ID   RXLAA_PHYIT             Reviewed;         154 AA.
AC   P0CU89; D0NSE5;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2019, sequence version 1.
DT   03-AUG-2022, entry version 10.
DE   RecName: Full=Secreted RxLR effector protein PITG_15718 {ECO:0000303|PubMed:31234322};
DE   Flags: Precursor;
GN   ORFNames=PITG_15718;
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], AND INDUCTION.
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, AND FUNCTION.
RX   PubMed=31234322; DOI=10.3390/ijms20123031;
RA   Wang J., Gao C., Li L., Cao W., Dong R., Ding X., Zhu C., Chu Z.;
RT   "Transgenic RXLR effector PITG_15718.2 suppresses immunity and reduces
RT   vegetative growth in potato.";
RL   Int. J. Mol. Sci. 20:0-0(2019).
CC   -!- FUNCTION: Secreted effector that is involved in host plant infection
CC       (PubMed:31234322). Increases the susceptibility to P.infestans and
CC       reduces the plant growth (PubMed:31234322). Affects the expression of
CC       host genes (PubMed:31234322). PITG_15718-induced genes such as abscisic
CC       acid 8'-hydroxylase, a homolog of a salicylic acid-binding protein or a
CC       cysteine protease inhibitor gene, may negatively regulate the plant
CC       immunity or vegetative growth (PubMed:31234322). The down-regulated
CC       genes include cytochrome P450 monooxygenases essential for
CC       lignification and defense against predators and pathogens, and a member
CC       of YUCCA gene family, which is an important regulator of the
CC       phytohormone indole-3-acetic acid (IAA) biosynthesis (PubMed:31234322).
CC       Reduction of the content of IAA particularly results in the suppression
CC       of the plant immunity and reduced growth (PubMed:31234322).
CC       {ECO:0000269|PubMed:31234322}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31234322}. Host cell
CC       {ECO:0000269|PubMed:31234322}.
CC   -!- INDUCTION: Expression is up-regulated during the infection stage of
CC       P.infestans with an increase to over 1900-fold when the sporangium and
CC       zoospore attach to plant tissue (PubMed:31234322). High expression
CC       levels are then maintained throughout the infection phase
CC       (PubMed:31234322). {ECO:0000269|PubMed:31234322}.
CC   -!- DOMAIN: The RxLR-dEER motif acts to carry the protein into the host
CC       cell cytoplasm through binding to cell surface phosphatidylinositol-3-
CC       phosphate. {ECO:0000305|PubMed:31234322}.
CC   -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR   EMBL; DS028157; EEY64490.1; -; Genomic_DNA.
DR   RefSeq; XP_002897993.1; XM_002897947.1.
DR   RefSeq; XP_002996886.1; XM_002996840.1.
DR   AlphaFoldDB; P0CU89; -.
DR   EnsemblProtists; PITG_15718T0; PITG_15718T0; PITG_15718.
DR   EnsemblProtists; PITG_21681T0; PITG_21681T0; PITG_21681.
DR   GeneID; 9473566; -.
DR   GeneID; 9475463; -.
DR   KEGG; pif:PITG_15718; -.
DR   KEGG; pif:PITG_21681; -.
DR   VEuPathDB; FungiDB:PITG_15718; -.
DR   VEuPathDB; FungiDB:PITG_21681; -.
DR   Proteomes; UP000006643; Partially assembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0043657; C:host cell; IEA:UniProtKB-SubCell.
DR   InterPro; IPR031825; RXLR.
DR   Pfam; PF16810; RXLR; 1.
PE   2: Evidence at transcript level;
KW   Reference proteome; Secreted; Signal; Virulence.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..154
FT                   /note="Secreted RxLR effector protein PITG_15718"
FT                   /id="PRO_5010111076"
FT   REGION          42..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           53..72
FT                   /note="RxLR-dEER"
FT                   /evidence="ECO:0000305|PubMed:31234322"
SQ   SEQUENCE   154 AA;  17417 MW;  5BEF043B40E6F6F8 CRC64;
     MRRYAALMVI DAVLLSTSQA LSSSHASELR SQLSAADAMF PSAERDGGIP NKRSLRRISV
     TESNDGERDE ERGFQISILT KLQKWATKMK LPKTTKNLQF RIWPKEKKDP KAVYAELKLA
     GLDPKAAKAN PEFADYLAYS KIWNHRGGRY MTRS