AVH6_PHYSP
ID AVH6_PHYSP Reviewed; 125 AA.
AC G4ZLE6; L7WWG5;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 25-MAY-2022, entry version 23.
DE RecName: Full=RxLR effector protein Avh6 {ECO:0000303|PubMed:23550527};
DE AltName: Full=Avirulence homolog protein 6 {ECO:0000303|PubMed:23550527};
DE AltName: Full=Avirulence protein 1d {ECO:0000303|PubMed:23550527};
DE Flags: Precursor;
GN Name=Avh6 {ECO:0000303|PubMed:23550527};
GN Synonyms=Avh6-1 {ECO:0000303|PubMed:23550527},
GN Avr1d {ECO:0000303|PubMed:23550527};
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 [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE,
RP PTDINS(4)P-BINDING, AND MUTAGENESIS OF 48-ARG--ARG-51 AND 104-LYS--LYS-107.
RC STRAIN=P6497;
RX PubMed=23550527; DOI=10.1094/mpmi-02-13-0036-r;
RA Na R., Yu D., Qutob D., Zhao J., Gijzen M.;
RT "Deletion of the Phytophthora sojae avirulence gene Avr1d causes gain of
RT virulence on Rps1d.";
RL Mol. Plant Microbe Interact. 26:969-976(2013).
RN [2]
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 [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=23594349; DOI=10.1094/mpmi-02-13-0035-r;
RA Yin W., Dong S., Zhai L., Lin Y., Zheng X., Wang Y.;
RT "The Phytophthora sojae Avr1d gene encodes an RxLR-dEER effector with
RT presence and absence polymorphisms among pathogen strains.";
RL Mol. Plant Microbe Interact. 26:958-968(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 (PubMed:23550527). Triggers a
CC hypersensitive response (HR) in the presence of Rps1d (PubMed:23550527,
CC PubMed:23594349). Suppresses BAX-induced cell death and enhan,ced
CC P.capsici infection in Nicotiana benthamiana. Also suppresses effector-
CC triggered immunity induction by associating with Avr1b and Rps1b,
CC suggesting a role in suppressing plant immunity (PubMed:23594349).
CC {ECO:0000269|PubMed:23550527, ECO:0000269|PubMed:23594349}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23550527}. Host cell
CC {ECO:0000305|PubMed:23550527}.
CC -!- INDUCTION: Expression is induced in preinfection structures and during
CC infection. {ECO:0000269|PubMed:23594349}.
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:23550527}.
CC -!- DISRUPTION PHENOTYPE: Leads to the gain of virulence via impairing
CC effector-triggered immunity (ETI) allowed by host resistance (R)
CC protein Rps1d. {ECO:0000269|PubMed:23550527}.
CC -!- MISCELLANEOUS: Avh6 is present in P.sojae strains that are avirulent on
CC Rps1d hosts, whereas the gene is deleted from the genome of virulent
CC strains. {ECO:0000305|PubMed:23550527}.
CC -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR EMBL; KC004057; AGC92778.1; -; Genomic_DNA.
DR EMBL; JH159155; EGZ16228.1; -; Genomic_DNA.
DR RefSeq; XP_009529977.1; XM_009531682.1.
DR PDB; 7C96; X-ray; 2.51 A; A=71-125.
DR PDBsum; 7C96; -.
DR AlphaFoldDB; G4ZLE6; -.
DR SMR; G4ZLE6; -.
DR EnsemblProtists; EGZ16228; EGZ16228; PHYSODRAFT_354880.
DR GeneID; 20649722; -.
DR KEGG; psoj:PHYSODRAFT_354880; -.
DR HOGENOM; CLU_1790698_0_0_1; -.
DR OMA; RSHHTED; -.
DR OrthoDB; 1810651at2759; -.
DR PHI-base; PHI:2941; -.
DR PHI-base; PHI:2943; -.
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 3D-structure; Reference proteome; Secreted; Signal; Virulence.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..125
FT /note="RxLR effector protein Avh6"
FT /id="PRO_5003472330"
FT MOTIF 48..70
FT /note="RxLR-dEER"
FT /evidence="ECO:0000305|PubMed:23550527"
FT MUTAGEN 48..51
FT /note="RFLR->EEEE: Does not affect the phospholipid-binding
FT properties."
FT /evidence="ECO:0000269|PubMed:23550527"
FT MUTAGEN 104..107
FT /note="KKIK->EEEE: Drastically alters lipid-binding."
FT /evidence="ECO:0000269|PubMed:23550527"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:7C96"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:7C96"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:7C96"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:7C96"
SQ SEQUENCE 125 AA; 13979 MW; 55EC1C14E6C6EC31 CRC64;
MRLSSTTFVV LAAVLLASGT AVSKADETGV TNVNAVHSPN VLAGVDKRFL RSHHTEDGEA
KLSNYDNEER NGLFGANTLS NMGKDTILRF QMFTKWKANG YLPKKIKDDI PRSLYKAYKI
HYRMN
