PSR1_PHYSP
ID PSR1_PHYSP Reviewed; 106 AA.
AC G4YRX5;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=RxLR effector protein PSR1 {ECO:0000303|PubMed:21653195};
DE AltName: Full=Avirulence homolog protein 18 {ECO:0000303|PubMed:21653195};
DE AltName: Full=Suppressor of RNA silencing protein 1 {ECO:0000303|PubMed:23377181};
DE Flags: Precursor;
GN Name=PSR1 {ECO:0000303|PubMed:23377181};
GN Synonyms=Avh18 {ECO:0000303|PubMed:21653195}; ORFNames=PHYSODRAFT_284677;
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, DOMAIN, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 56-ARG--PHE-69.
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 INTERACTION WITH HOST PINP1.
RX PubMed=25902521; DOI=10.1073/pnas.1421475112;
RA Qiao Y., Shi J., Zhai Y., Hou Y., Ma W.;
RT "Phytophthora effector targets a novel component of small RNA pathway in
RT plants to promote infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:5850-5855(2015).
RN [5]
RP DOMAIN, FUNCTION, AND MUTAGENESIS OF LYS-32; GLU-39; GLU-43; LYS-54; LYS-57
RP AND GLU-62.
RX PubMed=29029698; DOI=10.1016/j.funbio.2017.07.005;
RA Shen D., Li Q., Sun P., Zhang M., Dou D.;
RT "Intrinsic disorder is a common structural characteristic of RxLR effectors
RT in oomycete pathogens.";
RL Fungal Biol. 121:911-919(2017).
RN [6]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF TRP-72 AND TYR-100.
RX PubMed=30963588; DOI=10.1111/nph.15836;
RA Zhang P., Jia Y., Shi J., Chen C., Ye W., Wang Y., Ma W., Qiao Y.;
RT "The WY domain in the Phytophthora effector PSR1 is required for infection
RT and RNA silencing suppression activity.";
RL New Phytol. 223:839-852(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:25902521, PubMed:29029698,
CC PubMed:30963588). Interferes with secondary siRNA production by
CC associating with host nuclear protein PINP1 that acts as a regulator of
CC the accumulation of both microRNAs and endogenous small interfering
CC RNAs (PubMed:25902521). {ECO:0000269|PubMed:23377181,
CC ECO:0000269|PubMed:25902521, ECO:0000269|PubMed:29029698,
CC ECO:0000269|PubMed:30963588}.
CC -!- SUBUNIT: Interacts with host PINP1. {ECO:0000269|PubMed:25902521}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25902521}. Host
CC nucleus {ECO:0000269|PubMed:25902521}. Note=The nuclear localization is
CC required for this interaction. {ECO:0000269|PubMed:25902521}.
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 nuclear localization signal (NLS) is required for
CC localization to the host nucleus and RNA silencing suppression
CC activity. {ECO:0000269|PubMed:23377181}.
CC -!- DOMAIN: The single WY domain is required for binding to host PINP1 and
CC subsequent RNA-silencing suppression activity, pathogenicity and
CC perturbation of plant development. {ECO:0000269|PubMed:30963588}.
CC -!- DOMAIN: The disordered structure between residues 29 and 65 contributes
CC to the effector function in cell death activation.
CC {ECO:0000269|PubMed:29029698}.
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; JH159152; EGZ22952.1; -; Genomic_DNA.
DR RefSeq; XP_009518240.1; XM_009519945.1.
DR AlphaFoldDB; G4YRX5; -.
DR EnsemblProtists; EGZ22952; EGZ22952; PHYSODRAFT_284677.
DR GeneID; 20639842; -.
DR KEGG; psoj:PHYSODRAFT_284677; -.
DR Proteomes; UP000002640; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..106
FT /note="RxLR effector protein PSR1"
FT /id="PRO_5003471535"
FT REGION 29..65
FT /note="Disordered"
FT /evidence="ECO:0000305|PubMed:29029698"
FT REGION 50..106
FT /note="WY domain"
FT /evidence="ECO:0000305|PubMed:30963588"
FT MOTIF 33..46
FT /note="RxLR-dEER"
FT /evidence="ECO:0000305|PubMed:21653195"
FT MOTIF 56..69
FT /note="Bipartite nuclear localization signal (NLS)"
FT /evidence="ECO:0000269|PubMed:23377181"
FT MUTAGEN 32
FT /note="K->A: Leads to the transition from disordered
FT structure to ordered structure and abolishes the function
FT in cell death activation; when associated with A-39, A-43,
FT A-54, A-57 and A-62."
FT /evidence="ECO:0000269|PubMed:29029698"
FT MUTAGEN 39
FT /note="E->A: Leads to the transition from disordered
FT structure to ordered structure and abolishes the function
FT in cell death activation; when associated with A-32, A-43,
FT A-54, A-57 and A-62."
FT /evidence="ECO:0000269|PubMed:29029698"
FT MUTAGEN 43
FT /note="E->A: Leads to the transition from disordered
FT structure to ordered structure and abolishes the function
FT in cell death activation; when associated with A-32, A-39,
FT A-54, A-57 and A-62."
FT /evidence="ECO:0000269|PubMed:29029698"
FT MUTAGEN 54
FT /note="K->A: Leads to the transition from disordered
FT structure to ordered structure and abolishes the function
FT in cell death activation; when associated with A-32, A-39,
FT A-43, A-57 and A-62."
FT /evidence="ECO:0000269|PubMed:29029698"
FT MUTAGEN 56..69
FT /note="RKMLGDETYRLKKF->AAAAAAAAAAAAAA: Loses the nuclear
FT localization as well as the RNA silencing suppression
FT activity."
FT /evidence="ECO:0000269|PubMed:23377181"
FT MUTAGEN 57
FT /note="K->A: Leads to the transition from disordered
FT structure to ordered structure and abolishes the function
FT in cell death activation; when associated with A-32, A-39,
FT A-43, A-54 and A-62."
FT /evidence="ECO:0000269|PubMed:29029698"
FT MUTAGEN 62
FT /note="E->A: Leads to the transition from disordered
FT structure to ordered structure and abolishes the function
FT in cell death activation; when associated with A-32, A-39,
FT A-43, A-54 and A-57."
FT /evidence="ECO:0000269|PubMed:29029698"
FT MUTAGEN 72
FT /note="W->A: Abolishes the interaction with host target
FT PINP1 and lowers the size of lesions in leaves after
FT infection."
FT /evidence="ECO:0000269|PubMed:30963588"
FT MUTAGEN 100
FT /note="Y->A: Abolishes the interaction with host target
FT PINP1 and lowers the size of lesions in leaves after
FT infection."
FT /evidence="ECO:0000269|PubMed:30963588"
SQ SEQUENCE 106 AA; 12304 MW; DCDE91B059ABF2CF CRC64;
MRLTYVLLVA VTTLLVSCDA TKPSTEATAV SKRLLRFVEA ADEEERRIDF SPEKLRKMLG
DETYRLKKFG KWDSDGHTFD GLKHYLLLSD SSMVKLRNMY KAWLEQ
