ID   RL104_PLAVT             Reviewed;         484 AA.
AC   P0CV41;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2019, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Secreted RxLR effector protein 104 {ECO:0000303|PubMed:29706971};
DE   Flags: Precursor;
GN   Name=RXLR104 {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; P0CV41; -.
DR   SMR; P0CV41; -.
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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..484
FT                   /note="Secreted RxLR effector protein 104"
FT                   /id="PRO_0000447950"
FT   REGION          324..463
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        328..347
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..410
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..432
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..462
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        175
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   484 AA;  53837 MW;  3A2B2118F3478856 CRC64;
     MRSAYPVLTA LLVVASSQIA AGSGHQLQAY DHDRITDDNA VMKSLSTRFL RGSRDVHNNV
     ANEERSVYSV LARMIKKGIK KMPRTAEVLK MKPHIKKASK KSPHEARLVK ELFHAAEAKE
     TMQGAREYKK LRRATRAAVE ALEKHWNPSK TAVSGDAFHD IHSNQMLSVK KWKFNLTGLK
     PMVVNDEHHG MIDSVHKAFL TVCDKNVKPT RAETSYLWGL MNWKLAKYPR RSHKESLIEH
     AQRRVLLDMR KMKATKKVWP EWENLPDSLK FGVLDYLLNL HYQRLVRMYN IFARNRPDRN
     PAPLNPELNP VGNTGTSAAM AVAENPKGQS PYPSTPLTAA STSKGGRSNL KKRSKRTSDG
     NTDTASFPSK KLKVRSSKSV MPLLTEPTTS GDHSAPAKKS KSSSSGPSRA FAPDKSGDQT
     FITENSRLSF DGPSSAVDPF KQSKVHESKS LAPSSSVLTP EDVDTELSLG GIYDRSTYKA
     PSKP