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Cysteine and histidine-rich domain-containing protein RAR1 (AtRAR1) (CHORD domain-containing protein RAR1) (Protein PPHB SUSCEPTIBLE 2) (Protein REQUIRED FOR MLA12 RESISTANCE 1)

 RAR1_ARATH              Reviewed;         226 AA.
Q9SE33; Q9FLI9;
11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
07-JUN-2017, entry version 86.
RecName: Full=Cysteine and histidine-rich domain-containing protein RAR1;
AltName: Full=AtRAR1;
AltName: Full=CHORD domain-containing protein RAR1;
AltName: Full=Protein PPHB SUSCEPTIBLE 2;
AltName: Full=Protein REQUIRED FOR MLA12 RESISTANCE 1;
Name=RAR1; Synonyms=PBS2, RPR2; OrderedLocusNames=At5g51700;
ORFNames=MIO24.17;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
PubMed=10571178; DOI=10.1016/S0092-8674(00)81522-6;
Shirasu K., Lahaye T., Tan M.-W., Zhou F., Azevedo C.,
Schulze-Lefert P.;
"A novel class of eukaryotic zinc-binding proteins is required for
disease resistance signaling in barley and development in C.
elegans.";
Cell 99:355-366(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9628582; DOI=10.1093/dnares/5.1.41;
Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. IV.
Sequence features of the regions of 1,456,315 bp covered by nineteen
physically assigned P1 and TAC clones.";
DNA Res. 5:41-54(1998).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia, and cv. Landsberg erecta;
PubMed=12034891; DOI=10.1105/tpc.001040;
Muskett P.R., Kahn K., Austin M.J., Moisan L.J., Sadanandom A.,
Shirasu K., Jones J.D., Parker J.E.;
"Arabidopsis RAR1 exerts rate-limiting control of R gene-mediated
defenses against multiple pathogens.";
Plant Cell 14:979-992(2002).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=12034893; DOI=10.1105/tpc.001032;
Tornero P., Merritt P., Sadanandom A., Shirasu K., Innes R.W.,
Dangl J.L.;
"RAR1 and NDR1 contribute quantitatively to disease resistance in
Arabidopsis, and their relative contributions are dependent on the R
gene assayed.";
Plant Cell 14:1005-1015(2002).
[7]
INTERACTION WITH SGT1A AND SGT1B.
PubMed=11847307; DOI=10.1126/science.1067554;
Azevedo C., Sadanandom A., Kitagawa K., Freialdenhoven A., Shirasu K.,
Schulze-Lefert P.;
"The RAR1 interactor SGT1, an essential component of R gene-triggered
disease resistance.";
Science 295:2073-2076(2002).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia, and cv. Landsberg erecta;
PubMed=11847308; DOI=10.1126/science.1067747;
Austin M.J., Muskett P., Kahn K., Feys B.J., Jones J.D., Parker J.E.;
"Regulatory role of SGT1 in early R gene-mediated plant defenses.";
Science 295:2077-2080(2002).
[9]
FUNCTION, AND INTERACTION WITH HSP90-2.
PubMed=14592967; DOI=10.1093/emboj/cdg547;
Hubert D.A., Tornero P., Belkhadir Y., Krishna P., Takahashi A.,
Shirasu K., Dangl J.L.;
"Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1
disease resistance protein.";
EMBO J. 22:5679-5689(2003).
[10]
INTERACTION WITH HSP90-1.
PubMed=14504384; DOI=10.1073/pnas.2033934100;
Takahashi A., Casais C., Ichimura K., Shirasu K.;
"HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated
disease resistance in Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 100:11777-11782(2003).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15976272; DOI=10.1126/science.1109977;
Holt B.F. III, Belkhadir Y., Dangl J.L.;
"Antagonistic control of disease resistance protein stability in the
plant immune system.";
Science 309:929-932(2005).
[12]
FUNCTION, AND INTERACTION WITH SGT1B AND HSP90-1.
PubMed=17148606; DOI=10.1073/pnas.0607279103;
Shang Y., Li X., Cui H., He P., Thilmony R., Chintamanani S.,
Zwiesler-Vollick J., Gopalan S., Tang X., Zhou J.M.;
"RAR1, a central player in plant immunity, is targeted by Pseudomonas
syringae effector AvrB.";
Proc. Natl. Acad. Sci. U.S.A. 103:19200-19205(2006).
[13]
DOMAIN.
PubMed=17279625; DOI=10.1021/bi062174k;
Heise C.T., Le Duff C.S., Boter M., Casais C., Airey J.E., Leech A.P.,
Amigues B., Guerois R., Moore G.R., Shirasu K., Kleanthous C.;
"Biochemical characterization of RAR1 cysteine- and histidine-rich
domains (CHORDs): a novel class of zinc-dependent protein-protein
interaction modules.";
Biochemistry 46:1612-1623(2007).
