ID   RL108_PLAVT             Reviewed;         510 AA.
AC   P0CV43;
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 108 {ECO:0000303|PubMed:29706971};
DE   Flags: Precursor;
GN   Name=RXLR108 {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; P0CV43; -.
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..510
FT                   /note="Secreted RxLR effector protein 108"
FT                   /id="PRO_0000447952"
FT   REGION          111..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          386..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           48..65
FT                   /note="RxLR-dEER"
FT                   /evidence="ECO:0000305|PubMed:29706971"
FT   COMPBIAS        111..125
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   510 AA;  57055 MW;  72CEC18DB7832D08 CRC64;
     MRGAYYVLTA LFVVTSSDIA AESDHPLHNF NHHVITAGNA VVKALPNRSL RGSRDGRNDL
     ANEERSISSF LANMIDEGVA KLPLVAEIIK TKPLAAKAVK QKPRAMKKKF RAAKAVEEKS
     RPAKAAKKTP RAAKAAKKTP PQAKVVDEIL YGVEATKEMG KSEEYGVLKA ATEGADQALK
     KHWDPSRETA VIVAPSRDIS GNVILSLRKW KVGFNGMRPM VVLDKHKDNI DRVHGAFGTL
     CDKNMQITPV ETSYLWSMLD WNIEKNFKKK HKQTLVRLAQ RYVLIGLRQV KKDRKVWNQW
     KKLPDPLKFG VLNYLLNLHY QRWVRMYNIF RRYRPDQNGV PSTLGGNANI NRALALQKHS
     KVRSVFPYEP FDVAWASKGR RSVLSKRSRR TFDGNTDTAS LPSKQLKTRS SESSMPPLIE
     STTSGDDSVP TKEIKSSFDD PKSAFAPFKP GDDFVHTENS RLSFGGLSSA FVPYRRPNVH
     NSQSLTSPIT VSSMPSLMKS TTSGDGLRPY