ATR1_HYAAE
ID ATR1_HYAAE Reviewed; 311 AA.
AC M4B6G6; Q4VKJ6;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 25-MAY-2022, entry version 25.
DE RecName: Full=Avirulence protein ATR1 {ECO:0000303|PubMed:15894715};
DE AltName: Full=Arabidopsis thaliana recognized protein 1 {ECO:0000303|PubMed:15894715};
DE Flags: Precursor;
GN Name=ATR1 {ECO:0000303|PubMed:15894715};
GN Synonyms=ATR1-NdWsB {ECO:0000303|PubMed:15894715};
OS Hyaloperonospora arabidopsidis (strain Emoy2) (Downy mildew agent)
OS (Peronospora arabidopsidis).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Hyaloperonospora.
OX NCBI_TaxID=559515;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DOMAIN.
RC STRAIN=Emoy2, Hiks1, and Waco5;
RX PubMed=15894715; DOI=10.1105/tpc.105.031807;
RA Rehmany A.P., Gordon A., Rose L.E., Allen R.L., Armstrong M.R.,
RA Whisson S.C., Kamoun S., Tyler B.M., Birch P.R., Beynon J.L.;
RT "Differential recognition of highly divergent downy mildew avirulence gene
RT alleles by RPP1 resistance genes from two Arabidopsis lines.";
RL Plant Cell 17:1839-1850(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Emoy2;
RX PubMed=21148394; DOI=10.1126/science.1195203;
RA Baxter L., Tripathy S., Ishaque N., Boot N., Cabral A., Kemen E.,
RA Thines M., Ah-Fong A., Anderson R., Badejoko W., Bittner-Eddy P.,
RA Boore J.L., Chibucos M.C., Coates M., Dehal P., Delehaunty K., Dong S.,
RA Downton P., Dumas B., Fabro G., Fronick C., Fuerstenberg S.I., Fulton L.,
RA Gaulin E., Govers F., Hughes L., Humphray S., Jiang R.H., Judelson H.,
RA Kamoun S., Kyung K., Meijer H., Minx P., Morris P., Nelson J.,
RA Phuntumart V., Qutob D., Rehmany A., Rougon-Cardoso A., Ryden P.,
RA Torto-Alalibo T., Studholme D., Wang Y., Win J., Wood J., Clifton S.W.,
RA Rogers J., Van den Ackerveken G., Jones J.D., McDowell J.M., Beynon J.,
RA Tyler B.M.;
RT "Signatures of adaptation to obligate biotrophy in the Hyaloperonospora
RT arabidopsidis genome.";
RL Science 330:1549-1551(2010).
RN [3]
RP IDENTIFICATION.
RC STRAIN=Emoy2;
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
RN [4]
RP DOMAIN.
RX PubMed=19047742; DOI=10.1099/mic.0.2008/021964-0;
RA Grouffaud S., van West P., Avrova A.O., Birch P.R., Whisson S.C.;
RT "Plasmodium falciparum and Hyaloperonospora parasitica effector
RT translocation motifs are functional in Phytophthora infestans.";
RL Microbiology 154:3743-3751(2008).
RN [5]
RP FUNCTION.
RX PubMed=22194907; DOI=10.1371/journal.pone.0028765;
RA Krasileva K.V., Zheng C., Leonelli L., Goritschnig S., Dahlbeck D.,
RA Staskawicz B.J.;
RT "Global analysis of Arabidopsis/downy mildew interactions reveals
RT prevalence of incomplete resistance and rapid evolution of pathogen
RT recognition.";
RL PLoS ONE 6:E28765-E28765(2011).
RN [6]
RP DOMAIN.
RX PubMed=23425855; DOI=10.4161/psb.23865;
RA Yaeno T., Shirasu K.;
RT "The RXLR motif of oomycete effectors is not a sufficient element for
RT binding to phosphatidylinositol monophosphates.";
RL Plant Signal. Behav. 8:E23865-E23865(2013).
RN [7]
RP FUNCTION, AND INTERACTION WITH RPP1-NDA AND RPP1-WSB.
