EPIC1_PHYIT
ID EPIC1_PHYIT Reviewed; 126 AA.
AC D0NBV1;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Cystatin-like cysteine protease inhibitor EPIC1 {ECO:0000303|PubMed:17085509};
DE AltName: Full=Extracellular protease inhibitor with cystatin-like domain protein 1 {ECO:0000303|PubMed:17085509};
DE AltName: Full=Secreted effector EPIC1 {ECO:0000303|PubMed:17085509};
DE Flags: Precursor;
GN Name=EPIC1 {ECO:0000303|PubMed:17085509}; ORFNames=PITG_09169;
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, AND SUBCELLULAR LOCATION.
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).
RN [5]
RP EPIC1-C14 COMPLEX STRUCTURE MODELING.
RX PubMed=21301220; DOI=10.4161/psb.6.1.14190;
RA Kaschani F., Van der Hoorn R.A.;
RT "A model of the C14-EPIC complex indicates hotspots for a protease-
RT inhibitor arms race in the oomycete-potato interaction.";
RL Plant Signal. Behav. 6:109-112(2011).
CC -!- FUNCTION: Secreted effector that interacts with and inhibits the
CC pathogenesis-related papain-like cysteine proteases C147 and RCR3 of
CC 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 RCR3
CC (PubMed:19171904). Interacts with the host papain-like cysteine
CC protease C14 (PubMed:20940351) (Probable).
CC {ECO:0000269|PubMed:19171904, ECO:0000269|PubMed:20940351,
CC ECO:0000305|PubMed:21301220}.
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; EEY55256.1; -; Genomic_DNA.
DR RefSeq; XP_002903480.1; XM_002903434.1.
DR AlphaFoldDB; D0NBV1; -.
DR SMR; D0NBV1; -.
DR EnsemblProtists; PITG_09169T0; PITG_09169T0; PITG_09169.
DR GeneID; 9470507; -.
DR KEGG; pif:PITG_09169; -.
DR VEuPathDB; FungiDB:PITG_09169; -.
DR eggNOG; ENOG502RGHP; Eukaryota.
DR HOGENOM; CLU_117422_0_0_1; -.
DR InParanoid; D0NBV1; -.
DR OMA; AITDAPW; -.
DR OrthoDB; 1565344at2759; -.
DR PHI-base; PHI:6286; -.
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 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..126
FT /note="Cystatin-like cysteine protease inhibitor EPIC1"
FT /id="PRO_5003013190"
FT MOTIF 69..73
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 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 126 AA; 13711 MW; D4021C6B18020532 CRC64;
MTFLRPILAL LAATALVTTS AQVDGGYSKK EVTPEDMELL QKAQSNVSAY NSDVTSRICY
LKVDSLETQV VSGENYKFHV SGCSVNSDNE LGGCANQNCE SSKYDIVIYS QSWTNTLEVT
SITPVK
