RGA5R_ORYSJ
ID RGA5R_ORYSJ Reviewed; 1116 AA.
AC F7J0N2; F7J0M8; F7J0M9; R9RW76;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Disease resistance protein RGA5 {ECO:0000305};
DE AltName: Full=Os11gRGA5 {ECO:0000312|EMBL:BAK39930.1};
DE AltName: Full=SasRGA5 {ECO:0000303|PubMed:21251109};
GN Name=RGA5 {ECO:0000303|PubMed:21251109};
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 [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Aichi asahi {ECO:0000312|EMBL:BAK39930.1}, and
RC cv. Sasanishiki {ECO:0000312|EMBL:BAK39926.1, ECO:0000312|EMBL:BAK39927.1,
RC ECO:0000312|EMBL:BAK39930.1};
RC TISSUE=Leaf {ECO:0000312|EMBL:BAK39926.1, ECO:0000312|EMBL:BAK39927.1,
RC ECO:0000312|EMBL:BAK39930.1};
RX PubMed=21251109; DOI=10.1111/j.1365-313x.2011.04502.x;
RA Okuyama Y., Kanzaki H., Abe A., Yoshida K., Tamiru M., Saitoh H.,
RA Fujibe T., Matsumura H., Shenton M., Galam D.C., Undan J., Ito A., Sone T.,
RA Terauchi R.;
RT "A multifaceted genomics approach allows the isolation of the rice Pia-
RT blast resistance gene consisting of two adjacent NBS-LRR protein genes.";
RL Plant J. 66:467-479(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, FUNCTION,
RP INTERACTION WITH AVR1-CO39 AND AVR-PIA, AND DOMAIN.
RC STRAIN=cv. Sasanishiki {ECO:0000312|EMBL:AGM61351.1};
RC TISSUE=Leaf {ECO:0000312|EMBL:AGM61351.1};
RX PubMed=23548743; DOI=10.1105/tpc.112.107201;
RA Cesari S., Thilliez G., Ribot C., Chalvon V., Michel C., Jauneau A.,
RA Rivas S., Alaux L., Kanzaki H., Okuyama Y., Morel J.B., Fournier E.,
RA Tharreau D., Terauchi R., Kroj T.;
RT "The rice resistance protein pair RGA4/RGA5 recognizes the Magnaporthe
RT oryzae effectors AVR-Pia and AVR1-CO39 by direct binding.";
RL Plant Cell 25:1463-1481(2013).
RN [3]
RP INTERACTION WITH RGA4, SUBUNIT, FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Sasanishiki;
RX PubMed=25024433; DOI=10.15252/embj.201487923;
RA Cesari S., Kanzaki H., Fujiwara T., Bernoux M., Chalvon V., Kawano Y.,
RA Shimamoto K., Dodds P., Terauchi R., Kroj T.;
RT "The NB-LRR proteins RGA4 and RGA5 interact functionally and physically to
RT confer disease resistance.";
RL EMBO J. 33:1941-1959(2014).
RN [4]
RP REVIEW.
RX PubMed=25506347; DOI=10.3389/fpls.2014.00606;
RA Cesari S., Bernoux M., Moncuquet P., Kroj T., Dodds P.N.;
RT "A novel conserved mechanism for plant NLR protein pairs: the 'integrated
RT decoy' hypothesis.";
RL Front. Plant Sci. 5:606-606(2014).
RN [5]
RP FUNCTION.
RC STRAIN=cv. Kitaake;
RX PubMed=27289079; DOI=10.1111/tpj.13231;
RA Hutin M., Cesari S., Chalvon V., Michel C., Tran T.T., Boch J., Koebnik R.,
RA Szurek B., Kroj T.;
RT "Ectopic activation of the rice NLR heteropair RGA4/RGA5 confers resistance
RT to bacterial blight and bacterial leaf streak diseases.";
RL Plant J. 88:43-55(2016).
RN [6]
RP INTERACTION WITH AVR-PIA, AND DOMAIN.
RX PubMed=28087830; DOI=10.1105/tpc.16.00435;
RA Ortiz D., de Guillen K., Cesari S., Chalvon V., Gracy J., Padilla A.,
RA Kroj T.;
RT "Effector AVR-Pia by the decoy domain of the rice NLR immune receptor
RT RGA5.";
RL Plant Cell 29:156-168(2017).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) OF 982-1116.
RX PubMed=25664791; DOI=10.1107/s2053230x14028106;
RA Huang D., Zhang Y., Zhao Y., Liu J., Peng Y.L.;
RT "Expression, purification, crystallization and preliminary X-ray
RT diffraction analysis of the effector-interaction domain of the resistance
RT protein RGA5-A from Oryza sativa L. japonica.";
RL Acta Crystallogr. F Struct. Biol. Commun. 71:171-174(2015).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 982-1116 IN COMPLEX WITH THE
RP EFFECTOR AVR1-CO39.
