PSR2_PHYSP
ID PSR2_PHYSP Reviewed; 670 AA.
AC G5ADB3;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=RxLR effector protein PSR2 {ECO:0000303|PubMed:21653195};
DE AltName: Full=Avirulence homolog protein 146 {ECO:0000303|PubMed:21653195};
DE AltName: Full=Suppressor of RNA silencing protein 2 {ECO:0000303|PubMed:23377181};
DE Flags: Precursor;
GN Name=PSR2 {ECO:0000303|PubMed:23377181};
GN Synonyms=Avh146 {ECO:0000303|PubMed:21653195}; ORFNames=PHYSODRAFT_289089;
OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS (Phytophthora megasperma f. sp. glycines).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1094619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6497;
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H.Y., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M.B., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.-K.,
RA McDonald W.H., Medina M., Meijer H.J.G., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K.C., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W.S., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
RN [2]
RP IDENTIFICATION, AND DOMAIN.
RX PubMed=21653195; DOI=10.1105/tpc.111.086082;
RA Wang Q., Han C., Ferreira A.O., Yu X., Ye W., Tripathy S., Kale S.D.,
RA Gu B., Sheng Y., Sui Y., Wang X., Zhang Z., Cheng B., Dong S., Shan W.,
RA Zheng X., Dou D., Tyler B.M., Wang Y.;
RT "Transcriptional programming and functional interactions within the
RT Phytophthora sojae RXLR effector repertoire.";
RL Plant Cell 23:2064-2086(2011).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23377181; DOI=10.1038/ng.2525;
RA Qiao Y., Liu L., Xiong Q., Flores C., Wong J., Shi J., Wang X., Liu X.,
RA Xiang Q., Jiang S., Zhang F., Wang Y., Judelson H.S., Chen X., Ma W.;
RT "Oomycete pathogens encode RNA silencing suppressors.";
RL Nat. Genet. 45:330-333(2013).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=25387135; DOI=10.1094/mpmi-06-14-0190-r;
RA Xiong Q., Ye W., Choi D., Wong J., Qiao Y., Tao K., Wang Y., Ma W.;
RT "Phytophthora suppressor of RNA silencing 2 is a conserved RxLR effector
RT that promotes infection in soybean and Arabidopsis thaliana.";
RL Mol. Plant Microbe Interact. 27:1379-1389(2014).
RN [5]
RP FUNCTION, DOMAIN, AND INTERACTION WITH HOST DRB4.
RX PubMed=30595554; DOI=10.1016/j.chom.2018.11.007;
RA Hou Y., Zhai Y., Feng L., Karimi H.Z., Rutter B.D., Zeng L., Choi D.S.,
RA Zhang B., Gu W., Chen X., Ye W., Innes R.W., Zhai J., Ma W.;
RT "A Phytophthora Effector Suppresses Trans-Kingdom RNAi to Promote Disease
RT Susceptibility.";
RL Cell Host Microbe 25:153-165(2019).
CC -!- FUNCTION: Secreted effector that possesses RNA silencing suppression
CC activity by inhibiting the biogenesis of small RNAs in the host plant
CC to promote enhanced susceptibility of host to the pathogen during
CC infection (PubMed:23377181, PubMed:25387135, PubMed:30595554).
CC Interferes with secondary siRNA production by associating with host
CC dsRNA-binding protein DRB4 (PubMed:30595554). Inhibits the host
CC salicylic acid pathway during infection (PubMed:25387135).
CC {ECO:0000269|PubMed:23377181, ECO:0000269|PubMed:25387135,
CC ECO:0000269|PubMed:30595554}.
CC -!- SUBUNIT: Interacts with host dsRNA-binding protein DRB4.
CC {ECO:0000269|PubMed:30595554}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23377181}. Host cell
CC {ECO:0000305|PubMed:23377181}.
CC -!- INDUCTION: Expressed at specific infection stages in a transient manner
CC (PubMed:25387135). Is not expressed until 24 hours post-infection (hpi)
CC but quickly reaches the maximum expression level at approximately 36
CC hpi (PubMed:25387135). The abundance of transcripts exhibits a more
CC than twofold decrease at 48 hpi (PubMed:25387135).
CC {ECO:0000269|PubMed:25387135}.
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:21653195}.
