ID   RLR8_PLAVT              Reviewed;         457 AA.
AC   P0CU95;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2019, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Secreted RxLR effector protein 8 {ECO:0000303|PubMed:29706971};
DE   Flags: Precursor;
GN   Name=RXLR8 {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 completely suppresses the host cell
CC       death induced by cell death-inducing proteins.
CC       {ECO:0000269|PubMed:29706971}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29706971}. Host
CC       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; P0CU95; -.
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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..457
FT                   /note="Secreted RxLR effector protein 8"
FT                   /id="PRO_0000447904"
FT   REGION          110..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           48..69
FT                   /note="RxLR-dEER"
FT                   /evidence="ECO:0000305|PubMed:29706971"
FT   COMPBIAS        113..183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..457
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   457 AA;  51700 MW;  1F6D223C07F6A2D3 CRC64;
     MRGTLATALL LVISSRVATE SNQLDPQQLS NHVVGTYDKI YTKSSPRRFL RGSRKQRDDL
     APTAADENRT INNAIESAMH GITFSGGTTA ATRNAAREVV DINAFSKRPR LSLNVPPSET
     SAHLIEAPTF PQRNSASTST TSDIATSSSR TSNQRTPKTQ ASLDMSHKTM TRKSSSKNQF
     KKSTALKSTK RKVRARKIPA FVVNKVYTLY FDHVKTKSLG FDPTVKETKA MLSLYFESSV
     DPFYVSAVLS NFFRYFDDKE LTIHKKKLGT TLTSALSTLA ALELPPGMLK EIERPFVWYA
     SLKRWRVMYC DFFEFVKVNS DKITNSLPNK EFYRGETSDI VRDKLLATLK KETNTNTRYK
     RKRKLKNDLD DVLKKYNVKE EIGAAIRDLG EQFLKADRQT IPSRRPTRRP GASHIQPSNQ
     RTDLTPHGLQ VPGPEKNSYQ HIKSKDHARK KRPRSSS