ID   EPI10_PHYIN             Reviewed;         224 AA.
AC   Q6PQG3;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Extracellular protease inhibitor 10 {ECO:0000303|PubMed:15096512};
DE   AltName: Full=Secreted effector EPI10 {ECO:0000303|PubMed:15096512};
DE   Flags: Precursor;
GN   Name=EPI10 {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], AND INDUCTION.
RC   STRAIN=Isolate 88069;
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).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HOST P69B, AND INDUCTION.
RX   PubMed=15980196; DOI=10.1104/pp.105.061226;
RA   Tian M., Benedetti B., Kamoun S.;
RT   "A Second Kazal-like protease inhibitor from Phytophthora infestans
RT   inhibits and interacts with the apoplastic pathogenesis-related protease
RT   P69B of tomato.";
RL   Plant Physiol. 138:1785-1793(2005).
CC   -!- FUNCTION: Secreted effector that interacts with and inhibits the
CC       pathogenesis-related P69B subtilisin-like serine protease of host
CC       tomato (PubMed:15980196). 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:15980196). {ECO:0000269|PubMed:15980196}.
CC   -!- SUBUNIT: Interacts with host subtilisin-like protease P69B.
CC       {ECO:0000269|PubMed:15980196}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15980196}.
CC       Note=Localizes to host apoplast where it targets defense proteases for
CC       inhibition. {ECO:0000269|PubMed:15980196}.
CC   -!- INDUCTION: Expressed in zoospores (PubMed:15096512). Expressed during
CC       host infection (PubMed:15980196). {ECO:0000269|PubMed:15096512,
CC       ECO:0000269|PubMed:15980196}.
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DR   EMBL; AY586282; AAT00509.1; -; mRNA.
DR   AlphaFoldDB; Q6PQG3; -.
DR   SMR; Q6PQG3; -.
DR   MEROPS; I01.965; -.
DR   VEuPathDB; FungiDB:PITG_12129; -.
DR   PHI-base; PHI:4252; -.
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; PF00050; Kazal_1; 1.
DR   Pfam; PF07648; Kazal_2; 2.
DR   SMART; SM00280; KAZAL; 3.
DR   SUPFAM; SSF100895; SSF100895; 3.
DR   PROSITE; PS51465; KAZAL_2; 3.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Protease inhibitor; Repeat; Secreted;
KW   Serine protease inhibitor; Signal; Virulence.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..224
FT                   /note="Extracellular protease inhibitor 10"
FT                   /id="PRO_5004279619"
FT   DOMAIN          23..72
FT                   /note="Kazal-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DOMAIN          90..127
FT                   /note="Kazal-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DOMAIN          156..210
FT                   /note="Kazal-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   REGION          69..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            32..33
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   SITE            102..103
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   SITE            169..170
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   CARBOHYD        25
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        199
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        26..56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        30..49
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        38..70
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        96..126
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        100..119
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        162..193
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        167..186
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        175..208
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ   SEQUENCE   224 AA;  23481 MW;  F37BD28D992DC6E9 CRC64;
     MKSAFTLSLA LVAVTATISA AADDNCSFGC LDVYKPVCGS NGETYSNSCY LRLASCKSNN
     GITEAGDGEC ASTPASSATP SPVTSSTGST SGTVGCPDMC LDVYDPVSDE NGKEYSNQCY
     MEMAKCKGTG YDDNKRSGNP GISTLDAERK LAFAPGYQGP PCGDMLCPDN YAPVCGSDGE
     TYPNECDLGI TSCNHPEQNI TMVGEGPCPS QEQQQQQQQQ QQKL