RD28_PHYIT
ID RD28_PHYIT Reviewed; 144 AA.
AC D0MZL5;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=RxLR effector protein PITG_03192 {ECO:0000303|PubMed:19794118};
DE Flags: Precursor;
GN Name=PexRD28 {ECO:0000303|PubMed:19794118}; ORFNames=PITG_03192;
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 INDUCTION, AND DOMAIN.
RX PubMed=17914356; DOI=10.1038/nature06203;
RA Whisson S.C., Boevink P.C., Moleleki L., Avrova A.O., Morales J.G.,
RA Gilroy E.M., Armstrong M.R., Grouffaud S., van West P., Chapman S.,
RA Hein I., Toth I.K., Pritchard L., Birch P.R.;
RT "A translocation signal for delivery of oomycete effector proteins into
RT host plant cells.";
RL Nature 450:115-118(2007).
RN [3]
RP INDUCTION.
RX PubMed=19794118; DOI=10.1105/tpc.109.068247;
RA Oh S.K., Young C., Lee M., Oliva R., Bozkurt T.O., Cano L.M., Win J.,
RA Bos J.I., Liu H.Y., van Damme M., Morgan W., Choi D., Van der Vossen E.A.,
RA Vleeshouwers V.G., Kamoun S.;
RT "In planta expression screens of Phytophthora infestans RXLR effectors
RT reveal diverse phenotypes, including activation of the Solanum
RT bulbocastanum disease resistance protein Rpi-blb2.";
RL Plant Cell 21:2928-2947(2009).
RN [4]
RP FUNCTION, INTERACTION WITH HOST NTP1 AND NTP2, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=24130484; DOI=10.1371/journal.ppat.1003670;
RA McLellan H., Boevink P.C., Armstrong M.R., Pritchard L., Gomez S.,
RA Morales J., Whisson S.C., Beynon J.L., Birch P.R.;
RT "An RxLR effector from Phytophthora infestans prevents re-localisation of
RT two plant NAC transcription factors from the endoplasmic reticulum to the
RT nucleus.";
RL PLoS Pathog. 9:E1003670-E1003670(2013).
RN [5]
RP INDUCTION.
RX PubMed=28228125; DOI=10.1186/s12864-017-3585-x;
RA Ah-Fong A.M., Kim K.S., Judelson H.S.;
RT "RNA-seq of life stages of the oomycete Phytophthora infestans reveals
RT dynamic changes in metabolic, signal transduction, and pathogenesis genes
RT and a major role for calcium signaling in development.";
RL BMC Genomics 18:198-198(2017).
RN [6]
RP INDUCTION.
RX PubMed=29312401; DOI=10.3389/fpls.2017.02155;
RA Yin J., Gu B., Huang G., Tian Y., Quan J., Lindqvist-Kreuze H., Shan W.;
RT "Conserved RXLR effector genes of Phytophthora infestans expressed at the
RT early stage of potato infection are suppressive to host defense.";
RL Front. Plant Sci. 8:2155-2155(2017).
CC -!- FUNCTION: Effector that is required for full virulence
CC (PubMed:24130484). Targets host NTP1 and NTP2 transcription factors and
CC prevents their pathogen-associated molecular pattern (PAMP)-triggered
CC re-localization from the endoplasmic reticulum into the nucleus, where
CC they contribute to prevent disease progression by P.infestans
CC (PubMed:24130484). {ECO:0000269|PubMed:24130484}.
CC -!- SUBUNIT: Interacts with the C-terminal portions the ER-associated
CC potato NAC transcription factors NTP1 and NTP2.
CC {ECO:0000269|PubMed:24130484}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24130484}. Host
CC endoplasmic reticulum membrane {ECO:0000269|PubMed:24130484}; Single-
CC pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is induced during host plant infection.
CC {ECO:0000269|PubMed:17914356, ECO:0000269|PubMed:19794118,
CC ECO:0000269|PubMed:28228125, ECO:0000269|PubMed:29312401}.
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:17914356}.
CC -!- DISRUPTION PHENOTYPE: Decreases virulence on both potato and Nicitiana
CC benthamiana. {ECO:0000269|PubMed:24130484}.
CC -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR EMBL; DS028121; EEY65678.1; -; Genomic_DNA.
DR RefSeq; XP_002906277.1; XM_002906231.1.
DR AlphaFoldDB; D0MZL5; -.
DR SMR; D0MZL5; -.
DR EnsemblProtists; PITG_03192T0; PITG_03192T0; PITG_03192.
DR GeneID; 9464601; -.
DR KEGG; pif:PITG_03192; -.
DR VEuPathDB; FungiDB:PITG_03192; -.
DR eggNOG; ENOG502T20P; Eukaryota.
DR HOGENOM; CLU_1781144_0_0_1; -.
DR InParanoid; D0MZL5; -.
DR OMA; ISXDITR; -.
DR OrthoDB; 1492852at2759; -.
DR PHI-base; PHI:6301; -.
DR Proteomes; UP000006643; Partially assembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Glycoprotein; Host endoplasmic reticulum; Host membrane; Membrane;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix;
KW Virulence.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..144
FT /note="RxLR effector protein PITG_03192"
FT /id="PRO_5003011829"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 49..58
FT /note="RxLR-dEER"
FT /evidence="ECO:0000305|PubMed:17914356"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 144 AA; 16211 MW; 4B025C5786FDD2E8 CRC64;
MRVGFVFALL VVSVIVCFNG LTSAESTVVM NNRNPDSINV PISDDITSRN LRASGEERAY
AFVDKIKSLF SRPGISQKVE SLQKNPAMVK NLEKAALSQK GSSKVRDWFM HMYNNSSKRD
KFFILATLVM FPIGVWAVVT NYRR