ATR13_HYAAE
ID ATR13_HYAAE Reviewed; 187 AA.
AC M4C367; Q5G7L2;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Virulence protein ATR13 {ECO:0000303|PubMed:15591208};
DE AltName: Full=Arabidopsis thaliana recognized protein 13 {ECO:0000303|PubMed:15591208};
DE Flags: Precursor;
GN Name=ATR13 {ECO:0000303|PubMed:15591208};
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], AND FUNCTION.
RC STRAIN=Emoy2;
RX PubMed=15591208; DOI=10.1126/science.1104022;
RA Allen R.L., Bittner-Eddy P.D., Grenville-Briggs L.J., Meitz J.C.,
RA Rehmany A.P., Rose L.E., Beynon J.L.;
RT "Host-parasite coevolutionary conflict between Arabidopsis and downy
RT mildew.";
RL Science 306:1957-1960(2004).
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 FUNCTION.
RX PubMed=18165328; DOI=10.1105/tpc.107.054262;
RA Sohn K.H., Lei R., Nemri A., Jones J.D.;
RT "The downy mildew effector proteins ATR1 and ATR13 promote disease
RT susceptibility in Arabidopsis thaliana.";
RL Plant Cell 19:4077-4090(2007).
RN [5]
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 [6]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF ILE-152.
RX PubMed=18198274; DOI=10.1073/pnas.0711215105;
RA Rentel M.C., Leonelli L., Dahlbeck D., Zhao B., Staskawicz B.J.;
RT "Recognition of the Hyaloperonospora parasitica effector ATR13 triggers
RT resistance against oomycete, bacterial, and viral pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:1091-1096(2008).
RN [7]
RP FUNCTION.
RX PubMed=19523099; DOI=10.1111/j.1364-3703.2009.00544.x;
RA Hall S.A., Allen R.L., Baumber R.E., Baxter L.A., Fisher K.,
RA Bittner-Eddy P.D., Rose L.E., Holub E.B., Beynon J.L.;
RT "Maintenance of genetic variation in plants and pathogens involves complex
RT networks of gene-for-gene interactions.";
RL Mol. Plant Pathol. 10:449-457(2009).
RN [8]
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 [9]
RP FUNCTION, MUTAGENESIS OF ASN-73 AND ILE-152, AND SUBCELLULAR LOCATION.
RX PubMed=22194684; DOI=10.1371/journal.ppat.1002428;
RA Leonelli L., Pelton J., Schoeffler A., Dahlbeck D., Berger J., Wemmer D.E.,
RA Staskawicz B.;
RT "Structural elucidation and functional characterization of the
RT Hyaloperonospora arabidopsidis effector protein ATR13.";
RL PLoS Pathog. 7:E1002428-E1002428(2011).
CC -!- FUNCTION: Secreted effector that acts as an elicitor of hypersensitive
CC response (HR) specifically on plants carrying defense protein RPP13.
CC Recognition of ATR13 by RPP13 initiates defense responses that are
CC effective against oomycete, bacterial and viral pathogens
CC (PubMed:15591208, PubMed:18165328, PubMed:18198274, PubMed:22194907).
CC Due to high polymorphism, ATR13-Emoy2 does not recognize RPP13-Nd, the
CC RPP13 defense protein from Arabidopsis thaliana ecotype Niederzenz
CC (PubMed:15591208, PubMed:18165328, PubMed:18198274, PubMed:22194684).
CC ATR13-Emoy2 is recognized by RPP13 variants RPP13-UKID44, RPP13-UKID65
CC and RPP13-UKID71 (PubMed:19523099). {ECO:0000269|PubMed:15591208,
CC ECO:0000269|PubMed:18165328, ECO:0000269|PubMed:18198274,
CC ECO:0000269|PubMed:19523099, ECO:0000269|PubMed:22194684,
CC ECO:0000269|PubMed:22194907}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22194684}. Host
CC nucleus, host nucleolus {ECO:0000269|PubMed:22194684}. Host cytoplasm
CC {ECO:0000269|PubMed:22194684}. Note=Localizes to the cytoplasmic
CC scaffolding and to discrete punctate spots along these strands.
CC {ECO:0000269|PubMed:22194684}.
CC -!- DOMAIN: Has the canonical translocation motif RxLR, but lacks the
CC canonical EER motif, which characterizes most oomycete effectors
CC identified so far. {ECO:0000305|PubMed:19047742}.
CC -!- DOMAIN: The leucine heptad repeat region contains five protein variants
CC with 12 amino acid polymorphisms. Leucine heptad repeats are a feature
CC of coiled coils where the leucines are embedded in an alpha helical
CC region. Three of the different variants were recognized by RPP13-Nd,
CC suggesting that alteration of the amino acid sequence in this region is
CC tolerated. {ECO:0000269|PubMed:18198274}.
