AVH5_PHYSO
ID AVH5_PHYSO Reviewed; 135 AA.
AC E0W547;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=RxLR effector protein Avh5 {ECO:0000303|PubMed:21653195};
DE AltName: Full=Avirulence homolog protein 5 {ECO:0000303|PubMed:21653195};
DE Flags: Precursor;
GN Name=Avh5 {ECO:0000303|PubMed:21653195};
OS Phytophthora sojae (Soybean stem and root rot agent) (Phytophthora
OS megasperma f. sp. glycines).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=67593;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND DOMAIN.
RC STRAIN=P7064, P7074, and P7076;
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 [2]
RP DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=20655469; DOI=10.1016/j.cell.2010.06.008;
RA Kale S.D., Gu B., Capelluto D.G., Dou D., Feldman E., Rumore A.,
RA Arredondo F.D., Hanlon R., Fudal I., Rouxel T., Lawrence C.B., Shan W.,
RA Tyler B.M.;
RT "External lipid PI3P mediates entry of eukaryotic pathogen effectors into
RT plant and animal host cells.";
RL Cell 142:284-295(2010).
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. {ECO:0000269|PubMed:21653195}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20655469}. Host cell
CC {ECO:0000269|PubMed:20655469}.
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 -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR EMBL; JN253639; AEK80452.1; -; Genomic_DNA.
DR EMBL; JN253640; AEK80453.1; -; Genomic_DNA.
DR EMBL; JN253641; AEK80454.1; -; Genomic_DNA.
DR RefSeq; XP_009528278.1; XM_009529983.1.
DR AlphaFoldDB; E0W547; -.
DR SMR; E0W547; -.
DR GeneID; 20640268; -.
DR KEGG; psoj:PHYSODRAFT_286169; -.
DR VEuPathDB; FungiDB:PHYSODRAFT_286169; -.
DR HOGENOM; CLU_1889900_0_0_1; -.
DR OMA; NDASKVP; -.
DR OrthoDB; 1598341at2759; -.
DR PHI-base; PHI:2692; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043657; C:host cell; IEA:UniProtKB-SubCell.
DR InterPro; IPR031825; RXLR.
DR Pfam; PF16810; RXLR; 1.
PE 3: Inferred from homology;
KW Secreted; Signal; Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..135
FT /note="RxLR effector protein Avh5"
FT /evidence="ECO:0000255"
FT /id="PRO_5007652829"
FT MOTIF 43..71
FT /note="RxLR-dEER"
FT /evidence="ECO:0000305|PubMed:21653195"
FT BINDING 81
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250|UniProtKB:G4ZKT3"
FT BINDING 83
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250|UniProtKB:G4ZKT3"
FT BINDING 84
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250|UniProtKB:G4ZKT3"
SQ SEQUENCE 135 AA; 15528 MW; 54E56B1BFA36E010 CRC64;
MRLQFFLVMA VATLATISAT RVPDDANLQS VNAPVQTVTR SRRFLRTADT DIVYEPKVHN
PGKKQVFIED KLQKALTDPK KNKKLYARWY NSGFTVKQVE GGLDQNENRE LELTYKNLAL
GYAKYYQARR SQEAK
