ID   RL138_PLAVT             Reviewed;         720 AA.
AC   P0CV57;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2019, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=Secreted RxLR effector protein 138 {ECO:0000303|PubMed:29706971};
DE   Flags: Precursor;
GN   Name=RXLR138 {ECO:0000303|PubMed:29706971};
OS   Plasmopara viticola (Downy mildew of grapevine) (Botrytis viticola).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Plasmopara.
OX   NCBI_TaxID=143451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DOMAIN, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=29706971; DOI=10.3389/fpls.2018.00286;
RA   Liu Y., Lan X., Song S., Yin L., Dry I.B., Qu J., Xiang J., Lu J.;
RT   "In planta functional analysis and subcellular localization of the oomycete
RT   pathogen Plasmopara viticola candidate RXLR effector repertoire.";
RL   Front. Plant Sci. 9:286-286(2018).
CC   -!- FUNCTION: Secreted effector that acts as an elicitor that induces cell
CC       death in host plant cells. {ECO:0000269|PubMed:29706971}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29706971}. Host
CC       nucleus {ECO:0000269|PubMed:29706971}. Note=Accumulates at the margin
CC       of the nucleolus, but is absent within it.
CC       {ECO:0000269|PubMed:29706971}.
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:29706971}.
CC   -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR   AlphaFoldDB; P0CV57; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Host nucleus; Secreted; Signal; Virulence.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..720
FT                   /note="Secreted RxLR effector protein 138"
FT                   /id="PRO_0000447967"
FT   REGION          264..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           56..71
FT                   /note="RxLR-dEER"
FT                   /evidence="ECO:0000305|PubMed:29706971"
FT   COMPBIAS        318..335
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        609
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   720 AA;  80663 MW;  D37161BA841AF162 CRC64;
     MRSAFYVAIV LLVAAGSQTA AKCDQDEPQH APSNNFMASF DRVDQMLPSQ VLQASRNLKD
     DFMFSAGDEE RTPLAPSKLL KKVKFPDSVI STASAMRTTE DVNAIEIASK NLNQLRSNKR
     QRIVQTPNKM AGQAVVTPPA LDIPLVSVAN EKSLKLPKRR TRKRPTAVVE NAARSVPQHD
     YHSAPQDSFK INAEAPNARL YNQLITQKAL QLEKNEHLEK NAREEELVSF DLLHLFEKSA
     HPAAGNRQEA NAIKVASKNL IQLESNTRKR NNVVGQVKRK RPNRDRSPVS VANGKPLGLA
     KRRKSNHPTA VAKNAASSVK QHDHRVAPPE PSRLDAKALD GRINNQQITQ KASQLDKNEH
     VDKRSWREEL VSVDELMHLF DEFDKSAHPT TVSRQETSAI EATSKSLIPA ESSTHKGIAL
     TSNDVVEVGV HAPPDPDKFL VLVADNMPMI LAERLKTTSP TAIMNNAARF VTQHYERLAH
     LESSTTNAEA LSGRLINQPI TQKALQLDKS QHVDDVEDIE KQFSRAVGHF WHLREVNDKS
     AHTTAVYRQT VPDDWNAEYA KGPKTLSQDG KINNDVKEVH AAFLEAFNLP FHQYPQETAI
     MLKIVQRKNK SSPNNFRTFK TFKLLAQNQM ILSHLQELLA PDLKKLLGYG NMALPITLKN
     LKEALNVKLV IMYDLFIIFC HERVDLVKDL PPKPTPSQWI FEISTLSSGN KNRQVLPPHD