CC -!- DOMAIN: All ATR13 variants contain at least one 11-amino-acid direct
CC repeat region. This region is involved in nucleolar localization. A
CC single repeat unit is found in ATR13-Aswa1, ATR13-Emco5, ATR13-Goco1-A
CC and ATR13-Goco1-B (ATR13-Hind2 has one repeat unit followed by an
CC additional 3 amino acids), preventing nucleolar localization, whereas
CC three units are present in ATR13-Bico1, ATR13-Waco5 and ATR13-Wela3,
CC and four units are present in ATR13-Maks9, ATR13-Hiks1, ATR13-Cala2,
CC ATR13-Cand5, ATR13-Hind4, ATR13-Emwa1-A, ATR13-Emwa1-B, ATR13-Emoy2,
CC ATR13-Noks1 and ATR13-Ahnd1. In addition there are 14 polymorphic
CC positions, resulting in a total of seven variant forms within this
CC domain. No association between the number or sequence identity of these
CC repeats and recognition by RPP13-Nd could be detected.
CC {ECO:0000269|PubMed:18198274, ECO:0000269|PubMed:22194684}.
CC -!- DOMAIN: The highly variable C-terminus domain and is involved in the
CC specificity for the recognition by RPP13-Nd. 'Thr-152' and 'Arg-181'
CC are critical for recognition by A.thaliana RPP13-Nd.
CC {ECO:0000269|PubMed:18198274}.
CC -!- MISCELLANEOUS: The ATR13 effector protein is a highly polymorphic
CC member of the RXLR class, yet only a small subset of the polymorphic
CC residues appear to be involved in RPP13Nd-mediated recognition.
CC Polymorphic residues of ATR13 appear as clusters across the surface of
CC the protein. ATR13-Emoy2 is not recognized by RPP13-Nd because it has
CC Ile-152 and Gln-181 rather than 'Thr-152' and 'Arg-181' within the
CC highly variable C-terminus domain. {ECO:0000269|PubMed:15591208,
CC ECO:0000269|PubMed:18198274, ECO:0000269|PubMed:22194684}.
CC -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR EMBL; AY785302; AAW63764.1; -; Genomic_DNA.
DR EMBL; JH598153; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M4C367; -.
DR SMR; M4C367; -.
DR EnsemblProtists; HpaT813534; HpaP813534; HpaG813534.
DR VEuPathDB; FungiDB:HpaG813534; -.
DR HOGENOM; CLU_1450271_0_0_1; -.
DR PHI-base; PHI:2422; -.
DR Proteomes; UP000011713; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR Gene3D; 1.25.40.640; -; 2.
DR InterPro; IPR031791; ATR13.
DR InterPro; IPR038525; ATR13_sf.
DR Pfam; PF16829; ATR13; 2.
PE 1: Evidence at protein level;
KW Host cytoplasm; Host nucleus; Reference proteome; Repeat; Secreted; Signal;
KW Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..187
FT /note="Virulence protein ATR13"
FT /id="PRO_5004049112"
FT REPEAT 93..103
FT /note="1"
FT /evidence="ECO:0000305|PubMed:18198274"
FT REPEAT 104..114
FT /note="2"
FT /evidence="ECO:0000305|PubMed:18198274"
FT REPEAT 115..125
FT /note="3"
FT /evidence="ECO:0000305|PubMed:18198274"
FT REPEAT 126..136
FT /note="4"
FT /evidence="ECO:0000305|PubMed:18198274"
FT REGION 50..92
FT /note="Leucine heptad repeat region"
FT /evidence="ECO:0000305|PubMed:18198274"
FT REGION 93..136
FT /note="4 X 11 AA tandem repeats"
FT /evidence="ECO:0000305|PubMed:18198274"
FT REGION 104..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..187
FT /note="Highly variable C-terminus domain"
FT /evidence="ECO:0000305|PubMed:18198274"
FT MOTIF 38..41
FT /note="RxLR"
FT /evidence="ECO:0000305|PubMed:18198274"
FT COMPBIAS 108..127
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 73
FT /note="N->I,S,Y: Leads the gain of recognition (GOR) by
FT RPP13-Nd."
FT /evidence="ECO:0000269|PubMed:22194684"
FT MUTAGEN 152
FT /note="I->T: Leads to gain of recognition (GOR) by RPP13-
FT Nd."
FT /evidence="ECO:0000269|PubMed:18198274,
FT ECO:0000269|PubMed:22194684"
SQ SEQUENCE 187 AA; 20704 MW; 007ABDE8FBF97CC3 CRC64;
MRLVHAVLLP GIIVFVSNGN LLHAHALHED ETGVTAGRQL RAAASEVFGL SRASFGLGKA
QDPLDKFFRK IINSRKPIET SYSAKGIHEK IIKAYDRHVF ESKKAHDRHV SKSKKAHGRH
VSKSKMAHDR HVSKSEKAPI QYASVADYLK KIYPGTDIER IVSTLKRHDE VGAKDLGAKL
QTAVASQ