CC -!- DOMAIN: The C-terminal region (residues 79 to 670) consists of seven
CC imperfect tandem repeats, including one W-Y motif (WY1) and six L-W-Y
CC motifs (LWY2 to LWY7) (By similarity). WY1 forms a 3 alpha-helix fold
CC with one hydrophobic core and each L-W-Y motif forms a highly conserved
CC fold consisting of 5 alpha-helices (By similarity). The units
CC contribute differently to the virulence since WY1, LWY2 and LWY6 are
CC important for the ability to suppress the biogenesis of small RNA in
CC host and virulence activity of the pathogen, whereas LWY3, LWY4, LWY5
CC and LWY7 are dispensable for PSR2 function (By similarity). WY1 and
CC LWY2 are sufficient for association with DRB4, suppress gene silencing
CC and promote infection (PubMed:30595554). These units may function as
CC basic building blocks of Phytophthora effectors to enable virulence
CC activity and accelerate the evolution of novel functions (By
CC similarity). {ECO:0000250|UniProtKB:E0W4V5,
CC ECO:0000269|PubMed:30595554}.
CC -!- DISRUPTION PHENOTYPE: Exhibits significantly decreased virulence when
CC infecting soybean seedlings. {ECO:0000269|PubMed:23377181}.
CC -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH159164; EGZ06166.1; -; Genomic_DNA.
DR RefSeq; XP_009538063.1; XM_009539768.1.
DR AlphaFoldDB; G5ADB3; -.
DR SMR; G5ADB3; -.
DR EnsemblProtists; EGZ06166; EGZ06166; PHYSODRAFT_289089.
DR GeneID; 20640800; -.
DR KEGG; psoj:PHYSODRAFT_289089; -.
DR InParanoid; G5ADB3; -.
DR OMA; TLYMKTD; -.
DR PHI-base; PHI:3353; -.
DR Proteomes; UP000002640; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043657; C:host cell; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Glycoprotein; Reference proteome; Repeat; Secreted; Signal; Virulence.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..670
FT /note="RxLR effector protein PSR2"
FT /id="PRO_5003473269"
FT REPEAT 79..126
FT /note="WY1"
FT /evidence="ECO:0000250|UniProtKB:E0W4V5"
FT REPEAT 127..217
FT /note="LWY2"
FT /evidence="ECO:0000250|UniProtKB:E0W4V5"
FT REPEAT 218..308
FT /note="LWY3"
FT /evidence="ECO:0000250|UniProtKB:E0W4V5"
FT REPEAT 309..399
FT /note="LWY4"
FT /evidence="ECO:0000250|UniProtKB:E0W4V5"
FT REPEAT 400..492
FT /note="LWY5"
FT /evidence="ECO:0000250|UniProtKB:E0W4V5"
FT REPEAT 493..583
FT /note="LWY6"
FT /evidence="ECO:0000250|UniProtKB:E0W4V5"
FT REPEAT 584..670
FT /note="LWY7"
FT /evidence="ECO:0000250|UniProtKB:E0W4V5"
FT REGION 79..670
FT /note="7 X 93 AA tandem repeats"
FT /evidence="ECO:0000250|UniProtKB:E0W4V5"
FT MOTIF 39..54
FT /note="RxLR-dEER"
FT /evidence="ECO:0000305|PubMed:21653195"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 670 AA; 74613 MW; 44212A36D69674C0 CRC64;
MRLQCVVLFA ALTLVAATHA PPNVKTVLSA EQHDIPVKRL LRPGNPAGKE DEERGINFSS
VPGFEKLANL LKPKPGLKKL LKWADAKKPP ETVFTRLRLD KTGTQLFDNT DFPVWAAYTR
SVAQTDSEAS AVMLKTLVSR YSDEVLSGMI AAAKKSSKTE SIATKLETEQ MRTWLAAKKT
PDDMFLVFKL NKAGDDILSS PLLSAWTNYM KLSNKENPKA QTTLIATMTK HYGDSGVSQI
LAAARKSPAT QSTAKRLEAE QVQLWLKKGR TPDDTFTLLS LDRAGDDLLA SPQFNTWMKY
INYYNKENPD EKTTVLAKLM THFDDEELTP ILVVARKVPS TESTAAKLQA EQFKNWLSAD
KSPEEAFTLL QLDKAGDDLL TNPQLTNWLK YTENFNLNKE INEQVTAIQV FRAQYVDDSR
IANMVIAAEK VPNTQAIAKR VEDELFKGWT VVLNKPDDVF INLKLETVGE NVFESPLWSF
YTKFLEKYNT ANPGKEQTMI SGLARGYNDV TLTNMLLKAK EAPSTKTLAT KLEDELVQYW
LADKKLPDKL FGYLELKESV DGILTNPVFN VWLKYLNAFN DKAPVKKALM IDTLKSAFGD
VAVSNMLFAA KKDPGTAKVA ATLQTALLSK WVLEKKTPGQ VSAILKEGAG ADVSAKLLAT
YSAKFKVRWG