RX PubMed=29633975; DOI=10.1107/s2053230x18003618;
RA Guo L., Zhang Y., Ma M., Liu Q., Zhang Y., Peng Y., Liu J.;
RT "Crystallization of the rice immune receptor RGA5A_S with the rice blast
RT fungus effector AVR1-CO39 prepared via mixture and tandem strategies.";
RL Acta Crystallogr. F Struct. Biol. Commun. 74:262-267(2018).
CC -!- FUNCTION: Disease resistance (R) protein that recognizes the AVR-Pia
CC and AVR1-CO39 effector avirulence proteins from M.oryzae. Resistance
CC proteins guard the plant against pathogens that contain an appropriate
CC avirulence protein via an indirect interaction with this avirulence
CC protein. That triggers a defense system including the hypersensitive
CC response, which restricts the pathogen growth. Contribution of RGA4 is
CC required to recognize the effector avirulence proteins AVR-Pia and
CC AVR1-CO39 from M.oryzae (PubMed:21251109, PubMed:23548743). Acts as a
CC repressor of the RGA4-mediated cell death activation. Upon infection,
CC recognition and binding of the AVR effectors relieve the RGA5-mediated
CC repression and triggers the hypersensitive response (PubMed:25024433).
CC Immune response triggered by the RGA4-RGA5 -mediated recognition of
CC AVR1-CO39 confers resistance to X.oryzae pathovars (PubMed:27289079).
CC {ECO:0000269|PubMed:21251109, ECO:0000269|PubMed:23548743,
CC ECO:0000269|PubMed:25024433, ECO:0000269|PubMed:27289079}.
CC -!- SUBUNIT: Forms homodimer or heterodimer with RGA4 through its coiled
CC coil (CC) domain (PubMed:25024433). Interacts with AVR1-Pia and AVR-
CC CO39 through its C-terminal part containing the HMA-like domain
CC (PubMed:23548743, PubMed:28087830). {ECO:0000269|PubMed:23548743,
CC ECO:0000269|PubMed:25024433, ECO:0000269|PubMed:28087830}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25024433}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=RGA5-A {ECO:0000303|PubMed:21251109,
CC ECO:0000303|PubMed:23548743};
CC IsoId=F7J0N2-1; Sequence=Displayed;
CC Name=2; Synonyms=RGA5-B {ECO:0000303|PubMed:23548743};
CC IsoId=F7J0N2-2; Sequence=VSP_059636, VSP_059637;
CC -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:21251109}.
CC -!- DOMAIN: The HMA-like (RATX1) domain is responsible for the specific
CC recognition of AVR effectors. {ECO:0000269|PubMed:23548743,
CC ECO:0000269|PubMed:28087830}.
CC -!- SIMILARITY: Belongs to the disease resistance NB-LRR family.
CC {ECO:0000305}.
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DR EMBL; AB604626; BAK39926.1; -; Genomic_DNA.
DR EMBL; AB604626; BAK39927.1; -; Genomic_DNA.
DR EMBL; AB604627; BAK39930.1; -; mRNA.
DR EMBL; KC777365; AGM61351.1; -; mRNA.
DR PDB; 5ZNE; X-ray; 1.78 A; A=982-1116.
DR PDB; 5ZNG; X-ray; 2.19 A; A=982-1116.
DR PDB; 7DV8; X-ray; 2.45 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=997-1069.
DR PDB; 7DVG; X-ray; 2.80 A; A/B=997-1069.
DR PDBsum; 5ZNE; -.
DR PDBsum; 5ZNG; -.
DR PDBsum; 7DV8; -.
DR PDBsum; 7DVG; -.
DR AlphaFoldDB; F7J0N2; -.
DR SMR; F7J0N2; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043621; F:protein self-association; IPI:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR GO; GO:0002758; P:innate immune response-activating signal transduction; IDA:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
DR GO; GO:0009626; P:plant-type hypersensitive response; IMP:UniProtKB.
DR CDD; cd14798; RX-CC_like; 1.
DR Gene3D; 1.10.8.430; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR042197; Apaf_helical.
DR InterPro; IPR044974; Disease_R_plants.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002182; NB-ARC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038005; RX-like_CC.
DR InterPro; IPR041118; Rx_N.
DR PANTHER; PTHR23155; PTHR23155; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR Pfam; PF18052; Rx_N; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Coiled coil; Cytoplasm;
KW Leucine-rich repeat; Nucleotide-binding; Plant defense; Repeat.
