EPI2B_PHYIT
ID EPI2B_PHYIT Reviewed; 125 AA.
AC D0NBV3;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Cystatin-like cysteine protease inhibitor EPIC2B {ECO:0000303|PubMed:17085509};
DE AltName: Full=Extracellular protease inhibitor with cystatin-like domain protein 2B {ECO:0000303|PubMed:17085509};
DE AltName: Full=Secreted effector EPIC2B {ECO:0000303|PubMed:17085509};
DE Flags: Precursor;
GN Name=EPIC2B {ECO:0000303|PubMed:17085509}; ORFNames=PITG_09173;
OS Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=403677;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T30-4;
RX PubMed=19741609; DOI=10.1038/nature08358;
RG The Broad Institute Genome Sequencing Platform;
RA Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA Nusbaum C.;
RT "Genome sequence and analysis of the Irish potato famine pathogen
RT Phytophthora infestans.";
RL Nature 461:393-398(2009).
RN [2]
RP INDUCTION, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HOST PIP1.
RX PubMed=17085509; DOI=10.1104/pp.106.090050;
RA Tian M., Win J., Song J., van der Hoorn R., van der Knaap E., Kamoun S.;
RT "A Phytophthora infestans cystatin-like protein targets a novel tomato
RT papain-like apoplastic protease.";
RL Plant Physiol. 143:364-377(2007).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HOST RCR3.
RX PubMed=19171904; DOI=10.1073/pnas.0809201106;
RA Song J., Win J., Tian M., Schornack S., Kaschani F., Ilyas M.,
RA van der Hoorn R.A., Kamoun S.;
RT "Apoplastic effectors secreted by two unrelated eukaryotic plant pathogens
RT target the tomato defense protease Rcr3.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1654-1659(2009).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HOST C14.
RX PubMed=20940351; DOI=10.1104/pp.110.158030;
RA Kaschani F., Shabab M., Bozkurt T., Shindo T., Schornack S., Gu C.,
RA Ilyas M., Win J., Kamoun S., van der Hoorn R.A.;
RT "An effector-targeted protease contributes to defense against Phytophthora
RT infestans and is under diversifying selection in natural hosts.";
RL Plant Physiol. 154:1794-1804(2010).
CC -!- FUNCTION: Secreted effector that interacts with and inhibits the
CC pathogenesis-related papain-like cysteine proteases C14, PIP1 and RCR3
CC of host plants (PubMed:17085509, PubMed:19171904, PubMed:20940351).
CC Inhibition of host proteases by a pathogen extracellular protease
CC inhibitor forms a specific type of defense-counterdefense mechanism
CC between plants and microbial pathogens (PubMed:17085509,
CC PubMed:19171904, PubMed:20940351). {ECO:0000269|PubMed:17085509,
CC ECO:0000269|PubMed:19171904, ECO:0000269|PubMed:20940351}.
CC -!- SUBUNIT: Interacts with the host papain-like cysteine protease PIP1
CC (PubMed:17085509). Interacts with the host papain-like cysteine
CC protease RCR3 (PubMed:19171904). Interacts with the host papain-like
CC cysteine protease C14 (PubMed:20940351). {ECO:0000269|PubMed:17085509,
CC ECO:0000269|PubMed:19171904, ECO:0000269|PubMed:20940351}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17085509,
CC ECO:0000269|PubMed:19171904, ECO:0000269|PubMed:20940351}.
CC Note=Localizes to host apoplast where it targets defense proteases for
CC inhibition. {ECO:0000269|PubMed:17085509, ECO:0000269|PubMed:19171904,
CC ECO:0000269|PubMed:20940351}.
CC -!- INDUCTION: Expression is up-regulated during infection of host tomato.
CC {ECO:0000269|PubMed:17085509}.
CC -!- SIMILARITY: Belongs to the cystatin family. {ECO:0000305}.
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DR EMBL; DS028131; EEY55258.1; -; Genomic_DNA.
DR RefSeq; XP_002903482.1; XM_002903436.1.
DR AlphaFoldDB; D0NBV3; -.
DR SMR; D0NBV3; -.
DR MEROPS; I25.048; -.
DR EnsemblProtists; PITG_09173T0; PITG_09173T0; PITG_09173.
DR GeneID; 9470509; -.
DR KEGG; pif:PITG_09173; -.
DR VEuPathDB; FungiDB:PITG_09173; -.
DR eggNOG; ENOG502RGHP; Eukaryota.
DR HOGENOM; CLU_117422_0_0_1; -.
DR InParanoid; D0NBV3; -.
DR OMA; TTSAYEV; -.
DR OrthoDB; 1565344at2759; -.
DR PHI-base; PHI:6287; -.
DR Proteomes; UP000006643; Partially assembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00042; CY; 1.
DR InterPro; IPR000010; Cystatin_dom.
DR InterPro; IPR046350; Cystatin_sf.
DR SUPFAM; SSF54403; SSF54403; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Protease inhibitor; Reference proteome; Secreted; Signal;
KW Thiol protease inhibitor; Virulence.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..125
FT /note="Cystatin-like cysteine protease inhibitor EPIC2B"
FT /id="PRO_5003013178"
FT MOTIF 68..72
FT /note="Secondary area of contact"
FT /evidence="ECO:0000250|UniProtKB:P01040"
FT SITE 25
FT /note="Reactive site"
FT /evidence="ECO:0000250|UniProtKB:P01040"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 125 AA; 13610 MW; 4E870318D7082EA5 CRC64;
MSFLRPTLAL LAVTALVTTS AQLNGYSKKE VTPEDTELLQ KAQSNVSAYN SDVTSRICYL
KVDSLETQVV SGENYKFHVS GCSVNSDKEL GGCANQNCES SKYDIVIYSQ SWTNTLKVTS
ITPAN
