ID   CASSI_CORCC             Reviewed;          27 AA.
AC   P84902;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Cassiicolin;
OS   Corynespora cassiicola (Target leaf spot disease fungus) (Helminthosporium
OS   cassiicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Corynesporascaceae; Corynespora.
OX   NCBI_TaxID=59586;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY,
RP   PYROGLUTAMATE FORMATION AT GLN-1, AND GLYCOSYLATION AT THR-2.
RC   STRAIN=CCP {ECO:0000269|PubMed:17113837};
RX   PubMed=17113837; DOI=10.1016/j.jchromb.2006.10.051;
RA   de Lamotte F., Duviau M.-P., Sanier C., Thai R., Poncet J., Bieysse D.,
RA   Breton F., Pujade-Renaud V.;
RT   "Purification and characterization of cassiicolin, the toxin produced by
RT   Corynespora cassiicola, causal agent of the leaf fall disease of rubber
RT   tree.";
RL   J. Chromatogr. B 849:357-362(2007).
RN   [2] {ECO:0000305}
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RA   Breton F., Sanier C., d'Auzac J.;
RT   "Role of cassiicolin, a host-slective toxin, in the pathogenicity of
RT   Corynespora cassiicola, causal agent of a leaf fall disease of hevea.";
RL   J. Rubber Res. 3:115-128(2000).
RN   [3] {ECO:0000305}
RP   STRUCTURE BY NMR, FUNCTION, DISULFIDE BONDS, PYROGLUTAMATE FORMATION AT
RP   GLN-1, AND GLYCOSYLATION AT THR-2.
RC   STRAIN=CCP {ECO:0000269|PubMed:17234212};
RX   PubMed=17234212; DOI=10.1016/j.jmb.2006.11.086;
RA   Barthe P., Pujade-Renaud V., Breton F., Gargani D., Thai R., Roumestand C.,
RA   de Lamotte F.;
RT   "Structural analysis of cassiicolin, a host-selective protein toxin from
RT   Corynespora cassiicola.";
RL   J. Mol. Biol. 367:89-101(2007).
CC   -!- FUNCTION: Toxin, essential for pathogenicity. Causes symptoms of
CC       Corynespora leaf fall disease (CLF) in rubber trees, including
CC       chlorosis, development of brown spots and necrosis. Alters leaf cell
CC       ultrastructure, causing plasmolysis in most cell types. In extreme
CC       cases the plasmolysis leads to disruption of the plasma membrane. Also
CC       affects chloroplast structure, causing lamellae distortion and reduced
CC       thylakoids stacking together. Causes accumulation of starch grains.
CC       Does not affect the nucleus or mitochondria. Toxic to N.tabacum,
CC       L.esculentum, S.ionantha, F.lyrata, P.violacea, S.melongena, and G.max.
CC       Not toxic to P.alba, G.hirsutum, P.acerifolia, R.pseudoacacia,
CC       T.zebrina, M.alba, and Q.ilex. {ECO:0000269|PubMed:17234212,
CC       ECO:0000269|Ref.2}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2}.
CC   -!- PTM: O-glycosylated with 3-O-methyl-O-alpha-D-mannopyranosyl.
CC       {ECO:0000269|PubMed:17113837, ECO:0000269|PubMed:17234212}.
CC   -!- MASS SPECTROMETRY: Mass=2884.96; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17113837};
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   PDB; 2HGO; NMR; -; A=2-27.
DR   PDBsum; 2HGO; -.
DR   AlphaFoldDB; P84902; -.
DR   SMR; P84902; -.
DR   iPTMnet; P84902; -.
DR   ABCD; P84902; 1 sequenced antibody.
DR   EvolutionaryTrace; P84902; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Pyrrolidone carboxylic acid; Secreted; Toxin.
FT   PEPTIDE         1..27
FT                   /note="Cassiicolin"
FT                   /evidence="ECO:0000269|PubMed:17113837"
FT                   /id="PRO_0000279697"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:17113837,
FT                   ECO:0000269|PubMed:17234212"
FT   CARBOHYD        2
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000269|PubMed:17113837,
FT                   ECO:0000269|PubMed:17234212"
FT   DISULFID        3..18
FT                   /evidence="ECO:0000269|PubMed:17234212"
FT   DISULFID        6..27
FT                   /evidence="ECO:0000269|PubMed:17234212"
FT   DISULFID        14..24
FT                   /evidence="ECO:0000269|PubMed:17234212"
FT   STRAND          7..9
FT                   /evidence="ECO:0007829|PDB:2HGO"
FT   TURN            10..12
FT                   /evidence="ECO:0007829|PDB:2HGO"
FT   STRAND          13..15
FT                   /evidence="ECO:0007829|PDB:2HGO"
FT   STRAND          17..19
FT                   /evidence="ECO:0007829|PDB:2HGO"
FT   STRAND          21..23
FT                   /evidence="ECO:0007829|PDB:2HGO"
SQ   SEQUENCE   27 AA;  2734 MW;  CEDDDA366C6E44C4 CRC64;
     QTCVSCVNFG NGFCGDNCGN SWACSGC