ID   CYAE_AMAPH              Reviewed;          34 AA.
AC   P0CU61;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2018, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Cycloamanide E proprotein {ECO:0000303|PubMed:27978833};
DE   Contains:
DE     RecName: Full=Cycloamanide E {ECO:0000303|PubMed:27978833};
DE   Flags: Precursor;
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 [LARGE SCALE GENOMIC DNA], AND FUNCTION.
RX   PubMed=27978833; DOI=10.1186/s12864-016-3378-7;
RA   Pulman J.A., Childs K.L., Sgambelluri R.M., Walton J.D.;
RT   "Expansion and diversification of the MSDIN family of cyclic peptide genes
RT   in the poisonous agarics Amanita phalloides and A. bisporigera.";
RL   BMC Genomics 17:1038-1038(2016).
CC   -!- FUNCTION: Cyclic heptapeptide that belongs to the MSDIN-like toxin
CC       family responsible for a large number of food poisoning cases and
CC       deaths (PubMed:27978833). Cycloaminide E is structurally related to
CC       other cycloamanides that are non-toxic to mammals but show
CC       immunosuppressive activity (PubMed:27978833).
CC       {ECO:0000305|PubMed:27978833}.
CC   -!- PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a
CC       cyclic decapeptide (By similarity). POPB first removes 10 residues from
CC       the N-terminus (By similarity). Conformational trapping of the
CC       remaining peptide forces the enzyme to release this intermediate rather
CC       than proceed to macrocyclization (By similarity). The enzyme rebinds
CC       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   AlphaFoldDB; P0CU61; -.
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:27978833"
FT                   /id="PRO_0000443783"
FT   PEPTIDE         11..17
FT                   /note="Cycloamanide E"
FT                   /evidence="ECO:0000305|PubMed:27978833"
FT                   /id="PRO_0000443784"
FT   PROPEP          18..34
FT                   /evidence="ECO:0000305|PubMed:27978833"
FT                   /id="PRO_0000443785"
FT   CROSSLNK        11..17
FT                   /note="Cyclopeptide (Ser-Pro)"
FT                   /evidence="ECO:0000305|PubMed:27978833"
SQ   SEQUENCE   34 AA;  3775 MW;  D57E7F1E8B1EAE16 CRC64;
     MSDINAARLP SFFFPVPCIS DDIEMVLTRG ESLC