AV240_PHYSP
ID AV240_PHYSP Reviewed; 194 AA.
AC G5A8M1;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 25-MAY-2022, entry version 25.
DE RecName: Full=RxLR effector protein Avh240 {ECO:0000303|PubMed:21653195};
DE AltName: Full=Avirulence homolog protein 2402 {ECO:0000303|PubMed:21653195};
DE Flags: Precursor;
GN Name=Avh240 {ECO:0000303|PubMed:21653195}; ORFNames=PHYSODRAFT_288823;
OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS (Phytophthora megasperma f. sp. glycines).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1094619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6497;
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H.Y., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M.B., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.-K.,
RA McDonald W.H., Medina M., Meijer H.J.G., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K.C., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W.S., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
RN [2]
RP IDENTIFICATION, FUNCTION, AND DOMAIN.
RX PubMed=21653195; DOI=10.1105/tpc.111.086082;
RA Wang Q., Han C., Ferreira A.O., Yu X., Ye W., Tripathy S., Kale S.D.,
RA Gu B., Sheng Y., Sui Y., Wang X., Zhang Z., Cheng B., Dong S., Shan W.,
RA Zheng X., Dou D., Tyler B.M., Wang Y.;
RT "Transcriptional programming and functional interactions within the
RT Phytophthora sojae RXLR effector repertoire.";
RL Plant Cell 23:2064-2086(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 58-194, SUBUNIT, FUNCTION,
RP INTERACTION WITH HOST AP1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 58-LEU--SER-108 AND TYR-180.
RX PubMed=30703565; DOI=10.1016/j.molp.2019.01.017;
RA Guo B., Wang H., Yang B., Jiang W., Jing M., Li H., Xia Y., Xu Y., Hu Q.,
RA Wang F., Yu F., Wang Y., Ye W., Dong S., Xing W., Wang Y.;
RT "Phytophthora sojae effector PsAvh240 inhibits a host aspartic protease
RT secretion to promote infection.";
RL Mol. Plant 12:552-564(2019).
CC -!- FUNCTION: Effector that suppresses plant defense responses during the
CC early stages of pathogen infection. Suppresses cell death induced by
CC effectors and PAMPs in plant hosts (PubMed:21653195). Avh240 dimerizes
CC and localizes at the plasma membrane to interfere with aspartic
CC protease AP1 secretion, which presents an effective mechanism by which
CC effector proteins suppress plant apoplastic immunity (PubMed:30703565).
CC {ECO:0000269|PubMed:21653195, ECO:0000269|PubMed:30703565}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with host soybean
CC aspartic protease AP1 (PubMed:30703565). {ECO:0000250|UniProtKB:E0W4T1,
CC ECO:0000269|PubMed:30703565}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30703565}. Host cell
CC membrane {ECO:0000269|PubMed:30703565}. Note=Plasma membrane
CC localization is independent on self-dimerization but required for
CC virulence. {ECO:0000269|PubMed:30703565}.
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:21653195}.
CC -!- DOMAIN: The alpha 1 and alpha 2 helices (residues 58-108) are required
CC for the localization the plasma membrane.
CC {ECO:0000250|UniProtKB:E0W4T1}.
CC -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR EMBL; JH159161; EGZ08247.1; -; Genomic_DNA.
DR RefSeq; XP_009536419.1; XM_009538124.1.
DR PDB; 6J8L; X-ray; 2.30 A; A/B=58-135.
DR PDBsum; 6J8L; -.
DR AlphaFoldDB; G5A8M1; -.
DR SMR; G5A8M1; -.
DR EnsemblProtists; EGZ08247; EGZ08247; PHYSODRAFT_288823.
DR GeneID; 20640723; -.
DR KEGG; psoj:PHYSODRAFT_288823; -.
DR InParanoid; G5A8M1; -.
DR OMA; TNEHARH; -.
DR Proteomes; UP000002640; Unassembled WGS sequence.
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 3D-structure; Host cell membrane; Host membrane; Membrane;
KW Reference proteome; Secreted; Signal; Virulence.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..194
FT /note="RxLR effector protein Avh240"
FT /id="PRO_5003473077"
FT REGION 58..108
FT /note="Host plasma membrane-binding"
FT /evidence="ECO:0000250|UniProtKB:E0W4T1"
FT MOTIF 38..57
FT /note="RxLR-dEER"
FT /evidence="ECO:0000305|PubMed:30703565"
FT MUTAGEN 58..108
FT /note="Missing: Impairs host plasma membrane localization,
FT host AP1-binding, and virulence."
FT /evidence="ECO:0000269|PubMed:30703565"
FT MUTAGEN 180
FT /note="Y->A: Impairs homodimerization and affect soybean
FT infection."
FT /evidence="ECO:0000269|PubMed:30703565"
SQ SEQUENCE 194 AA; 22225 MW; AC0C5C064CDDCC39 CRC64;
MRPYFTLLLA LAFILACTNL VEADAGRVLE TTTNEHARHL RTAVASVVDL PDDEDERLLG
YNTVQLWRMR RTANKLMNGK LTTQKEAALK KWMASQQDKF LAKWLKSSSV YPDQVYSKLG
LTKLGASAKS SPNYQLYEKY TEALLQRWTN FKASPDTVYK SLRLDKLGAK APQSPSYPMY
EKYLQTFFRN QPAN
