ATR13_HYAAB
ID ATR13_HYAAB Reviewed; 154 AA.
AC Q5G7K8;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Avirulence 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 (Peronospora arabidopsidis).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Hyaloperonospora.
OX NCBI_TaxID=272952;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=Emco5, and Goco1;
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 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 [3]
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 [4]
RP FUNCTION, AND DOMAIN.
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 [5]
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 [6]
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 [7] {ECO:0007744|PDB:2LAI}
RP STRUCTURE BY NMR OF 54-154, FUNCTION, MUTAGENESIS OF PHE-73 AND THR-119,
RP 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 The allele ATR13-Emco5 recognizes RPP13-Nd, the RPP13 defense protein
CC from Arabidopsis thaliana ecotype Niederzenz (PubMed:19523099).
CC {ECO:0000269|PubMed:15591208, ECO:0000269|PubMed:18165328,
CC ECO:0000269|PubMed:18198274, ECO:0000269|PubMed:19523099,
CC ECO:0000269|PubMed:22194907}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22194684}. Host
CC cytoplasm {ECO:0000269|PubMed:22194684}. Note=Localizes to the
CC cytoplasmic scaffolding and to discrete punctate spots along these
CC strands. {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:0000305|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-119 and Arg-148 are
CC critical for recognition by A.thaliana RPP13-Nd.
CC {ECO:0000305|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-Emco5 is recognized by RPP13-Nd because it has the
CC critical residues Phe-73, as well as Thr-119 and Arg-148 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; AY785305; AAW63767.1; -; Genomic_DNA.
DR EMBL; AY785306; AAW63768.1; -; Genomic_DNA.
DR PDB; 2LAI; NMR; -; A=54-154.
DR PDBsum; 2LAI; -.
DR AlphaFoldDB; Q5G7K8; -.
DR SMR; Q5G7K8; -.
DR VEuPathDB; FungiDB:HpaG813534; -.
DR PHI-base; PHI:2402; -.
DR PHI-base; PHI:2410; -.
DR PHI-base; PHI:2423; -.
DR PHI-base; PHI:4754; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR Gene3D; 1.25.40.640; -; 1.
DR InterPro; IPR031791; ATR13.
DR InterPro; IPR038525; ATR13_sf.
DR Pfam; PF16829; ATR13; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host cytoplasm; Secreted; Signal; Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..154
FT /note="Avirulence protein ATR13"
FT /id="PRO_5007705857"
FT REGION 50..92
FT /note="Leucine heptad repeat region"
FT /evidence="ECO:0000305|PubMed:18198274"
FT REGION 93..103
FT /note="Single repeat region"
FT /evidence="ECO:0000305|PubMed:18198274"
FT REGION 104..154
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:19047742"
FT MUTAGEN 73
FT /note="F->N: Leads the loss of recognition (LOR) by RPP13-
FT Nd; when associated with I-119."
FT /evidence="ECO:0000269|PubMed:22194684"
FT MUTAGEN 119
FT /note="T->I: Leads the loss of recognition (LOR) by RPP13-
FT Nd; when associated with N-73."
FT /evidence="ECO:0000269|PubMed:22194684"
FT TURN 70..74
FT /evidence="ECO:0007829|PDB:2LAI"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2LAI"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2LAI"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:2LAI"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:2LAI"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:2LAI"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:2LAI"
FT HELIX 123..135
FT /evidence="ECO:0007829|PDB:2LAI"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:2LAI"
FT HELIX 141..147
FT /evidence="ECO:0007829|PDB:2LAI"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:2LAI"
SQ SEQUENCE 154 AA; 16884 MW; C814822C986E0286 CRC64;
MRLVHAVLLP GIIVFVSNGN LLHAHALHED ETGVTAGRQL RAAASEVFGL SRASFGLGKA
QDPLDKFFSK IIFSGKPIET SYSAKGIHEK IIEAHDLHVS KSKNAPIQYA SVMEYLKKTY
PGPDIERIVS TLERHDEVGA KDLGAKLRDA LDRQ
