ELIA_PHYSY
ID ELIA_PHYSY Reviewed; 98 AA.
AC P85436;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Alpha-elicitin syringicin;
OS Phytophthora syringae (Fruit rot disease fungus).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=67594;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RX PubMed=11551548; DOI=10.1016/s0031-9422(01)00201-1;
RA Capasso R., Cristinzio G., Di Maro A., Ferranti P., Parente A.;
RT "Syringicin, a new alpha-elicitin from an isolate of Phytophthora syringae,
RT pathogenic to citrus fruit.";
RL Phytochemistry 58:257-262(2001).
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:11551548,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11551548}.
CC -!- MASS SPECTROMETRY: Mass=10194.6; Mass_error=0.2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11551548};
CC -!- SIMILARITY: Belongs to the elicitin family. {ECO:0000255}.
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 AlphaFoldDB; P85436; -.
DR SMR; P85436; -.
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 syringicin"
FT /id="PRO_0000320155"
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