000305|PubMed:18025465"
FT                   /id="PRO_0000443673"
FT   CROSSLNK        11..18
FT                   /note="Cyclopeptide (Ile-Pro)"
FT                   /evidence="ECO:0000305|PubMed:18025465"
FT   NON_TER         32
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   32 AA;  3421 MW;  0BF6B5B7CBD761F8 CRC64;
     MSDINATRLP IIGILLPPCI GDDVTLLLTR GE