RAR1_ARATH
ID RAR1_ARATH Reviewed; 226 AA.
AC Q9SE33; Q9FLI9;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Cysteine and histidine-rich domain-containing protein RAR1;
DE AltName: Full=AtRAR1;
DE AltName: Full=CHORD domain-containing protein RAR1;
DE AltName: Full=Protein PPHB SUSCEPTIBLE 2;
DE AltName: Full=Protein REQUIRED FOR MLA12 RESISTANCE 1;
GN Name=RAR1; Synonyms=PBS2, RPR2; OrderedLocusNames=At5g51700;
GN ORFNames=MIO24.17;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=10571178; DOI=10.1016/s0092-8674(00)81522-6;
RA Shirasu K., Lahaye T., Tan M.-W., Zhou F., Azevedo C., Schulze-Lefert P.;
RT "A novel class of eukaryotic zinc-binding proteins is required for disease
RT resistance signaling in barley and development in C. elegans.";
RL Cell 99:355-366(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=12034891; DOI=10.1105/tpc.001040;
RA Muskett P.R., Kahn K., Austin M.J., Moisan L.J., Sadanandom A., Shirasu K.,
RA Jones J.D., Parker J.E.;
RT "Arabidopsis RAR1 exerts rate-limiting control of R gene-mediated defenses
RT against multiple pathogens.";
RL Plant Cell 14:979-992(2002).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=12034893; DOI=10.1105/tpc.001032;
RA Tornero P., Merritt P., Sadanandom A., Shirasu K., Innes R.W., Dangl J.L.;
RT "RAR1 and NDR1 contribute quantitatively to disease resistance in
RT Arabidopsis, and their relative contributions are dependent on the R gene
RT assayed.";
RL Plant Cell 14:1005-1015(2002).
RN [7]
RP INTERACTION WITH SGT1A AND SGT1B.
RX PubMed=11847307; DOI=10.1126/science.1067554;
RA Azevedo C., Sadanandom A., Kitagawa K., Freialdenhoven A., Shirasu K.,
RA Schulze-Lefert P.;
RT "The RAR1 interactor SGT1, an essential component of R gene-triggered
RT disease resistance.";
RL Science 295:2073-2076(2002).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=11847308; DOI=10.1126/science.1067747;
RA Austin M.J., Muskett P., Kahn K., Feys B.J., Jones J.D., Parker J.E.;
RT "Regulatory role of SGT1 in early R gene-mediated plant defenses.";
RL Science 295:2077-2080(2002).
RN [9]
RP FUNCTION, AND INTERACTION WITH HSP90-2.
RX PubMed=14592967; DOI=10.1093/emboj/cdg547;
RA Hubert D.A., Tornero P., Belkhadir Y., Krishna P., Takahashi A.,
RA Shirasu K., Dangl J.L.;
RT "Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease
RT resistance protein.";
RL EMBO J. 22:5679-5689(2003).
RN [10]
RP INTERACTION WITH HSP90-1.
RX PubMed=14504384; DOI=10.1073/pnas.2033934100;
RA Takahashi A., Casais C., Ichimura K., Shirasu K.;
RT "HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated
RT disease resistance in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11777-11782(2003).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15976272; DOI=10.1126/science.1109977;
RA Holt B.F. III, Belkhadir Y., Dangl J.L.;
RT "Antagonistic control of disease resistance protein stability in the plant
RT immune system.";
RL Science 309:929-932(2005).
RN [12]
RP FUNCTION, AND INTERACTION WITH SGT1B AND HSP90-1.
RX PubMed=17148606; DOI=10.1073/pnas.0607279103;
RA Shang Y., Li X., Cui H., He P., Thilmony R., Chintamanani S.,
RA Zwiesler-Vollick J., Gopalan S., Tang X., Zhou J.M.;
RT "RAR1, a central player in plant immunity, is targeted by Pseudomonas
RT syringae effector AvrB.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:19200-19205(2006).
RN [13]
RP DOMAIN.
RX PubMed=17279625; DOI=10.1021/bi062174k;
RA Heise C.T., Le Duff C.S., Boter M., Casais C., Airey J.E., Leech A.P.,
RA Amigues B., Guerois R., Moore G.R., Shirasu K., Kleanthous C.;
RT "Biochemical characterization of RAR1 cysteine- and histidine-rich domains
RT (CHORDs): a novel class of zinc-dependent protein-protein interaction
RT modules.";
RL Biochemistry 46:1612-1623(2007).
RN [14]
RP FUNCTION.
