位置:首页 > 蛋白库 > RGA4R_ORYSJ
RGA4R_ORYSJ
ID   RGA4R_ORYSJ             Reviewed;         996 AA.
AC   F7J0M4; F7J0M2; F7J0M3;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Disease resistance protein RGA4 {ECO:0000305};
DE   AltName: Full=Os11gRGA4 {ECO:0000312|EMBL:BAK39922.1};
DE   AltName: Full=SasRGA4 {ECO:0000303|PubMed:21251109};
GN   Name=RGA4 {ECO:0000303|PubMed:21251109};
GN   Synonyms=PIA {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], FUNCTION, TISSUE SPECIFICITY, AND
RP   MUTAGENESIS OF CYS-349.
RC   STRAIN=cv. Aichi asahi {ECO:0000312|EMBL:BAK39920.1,
RC   ECO:0000312|EMBL:BAK39921.1, ECO:0000312|EMBL:BAK39922.1}, and
RC   cv. Sasanishiki {ECO:0000312|EMBL:BAK39920.1, ECO:0000312|EMBL:BAK39921.1,
RC   ECO:0000312|EMBL:BAK39922.1};
RC   TISSUE=Leaf {ECO:0000312|EMBL:BAK39920.1, ECO:0000312|EMBL:BAK39921.1,
RC   ECO:0000312|EMBL:BAK39922.1};
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   FUNCTION, AND MUTAGENESIS OF CYS-349.
RC   STRAIN=cv. Sasanishiki;
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 RGA5, SUBUNIT, FUNCTION, MUTAGENESIS OF LYS-209 AND
RP   GLY-502, 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).
CC   -!- FUNCTION: Disease resistance (R) protein. Resistance proteins guard the
CC       plant against pathogens that contain an appropriate avirulence protein
CC       via an indirect interaction with this avirulence protein. That triggers
CC       a defense system including the hypersensitive response, which restricts
CC       the pathogen growth. Contribution of RGA5 is required to recognize the
CC       effector avirulence proteins AVR-Pia and AVR1-CO39 from M.oryzae
CC       (PubMed:21251109, PubMed:23548743). Acts as a constitutively active
CC       cell death inducer that is repressed by RGA5 (PubMed:25024433). Immune
CC       response triggered by the RGA4-RGA5 -mediated recognition of AVR1-CO39
CC       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 RGA5 through its coiled
CC       coil (CC) domain. {ECO:0000269|PubMed:25024433}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25024433}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:21251109}.
CC   -!- SIMILARITY: Belongs to the disease resistance NB-LRR family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB604621; BAK39920.1; -; Genomic_DNA.
DR   EMBL; AB604621; BAK39921.1; -; Genomic_DNA.
DR   EMBL; AB604622; BAK39922.1; -; mRNA.
DR   AlphaFoldDB; F7J0M4; -.
DR   SMR; F7J0M4; -.
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:0009626; P:plant-type hypersensitive response; IMP:UniProtKB.
DR   GO; GO:0010942; P:positive regulation of cell death; IMP:UniProtKB.
DR   Gene3D; 1.10.10.10; -; 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; IPR041118; Rx_N.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR23155; PTHR23155; 1.
DR   Pfam; PF00931; NB-ARC; 1.
DR   Pfam; PF18052; Rx_N; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Coiled coil; Cytoplasm; Leucine-rich repeat;
KW   Nucleotide-binding; Plant defense; Repeat.
FT   CHAIN           1..996
FT                   /note="Disease resistance protein RGA4"
FT                   /id="PRO_0000444659"
FT   DOMAIN          180..462
FT                   /note="NB-ARC"
FT                   /evidence="ECO:0000255"
FT   REPEAT          481..503
FT                   /note="LRR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          504..528
FT                   /note="LRR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          529..549
FT                   /note="LRR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          577..599
FT                   /note="LRR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          600..621
FT                   /note="LRR 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          622..644
FT                   /note="LRR 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          698..722
FT                   /note="LRR 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          759..781
FT                   /note="LRR 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          782..804
FT                   /note="LRR 9"
FT                   /evidence="ECO:0000255"
FT   REPEAT          805..830
FT                   /note="LRR 10"
FT                   /evidence="ECO:0000255"
FT   REPEAT          851..874
FT                   /note="LRR 11"
FT                   /evidence="ECO:0000255"
FT   REGION          1..176
FT                   /note="Structured coiled coil (CC) domain"
FT                   /evidence="ECO:0000303|PubMed:21251109"
FT   COILED          111..138
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         209
FT                   /note="K->R: Abolishes resistance to M.oryzae pathogen."
FT                   /evidence="ECO:0000269|PubMed:25024433"
FT   MUTAGEN         349
FT                   /note="C->F: Abolishes resistance to M.oryzae pathogen."
FT                   /evidence="ECO:0000269|PubMed:21251109,
FT                   ECO:0000269|PubMed:23548743"
FT   MUTAGEN         502
FT                   /note="G->D: Abolishes resistance to M.oryzae pathogen."
FT                   /evidence="ECO:0000269|PubMed:25024433"
SQ   SEQUENCE   996 AA;  111685 MW;  91FD8843AC096B07 CRC64;
     MEAALLSGFI KAILPRLFSL VDDKHKLHKG VKGDIDFLIK ELRMIVGAID DDLSLDHPAA
     AAVQTLCMED LRELAHGIED CIDGVLYRAA RDQQQSPVRR AVQAPKKLQR NLQLAQQLQR
     LKRMAAEANQ RKQRYTAAAP GQHGQVYSSA AAQVDEPWPS CSSASDPRIH EADLVGVDAD
     REELLEQLAE RQPEQLKVIA IVGFCGLGKT ALAAEAYNRE TGGGRFERHA WVCAGHRSAR
     EVLGELLRRL DADGRSFHGD SDAGQLCVDI RQQLEKNRYF IVIDDIQTED QWKSIKSAFP
     TDKDIGSRIV VTTTIQSVAN ACCSANGYLH KMSRLDKNCS KQLLSKKACP ERYSHYKQPD
     SAAILKKCDG QPLALVTIGE FLQANGWPTG PNCEDLCNRL HYHLENDKTL ERMWRVLVRN
     YTSLPGHALK ACLLYFGMFP SDHPIRRKSL LRRWLAEGFV EPLSSSSNID STAAFNVLMD
     RNIIEPINVS NNDKVKTCQT YGMMREFISH MSISQNFVTF FCDDKFVPKY VRRLSLHGDT
     VVNGDNFNGI DLSLVRSLAV FGEAGTTVLD FSKYQLLRVL DLEKCDDLKD DHLKEICNLV
     LLKYLSLGGN ISKLPKDIAK LKDLEALDVR RSKVKIMPVE VFGLPCLIHL LGKFKLSDKV
     KQKTEVQEFL LKGKSNLQTL AGFASNGSEG FLHLMRYMNK LRKLKIWCTS SAGSTDWTDL
     REAIQQFILD EKEANIGTRS LSLHFSGCSE DAINSLKEPC YLSSLKLHGN FPQLPQFVTS
     LRGLKELCLS STKFTTGLLE ALSNLSYLQY LKLVADELEK FIIKVQGFPR LLRLCIVLQY
     PTFPVIEEGA LPFLVTLQLL CKDLHGLSDI QIECFKHLQE VTLHSGVTPA TRQEWVKAAK
     EHPNRPKVLL LKSVDTAESE HTDVDSVMEA VKSETTEYSI APEGPEQVNN KMQLDHGLES
     SSVLNKQNNF ADQSSSKDQL HYSFNNMGLS DVSCCE
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024