ID   EPI1_PHYIN              Reviewed;         149 AA.
AC   Q6PQH2;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Extracellular protease inhibitor 1 {ECO:0000303|PubMed:15096512};
DE   AltName: Full=Secreted effector EPI1 {ECO:0000303|PubMed:15096512};
DE   Flags: Precursor;
GN   Name=EPI1 {ECO:0000303|PubMed:15096512};
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], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP   WITH HOST P69B, AND INDUCTION.
RC   STRAIN=90128;
RX   PubMed=15096512; DOI=10.1074/jbc.m400941200;
RA   Tian M., Huitema E., Da Cunha L., Torto-Alalibo T., Kamoun S.;
RT   "A Kazal-like extracellular serine protease inhibitor from Phytophthora
RT   infestans targets the tomato pathogenesis-related protease P69B.";
RL   J. Biol. Chem. 279:26370-26377(2004).
CC   -!- FUNCTION: Secreted effector that interacts with and inhibits the
CC       pathogenesis-related P69B subtilisin-like serine protease of host
CC       tomato (PubMed:15096512). Inhibition of host proteases by a pathogen
CC       extracellular protease inhibitor forms a specific type of defense-
CC       counterdefense mechanism between plants and microbial pathogens
CC       (PubMed:15096512). {ECO:0000269|PubMed:15096512}.
CC   -!- SUBUNIT: Interacts with host subtilisin-like protease P69B.
CC       {ECO:0000269|PubMed:15096512}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:15096512}.
CC       Note=Localizes to host apoplast where it targets defense proteases for
CC       inhibition. {ECO:0000269|PubMed:15096512}.
CC   -!- INDUCTION: Expressed during host infection with the highest mRNA levels
CC       3 days post-inoculation (PubMed:15096512). EPI1 and its host target
CC       P69B are concurrently expressed during infection of tomato by
CC       P.infestans (PubMed:15096512). {ECO:0000269|PubMed:15096512}.
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DR   EMBL; AY586273; AAT00500.1; -; mRNA.
DR   AlphaFoldDB; Q6PQH2; -.
DR   MEROPS; I01.040; -.
DR   VEuPathDB; FungiDB:PITG_22681; -.
DR   OMA; RAKCHNE; -.
DR   PHI-base; PHI:4251; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   Pfam; PF07648; Kazal_2; 2.
DR   SMART; SM00280; KAZAL; 2.
DR   SUPFAM; SSF100895; SSF100895; 2.
DR   PROSITE; PS51465; KAZAL_2; 2.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Protease inhibitor; Repeat; Secreted;
KW   Serine protease inhibitor; Signal; Virulence.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..149
FT                   /note="Extracellular protease inhibitor 1"
FT                   /id="PRO_5004278549"
FT   DOMAIN          29..86
FT                   /note="Kazal-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DOMAIN          88..141
FT                   /note="Kazal-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   SITE            41..42
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   SITE            100..101
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        35..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        39..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        94..124
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        98..117
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        106..139
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ   SEQUENCE   149 AA;  16097 MW;  27AD694A4497F188 CRC64;
     MKSALLFTLV VAAVHAQSPQ VISPAPRRES NEIDCPEYCL DVYDPVGDGE GNTYSNECYM
     KRAKCHNETT PPAWKDLVLI TGSSTGEQPP SKKCSTVCPD VELPVCGSNR VRYGNPCELR
     IAACEHPELN IVEDSGKACV GSKVTPQEG