MSD7_AMAEX
ID MSD7_AMAEX Reviewed; 34 AA.
AC U5L3J7;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 1.
DT 25-MAY-2022, entry version 11.
DE RecName: Full=MSDIN-like toxin proprotein 7 {ECO:0000303|PubMed:24050899};
DE Contains:
DE RecName: Full=Toxin MSD7 {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 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}.
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; KF387484; AGW83708.1; -; mRNA.
DR AlphaFoldDB; U5L3J7; -.
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_0000443770"
FT PEPTIDE 11..17
FT /note="Toxin MSD7"
FT /evidence="ECO:0000305|PubMed:24050899"
FT /id="PRO_0000443771"
FT PROPEP 18..34
FT /evidence="ECO:0000305|PubMed:24050899"
FT /id="PRO_0000443772"
FT CROSSLNK 11..17
FT /note="Cyclopeptide (Ala-Pro)"
FT /evidence="ECO:0000305|PubMed:24050899"
SQ SEQUENCE 34 AA; 3736 MW; 6576CEEE0D972E58 CRC64;
MSDINATRLP AWLTDCPCVG DDVNRLLTRG ESLC