ID   EPI2B_PHYIN             Reviewed;         125 AA.
AC   A1L017;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-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};
OS   Phytophthora infestans (Potato late blight agent) (Botrytis infestans).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, FUNCTION, SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH HOST PIP1.
RC   STRAIN=90128;
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   [2]
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   [3]
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; AY935252; AAY21183.1; -; mRNA.
DR   AlphaFoldDB; A1L017; -.
DR   SMR; A1L017; -.
DR   DIP; DIP-48695N; -.
DR   IntAct; A1L017; 1.
DR   MEROPS; I25.048; -.
DR   VEuPathDB; FungiDB:PITG_09173; -.
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; 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_5002635676"
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;  13596 MW;  49677AFF4971CEDB CRC64;
     MSFLRPTLAL LAVTALVTTS GQLNGYSKKE VTPEDTELLQ KAQSNVSAYN SDVTSRICYL
     KVDSLETQVV SGENYKFHVS GCSVNSDKEL GGCANQNCES SKYDIVIYSQ SWTNTLKVTS
     ITPAN