RX PubMed=19304739; DOI=10.1093/pcp/pcp044;
RA Kawamura Y., Takenaka S., Hase S., Kubota M., Ichinose Y., Kanayama Y.,
RA Nakaho K., Klessig D.F., Takahashi H.;
RT "Enhanced defense responses in Arabidopsis induced by the cell wall protein
RT fractions from Pythium oligandrum require SGT1, RAR1, NPR1 and JAR1.";
RL Plant Cell Physiol. 50:924-934(2009).
RN [15]
RP FUNCTION, AND INTERACTION WITH HSP90-2.
RX PubMed=19487680; DOI=10.1073/pnas.0904877106;
RA Hubert D.A., He Y., McNulty B.C., Tornero P., Dangl J.L.;
RT "Specific Arabidopsis HSP90.2 alleles recapitulate RAR1 cochaperone
RT function in plant NB-LRR disease resistance protein regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9556-9563(2009).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 149-221 IN COMPLEX WITH SGT1A;
RP BARLEY HSP90 AND ZINC IONS, SUBUNIT, AND MUTAGENESIS OF ARG-14; PRO-38;
RP LYS-45; ILE-153; GLU-170 AND TRP-217.
RX PubMed=20670895; DOI=10.1016/j.molcel.2010.05.010;
RA Zhang M., Kadota Y., Prodromou C., Shirasu K., Pearl L.H.;
RT "Structural basis for assembly of Hsp90-Sgt1-CHORD protein complexes:
RT implications for chaperoning of NLR innate immunity receptors.";
RL Mol. Cell 39:269-281(2010).
CC -!- FUNCTION: Required specifically for plant innate immunity. Is essential
CC for resistance conferred by multiple R genes recognizing different
CC bacterial and oomycete pathogen isolates like avirulent P.syringae or
CC H.parasitica (downy mildew). Contributes additively with SGT1B to RPP5-
CC dependent resistance. Functions as positive regulator of RPS5
CC accumulation by assisting its stabilization. May function as co-
CC chaperone of HSP90-2 to positively regulate the steady-state
CC accumulation of RPM1 and protect it from SGT1-mediated degradation.
CC Acts as negative regulator of pathogen-associated molecular pattern
CC (PAMP)-triggered immunity. {ECO:0000269|PubMed:11847308,
CC ECO:0000269|PubMed:12034891, ECO:0000269|PubMed:12034893,
CC ECO:0000269|PubMed:14592967, ECO:0000269|PubMed:15976272,
CC ECO:0000269|PubMed:17148606, ECO:0000269|PubMed:19304739,
CC ECO:0000269|PubMed:19487680}.
CC -!- SUBUNIT: Interacts with HSP90-1, HSP90-2, SGT1A and SGT1B. Forms a
CC ternary complex with SGT1A and barley HSP90.
CC {ECO:0000269|PubMed:11847307, ECO:0000269|PubMed:14504384,
CC ECO:0000269|PubMed:14592967, ECO:0000269|PubMed:17148606,
CC ECO:0000269|PubMed:19487680, ECO:0000269|PubMed:20670895}.
CC -!- INTERACTION:
CC Q9SE33; Q9SUT5: SGT1B; NbExp=3; IntAct=EBI-1781969, EBI-1581364;
CC Q9SE33; Q0Q0I7: HSP90-2; Xeno; NbExp=4; IntAct=EBI-1781969, EBI-8081141;
CC -!- DOMAIN: The 2 cysteine and histidine-rich (CHORD) domains bind each 2
CC zinc ions, and the plant-specific 20 amino acid cysteine and histidine-
CC containing motif (CCCH motif), located between the two CHORDs, binds 1
CC zinc ion. {ECO:0000269|PubMed:17279625}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC condition. In case of infection, plants loose R gene resistance
CC mediated by RPP4, RPP5, RPS2, RPS4, RPS5 and RPM1.
CC {ECO:0000269|PubMed:11847308, ECO:0000269|PubMed:12034891,
CC ECO:0000269|PubMed:12034893, ECO:0000269|PubMed:15976272}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11239.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF192262; AAF18433.1; -; mRNA.
DR EMBL; AB010074; BAB11239.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96116.1; -; Genomic_DNA.
DR EMBL; AY088919; AAM67225.1; -; mRNA.
DR RefSeq; NP_568762.6; NM_124549.8.
DR PDB; 2XCM; X-ray; 2.20 A; E/F=149-221.
DR PDBsum; 2XCM; -.
DR AlphaFoldDB; Q9SE33; -.
DR SMR; Q9SE33; -.
DR BioGRID; 20489; 6.