RX PubMed=25671309; DOI=10.1371/journal.ppat.1004665;
RA Steinbrenner A.D., Goritschnig S., Staskawicz B.J.;
RT "Recognition and activation domains contribute to allele-specific responses
RT of an Arabidopsis NLR receptor to an oomycete effector protein.";
RL PLoS Pathog. 11:E1004665-E1004665(2015).
RN [8]
RP FUNCTION, INTERACTION WITH RPP1-ESTA AND RPP1-ZDRA, AND DOMAIN.
RX PubMed=26725254; DOI=10.1111/nph.13823;
RA Goritschnig S., Steinbrenner A.D., Grunwald D.J., Staskawicz B.J.;
RT "Structurally distinct Arabidopsis thaliana NLR immune receptors recognize
RT tandem WY domains of an oomycete effector.";
RL New Phytol. 210:984-996(2016).
RN [9]
RP FUNCTION.
RX PubMed=27427964; DOI=10.1371/journal.ppat.1005769;
RA Schreiber K.J., Bentham A., Williams S.J., Kobe B., Staskawicz B.J.;
RT "Multiple domain associations within the Arabidopsis immune receptor RPP1
RT regulate the activation of programmed cell death.";
RL PLoS Pathog. 12:E1005769-E1005769(2016).
RN [10]
RP FUNCTION.
RX PubMed=29794019; DOI=10.1104/pp.18.00462;
RA Atanasov K.E., Liu C., Erban A., Kopka J., Parker J.E., Alcazar R.;
RT "NLR mutations suppressing immune hybrid incompatibility and their effects
RT on disease resistance.";
RL Plant Physiol. 177:1152-1169(2018).
RN [11] {ECO:0007744|PDB:3RMR}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 52-311, FUNCTION, SUBUNIT, AND
RP DOMAIN.
RX PubMed=21788488; DOI=10.1073/pnas.1109791108;
RA Chou S., Krasileva K.V., Holton J.M., Steinbrenner A.D., Alber T.,
RA Staskawicz B.J.;
RT "Hyaloperonospora arabidopsidis ATR1 effector is a repeat protein with
RT distributed recognition surfaces.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13323-13328(2011).
CC -!- FUNCTION: Secreted effector that acts as an elicitor of hypersensitive
CC response (HR) specifically on plants carrying both defense protein RPP1
CC from several ecotypes including RPP1-NdA, RPP1-WsB, RPP1-EstA and RPP1-
CC ZdrA. {ECO:0000269|PubMed:15894715, ECO:0000269|PubMed:22194907,
CC ECO:0000269|PubMed:25671309, ECO:0000269|PubMed:26725254,
CC ECO:0000269|PubMed:27427964, ECO:0000269|PubMed:29794019}.
CC -!- SUBUNIT: Monomer (PubMed:21788488). Interacts with defense protein RPP1
CC from several ecotypes including RPP1-NdA, RPP1-WsB, RPP1-EstA and RPP1-
CC ZdrA, via their leucine-rich repeats (LLRs) (PubMed:25671309,
CC PubMed:26725254). {ECO:0000269|PubMed:21788488,
CC ECO:0000269|PubMed:25671309, ECO:0000269|PubMed:26725254}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15894715}. Host
CC cytoplasm {ECO:0000269|PubMed:15894715}.
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 (PIP). However ATR1 does not bind to PIPs, even though it
CC harbors the RxLR-dEER motif at the N-terminus, suggesting that the
CC RxLR-dEER motif is insufficient for PIP binding.
CC {ECO:0000269|PubMed:19047742, ECO:0000269|PubMed:23425855,
CC ECO:0000305|PubMed:15894715}.
CC -!- DOMAIN: The tandem repeated WY domains are involved in the recognition
CC of the RPP1 defense proteins of the different Arabidopsis thaliana
CC ecotypes. {ECO:0000269|PubMed:21788488, ECO:0000269|PubMed:26725254}.
CC -!- MISCELLANEOUS: The ATR1 effector protein of Hyaloperonospora
CC arabidopsidis is a polymorphic member of the RXLR class of secreted
CC effectors. The ATR1 alleles are differentially recognized by RPP1 genes
CC from different Arabidopsis ecotypes (Niederzenz, Wassilewskija, Estland
CC and Zdarec). {ECO:0000269|PubMed:15894715, ECO:0000269|PubMed:22194907,
CC ECO:0000269|PubMed:25671309, ECO:0000269|PubMed:26725254}.
