ID   RL111_PLAVT             Reviewed;         451 AA.
AC   P0CV44;
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 111 {ECO:0000303|PubMed:29706971};
DE   Flags: Precursor;
GN   Name=RXLR111 {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=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; P0CV44; -.
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..451
FT                   /note="Secreted RxLR effector protein 111"
FT                   /id="PRO_0000447953"
FT   REGION          175..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          404..451
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        410..429
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   451 AA;  50375 MW;  7D08EC1033C6CCC4 CRC64;
     MRGTLATALL LVASCRIAAE SNQINPQQAS HHVGTTLNKL FTKSSPRRFL RDNREQRVAL
     ALTAANESRT IENAVTSAVH GITDASTTTA ATRDAARDIL NQHAFPKEGI RPQFDLNLPP
     SETSALLTGA SNIPQRNHAF SSITSGIAVS SSRTSNQRTA KTQANLDMSH QGTVRKTLSK
     TQFKNPAASK STKRRKKARI IPPFVVNKVD TLYREHLTAK SLEFDPTIKE TEAMLKLYVE
     STVDPLPVST VHFNHFRYFK DQDLTLLKEK LGTTLESALS TLAALNLPPG MLKAIERPFV
     WYASLARWRA MYCDFFEFLN ANSNKIATSL PNVEFFGGET SSTVRDQLLA TLKEEMKTRT
     KTRRNGKIMN DLKVVLAKYN VEEEIKAAIR GLGEQFLKRD HEIIPLQRHS RRSPASQSRS
     NNQRTGLTPY GLQIPGPERD SFRHIESNKH A