RL207_PHYCP
ID RL207_PHYCP Reviewed; 174 AA.
AC A0A411NN20;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=RxLR effector protein 207 {ECO:0000303|PubMed:30703564};
DE AltName: Full=Avirulence protein homolog 207 {ECO:0000303|PubMed:29029698};
DE Flags: Precursor;
GN Name=RxLR207 {ECO:0000303|PubMed:30703564};
GN Synonyms=Avh207 {ECO:0000303|PubMed:29029698};
OS Phytophthora capsici.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4784;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE,
RP INDUCTION, INTERACTION WITH HOST ACD11; BPA1; BPL1; BPL2; BPL3 AND BPL4,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=LT263;
RX PubMed=30703564; DOI=10.1016/j.molp.2019.01.018;
RA Li Q., Ai G., Shen D., Zou F., Wang J., Bai T., Chen Y., Li S., Zhang M.,
RA Jing M., Dou D.;
RT "A Phytophthora capsici effector targets ACD11 binding partners that
RT regulate ROS-mediated defense response in Arabidopsis.";
RL Mol. Plant 12:565-581(2019).
RN [2]
RP DOMAIN, FUNCTION, AND MUTAGENESIS OF LYS-86 AND LYS-94.
RX PubMed=29029698; DOI=10.1016/j.funbio.2017.07.005;
RA Shen D., Li Q., Sun P., Zhang M., Dou D.;
RT "Intrinsic disorder is a common structural characteristic of RxLR effectors
RT in oomycete pathogens.";
RL Fungal Biol. 121:911-919(2017).
CC -!- FUNCTION: Secreted effector that activates ROS-mediated cell death in
CC plant host and is essential for virulence (PubMed:30703564,
CC PubMed:29029698). Plays a role in the transition from the biotrophic to
CC necrotrophic stage (PubMed:30703564). Associates with and promotes the
CC degradation of Nicotiana benthamiana BPA1, BPL1, BPL2, and BPL4 to
CC disrupt ACD11 stabilization in a 26S proteasome-dependent manner
CC (PubMed:30703564). {ECO:0000269|PubMed:29029698,
CC ECO:0000269|PubMed:30703564}.
CC -!- SUBUNIT: Interacts with Nicotiana benthamiana ACD11, BPA1 (binding
CC partner of ACD11), as well as BPA-like proteins BPL1, BPL2, BPL3 and
CC BPL4. {ECO:0000269|PubMed:30703564}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30703564}. Host cell
CC membrane {ECO:0000269|PubMed:30703564}.
CC -!- INDUCTION: Expression is induced at 9-18 hours post-infiltration (hpi).
CC {ECO:0000269|PubMed:30703564}.
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:30703564}.
CC -!- DOMAIN: The disordered structure between residues 82 and 99 contributes
CC to the effector function in cell death activation.
CC {ECO:0000269|PubMed:29029698}.
CC -!- DISRUPTION PHENOTYPE: Exhibits significantly reduced virulence with
CC smaller lesions on Nicotiana benthamiana infected leaves.
CC {ECO:0000269|PubMed:30703564}.
CC -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR EMBL; MK530529; QBF53359.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411NN20; -.
DR VEuPathDB; FungiDB:DVH05_002571; -.
DR PHI-base; PHI:8809; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Host cell membrane; Host membrane; Membrane; Secreted; Signal; Virulence.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..174
FT /note="RxLR effector protein 207"
FT /id="PRO_5019054076"
FT REGION 82..99
FT /note="Disordered"
FT /evidence="ECO:0000305|PubMed:29029698"
FT MOTIF 46..62
FT /note="RxLR-dEER"
FT /evidence="ECO:0000305|PubMed:30703564"
FT MUTAGEN 86
FT /note="K->F: Leads to the transition from disordered
FT structure to ordered structure and abolishes the function
FT in cell death activation; when associated with A-94."
FT /evidence="ECO:0000269|PubMed:29029698"
FT MUTAGEN 94
FT /note="K->F: Leads to the transition from disordered
FT structure to ordered structure and abolishes the function
FT in cell death activation; when associated with A-86."
FT /evidence="ECO:0000269|PubMed:29029698"
SQ SEQUENCE 174 AA; 19252 MW; FEFF73A8521D1CC7 CRC64;
MSKVFLLLVL SVFALVSCDA LSAPVGSKLS LSKTDELNAQ PIDAKRMLRA QEEPTNAADE
ERGMTELANK FKAWAAAIKT WVTNSKLVQS MNNKLASLTQ KGRVGQIEKL LKQDNVNVNV
LYQNKVKPDE LFLALKLDPK LKLIADAPAA WANNPGLSMF YQYATYYAKM TTKA
