ID   RXL62_HYAAE             Reviewed;         131 AA.
AC   M4C319; G3C9P9;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=RxLR effector protein 62 {ECO:0000303|PubMed:22072967};
DE   Flags: Precursor;
GN   Name=RxL62 {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 [MRNA] OF 22-131, AND FUNCTION.
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   [2]
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   [3]
RP   IDENTIFICATION.
RC   STRAIN=Emoy2;
RG   EnsemblProtists;
RL   Submitted (JUN-2015) to UniProtKB.
RN   [4]
RP   FUNCTION.
RX   PubMed=23734779; DOI=10.1094/mpmi-06-12-0154-r;
RA   Badel J.L., Piquerez S.J., Greenshields D., Rallapalli G., Fabro G.,
RA   Ishaque N., Jones J.D.;
RT   "In planta effector competition assays detect Hyaloperonospora
RT   arabidopsidis effectors that contribute to virulence and localize to
RT   different plant subcellular compartments.";
RL   Mol. Plant Microbe Interact. 26:745-757(2013).
RN   [5]
RP   INDUCTION, AND FUNCTION.
RX   PubMed=25329884; DOI=10.1371/journal.ppat.1004443;
RA   Asai S., Rallapalli G., Piquerez S.J., Caillaud M.C., Furzer O.J.,
RA   Ishaque N., Wirthmueller L., Fabro G., Shirasu K., Jones J.D.;
RT   "Expression profiling during arabidopsis/downy mildew interaction reveals a
RT   highly-expressed effector that attenuates responses to salicylic acid.";
RL   PLoS Pathog. 10:E1004443-E1004443(2014).
CC   -!- FUNCTION: Secreted effector that suppresses callose deposition, a
CC       hallmark of pathogen-associated molecular pattern (PAMP)-triggered
CC       immunity (PTI) and renders host plants more susceptible to bacterial
CC       infection (PubMed:22072967, PubMed:23734779). Reduces host plant
CC       responsiveness to salicylic acid (SA) in haustoriated cells into which
CC       host-translocated effectors are delivered (PubMed:25329884).
CC       {ECO:0000269|PubMed:22072967, ECO:0000269|PubMed:23734779,
CC       ECO:0000269|PubMed:25329884}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:25329884}. Host cell
CC       {ECO:0000305|PubMed:25329884}.
CC   -!- INDUCTION: Highly expressed during infection.
CC       {ECO:0000269|PubMed:25329884}.
CC   -!- DOMAIN: The RxLR-dEER motif is required for the delivery of the
CC       effector to the host cell cytoplasm but does not bind
CC       phosphatidylinositol monophosphates. {ECO:0000305|PubMed:22072967}.
CC   -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR   EMBL; HE574747; CCC55825.1; -; mRNA.
DR   EMBL; JH598148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; M4C319; -.
DR   SMR; M4C319; -.
DR   EnsemblProtists; HpaT813486; HpaP813486; HpaG813486.
DR   VEuPathDB; FungiDB:HpaG813486; -.
DR   HOGENOM; CLU_1931589_0_0_1; -.
DR   PHI-base; PHI:4770; -.
DR   PHI-base; PHI:4856; -.
DR   Proteomes; UP000011713; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0043657; C:host cell; IEA:UniProtKB-SubCell.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Reference proteome; Secreted; Signal; Virulence.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..131
FT                   /note="RxLR effector protein 62"
FT                   /id="PRO_5004049109"
FT   MOTIF           49..60
FT                   /note="RxLR-dEER"
FT                   /evidence="ECO:0000305|PubMed:22072967"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   131 AA;  15225 MW;  D6191921E1C8CDFC CRC64;
     MRLDILLFTL SSSTSLALSY SLPMDPAHSS VHTLSAADRH IGERVTRQRH LREEPANEAR
     NYSDLAVEIK RLVEELDSRV LEQADISLLD RHYAGDYKAF RSDLMTYGYQ TRFAEQYKLF
     KKLGIDFKHN Y