ID   AT392_HYAAE             Reviewed;         187 AA.
AC   M4BUU2;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Avirulence protein ATR39-2 {ECO:0000303|PubMed:22359513};
DE   AltName: Full=Arabidopsis thaliana recognized protein 39-2 {ECO:0000303|PubMed:22359513};
DE   Flags: Precursor;
GN   Name=ATR39-2 {ECO:0000303|PubMed:22359513};
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 [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   [2]
RP   IDENTIFICATION.
RC   STRAIN=Emoy2;
RG   EnsemblProtists;
RL   Submitted (JUN-2015) to UniProtKB.
RN   [3]
RP   FUNCTION, AND MUTAGENESIS OF 168-GLU-VAL-169.
RX   PubMed=22359513; DOI=10.1371/journal.pgen.1002502;
RA   Goritschnig S., Krasileva K.V., Dahlbeck D., Staskawicz B.J.;
RT   "Computational prediction and molecular characterization of an oomycete
RT   effector and the cognate Arabidopsis resistance gene.";
RL   PLoS Genet. 8:E1002502-E1002502(2012).
CC   -!- FUNCTION: Secreted effector that acts as an elicitor of hypersensitive
CC       response (HR) specifically on plants carrying defense protein RPP39
CC       (PubMed:22359513). The allele ATR39-1 is recognized by RPP39, whereas
CC       the ATR39-2 allele is nor recognized (PubMed:22359513).
CC       {ECO:0000269|PubMed:22359513}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:22359513}. Host cell
CC       {ECO:0000305|PubMed:22359513}.
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:22359513}.
CC   -!- MISCELLANEOUS: ATR39 has 2 polymorphic alleles that are highly
CC       conserved among Hyaloperonospora arabidopsidis isolate. This
CC       conservation is in stark contrast with other characterized
CC       H.arabidopsidis effectors ATR1, ATR5 and ATR13, which are highly
CC       divergent. The presence of amino acids Glu-168 and Val-169 in ATR39-2
CC       blocks recognition by host defense protein RPP39.
CC       {ECO:0000269|PubMed:22359513}.
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; JH597954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; M4BUU2; -.
DR   EnsemblProtists; HpaT810281; HpaP810281; HpaG810281.
DR   VEuPathDB; FungiDB:HpaG810281; -.
DR   HOGENOM; CLU_1450268_0_0_1; -.
DR   Proteomes; UP000011713; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0043657; C:host cell; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Reference proteome; Secreted; Signal; Virulence.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..187
FT                   /note="Avirulence protein ATR39-2"
FT                   /id="PRO_5004048953"
FT   MOTIF           49..66
FT                   /note="RxLR-dEER"
FT                   /evidence="ECO:0000305|PubMed:22359513"
FT   MUTAGEN         168..169
FT                   /note="Missing: Results in a gain of recognition by host
FT                   defense protein RPP39."
FT                   /evidence="ECO:0000269|PubMed:22359513"
SQ   SEQUENCE   187 AA;  20405 MW;  115BCC56ECDC9C2F CRC64;
     MVKCTPLLAL TVIVSAGSDA LSDPTVKRLA KLATINQAPA TQSNSDSKRV LRASDVPNEV
     AAGESRSPKS LWPWEVEDKL APLKEKLIST SADDLEAGGS AKKNALPMTW RWLWQNQIET
     KKTPIDEISK EVQTAMDLIS SKATHEELNK AGVSVSDYVK ALKLTLPEVD VDVVNRGMEY
     NIHLGNK