ID   PHAD1_AMAPH             Reviewed;          34 AA.
AC   P0CU63;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2018, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=Phalloidin proprotein {ECO:0000303|PubMed:27978833};
DE   Contains:
DE     RecName: Full=Phalloidin {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).
RN   [2]
RP   FUNCTION.
RX   PubMed=6452160; DOI=10.1021/bi00507a006;
RA   Estes J.E., Selden L.A., Gershman L.C.;
RT   "Mechanism of action of phalloidin on the polymerization of muscle actin.";
RL   Biochemistry 20:708-712(1981).
CC   -!- FUNCTION: Toxin that belongs to the bicyclic heptapeptides called
CC       phallotoxins (PubMed:27978833). Although structurally related to
CC       amatoxins, phallotoxins have a different mode of action, which is the
CC       stabilization of F-actin (PubMed:6452160). Phallotoxins are poisonous
CC       when administered parenterally, but not orally because of poor
CC       absorption (PubMed:27978833). {ECO:0000269|PubMed:6452160,
CC       ECO:0000305|PubMed:27978833}.
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   PDB; 6W17; EM; 3.90 A; M/N/O/P/Q=10-16.
DR   PDBsum; 6W17; -.
DR   AlphaFoldDB; P0CU63; -.
DR   SMR; P0CU63; -.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR027582; Amanitin/phalloidin.
DR   TIGRFAMs; TIGR04309; amanitin; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Thioether bond; Toxin.
FT   PROPEP          1..10
FT                   /evidence="ECO:0000305|PubMed:27978833"
FT                   /id="PRO_0000443789"
FT   PEPTIDE         11..17
FT                   /note="Phalloidin"
FT                   /evidence="ECO:0000305|PubMed:27978833"
FT                   /id="PRO_0000443790"
FT   PROPEP          18..34
FT                   /evidence="ECO:0000305|PubMed:27978833"
FT                   /id="PRO_0000443791"
FT   CROSSLNK        11..17
FT                   /note="Cyclopeptide (Ala-Pro)"
FT                   /evidence="ECO:0000305|PubMed:27978833"
FT   CROSSLNK        12..16
FT                   /note="2'-cysteinyl-6'-hydroxytryptophan sulfoxide (Trp-
FT                   Cys)"
FT                   /evidence="ECO:0000250|UniProtKB:P85421"
SQ   SEQUENCE   34 AA;  3547 MW;  ADEC54E2B4DD6B5A CRC64;
     MSDINTTCLP AWLATCPCTG DDVNPTLTCG ESLC