DR DIP; DIP-41228N; -.
DR IntAct; Q9SE33; 6.
DR MINT; Q9SE33; -.
DR STRING; 3702.AT5G51700.1; -.
DR iPTMnet; Q9SE33; -.
DR PaxDb; Q9SE33; -.
DR PRIDE; Q9SE33; -.
DR ProteomicsDB; 236614; -.
DR EnsemblPlants; AT5G51700.1; AT5G51700.1; AT5G51700.
DR GeneID; 835244; -.
DR Gramene; AT5G51700.1; AT5G51700.1; AT5G51700.
DR KEGG; ath:AT5G51700; -.
DR Araport; AT5G51700; -.
DR TAIR; locus:2165316; AT5G51700.
DR eggNOG; KOG1667; Eukaryota.
DR HOGENOM; CLU_040079_2_0_1; -.
DR InParanoid; Q9SE33; -.
DR OMA; MKQWSCC; -.
DR OrthoDB; 1163528at2759; -.
DR PhylomeDB; Q9SE33; -.
DR EvolutionaryTrace; Q9SE33; -.
DR PRO; PR:Q9SE33; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SE33; baseline and differential.
DR Genevisible; Q9SE33; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0051879; F:Hsp90 protein binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0009626; P:plant-type hypersensitive response; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:TAIR.
DR GO; GO:0002679; P:respiratory burst involved in defense response; IMP:UniProtKB.
DR InterPro; IPR007051; CHORD_dom.
DR InterPro; IPR043316; RAR1.
DR PANTHER; PTHR47895; PTHR47895; 1.
DR Pfam; PF04968; CHORD; 2.
DR PROSITE; PS51401; CHORD; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Immunity; Innate immunity; Metal-binding; Plant defense;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..226
FT /note="Cysteine and histidine-rich domain-containing
FT protein RAR1"
FT /id="PRO_0000403646"
FT DOMAIN 12..71
FT /note="CHORD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT DOMAIN 159..218
FT /note="CHORD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT MOTIF 104..124
FT /note="CCCH"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:20670895,
FT ECO:0007744|PDB:2XCM"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:20670895,
FT ECO:0007744|PDB:2XCM"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:20670895,
FT ECO:0007744|PDB:2XCM"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:20670895,
FT ECO:0007744|PDB:2XCM"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:20670895,
FT ECO:0007744|PDB:2XCM"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:20670895,
FT ECO:0007744|PDB:2XCM"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:20670895,
FT ECO:0007744|PDB:2XCM"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:20670895,
FT ECO:0007744|PDB:2XCM"
FT MUTAGEN 14
FT /note="R->D: No effect on the interaction with SGT1A and
FT barley HSP90."
FT /evidence="ECO:0000269|PubMed:20670895"
FT MUTAGEN 38
FT /note="P->L: Diminishes the interaction with barley HSP90.
FT No effect on the interaction with SGT1A."
FT /evidence="ECO:0000269|PubMed:20670895"
FT MUTAGEN 45
FT /note="K->E: Diminishes the interaction with barley HSP90.
FT No effect on the interaction with SGT1A."
FT /evidence="ECO:0000269|PubMed:20670895"
FT MUTAGEN 153
FT /note="I->Q: Disrupts the interaction with SGT1A. No effect
FT on the interaction with barley HSP90."
FT /evidence="ECO:0000269|PubMed:20670895"
FT MUTAGEN 170
FT /note="E->K: Disrupts the interaction with SGT1A. No effect
FT on the interaction with barley HSP90."
FT /evidence="ECO:0000269|PubMed:20670895"
FT MUTAGEN 217
FT /note="W->T: Disrupts the interaction with SGT1A. No effect
FT on the interaction with barley HSP90."
FT /evidence="ECO:0000269|PubMed:20670895"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:2XCM"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:2XCM"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:2XCM"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:2XCM"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:2XCM"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:2XCM"
SQ SEQUENCE 226 AA; 24961 MW; F8F9D30B9BF3A51E CRC64;
MEVGSATKKL QCQRIGCNAM FTDDDNPQGS CQFHASGPFF HDGMKEWSCC KQRSHDFSLF
LEIPGCKTGK HTTEKPVLAK SVPKHPVAAP TSSPDANAAT KDSCSRCRQG FFCSDHGSQP
KEQIKQTLNT PGQAEEEKIE PLAPPVQKAV IDINQPQVCK NKGCGQTFKE RDNHETACSH
HPGPAVFHDR LRGWKCCDVH VKEFDEFMEI PPCTKGWHSS SPDPAV
