AVH23_PHYSP
ID AVH23_PHYSP Reviewed; 140 AA.
AC G4ZJX4;
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 Avh23 {ECO:0000303|PubMed:21653195};
DE AltName: Full=Avirulence homolog protein 23 {ECO:0000303|PubMed:21653195};
DE Flags: Precursor;
GN Name=Avh23 {ECO:0000303|PubMed:21653195}; ORFNames=PHYSODRAFT_286162;
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 FUNCTION, DISRUPTION PHENOTYPE, DOMAIN, AND MUTAGENESIS OF PHE-109;
RP VAL-110; ARG-112; PHE-123; VAL-124 AND ARG-126.
RX PubMed=28318979; DOI=10.1016/j.cub.2017.02.044;
RA Kong L., Qiu X., Kang J., Wang Y., Chen H., Huang J., Qiu M., Zhao Y.,
RA Kong G., Ma Z., Wang Y., Ye W., Dong S., Ma W., Wang Y.;
RT "A Phytophthora effector manipulates host histone acetylation and
RT reprograms defense gene expression to promote infection.";
RL Curr. Biol. 27:981-991(2017).
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). Acts as a
CC modulator of histone acetyltransferase (HAT) in plants. Avh23 binds to
CC the ADA2 subunit of the HAT complex SAGA and disrupts its assembly by
CC interfering with the association of ADA2 with the catalytic subunit
CC GCN5. As such, Avh23 suppresses H3K9 acetylation mediated by the
CC ADA2/GCN5 module and increases plant susceptibility (PubMed:28318979).
CC {ECO:0000269|PubMed:21653195, ECO:0000269|PubMed:28318979}.
CC -!- SUBUNIT: Interacts with host histone acetyl transferase SAGA complex
CC subunit ADA2. {ECO:0000269|PubMed:28318979}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28318979}. Host
CC nucleus {ECO:0000269|PubMed:28318979}. Host cytoplasm
CC {ECO:0000269|PubMed:28318979}. Note=Location into the host nucleus is
CC required for virulence. {ECO:0000269|PubMed:28318979}.
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 two internal repeats IR1 and IR2, in the C-terminus, are
CC required for the interaction with host ADA2.
CC {ECO:0000269|PubMed:28318979}.
CC -!- DISRUPTION PHENOTYPE: Leads to reduced virulence on etiolated soybean
CC hypocotyls. {ECO:0000269|PubMed:28318979}.
CC -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR EMBL; JH159155; EGZ14456.1; -; Genomic_DNA.
DR RefSeq; XP_009528205.1; XM_009529910.1.
DR AlphaFoldDB; G4ZJX4; -.
DR EnsemblProtists; EGZ14456; EGZ14456; PHYSODRAFT_286162.
DR GeneID; 20640264; -.
DR KEGG; psoj:PHYSODRAFT_286162; -.
DR InParanoid; G4ZJX4; -.
DR Proteomes; UP000002640; Unassembled WGS sequence.
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 InterPro; IPR031825; RXLR.
DR Pfam; PF16810; RXLR; 1.
PE 1: Evidence at protein level;
KW Host cytoplasm; Host nucleus; Reference proteome; Repeat; Secreted; Signal;
KW Virulence.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..140
FT /note="RxLR effector protein Avh23"
FT /id="PRO_5003472259"
FT REPEAT 100..113
FT /note="ADA2-binding IR1"
FT /evidence="ECO:0000269|PubMed:28318979"
FT REPEAT 114..127
FT /note="ADA2-binding IR2"
FT /evidence="ECO:0000269|PubMed:28318979"
FT MOTIF 54..72
FT /note="RxLR-dEER"
FT /evidence="ECO:0000305|PubMed:21653195"
FT MUTAGEN 109
FT /note="F->A: Impairs interaction with host ADA2 and
FT subsequent virulence; when associated with A-110, A-112, A-
FT 123, A-124 and A-126."
FT /evidence="ECO:0000269|PubMed:28318979"
FT MUTAGEN 110
FT /note="V->A: Impairs interaction with host ADA2 and
FT subsequent virulence; when associated with A-109, A-112, A-
FT 123, A-124 and A-126."
FT /evidence="ECO:0000269|PubMed:28318979"
FT MUTAGEN 112
FT /note="R->A: Impairs interaction with host ADA2 and
FT subsequent virulence; when associated with A-1090, A-110,
FT A-123, A-124 and A-1267."
FT /evidence="ECO:0000269|PubMed:28318979"
FT MUTAGEN 123
FT /note="F->A: Impairs interaction with host ADA2 and
FT subsequent virulence; when associated with A-109, A-110, A-
FT 112, A-124 and A-126."
FT /evidence="ECO:0000269|PubMed:28318979"
FT MUTAGEN 124
FT /note="V->A: Impairs interaction with host ADA2 and
FT subsequent virulence; when associated with A-109, A-110, A-
FT 112, A-123 and A-126."
FT /evidence="ECO:0000269|PubMed:28318979"
FT MUTAGEN 126
FT /note="R->A: Impairs interaction with host ADA2 and
FT subsequent virulence; when associated with A-109, A-110, A-
FT 112, A-123 and A-124."
FT /evidence="ECO:0000269|PubMed:28318979"
SQ SEQUENCE 140 AA; 15470 MW; 39B9667D5FD06C4E CRC64;
MRLTYFLTVI VVATLHAGGT ALATAEAPNH AAIVNVASAD NVHSLDTTAE IGGRMLRKVK
EDTVSKKDHE ERGPGAILER QTAFVKKLFS RQNAIVNRAQ GAFQRQNAFV NRDQGAFQRQ
NAFVKRAIQR QNHFKLSDNA