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; AY842877; AAX51198.1; -; Genomic_DNA.
DR EMBL; AH014899; AAY58904.1; -; Genomic_DNA.
DR EMBL; AY973540; AAY58900.1; -; Genomic_DNA.
DR EMBL; AY842879; AAX51200.1; -; Genomic_DNA.
DR EMBL; AY842878; AAX51199.1; -; Genomic_DNA.
DR EMBL; JH598543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 3RMR; X-ray; 2.30 A; A/B/C=52-311.
DR PDB; 7CRB; EM; 3.16 A; J=1-311.
DR PDB; 7CRC; EM; 3.02 A; E/F/G/H=1-311.
DR PDBsum; 3RMR; -.
DR PDBsum; 7CRB; -.
DR PDBsum; 7CRC; -.
DR AlphaFoldDB; M4B6G6; -.
DR SMR; M4B6G6; -.
DR EnsemblProtists; HpaT801867; HpaP801867; HpaG801867.
DR VEuPathDB; FungiDB:HpaG801867; -.
DR HOGENOM; CLU_895597_0_0_1; -.
DR PHI-base; PHI:2420; -.
DR PHI-base; PHI:4253; -.
DR PHI-base; PHI:4254; -.
DR PHI-base; PHI:4255; -.
DR PHI-base; PHI:4256; -.
DR PHI-base; PHI:4257; -.
DR PHI-base; PHI:531; -.
DR Proteomes; UP000011713; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:PHI-base.
DR GO; GO:0042025; C:host cell nucleus; IDA:PHI-base.
DR GO; GO:0140418; P:effector-mediated modulation of host process by symbiont; IMP:PHI-base.
PE 1: Evidence at protein level;
KW 3D-structure; Host cytoplasm; Reference proteome; Repeat; Secreted; Signal;
KW Virulence.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..311
FT /note="Avirulence protein ATR1"
FT /id="PRO_5012000082"
FT REGION 127..209
FT /note="WY domain 1"
FT /evidence="ECO:0000305|PubMed:21788488"
FT REGION 210..311
FT /note="WY domain 2"
FT /evidence="ECO:0000305|PubMed:21788488"
FT MOTIF 48..62
FT /note="RxLR-dEER"
FT /evidence="ECO:0000305|PubMed:15894715"
FT HELIX 69..82
FT /evidence="ECO:0007829|PDB:3RMR"
FT HELIX 87..103
FT /evidence="ECO:0007829|PDB:3RMR"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:3RMR"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:3RMR"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:7CRC"
FT HELIX 127..150
FT /evidence="ECO:0007829|PDB:3RMR"
FT HELIX 160..177
FT /evidence="ECO:0007829|PDB:3RMR"
FT HELIX 181..188
FT /evidence="ECO:0007829|PDB:3RMR"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:3RMR"
FT HELIX 199..209
FT /evidence="ECO:0007829|PDB:3RMR"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:3RMR"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:3RMR"
FT HELIX 227..239
FT /evidence="ECO:0007829|PDB:3RMR"
FT HELIX 245..261
FT /evidence="ECO:0007829|PDB:3RMR"
FT HELIX 266..275
FT /evidence="ECO:0007829|PDB:3RMR"
FT HELIX 295..308
FT /evidence="ECO:0007829|PDB:3RMR"
SQ SEQUENCE 311 AA; 35102 MW; 6CE8B86F48628C43 CRC64;
MRVCYFVLVP SVALAVIATE SSETSGTIVH VFPLRDVADH RNDALINRAL RAQTALDDDE
ERWPFGPSAV EALIETIDRH GRVSLNDEAK MKKVVRTWKK LIERDDLIGE IGKHYFEAPG
PLHDTYDEAL ATRLVTTYSD RGVARAILHT RPSDPLSKKA GQAHRLEEAV ASLWKGRGYT
SDNVVSSIAT GHDVDFFAPT AFTFLVKCVE SEDDANNAIF EYFGSNPSRY FSAVLHAMEK
PDADSRVLES SKKWMFQCYA QKQFPTPVFE RTLAAYQSED YAIRGARNHY EKLSLSQIEE
LVEEYSRIYS V
