NPR1_ORYSJ
ID NPR1_ORYSJ Reviewed; 582 AA.
AC Q9FDY4; Q7XBH3;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=BTB/POZ domain and ankyrin repeat-containing protein NPR1 {ECO:0000305};
DE Short=OsNPR1 {ECO:0000303|PubMed:17309686};
DE AltName: Full=NPR1 homolog 1 {ECO:0000305};
DE Short=OsNH1 {ECO:0000305};
GN Name=NPR1 {ECO:0000303|PubMed:17309686}; Synonyms=NH1 {ECO:0000305};
GN OrderedLocusNames=Os01g0194300 {ECO:0000312|EMBL:BAF04200.1},
GN LOC_Os01g09800 {ECO:0000305};
GN ORFNames=P0001B06.13 {ECO:0000312|EMBL:BAB16860.1},
GN P0671B11.44 {ECO:0000312|EMBL:BAB12719.1};
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, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF CYS-76 AND CYS-216.
RX PubMed=17309686; DOI=10.1111/j.1467-7652.2007.00243.x;
RA Yuan Y., Zhong S., Li Q., Zhu Z., Lou Y., Wang L., Wang J., Wang M., Li Q.,
RA Yang D., He Z.;
RT "Functional analysis of rice NPR1-like genes reveals that OsNPR1/NH1 is the
RT rice orthologue conferring disease resistance with enhanced herbivore
RT susceptibility.";
RL Plant Biotechnol. J. 5:313-324(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Quanhong Y., Rihe P., Aisheng X.;
RT "Rice NPR1-like protein, cloned from SA treated seedling cDNA libary, shows
RT disease resistent characteristics.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Dongjin;
RA Moon S.-J., Shin D., Kim B.-G., Park S.R., Byun M.-O.;
RT "Oryza sativa japonica group cultivar Dongjin putative NPR1-like protein 2
RT (NPR2) mRNA.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [5]
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 [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [9]
RP FUNCTION.
RX PubMed=20924648; DOI=10.1007/s11103-010-9695-3;
RA Sugano S., Jiang C.J., Miyazawa S., Masumoto C., Yazawa K., Hayashi N.,
RA Shimono M., Nakayama A., Miyao M., Takatsuji H.;
RT "Role of OsNPR1 in rice defense program as revealed by genome-wide
RT expression analysis.";
RL Plant Mol. Biol. 74:549-562(2010).
RN [10]
RP INTERACTION WITH NRR; RH1; RH2 AND RH3.
RX PubMed=22353606; DOI=10.1186/1746-4811-8-6;
RA Chern M., Bai W., Sze-To W.H., Canlas P.E., Bartley L.E., Ronald P.C.;
RT "A rice transient assay system identifies a novel domain in NRR required
RT for interaction with NH1/OsNPR1 and inhibition of NH1-mediated
RT transcriptional activation.";
RL Plant Methods 8:6-6(2012).
RN [11]
RP FUNCTION, AND INDUCTION.
RX PubMed=22694163; DOI=10.1111/j.1399-3054.2012.01666.x;
RA Li R., Afsheen S., Xin Z., Han X., Lou Y.;
RT "OsNPR1 negatively regulates herbivore-induced JA and ethylene signaling
RT and plant resistance to a chewing herbivore in rice.";
RL Physiol. Plantarum 147:340-351(2013).
RN [12]
RP INTERACTION WITH TGA2.1; TGA2.2; TGA2.3; LG2; TGAL1; TGAL4; NRR; RH1; RH2
RP AND RH3.
RX PubMed=24919709; DOI=10.1186/1471-2164-15-461;
RA Chern M., Bai W., Ruan D., Oh T., Chen X., Ronald P.C.;
RT "Interaction specificity and coexpression of rice NPR1 homologs 1 and 3
RT (NH1 and NH3), TGA transcription factors and negative regulator of
RT resistance (NRR) proteins.";
RL BMC Genomics 15:461-461(2014).
RN [13]
RP FUNCTION, AND INDUCTION BY BTH.
RX PubMed=27176732; DOI=10.1371/journal.pgen.1006049;
RA Chern M., Xu Q., Bart R.S., Bai W., Ruan D., Sze-To W.H., Canlas P.E.,
RA Jain R., Chen X., Ronald P.C.;
RT "A genetic screen identifies a requirement for cysteine-rich-receptor-like
RT kinases in rice NH1 (OsNPR1)-mediated immunity.";
RL PLoS Genet. 12:E1006049-E1006049(2016).
CC -!- FUNCTION: Key positive factor of disease resistance. Plays an essential
CC role in benzothiadiazole (BTH)-induced resistance to the blast fungus
CC disease caused by Magnaporthe oryzae (PubMed:20924648). Involved in
CC defense response against the bacterial blight disease caused by
CC Xanthomonas oryzae pv. oryzae (Xoo). Over-expression of NPR1/NH1
CC confers disease resistance to Xoo, but also enhances herbivore
CC susceptibility (PubMed:17309686). Functions as a transcriptional
CC coactivator of TGA2.1 and LG2 in vitro (PubMed:22353606). Involved in
CC defense response against herbivore. Plants silencing NPR1/NH1 have
CC increased herbivore-induced trypsin proteinase inhibitors and
CC volatiles, which reduces the performance of the striped stem borer
CC (SSB) Chilo suppressalis (PubMed:22694163).
CC {ECO:0000269|PubMed:17309686, ECO:0000269|PubMed:20924648,
CC ECO:0000269|PubMed:22353606, ECO:0000269|PubMed:22694163}.
