EPI10_PHYIT
ID EPI10_PHYIT Reviewed; 228 AA.
AC D0NJ41;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 56.
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}; ORFNames=PITG_12129;
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 IDENTIFICATION, AND INDUCTION.
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 [3]
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; DS028141; EEY59559.1; -; Genomic_DNA.
DR RefSeq; XP_002900752.1; XM_002900706.1.
DR AlphaFoldDB; D0NJ41; -.
DR SMR; D0NJ41; -.
DR STRING; 4787.PITG_12129T0; -.
DR MEROPS; I01.965; -.
DR EnsemblProtists; PITG_12129T0; PITG_12129T0; PITG_12129.
DR GeneID; 9473138; -.
DR KEGG; pif:PITG_12129; -.
DR VEuPathDB; FungiDB:PITG_12129; -.
DR eggNOG; KOG3649; Eukaryota.
DR HOGENOM; CLU_057241_1_0_1; -.
DR InParanoid; D0NJ41; -.
DR OMA; CSDYPKP; -.
DR OrthoDB; 1283825at2759; -.
DR Proteomes; UP000006643; Partially assembled WGS sequence.
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; Reference proteome;
KW Repeat; Secreted; Serine protease inhibitor; Signal; Virulence.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..228
FT /note="Extracellular protease inhibitor 10"
FT /id="PRO_5003012102"
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..208
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 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"
SQ SEQUENCE 228 AA; 23487 MW; 9D8C45CE881B110E CRC64;
MKSAFTLSLA LVAVTATISA AADDNCSFGC LDVYKPVCGS NGETYSNSCY LRLASCKSNN
GITEAGDGEC ASTPASSATP SPVTSSTGST SGTVGCPDMC LDVYDPVSDE NGKEYSNQCY
MEMAKCKGTG YDDNKRSGNP GISTLDAERK LAFAPGYQGP PCGDMLCPDN YAPVCGSDGE
TYPNECDLGI TSCNHPEQNI TMVGEGTLPV TGAATATATA TAEVVTRW
