AV262_PHYSP
ID AV262_PHYSP Reviewed; 123 AA.
AC G5A731;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=RxLR effector protein Avh262 {ECO:0000303|PubMed:21653195};
DE AltName: Full=Avirulence homolog protein 262 {ECO:0000303|PubMed:21653195};
DE Flags: Precursor;
GN Name=Avh262 {ECO:0000303|PubMed:21653195}; ORFNames=PHYSODRAFT_288708;
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, 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, MUTAGENESIS OF 60-LEU--THR-82,
RP INTERACTION WITH HOST BIP1; BIP2; BIP3 AND BIP4, AND SUBCELLULAR LOCATION.
RX PubMed=27256489; DOI=10.1038/ncomms11685;
RA Jing M., Guo B., Li H., Yang B., Wang H., Kong G., Zhao Y., Xu H., Wang Y.,
RA Ye W., Dong S., Qiao Y., Tyler B.M., Ma W., Wang Y.;
RT "A Phytophthora sojae effector suppresses endoplasmic reticulum stress-
RT mediated immunity by stabilizing plant Binding immunoglobulin Proteins.";
RL Nat. Commun. 7:11685-11685(2016).
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, PubMed:27256489).
CC Avh262 stabilizes endoplasmic reticulum (ER)-luminal binding
CC immunoglobulin proteins (BiPs), which act as negative regulators of
CC plant resistance to Phytophthora. By stabilizing BiPs, Avh262
CC suppresses ER stress-triggered cell death and facilitates Phytophthora
CC infection (PubMed:27256489). {ECO:0000269|PubMed:21653195,
CC ECO:0000269|PubMed:27256489}.
CC -!- SUBUNIT: Interacts with host plant ER-luminal binding immunoglobulin
CC proteins (BiPs) such as soybean BiP1, BiP2, BiP3 and BiP4.
CC {ECO:0000269|PubMed:27256489}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27256489}. Host
CC endoplasmic reticulum {ECO:0000269|PubMed:27256489}.
CC -!- DOMAIN: Residues 60 to 82 are required for the interaction with host
CC plant binding immunoglobulin proteins (BiPs) and subsequent virulence.
CC {ECO:0000269|PubMed:27256489}.
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 -!- DISRUPTION PHENOTYPE: Leads to reduced virulence on etiolated soybean
CC seedlings. {ECO:0000269|PubMed:27256489}.
CC -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR EMBL; JH159160; EGZ09136.1; -; Genomic_DNA.
DR RefSeq; XP_009535769.1; XM_009537474.1.
DR AlphaFoldDB; G5A731; -.
DR SMR; G5A731; -.
DR EnsemblProtists; EGZ09136; EGZ09136; PHYSODRAFT_288708.
DR GeneID; 20640676; -.
DR KEGG; psoj:PHYSODRAFT_288708; -.
DR Proteomes; UP000002640; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Host endoplasmic reticulum; Reference proteome; Secreted; Signal;
KW Virulence.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..123
FT /note="RxLR effector protein Avh262"
FT /id="PRO_5003473018"
FT REGION 24..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..82
FT /note="BiP-binding"
FT /evidence="ECO:0000269|PubMed:27256489"
FT MOTIF 30..50
FT /note="RxLR-dEER"
FT /evidence="ECO:0000305|PubMed:21653195"
FT COMPBIAS 30..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 123 AA; 13259 MW; 394E442DCFCE6DCA CRC64;
MLPVAVVLVV FAVAVTSAES IHQVNPLPRR RRLKGTEEKG HHTNVNDEER VISLESASDL
ISKLKVKINA KLLAGDSAKP ATLSKAQVAS VAKEVVKEVK KTPKVWPPPM IKKGVRRGAG
GVR
