RLR24_PHYIT
ID RLR24_PHYIT Reviewed; 159 AA.
AC D0NYM3;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=RxLR effector protein 24 {ECO:0000303|PubMed:29671919};
DE Flags: Precursor;
GN Name=RxLR24 {ECO:0000303|PubMed:29671919}; ORFNames=PITG_18405;
OS Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=403677;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T30-4;
RX PubMed=19741609; DOI=10.1038/nature08358;
RG The Broad Institute Genome Sequencing Platform;
RA Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA Nusbaum C.;
RT "Genome sequence and analysis of the Irish potato famine pathogen
RT Phytophthora infestans.";
RL Nature 461:393-398(2009).
RN [2]
RP FUNCTION, AND INTERACTION WITH HOST RABA1A; RABA2A AND RABA4A.
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 potato RABA GTPases including RABA1a, RABA2a
CC and RABA4a. {ECO:0000269|PubMed:29671919}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A0A2L0WUE7}. Host
CC cell membrane {ECO:0000250|UniProtKB:A0A2L0WUE7}. Host endomembrane
CC system {ECO:0000250|UniProtKB:A0A2L0WUE7}. Note=The subcellular
CC localization to plasma and vesicular membranes is most likely the
CC result of binding of RxLR24 to membrane-localized RABA proteins.
CC {ECO:0000250|UniProtKB:A0A2L0WUE7}.
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:0000250|UniProtKB:A0A2L0WUE7}.
CC -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR EMBL; DS028189; EEY68645.1; -; Genomic_DNA.
DR RefSeq; XP_002997548.1; XM_002997502.1.
DR AlphaFoldDB; D0NYM3; -.
DR EnsemblProtists; PITG_18405T0; PITG_18405T0; PITG_18405.
DR GeneID; 9466355; -.
DR KEGG; pif:PITG_18405; -.
DR VEuPathDB; FungiDB:PITG_18405; -.
DR eggNOG; ENOG502RF03; Eukaryota.
DR HOGENOM; CLU_1638744_0_0_1; -.
DR InParanoid; D0NYM3; -.
DR OMA; ATEPRYE; -.
DR OrthoDB; 1620612at2759; -.
DR Proteomes; UP000006643; Partially assembled WGS sequence.
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.
PE 1: Evidence at protein level;
KW Host cell membrane; Host membrane; Membrane; Reference proteome; Secreted;
KW Signal; Virulence.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..159
FT /note="RxLR effector protein 24"
FT /evidence="ECO:0000255"
FT /id="PRO_5003012498"
FT REGION 109..159
FT /note="RABA-binding domain"
FT /evidence="ECO:0000250|UniProtKB:A0A2L0WUE7"
FT MOTIF 58..82
FT /note="RxLR-dEER"
FT /evidence="ECO:0000305|PubMed:29671919"
SQ SEQUENCE 159 AA; 17973 MW; DEE302B22F723ABA CRC64;
MRFLVWVFFV GLVTFVSGTH AISKLANSNE PQSTQLTMKD IDTLTRLLFV EDGDAAKRFL
RSNANQDLTT ANDDSDVKEE ERGLLPSKVT NLISKAKNGW AKWKANALEK AFQHMMKQGE
TPTSLAKRLE IGGAAELRYE KVYEKYTAWW INYHTVAGT
