RAR1_ORYSJ
ID RAR1_ORYSJ Reviewed; 233 AA.
AC Q6EPW7;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Cysteine and histidine-rich domain-containing protein RAR1;
DE AltName: Full=CHORD domain-containing protein RAR1;
DE AltName: Full=OsRAR1;
DE AltName: Full=Protein REQUIRED FOR MLA12 RESISTANCE 1;
GN Name=RAR1; OrderedLocusNames=Os02g0535400, LOC_Os02g33180;
GN ORFNames=B1136H02.25, OJ1112_G07.12;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [3]
RP FUNCTION, AND INTERACTION WITH RAC1 AND SGT1.
RX PubMed=18156216; DOI=10.1105/tpc.107.055517;
RA Thao N.P., Chen L., Nakashima A., Hara S., Umemura K., Takahashi A.,
RA Shirasu K., Kawasaki T., Shimamoto K.;
RT "RAR1 and HSP90 form a complex with Rac/Rop GTPase and function in innate-
RT immune responses in rice.";
RL Plant Cell 19:4035-4045(2007).
RN [4]
RP FUNCTION, INTERACTION WITH SGT1, AND SUBCELLULAR LOCATION.
RX PubMed=18257679; DOI=10.1094/mpmi-21-3-0294;
RA Wang Y., Gao M., Li Q., Wang L., Wang J., Jeon J.S., Qu N., Zhang Y.,
RA He Z.;
RT "OsRAR1 and OsSGT1 physically interact and function in rice basal disease
RT resistance.";
RL Mol. Plant Microbe Interact. 21:294-303(2008).
RN [5]
RP INTERACTION WITH RACK1A.
RX PubMed=18723578; DOI=10.1105/tpc.107.054395;
RA Nakashima A., Chen L., Thao N.P., Fujiwara M., Wong H.L., Kuwano M.,
RA Umemura K., Shirasu K., Kawasaki T., Shimamoto K.;
RT "RACK1 functions in rice innate immunity by interacting with the Rac1
RT immune complex.";
RL Plant Cell 20:2265-2279(2008).
CC -!- FUNCTION: Involved in basal disease resistance to virulent strain of
CC bacterial blight (X.oryzae) and compatible race of rice blast fungus
CC (M.grisea). May act as positive regulator of basal defense. Associates
CC with HSP90 and is essential for the pathogen-associated molecular
CC pattern (PAMP)-triggered immune responses specifically enhanced by
CC RAC1. {ECO:0000269|PubMed:18156216, ECO:0000269|PubMed:18257679}.
CC -!- SUBUNIT: Interacts (via CHORD2 domain) with SGT1 (via CS domain).
CC Interacts with RAC1 and RACK1A. {ECO:0000269|PubMed:18156216,
CC ECO:0000269|PubMed:18257679, ECO:0000269|PubMed:18723578}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18257679}. Nucleus
CC {ECO:0000269|PubMed:18257679}.
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.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD27802.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD29303.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP004156; BAD27802.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP005798; BAD29303.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015623436.1; XM_015767950.1.
DR AlphaFoldDB; Q6EPW7; -.
DR SMR; Q6EPW7; -.
DR STRING; 4530.OS02T0535400-01; -.
DR PaxDb; Q6EPW7; -.
DR PRIDE; Q6EPW7; -.
DR GeneID; 4329567; -.
DR KEGG; osa:4329567; -.
DR eggNOG; KOG1667; Eukaryota.
DR HOGENOM; CLU_040079_2_0_1; -.
DR InParanoid; Q6EPW7; -.
DR OrthoDB; 1163528at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q6EPW7; OS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0051879; F:Hsp90 protein binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; 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 Cytoplasm; Metal-binding; Nucleus; Plant defense; Reference proteome;
KW Repeat; Zinc.
FT CHAIN 1..233
FT /note="Cysteine and histidine-rich domain-containing
FT protein RAR1"
FT /id="PRO_0000403649"
FT DOMAIN 26..85
FT /note="CHORD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT DOMAIN 169..228
FT /note="CHORD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 117..137
FT /note="CCCH"
FT BINDING 26
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 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
SQ SEQUENCE 233 AA; 25348 MW; 54207A14B1EF2096 CRC64;
MSTEAETTSA AAPAPAPAPA SAPARCQRIG CDATFTDDNN PDGSCQYHPS GPMFHDGMKQ
WSCCKQKSHD FSLFLAIPGC KTGKHTTEKP ITKAVPTKPS KAVPVQTSKQ SVGADTCSRC
RQGFFCSDHG SQPKAQIPTA TSDTNMVPVE KPAVPPPKKK IDLNEPRVCK NKGCGKTYKE
KDNHDEACDY HPGPAVFRDR IRGWKCCDIH VKEFDEFMEI PPCTKGWHNA DAA