[14]
FUNCTION.
PubMed=19304739; DOI=10.1093/pcp/pcp044;
Kawamura Y., Takenaka S., Hase S., Kubota M., Ichinose Y.,
Kanayama Y., Nakaho K., Klessig D.F., Takahashi H.;
"Enhanced defense responses in Arabidopsis induced by the cell wall
protein fractions from Pythium oligandrum require SGT1, RAR1, NPR1 and
JAR1.";
Plant Cell Physiol. 50:924-934(2009).
[15]
FUNCTION, AND INTERACTION WITH HSP90-2.
PubMed=19487680; DOI=10.1073/pnas.0904877106;
Hubert D.A., He Y., McNulty B.C., Tornero P., Dangl J.L.;
"Specific Arabidopsis HSP90.2 alleles recapitulate RAR1 cochaperone
function in plant NB-LRR disease resistance protein regulation.";
Proc. Natl. Acad. Sci. U.S.A. 106:9556-9563(2009).
[16]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 149-221 IN COMPLEX WITH
SGT1A; BARLEY HSP90 AND ZINC IONS, SUBUNIT, AND MUTAGENESIS OF ARG-14;
PRO-38; LYS-45; ILE-153; GLU-170 AND TRP-217.
PubMed=20670895; DOI=10.1016/j.molcel.2010.05.010;
Zhang M., Kadota Y., Prodromou C., Shirasu K., Pearl L.H.;
"Structural basis for assembly of Hsp90-Sgt1-CHORD protein complexes:
implications for chaperoning of NLR innate immunity receptors.";
Mol. Cell 39:269-281(2010).
-!- FUNCTION: Required specifically for plant innate immunity. Is
essential for resistance conferred by multiple R genes recognizing
different bacterial and oomycete pathogen isolates like avirulent
P.syringae or H.parasitica (downy mildew). Contributes additively
with SGT1B to RPP5-dependent resistance. Functions as positive
regulator of RPS5 accumulation by assisting its stabilization. May
function as co-chaperone of HSP90-2 to positively regulate the
steady-state accumulation of RPM1 and protect it from SGT1-
mediated degradation. Acts as negative regulator of pathogen-
associated molecular pattern (PAMP)-triggered immunity.
{ECO:0000269|PubMed:11847308, ECO:0000269|PubMed:12034891,
ECO:0000269|PubMed:12034893, ECO:0000269|PubMed:14592967,
ECO:0000269|PubMed:15976272, ECO:0000269|PubMed:17148606,
ECO:0000269|PubMed:19304739, ECO:0000269|PubMed:19487680}.
-!- SUBUNIT: Interacts with HSP90-1, HSP90-2, SGT1A and SGT1B. Forms a
ternary complex with SGT1A and barley HSP90.
{ECO:0000269|PubMed:11847307, ECO:0000269|PubMed:14504384,
ECO:0000269|PubMed:14592967, ECO:0000269|PubMed:17148606,
ECO:0000269|PubMed:19487680, ECO:0000269|PubMed:20670895}.
-!- INTERACTION:
Q0Q0I7:HSP90-2 (xeno); NbExp=4; IntAct=EBI-1781969, EBI-8081141;
-!- DOMAIN: The 2 cysteine and histidine-rich (CHORD) domains bind
each 2 zinc ions, and the plant-specific 20 amino acid cysteine
and histidine-containing motif (CCCH motif), located between the
two CHORDs, binds 1 zinc ion. {ECO:0000269|PubMed:17279625}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
condition. In case of infection, plants loose R gene resistance
mediated by RPP4, RPP5, RPS2, RPS4, RPS5 and RPM1.
{ECO:0000269|PubMed:11847308, ECO:0000269|PubMed:12034891,
ECO:0000269|PubMed:12034893, ECO:0000269|PubMed:15976272}.
-!- SEQUENCE CAUTION:
Sequence=BAB11239.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF192262; AAF18433.1; -; mRNA.
EMBL; AB010074; BAB11239.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002688; AED96116.1; -; Genomic_DNA.
EMBL; AY088919; AAM67225.1; -; mRNA.
RefSeq; NP_568762.6; NM_124549.8.
UniGene; At.9103; -.
PDB; 2XCM; X-ray; 2.20 A; E/F=149-221.
PDBsum; 2XCM; -.
ProteinModelPortal; Q9SE33; -.
SMR; Q9SE33; -.
BioGrid; 20489; 6.
DIP; DIP-41228N; -.
IntAct; Q9SE33; 4.
MINT; MINT-232429; -.
STRING; 3702.AT5G51700.1; -.
iPTMnet; Q9SE33; -.
PaxDb; Q9SE33; -.
EnsemblPlants; AT5G51700.1; AT5G51700.1; AT5G51700.
GeneID; 835244; -.
