RX106_HYAAE
ID RX106_HYAAE Reviewed; 285 AA.
AC M4C4U1; G3C9R4;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=Secreted RxLR effector protein 106 {ECO:0000303|PubMed:22072967};
DE Flags: Precursor;
GN Name=RXL106 {ECO:0000303|PubMed:22072967};
OS Hyaloperonospora arabidopsidis (strain Emoy2) (Downy mildew agent)
OS (Peronospora arabidopsidis).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Hyaloperonospora.
OX NCBI_TaxID=559515;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Emoy2;
RX PubMed=21148394; DOI=10.1126/science.1195203;
RA Baxter L., Tripathy S., Ishaque N., Boot N., Cabral A., Kemen E.,
RA Thines M., Ah-Fong A., Anderson R., Badejoko W., Bittner-Eddy P.,
RA Boore J.L., Chibucos M.C., Coates M., Dehal P., Delehaunty K., Dong S.,
RA Downton P., Dumas B., Fabro G., Fronick C., Fuerstenberg S.I., Fulton L.,
RA Gaulin E., Govers F., Hughes L., Humphray S., Jiang R.H., Judelson H.,
RA Kamoun S., Kyung K., Meijer H., Minx P., Morris P., Nelson J.,
RA Phuntumart V., Qutob D., Rehmany A., Rougon-Cardoso A., Ryden P.,
RA Torto-Alalibo T., Studholme D., Wang Y., Win J., Wood J., Clifton S.W.,
RA Rogers J., Van den Ackerveken G., Jones J.D., McDowell J.M., Beynon J.,
RA Tyler B.M.;
RT "Signatures of adaptation to obligate biotrophy in the Hyaloperonospora
RT arabidopsidis genome.";
RL Science 330:1549-1551(2010).
RN [2]
RP IDENTIFICATION.
RC STRAIN=Emoy2;
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-285, FUNCTION, AND DOMAIN.
RC STRAIN=Emoy2;
RX PubMed=22072967; DOI=10.1371/journal.ppat.1002348;
RA Fabro G., Steinbrenner J., Coates M., Ishaque N., Baxter L.,
RA Studholme D.J., Koerner E., Allen R.L., Piquerez S.J., Rougon-Cardoso A.,
RA Greenshields D., Lei R., Badel J.L., Caillaud M.C., Sohn K.H.,
RA Van den Ackerveken G., Parker J.E., Beynon J., Jones J.D.;
RT "Multiple candidate effectors from the oomycete pathogen Hyaloperonospora
RT arabidopsidis suppress host plant immunity.";
RL PLoS Pathog. 7:E1002348-E1002348(2011).
RN [4]
RP DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=25284001; DOI=10.1111/tpj.12691;
RA Wirthmueller L., Roth C., Fabro G., Caillaud M.C., Rallapalli G., Asai S.,
RA Sklenar J., Jones A.M., Wiermer M., Jones J.D., Banfield M.J.;
RT "Probing formation of cargo/importin-alpha transport complexes in plant
RT cells using a pathogen effector.";
RL Plant J. 81:40-52(2015).
RN [5]
RP FUNCTION, INTERACTION WITH HOST RDC1 AND SRO1, AND DOMAIN.
RX PubMed=30156022; DOI=10.1111/nph.15277;
RA Wirthmueller L., Asai S., Rallapalli G., Sklenar J., Fabro G., Kim D.S.,
RA Lintermann R., Jaspers P., Wrzaczek M., Kangasjaervi J., MacLean D.,
RA Menke F.L.H., Banfield M.J., Jones J.D.G.;
RT "Arabidopsis downy mildew effector HaRxL106 suppresses plant immunity by
RT binding to RADICAL-INDUCED CELL DEATH1.";
RL New Phytol. 220:232-248(2018).
CC -!- FUNCTION: Secreted effector that suppresses pathogen-associated
CC molecular pattern (PAMP)-triggered immunity (PTI) in host plants
CC (PubMed:22072967, PubMed:30156022). Binds to RCD1 and SRO1
CC transcription co-regulators to attenuate transcriptional activation of
CC salicylic acid (SA)-induced defense genes and alters plant growth
CC responses to light (PubMed:30156022). Suppresses SA signal transduction
CC but not SA levels (PubMed:30156022). {ECO:0000269|PubMed:22072967,
CC ECO:0000269|PubMed:30156022}.
CC -!- SUBUNIT: Interacts with host RCD1 and SRO1 transcription co-regulators.
CC {ECO:0000269|PubMed:30156022}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22072967}. Host
CC nucleus {ECO:0000269|PubMed:25284001}. Note=Co-opts the host cell's
CC nuclear import system via its bipartite nuclear localization signal.
CC {ECO:0000269|PubMed:25284001}.
CC -!- DOMAIN: Has the canonical translocation RxLR motif, but lacks the
CC canonical EER motif, which characterizes most oomycete effectors
CC identified so far. {ECO:0000305|PubMed:22072967}.
CC -!- DOMAIN: The C-terminal 58 amino acids (residues 228-285) are required
CC for RCD1-binding and attenuation of light and defense signaling.
CC {ECO:0000269|PubMed:30156022}.
CC -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR EMBL; JH598250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; HE574762; CCC55840.1; -; mRNA.
DR AlphaFoldDB; M4C4U1; -.
DR IntAct; M4C4U1; 1.
DR EnsemblProtists; HpaT814111; HpaP814111; HpaG814111.
DR VEuPathDB; FungiDB:HpaG814111; -.
DR HOGENOM; CLU_978105_0_0_1; -.
DR PHI-base; PHI:4258; -.
DR PHI-base; PHI:4765; -.
DR PHI-base; PHI:4857; -.
DR Proteomes; UP000011713; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Glycoprotein; Host nucleus; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..285
FT /note="Secreted RxLR effector protein 106"
FT /evidence="ECO:0000255"
FT /id="PRO_5004049395"
FT REGION 220..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 42..54
FT /note="RxLR-dEER"
FT /evidence="ECO:0000305|PubMed:22072967"
FT MOTIF 239..264
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:25284001"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 285 AA; 32073 MW; 962316CB3B3D50C3 CRC64;
MSVRYAGLLL AAVAVSAHIN EVNSIVFPGS LHIDNRNGHV QRDLRSADNG NEERNAILET
LSNHLASAFG YLWTKEAQEM TNSAWSALRN KESSLPLYSE GVAREYIETA ALNTLTAEHR
LARAEAYMVS MIVALRGVEN PESLRNSADN LQQFLINVWK TGKKQPAQVF ELLEHVPYEE
GNASLVNDSK FAIWMAYMGK TFDHQFKNWA DVQHNEQLRI EGDKEKKGGP DYVEGTESRG
KKRGQTEAPD LEPGLTPKQK RLKRMELQRV KKILLNINLM GIGRS
