RL124_PLAVT
ID RL124_PLAVT Reviewed; 265 AA.
AC P0CV52;
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 124 {ECO:0000303|PubMed:29706971};
DE Flags: Precursor;
GN Name=RXLR124 {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 partially 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}. Host cytoplasm
CC {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P0CV52; -.
DR SMR; P0CV52; -.
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.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF12796; Ank_2; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; Glycoprotein; Host cytoplasm; Host nucleus; Repeat; Secreted;
KW Signal; Virulence.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..265
FT /note="Secreted RxLR effector protein 124"
FT /id="PRO_0000447961"
FT REPEAT 34..64
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 69..97
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 98..126
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 128..157
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 159..183
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 184..213
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT REPEAT 215..240
FT /note="ANK 7"
FT /evidence="ECO:0000255"
FT MOTIF 49..72
FT /note="RxLR-dEER"
FT /evidence="ECO:0000305|PubMed:29706971"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 265 AA; 29887 MW; EC1E6700C3F6BDB1 CRC64;
MPVLVSVALV ARHSDTLGAL QHVEQTISDF IDYSKCWTMA KAVSCRNIRL LRRILVHRGK
DDNEGSCMDI ERAMEVASAS GDMEMVQFLH ETYPQHGKTR CLELAASNGH LDVLRWIYKH
RNGKDTLTMS AFDFAAGNGH LDVVEWMHAN RSRGCSTRAM DCAARNGHLH IVQWLHAHRQ
EGCTTQAMDW AAQEGHFEVV QWLLLNRQEG CSSIAIDAAA SNGHLKLVHW LHEHCNVTCS
YFACAMAAER GHHHILEWIG QIEQT
