ID   ELIB_PHYCI              Reviewed;          98 AA.
AC   P15569;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Beta-elicitin cinnamomin;
OS   Phytophthora cinnamomi (Cinnamon fungus).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4785;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=2583277; DOI=10.1016/0014-5793(89)81557-1;
RA   Huet J.-C., Pernollet J.-C.;
RT   "Amino acid sequence of cinnamomin, a new member of the elicitin family,
RT   and its comparison to cryptogein and capsicein.";
RL   FEBS Lett. 257:302-306(1989).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND DISULFIDE BONDS.
RX   PubMed=12136143; DOI=10.1107/s0907444902010107;
RA   Rodrigues M.L., Archer M., Martel P., Jacquet A., Cravador A.,
RA   Carrondo M.A.;
RT   "Structure of beta-cinnamomin, a protein toxic to some plant species.";
RL   Acta Crystallogr. D 58:1314-1321(2002).
CC   -!- FUNCTION: Induces local and distal defense responses (incompatible
CC       hypersensitive reaction) in plants from the solanaceae and cruciferae
CC       families. Elicits leaf necrosis and causes the accumulation of
CC       pathogenesis-related proteins. Might interact with the lipidic
CC       molecules of the plasma membrane. Elicitins are able to load, carry,
CC       and transfer sterols between membranes.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the elicitin family. {ECO:0000305}.
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DR   PIR; S06671; S06671.
DR   PDB; 1LJP; X-ray; 1.80 A; A/B=1-98.
DR   PDB; 2A8F; X-ray; 1.35 A; A/B=1-98.
DR   PDB; 2AIB; X-ray; 1.10 A; A/B=1-98.
DR   PDBsum; 1LJP; -.
DR   PDBsum; 2A8F; -.
DR   PDBsum; 2AIB; -.
DR   AlphaFoldDB; P15569; -.
DR   SMR; P15569; -.
DR   EvolutionaryTrace; P15569; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR   GO; GO:0001907; P:killing by symbiont of host cells; IDA:PAMGO_VMD.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0034053; P:modulation by symbiont of host defense-related programmed cell death; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.239.10; -; 1.
DR   InterPro; IPR002200; Elicitin.
DR   InterPro; IPR036470; Elicitin_sf.
DR   Pfam; PF00964; Elicitin; 1.
DR   PRINTS; PR00948; ELICITIN.
DR   SMART; SM01187; Elicitin; 1.
DR   SUPFAM; SSF48647; SSF48647; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Hypersensitive response elicitation; Lipid transport; Lipid-binding;
KW   Secreted; Steroid-binding; Transport.
FT   CHAIN           1..98
FT                   /note="Beta-elicitin cinnamomin"
FT                   /id="PRO_0000185436"
FT   MOTIF           33..42
FT                   /note="Beak-like motif 1 (ligand binding)"
FT   MOTIF           72..83
FT                   /note="Beak-like motif 2 (ligand binding)"
FT   DISULFID        3..71
FT                   /evidence="ECO:0000269|PubMed:12136143"
FT   DISULFID        27..56
FT                   /evidence="ECO:0000269|PubMed:12136143"
FT   DISULFID        51..95
FT                   /evidence="ECO:0000269|PubMed:12136143"
FT   HELIX           5..15
FT                   /evidence="ECO:0007829|PDB:2AIB"
FT   HELIX           16..20
FT                   /evidence="ECO:0007829|PDB:2AIB"
FT   HELIX           22..31
FT                   /evidence="ECO:0007829|PDB:2AIB"
FT   TURN            35..37
FT                   /evidence="ECO:0007829|PDB:2AIB"
FT   HELIX           44..52
FT                   /evidence="ECO:0007829|PDB:2AIB"
FT   HELIX           54..65
FT                   /evidence="ECO:0007829|PDB:2AIB"
FT   STRAND          70..74
FT                   /evidence="ECO:0007829|PDB:2AIB"
FT   TURN            76..78
FT                   /evidence="ECO:0007829|PDB:2AIB"
FT   STRAND          81..83
FT                   /evidence="ECO:0007829|PDB:2AIB"
FT   HELIX           84..96
FT                   /evidence="ECO:0007829|PDB:2AIB"
SQ   SEQUENCE   98 AA;  10294 MW;  600DA552057CB46B CRC64;
     TACTATQQTA AYKTLVSILS ESSFSQCSKD SGYSMLTATA LPTNAQYKLM CASTACNTMI
     KKIVALNPPD CDLTVPTSGL VLDVYTYANG FSSKCASL