RD2_PHYIT
ID RD2_PHYIT Reviewed; 121 AA.
AC D0NIN5;
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 PexRD2 {ECO:0000303|PubMed:19794118};
DE Flags: Precursor;
GN Name=PexRD2 {ECO:0000303|PubMed:19794118}; ORFNames=PITG_11383;
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, SUBCELLULAR LOCATION, INTERACTION WITH MAPKKK EPSILON, DOMAIN,
RP MUTAGENESIS OF 85-LYS--GLU-101; LEU-109 AND LEU-112, AND SUBUNIT.
RX PubMed=24632534; DOI=10.1105/tpc.113.120055;
RA King S.R., McLellan H., Boevink P.C., Armstrong M.R., Bukharova T.,
RA Sukarta O., Win J., Kamoun S., Birch P.R., Banfield M.J.;
RT "Phytophthora infestans RXLR effector PexRD2 interacts with host MAPKKK
RT epsilon to suppress plant immune signaling.";
RL Plant Cell 26:1345-1359(2014).
RN [5]
RP FUNCTION.
RX PubMed=28386988; DOI=10.1111/nph.14542;
RA Franco-Orozco B., Berepiki A., Ruiz O., Gamble L., Griffe L.L., Wang S.,
RA Birch P.R.J., Kanyuka K., Avrova A.;
RT "A new proteinaceous pathogen-associated molecular pattern (PAMP)
RT identified in Ascomycete fungi induces cell death in Solanaceae.";
RL New Phytol. 214:1657-1672(2017).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=30329083; DOI=10.1093/jxb/ery360;
RA Wang S., McLellan H., Bukharova T., He Q., Murphy F., Shi J., Sun S.,
RA van Weymers P., Ren Y., Thilliez G., Wang H., Chen X., Engelhardt S.,
RA Vleeshouwers V., Gilroy E.M., Whisson S.C., Hein I., Wang X., Tian Z.,
RA Birch P.R.J., Boevink P.C.;
RT "Phytophthora infestans RXLR effectors act in concert at diverse
RT subcellular locations to enhance host colonization.";
RL J. Exp. Bot. 70:343-356(2019).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 57-121, SUBUNIT, AND DOMAIN.
RX PubMed=21813644; DOI=10.1074/jbc.m111.262303;
RA Boutemy L.S., King S.R., Win J., Hughes R.K., Clarke T.A.,
RA Blumenschein T.M., Kamoun S., Banfield M.J.;
RT "Structures of Phytophthora RXLR effector proteins: a conserved but
RT adaptable fold underpins functional diversity.";
RL J. Biol. Chem. 286:35834-35842(2011).
CC -!- FUNCTION: Effector that enhances P.infestans colonization of Nicotiana
CC benthamiana leaves (PubMed:24632534, PubMed:30329083). Induces a weak
CC Cell death response in N. benthamiana. PexRD2-induced cell death is
CC dependent on SGT1, suggesting that PexRD2 is recognized by the plant
CC immune system (PubMed:19794118). Interacts with the kinase domain of
CC the host MAPKKK epsilon, a positive regulator of cell death associated
CC with plant immunity, and perturbs signaling pathways triggered by
CC MAPKKK epsilon (PubMed:24632534, PubMed:28386988).
CC {ECO:0000269|PubMed:19794118, ECO:0000269|PubMed:24632534,
CC ECO:0000269|PubMed:28386988, ECO:0000269|PubMed:30329083}.
CC -!- SUBUNIT: Homodimer (PubMed:24632534, PubMed:21813644). Interacts with
CC host MAPKKK epsilon (via its kinase domain) (PubMed:24632534).
CC {ECO:0000269|PubMed:21813644, ECO:0000269|PubMed:24632534}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30329083}. Host
CC cytoplasm {ECO:0000269|PubMed:19794118, ECO:0000269|PubMed:30329083}.
CC Host nucleus {ECO:0000269|PubMed:30329083}.
CC -!- INDUCTION: Expression is induced during host plant infection.
CC {ECO:0000269|PubMed:17914356, ECO:0000269|PubMed:19794118}.
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 -!- DOMAIN: The WY domain contains 3 alpha-helices and is required for the
CC interaction with the host MAPKKK epsilon.
CC {ECO:0000305|PubMed:21813644}.
CC -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR EMBL; DS028140; EEY59369.1; -; Genomic_DNA.
DR RefSeq; XP_002900979.1; XM_002900933.1.
DR PDB; 3ZRG; X-ray; 1.75 A; A/B=57-121.
DR PDBsum; 3ZRG; -.
DR AlphaFoldDB; D0NIN5; -.
DR SMR; D0NIN5; -.
DR STRING; 4787.PITG_11383T0; -.
DR EnsemblProtists; PITG_11383T0; PITG_11383T0; PITG_11383.
DR GeneID; 9473460; -.
DR KEGG; pif:PITG_11383; -.
DR VEuPathDB; FungiDB:PITG_11383; -.
DR eggNOG; ENOG502RFES; Eukaryota.
DR HOGENOM; CLU_149657_1_0_1; -.
DR OrthoDB; 1588414at2759; -.
DR Proteomes; UP000006643; Partially assembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR InterPro; IPR040691; PexRD2_WYL.
DR Pfam; PF18488; WYL_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host cytoplasm; Host nucleus; Reference proteome; Secreted;
KW Signal; Virulence.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..121
FT /note="RxLR effector protein PexRD2"
FT /id="PRO_5003012473"
FT REGION 57..121
FT /note="WY domain"
FT /evidence="ECO:0000305|PubMed:21813644"
FT MOTIF 38..56
FT /note="RxLR-dEER"
FT /evidence="ECO:0000305|PubMed:17914356"
FT MUTAGEN 85..101
FT /note="KIAAAANSARAMEKLGE->DIAHAATSAGAMQQLGQ: In PexRD2-
FT hepta; retains the ability to oligomerize but weakens the
FT interaction with MAPKKK epsilon."
FT /evidence="ECO:0000269|PubMed:24632534"
FT MUTAGEN 85..101
FT /note="KIAAAANSARAMEKLGE->DIAHAETSAGAMQQLGQ: In PexRD2-oct;
FT retains the ability to oligomerize but abolishes the
FT interaction with MAPKKK epsilon."
FT /evidence="ECO:0000269|PubMed:24632534"
FT MUTAGEN 109
FT /note="L->D: Prevents the ability to oligomerize and the
FT interaction with MAPKKK epsilon."
FT /evidence="ECO:0000269|PubMed:24632534"
FT MUTAGEN 112
FT /note="L->D: Prevents the ability to oligomerize and the
FT interaction with MAPKKK epsilon."
FT /evidence="ECO:0000269|PubMed:24632534"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:3ZRG"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:3ZRG"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:3ZRG"
FT HELIX 93..100
FT /evidence="ECO:0007829|PDB:3ZRG"
FT HELIX 103..117
FT /evidence="ECO:0007829|PDB:3ZRG"
SQ SEQUENCE 121 AA; 13235 MW; 33FE3BF2D9C5F423 CRC64;
MRLSYVIVVI ATSFLVTTEA LSTNTGVQAA NVVGPAQRLL RKHYTAAEND DDSEARALNT
EKMKTMLKAG MTVDDYAAKL KLTDKIAAAA NSARAMEKLG ETLKMKKLLR YLNYVAEHTA
V
