ID   RLR24_PHYBB             Reviewed;         155 AA.
AC   A0A2L0WUE7;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   25-APR-2018, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=RxLR effector protein 24 {ECO:0000303|PubMed:29671919};
DE   Flags: Precursor;
GN   Name=RxLR24 {ECO:0000303|PubMed:29671919};
OS   Phytophthora brassicae.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=187813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, SUBCELLULAR LOCATION,
RP   DOMAIN, INTERACTION WITH HOST RABA1A; RABA1B; RABA1C; RABA1D; RABA1F;
RP   RABA2A; RABA2C; RABA2D; RABA4A; RABA4B AND RABA4C, AND MUTAGENESIS OF
RP   105-GLU--THR-155.
RX   PubMed=29671919; DOI=10.1111/tpj.13928;
RA   Tomczynska I., Stumpe M., Mauch F.;
RT   "A conserved RxLR effector interacts with host RABA-type GTPases to inhibit
RT   vesicle-mediated secretion of antimicrobial proteins.";
RL   Plant J. 95:187-203(2018).
CC   -!- FUNCTION: Effector protein that contributes to pathogen virulence
CC       (PubMed:29671919). Targets members of the RABA GTPases subfamily to
CC       inhibit vesicular secretion, leading to an accumulation of secretory
CC       proteins in the endoplasmic reticulum (PubMed:29671919).
CC       {ECO:0000269|PubMed:29671919}.
CC   -!- SUBUNIT: Interacts with Arabidopsis thaliana RABA GTPases including
CC       RABA1a, RABA1b, RABA1c, RABA1d, RABA1f, RABA2a, RABA2c, RABA2d, RABA4a,
CC       RABA4b and RABA4c. {ECO:0000269|PubMed:29671919}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29671919}. Host cell
CC       membrane {ECO:0000269|PubMed:29671919}. Host endomembrane system
CC       {ECO:0000269|PubMed:29671919}. Note=The subcellular localization to
CC       plasma and vesicular membranes is most likely the result of binding of
CC       RxLR24 to membrane-localized RABA proteins.
CC       {ECO:0000305|PubMed:29671919}.
CC   -!- INDUCTION: Expressed early in the interaction with Arabidopsis plants.
CC       {ECO:0000269|PubMed:29671919}.
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:29671919}.
CC   -!- DOMAIN: The C-terminal part (residues 105 to 155) is required for the
CC       binding to RABA GTPasesproteins, causes redirection of the truncated
CC       effector to the cytoplasm, and leads tio the loss of the ability to
CC       inhibit the host secretory pathway. {ECO:0000269|PubMed:29671919}.
CC   -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR   EMBL; MG489826; AVA31271.1; -; mRNA.
DR   AlphaFoldDB; A0A2L0WUE7; -.
DR   SMR; A0A2L0WUE7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0033645; C:host cell endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR031825; RXLR.
DR   Pfam; PF16810; RXLR; 1.
PE   1: Evidence at protein level;
KW   Host cell membrane; Host membrane; Membrane; Secreted; Signal; Virulence.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..155
FT                   /note="RxLR effector protein 24"
FT                   /id="PRO_5014856474"
FT   REGION          105..155
FT                   /note="RABA-binding domain"
FT                   /evidence="ECO:0000305|PubMed:29671919"
FT   MOTIF           52..78
FT                   /note="RxLR-dEER"
FT                   /evidence="ECO:0000305|PubMed:29671919"
FT   MUTAGEN         105..155
FT                   /note="Missing: Abolishes binding to RABA GTPases and
FT                   causes redirection of the truncated effector to the
FT                   cytoplasm."
FT                   /evidence="ECO:0000269|PubMed:29671919"
SQ   SEQUENCE   155 AA;  17649 MW;  1A508015E27D7214 CRC64;
     MRLLIWVLFV TLVTFVSNTT ATSTFTDPQV TSGDIEALTH LLDVESNADA KRFLRTESKN
     DLKSDADTNG IDIEDEERGF IPSSITNAFS KMKTGWSNFK SNQFEKAFQR MNQKGETPTT
     LAKRLDIGKT AEKRFEKTYE KYTAWWINHH TNAGT