AVH5_PHYSP
ID AVH5_PHYSP Reviewed; 135 AA.
AC G4ZKT3;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=RxLR effector protein Avh5 {ECO:0000303|PubMed:20655469};
DE AltName: Full=Avirulence homolog protein 5 {ECO:0000303|PubMed:20655469};
DE Flags: Precursor;
GN Name=Avh5 {ECO:0000303|PubMed:20655469}; ORFNames=PHYSODRAFT_286169;
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 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).
RN [3]
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 [4]
RP STRUCTURE BY NMR OF 20-135, PTDINS(3)P-BINDING, AND MUTAGENESIS OF
RP 43-ARG--ARG-46 AND 81-LYS--LYS-84.
RX PubMed=23075041; DOI=10.1094/mpmi-07-12-0184-r;
RA Sun F., Kale S.D., Azurmendi H.F., Li D., Tyler B.M., Capelluto D.G.;
RT "Structural basis for interactions of the Phytophthora sojae RxLR effector
RT Avh5 with phosphatidylinositol 3-phosphate and for host cell entry.";
RL Mol. Plant Microbe Interact. 26:330-344(2013).
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:0000269|PubMed:23075041}.
CC -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH159155; EGZ14529.1; -; Genomic_DNA.
DR RefSeq; XP_009528278.1; XM_009529983.1.
DR AlphaFoldDB; G4ZKT3; -.
DR SMR; G4ZKT3; -.
DR EnsemblProtists; EGZ14529; EGZ14529; PHYSODRAFT_286169.
DR GeneID; 20640268; -.
DR KEGG; psoj:PHYSODRAFT_286169; -.
DR InParanoid; G4ZKT3; -.
DR OMA; NDASKVP; -.
DR Proteomes; UP000002640; Unassembled WGS sequence.
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 1: Evidence at protein level;
KW Reference proteome; Secreted; Signal; Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..135
FT /note="RxLR effector protein Avh5"
FT /id="PRO_5003472292"
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:0000269|PubMed:23075041"
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:0000269|PubMed:23075041"
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:0000269|PubMed:23075041"
FT MUTAGEN 43..46
FT /note="RFLR->AAAA: Reduces PtdIns(3)P-binding and entry
FT into host cells."
FT /evidence="ECO:0000269|PubMed:23075041"
FT MUTAGEN 81..84
FT /note="KNKK->ANAA: Reduces PtdIns(3)P-binding and entry
FT into host cells."
FT /evidence="ECO:0000269|PubMed:23075041"
SQ SEQUENCE 135 AA; 15528 MW; 54E56B1BFA36E010 CRC64;
MRLQFFLVMA VATLATISAT RVPDDANLQS VNAPVQTVTR SRRFLRTADT DIVYEPKVHN
PGKKQVFIED KLQKALTDPK KNKKLYARWY NSGFTVKQVE GGLDQNENRE LELTYKNLAL
GYAKYYQARR SQEAK