Gramene; AT5G51700.1; AT5G51700.1; AT5G51700.
KEGG; ath:AT5G51700; -.
Araport; AT5G51700; -.
TAIR; locus:2165316; AT5G51700.
eggNOG; KOG1667; Eukaryota.
eggNOG; ENOG410XPV6; LUCA.
HOGENOM; HOG000265320; -.
InParanoid; Q9SE33; -.
KO; K13458; -.
OMA; GSCQYHP; -.
OrthoDB; EOG09360KV4; -.
PhylomeDB; Q9SE33; -.
EvolutionaryTrace; Q9SE33; -.
PRO; PR:Q9SE33; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9SE33; baseline and differential.
Genevisible; Q9SE33; AT.
GO; GO:0051879; F:Hsp90 protein binding; IPI:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
GO; GO:0009816; P:defense response to bacterium, incompatible interaction; IMP:UniProtKB.
GO; GO:0009817; P:defense response to fungus, incompatible interaction; IMP:UniProtKB.
GO; GO:0009626; P:plant-type hypersensitive response; IMP:UniProtKB.
GO; GO:0050821; P:protein stabilization; IMP:TAIR.
GO; GO:0002679; P:respiratory burst involved in defense response; IMP:UniProtKB.
InterPro; IPR007051; CHORD_dom.
Pfam; PF04968; CHORD; 2.
PROSITE; PS51401; CHORD; 2.
1: Evidence at protein level;
3D-structure; Complete proteome; Immunity; Innate immunity;
Metal-binding; Plant defense; Reference proteome; Repeat; Zinc.
CHAIN 1 226 Cysteine and histidine-rich domain-
containing protein RAR1.
/FTId=PRO_0000403646.
DOMAIN 12 71 CHORD 1. {ECO:0000255|PROSITE-
ProRule:PRU00734}.
DOMAIN 159 218 CHORD 2. {ECO:0000255|PROSITE-
ProRule:PRU00734}.
MOTIF 104 124 CCCH.
METAL 12 12 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00734}.
METAL 17 17 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00734}.
METAL 31 31 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00734}.
METAL 34 34 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00734}.
METAL 49 49 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00734}.
METAL 50 50 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00734}.
METAL 66 66 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00734}.
METAL 71 71 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00734}.
METAL 159 159 Zinc 3. {ECO:0000244|PDB:2XCM,
ECO:0000269|PubMed:20670895}.
METAL 164 164 Zinc 3. {ECO:0000244|PDB:2XCM,
ECO:0000269|PubMed:20670895}.
METAL 178 178 Zinc 3. {ECO:0000244|PDB:2XCM,
ECO:0000269|PubMed:20670895}.
METAL 181 181 Zinc 4. {ECO:0000244|PDB:2XCM,
ECO:0000269|PubMed:20670895}.
METAL 196 196 Zinc 4. {ECO:0000244|PDB:2XCM,
ECO:0000269|PubMed:20670895}.
METAL 197 197 Zinc 4. {ECO:0000244|PDB:2XCM,
ECO:0000269|PubMed:20670895}.
METAL 213 213 Zinc 4. {ECO:0000244|PDB:2XCM,
ECO:0000269|PubMed:20670895}.
METAL 218 218 Zinc 3. {ECO:0000244|PDB:2XCM,
ECO:0000269|PubMed:20670895}.
MUTAGEN 14 14 R->D: No effect on the interaction with
SGT1A and barley HSP90.
{ECO:0000269|PubMed:20670895}.
MUTAGEN 38 38 P->L: Diminishes the interaction with
barley HSP90. No effect on the
interaction with SGT1A.
{ECO:0000269|PubMed:20670895}.
MUTAGEN 45 45 K->E: Diminishes the interaction with
barley HSP90. No effect on the
interaction with SGT1A.
{ECO:0000269|PubMed:20670895}.
MUTAGEN 153 153 I->Q: Disrupts the interaction with
SGT1A. No effect on the interaction with
barley HSP90.
{ECO:0000269|PubMed:20670895}.
MUTAGEN 170 170 E->K: Disrupts the interaction with
SGT1A. No effect on the interaction with
barley HSP90.
{ECO:0000269|PubMed:20670895}.
MUTAGEN 217 217 W->T: Disrupts the interaction with
SGT1A. No effect on the interaction with
barley HSP90.
{ECO:0000269|PubMed:20670895}.
STRAND 178 181 {ECO:0000244|PDB:2XCM}.
STRAND 185 188 {ECO:0000244|PDB:2XCM}.
STRAND 191 194 {ECO:0000244|PDB:2XCM}.
TURN 195 198 {ECO:0000244|PDB:2XCM}.
HELIX 204 207 {ECO:0000244|PDB:2XCM}.
STRAND 214 216 {ECO:0000244|PDB:2XCM}.
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


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