RD24_PHYIT
ID RD24_PHYIT Reviewed; 154 AA.
AC D0N0Z8;
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 PexRD24 {ECO:0000303|PubMed:28758684};
DE Flags: Precursor;
GN Name=PexRD24 {ECO:0000303|PubMed:19794118}; ORFNames=PITG_04314;
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 IDENTIFICATION, DOMAIN, AND 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 [3]
RP INDUCTION.
RX PubMed=23055926; DOI=10.1371/journal.ppat.1002940;
RA Cooke D.E., Cano L.M., Raffaele S., Bain R.A., Cooke L.R.,
RA Etherington G.J., Deahl K.L., Farrer R.A., Gilroy E.M., Goss E.M.,
RA Gruenwald N.J., Hein I., MacLean D., McNicol J.W., Randall E., Oliva R.F.,
RA Pel M.A., Shaw D.S., Squires J.N., Taylor M.C., Vleeshouwers V.G.,
RA Birch P.R., Lees A.K., Kamoun S.;
RT "Genome analyses of an aggressive and invasive lineage of the Irish potato
RT famine pathogen.";
RL PLoS Pathog. 8:E1002940-E1002940(2012).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PP1C-1; PP1C-2 AND PP1C-3,
RP DOMAIN, AND MUTAGENESIS OF 138-LYS--PHE-141.
RX PubMed=26822079; DOI=10.1038/ncomms10311;
RA Boevink P.C., Wang X., McLellan H., He Q., Naqvi S., Armstrong M.R.,
RA Zhang W., Hein I., Gilroy E.M., Tian Z., Birch P.R.;
RT "A Phytophthora infestans RXLR effector targets plant PP1c isoforms that
RT promote late blight disease.";
RL Nat. Commun. 7:10311-10311(2016).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=28758684; DOI=10.1111/nph.14696;
RA Wang S., Boevink P.C., Welsh L., Zhang R., Whisson S.C., Birch P.R.J.;
RT "Delivery of cytoplasmic and apoplastic effectors from Phytophthora
RT infestans haustoria by distinct secretion pathways.";
RL New Phytol. 216:205-215(2017).
CC -!- FUNCTION: Effector that interacts with isoforms of host protein
CC phosphatase type 1c (PP1c), mimicking a regulatory subunit and causing
CC their re-localization within the host nucleus (PubMed:26822079). The
CC holoenzymes formed with PP1c isoforms act to promote late blight by
CC attenuating jasmonic acid (JA)- and salicylic acid (SA)-mediated
CC transcriptional responses of the host plant (PubMed:26822079).
CC {ECO:0000269|PubMed:26822079}.
CC -!- SUBUNIT: Interacts with the potato PP1c family proteins PP1c-1, PP1c-2
CC and PP1c-3. {ECO:0000269|PubMed:26822079}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26822079,
CC ECO:0000269|PubMed:28758684}. Host nucleus, host nucleoplasm
CC {ECO:0000269|PubMed:26822079, ECO:0000269|PubMed:28758684}. Host
CC nucleus, host nucleolus {ECO:0000269|PubMed:26822079,
CC ECO:0000269|PubMed:28758684}.
CC -!- INDUCTION: Expression is up-regulated during the biotrophic phase of
CC infection on potato plants. {ECO:0000269|PubMed:19741609,
CC ECO:0000269|PubMed:19794118, ECO:0000269|PubMed:23055926}.
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:19794118}.
CC -!- DOMAIN: The KVTF motif (residues 138 to 141) is required for the
CC interaction with the PP1c family proteins PP1c-1, PP1c-2 and PP1c-3.
CC {ECO:0000269|PubMed:26822079}.
CC -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR EMBL; DS028122; EEY67311.1; -; Genomic_DNA.
DR RefSeq; XP_002905959.1; XM_002905913.1.
DR AlphaFoldDB; D0N0Z8; -.
DR SMR; D0N0Z8; -.
DR EnsemblProtists; PITG_04314T0; PITG_04314T0; PITG_04314.
DR GeneID; 9479996; -.
DR KEGG; pif:PITG_04314; -.
DR VEuPathDB; FungiDB:PITG_04314; -.
DR eggNOG; ENOG502RGV3; Eukaryota.
DR HOGENOM; CLU_1707734_0_0_1; -.
DR InParanoid; D0N0Z8; -.
DR OMA; HTTENSF; -.
DR OrthoDB; 1859445at2759; -.
DR Proteomes; UP000006643; Partially assembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0044095; C:host cell nucleoplasm; IEA:UniProtKB-SubCell.
DR InterPro; IPR031825; RXLR.
DR Pfam; PF16810; RXLR; 1.
PE 1: Evidence at protein level;
KW Host nucleus; Reference proteome; Secreted; Signal; Virulence.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..154
FT /note="RxLR effector protein PexRD24"
FT /id="PRO_5003012822"
FT MOTIF 53..67
FT /note="RxLR-dEER"
FT /evidence="ECO:0000305|PubMed:19794118"
FT MOTIF 138
FT /note="PP1c-binding motif"
FT MUTAGEN 138..141
FT /note="KVTF->AAAA: Abolishes the interaction with PP1c-1,
FT PP1c-2 and PP1c-3, and attenuates infection."
FT /evidence="ECO:0000269|PubMed:26822079"
SQ SEQUENCE 154 AA; 17382 MW; 20568799F5B50405 CRC64;
MHSSLLWLGA VVALLAVNNV TAVSTEANGQ VALSTSKGQL AGERAEEENS IVRSLRAVET
SEDEEERDLL GLFAKSKLKK MMKSESFKLK RFGEWDDFTV GYIREKLKNK YPDLLLNYLN
VYKKAGNEIV RHANNPNKVT FSNKVRARIY KTNS
