ID   RL115_PLAVT             Reviewed;         447 AA.
AC   P0CV46;
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 115 {ECO:0000303|PubMed:29706971};
DE   Flags: Precursor;
GN   Name=RXLR115 {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 dos not suppress the host cell death
CC       induced by cell death-inducing proteins. {ECO:0000269|PubMed:29706971}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29706971}. Host
CC       nucleus {ECO:0000269|PubMed:29706971}. Host cytoplasm
CC       {ECO:0000269|PubMed:29706971}. Note=Localizes to speckle-like
CC       structures within the nucleus. {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; P0CV46; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Host cytoplasm; Host nucleus; Secreted; Signal; Virulence.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..447
FT                   /note="Secreted RxLR effector protein 115"
FT                   /id="PRO_0000447955"
FT   REGION          57..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           50..70
FT                   /note="RxLR-dEER"
FT                   /evidence="ECO:0000305|PubMed:29706971"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   447 AA;  49912 MW;  87C3E80222D02AC9 CRC64;
     MCGAHYVAIA LLVVAGSLAA AEFDQNEIQQ TSDDDVMASV NSTYELLQSR ILRERREPKD
     NLLSAGDEER TPSSPSSFLK ELKVSDSIMD AANVIRTEGG ASAIDAALKN LNQLNRKRRQ
     RIAPTSKNVA GHEVGTSSDT DKSLVSVENE TPFVLAKRRR TKRSAAMMTN AARSAKQHDY
     RLAPTESSTI PAKAPDDQLN KQPISQKALQ LDKNEHVDES LWREELMTVD EVLHLFEEFD
     KPAHPTAVNL QEPNAIETTS KKLNHLRRNK RKRKHIASTP KNVGQLVRAP PLSDKSPVLV
     AKGIPFVLAI RLKKNHPTAI MKNAAKFVTQ HDYRLTPSGP SMINAATPNS QLKFHLLGQK
     ALHLDKNEHA GDLNEESHTV EHIFHLRERN DKLAQTTAVN QQSVLKNWEA EIANGPLLLS
     RDRPDKMVKE IHAAFLETFN LPFHQYP