FT CHAIN 1..1116
FT /note="Disease resistance protein RGA5"
FT /id="PRO_0000444661"
FT DOMAIN 182..466
FT /note="NB-ARC"
FT /evidence="ECO:0000255"
FT REPEAT 608..631
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 633..653
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 654..675
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 677..701
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 732..755
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 786..808
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 810..830
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 835..857
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 858..882
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT DOMAIN 997..1066
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 1..177
FT /note="Structured coiled coil (CC) domain"
FT /evidence="ECO:0000303|PubMed:23548743"
FT REGION 935..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1070
FT /note="HMA-like domain"
FT /evidence="ECO:0000269|PubMed:23548743,
FT ECO:0000303|PubMed:21251109"
FT COMPBIAS 936..971
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1025..1071
FT /note="VDSVEITGEDKDRLVVVGRGIDPVRLVALLREKCGLAELLMVELVEK -> K
FT SAQIYSSGCAVLISTPTSLCLYACRGGQRGDNGGGQRPAGGGRPWH (in isoform
FT 2)"
FT /id="VSP_059636"
FT VAR_SEQ 1072..1116
FT /note="Missing (in isoform 2)"
FT /id="VSP_059637"
FT TURN 992..995
FT /evidence="ECO:0007829|PDB:5ZNG"
FT STRAND 998..1004
FT /evidence="ECO:0007829|PDB:5ZNE"
FT HELIX 1009..1020
FT /evidence="ECO:0007829|PDB:5ZNE"
FT STRAND 1025..1031
FT /evidence="ECO:0007829|PDB:5ZNE"
FT TURN 1032..1035
FT /evidence="ECO:0007829|PDB:5ZNE"
FT STRAND 1037..1044
FT /evidence="ECO:0007829|PDB:5ZNE"
FT HELIX 1047..1058
FT /evidence="ECO:0007829|PDB:5ZNE"
FT STRAND 1061..1068
FT /evidence="ECO:0007829|PDB:5ZNE"
SQ SEQUENCE 1116 AA; 124448 MW; A62DF8B1D4EC545F CRC64;
MDAPASFSLG AMGPLLRKLD SLLVAPEIRL PKPLKEGIEL LKEDLEEIGV SLVEHSVVDS
PTHKARFWMD EVRDLSYHIE DCIDTMFSMR SGGDDGKPRS ERRHKVGRAK IDGFSKKPKP
CTRMARIAEL RALVREASER LERYQLGDVC GSSSPVVFTA DGRARPLHHG VSANLVGVDE
FKTKLNRWLS DEEGPHLKVA AIVGPAGIGK TALATELYRD HRWQFECRAF VRASRKPDMQ
RLLGGILSQV QRRQRSSDAY ADSTVQSLID NLREHLQDRR YLIIIDGLWE TAVWNIANSA
FPDVNSFSRI LITADIEQVA LECCGYKYDY IMRMEPLGSL DSKKVFFNKV FGSEDQCPPE
LKEVSNTILE KCGGLPLAII SIAGLLGSQP ENPVLWDYVT KYLCSSLGTN PTLKDVVKET
LNLSYNSLPH PFKTCLLYLG MYPDGHIMLK ADLMKQWSAE GFVSANEAKD TEEIVDKYFD
ELVNRGILEP VEINKNGKVL SCTLHHAVHD LVMPKFNDDK FTMSVDYSQT ITGPSTMVRR
LSLHFSSTRY ATKPAGIILS RVRSLAFFGL LNCMPCIGEF KLLRVLILEF WGSHGEQRSL
NLIPVCRLFQ LRYLKTSGDV VVQLPAQISG LQYLETLEID ARVSAVPFDL VHLPNLLHLQ
LQDETKLPDG IGCMRSLRTL QYFDLGNNSV DNLRGLGELT NLQDLHLSYS APSSNEGLMI
NLNAITSSLS RLSNLKSLIL SPGAISMVIF FDISSIISVV PVFLQRLELL PPICIFCRLP
KSIGQLHKLC ILKVSVRELL TTDIDNLTGL PSLTVLSLYA QTAPEGRFIF KDGTLPVLKY
FKFGCGELCL AFMAGAMPNL QRLKLVFNIR KSEKYRHTLF GIEHLVSLQD IATRIGVDTS
TGESDRRAAE SAFKETVNKH PRCLRSSLQW VVSTEEESHP LEKQHHKREK GSSAGHGVLE
KESVEDSEKN TDRVQTLLSP QLSNMESVVE SALTGQRTKI VVKVHMPCGK SRAKAMALAA
SVNGVDSVEI TGEDKDRLVV VGRGIDPVRL VALLREKCGL AELLMVELVE KEKTQLAGGK
KGAYKKHPTY NLSPFDYVEY PPSAPIMQDI NPCSTM
