ID   ELIA_PHYHI              Reviewed;          98 AA.
AC   P85174;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Alpha-elicitin hibernalin;
OS   Phytophthora hibernalis.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=175300;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RX   PubMed=17977856; DOI=10.1093/jb/mvm201;
RA   Capasso R., Di Maro A., Cristinzio G., De Martino A., Chambery A.,
RA   Daniele A., Sannino F., Testa A., Parente A.;
RT   "Isolation, characterization and structure-elicitor activity relationships
RT   of hibernalin and its two oxidized forms from Phytophthora hibernalis Carne
RT   1925.";
RL   J. Biochem. 143:131-141(2008).
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. {ECO:0000269|PubMed:17977856,
CC       ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17977856}.
CC   -!- MASS SPECTROMETRY: Mass=10194.9; Mass_error=0.2; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17977856};
CC   -!- MASS SPECTROMETRY: Mass=10194.82; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:17977856};
CC   -!- SIMILARITY: Belongs to the elicitin family. {ECO:0000255}.
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DR   AlphaFoldDB; P85174; -.
DR   SMR; P85174; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Direct protein sequencing; Disulfide bond;
KW   Hypersensitive response elicitation; Secreted.
FT   CHAIN           1..98
FT                   /note="Alpha-elicitin hibernalin"
FT                   /id="PRO_0000320154"
FT   DISULFID        3..71
FT                   /evidence="ECO:0000250|UniProtKB:P15571"
FT   DISULFID        27..56
FT                   /evidence="ECO:0000250|UniProtKB:P15571"
FT   DISULFID        51..95
FT                   /evidence="ECO:0000250|UniProtKB:P15571"
SQ   SEQUENCE   98 AA;  10201 MW;  E31EE3DE8B726A17 CRC64;
     TTCTTTQQTA AYVALVSILS DSSFNQCATD SGYSMLTATA LPTTAQYKLM CASTACKTMI
     TKIVSLNAPD CELTVPTSGL VLNVYSYANG FSSTCASL