CC -!- SUBUNIT: Oligomer in an uninduced state; disulfide-linked. Forms
CC activated monomer upon changes in cellular redox potential
CC (PubMed:17309686). Interacts with TGA2.1, TGA2.2, TGA2.3, LG2, TGAL1
CC and TGAL4 (PubMed:24919709). Interacts with NRR, RH1, RH2 and RH3
CC (PubMed:22353606, PubMed:24919709). {ECO:0000269|PubMed:17309686,
CC ECO:0000269|PubMed:22353606, ECO:0000269|PubMed:24919709}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17309686}. Nucleus
CC {ECO:0000269|PubMed:17309686}. Note=Accumulation in nucleus when
CC present as monomer. {ECO:0000269|PubMed:17309686}.
CC -!- INDUCTION: By mechanical wounding, treatment with jasmonic acid (JA),
CC salicylic acid (SA) and benzothiadiazole (BTH), and in response to
CC infestation by the rice striped stem borer Chilo suppressalis and rice
CC leaf folder Cnaphalocrocis medinalis. {ECO:0000269|PubMed:22694163}.
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; DQ450947; ABE11613.1; -; mRNA.
DR EMBL; DQ450948; ABE11614.1; -; Genomic_DNA.
DR EMBL; AY323485; AAP92751.1; -; mRNA.
DR EMBL; HM991169; AEF30412.1; -; mRNA.
DR EMBL; AP002537; BAB16860.1; -; Genomic_DNA.
DR EMBL; AP002746; BAB12719.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF04200.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS70853.1; -; Genomic_DNA.
DR EMBL; AK120715; BAH00140.1; -; mRNA.
DR RefSeq; XP_015622114.1; XM_015766628.1.
DR AlphaFoldDB; Q9FDY4; -.
DR SMR; Q9FDY4; -.
DR STRING; 4530.OS01T0194300-01; -.
DR PaxDb; Q9FDY4; -.
DR PRIDE; Q9FDY4; -.
DR EnsemblPlants; Os01t0194300-01; Os01t0194300-01; Os01g0194300.
DR GeneID; 4327315; -.
DR Gramene; Os01t0194300-01; Os01t0194300-01; Os01g0194300.
DR KEGG; osa:4327315; -.
DR eggNOG; KOG0504; Eukaryota.
DR HOGENOM; CLU_034895_1_0_1; -.
DR InParanoid; Q9FDY4; -.
DR OMA; VAFMAQV; -.
DR OrthoDB; 342053at2759; -.
DR PlantReactome; R-OSA-6788019; Salicylic acid signaling.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:EnsemblPlants.
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:0106167; P:extracellular ATP signaling; IEA:EnsemblPlants.
DR GO; GO:0009682; P:induced systemic resistance; IEA:EnsemblPlants.
DR GO; GO:0031348; P:negative regulation of defense response; IEA:EnsemblPlants.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:EnsemblPlants.
DR GO; GO:2000022; P:regulation of jasmonic acid mediated signaling pathway; IBA:GO_Central.
DR GO; GO:2000031; P:regulation of salicylic acid mediated signaling pathway; IEA:EnsemblPlants.
DR GO; GO:0010112; P:regulation of systemic acquired resistance; IEA:EnsemblPlants.
DR GO; GO:0009408; P:response to heat; IEA:EnsemblPlants.
DR GO; GO:0080027; P:response to herbivore; IMP:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IEA:EnsemblPlants.
DR GO; GO:0009625; P:response to insect; IEA:EnsemblPlants.
DR GO; GO:0009611; P:response to wounding; IEA:EnsemblPlants.
DR GO; GO:0009862; P:systemic acquired resistance, salicylic acid mediated signaling pathway; IEA:EnsemblPlants.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR044292; NPR.
DR InterPro; IPR021094; NPR1/NIM1-like_C.
DR InterPro; IPR024228; NPR_central_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR46475; PTHR46475; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF11900; DUF3420; 1.
DR Pfam; PF12313; NPR1_like_C; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Cytoplasm; Disulfide bond; Nucleus; Plant defense;
KW Reference proteome; Repeat.
FT CHAIN 1..582
FT /note="BTB/POZ domain and ankyrin repeat-containing protein
FT NPR1"
FT /id="PRO_0000437000"
FT DOMAIN 55..140
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REPEAT 269..299
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 301..328
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 332..361
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 76
FT /note="Interchain (with C-216); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P93002"
FT DISULFID 216
FT /note="Interchain (with C-76); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P93002"
FT MUTAGEN 76
FT /note="C->A: Nuclear localization; when associated with A-
FT 216."
FT /evidence="ECO:0000269|PubMed:17309686"
FT MUTAGEN 216
FT /note="C->A: Nuclear localization; when associated with A-
FT 76."
FT /evidence="ECO:0000269|PubMed:17309686"
FT CONFLICT 112
FT /note="E -> G (in Ref. 2; AAP92751)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="K -> N (in Ref. 2; AAP92751)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="K -> Q (in Ref. 2; AAP92751)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="A -> G (in Ref. 2; AAP92751)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 582 AA; 63766 MW; EBAED95839E6E76A CRC64;
MEPPTSHVTN AFSDSDSASV EEGGADADAD VEALRRLSDN LAAAFRSPED FAFLADARIA
VPGGGGGGGD LLVHRCVLSA RSPFLRGVFA RRAAAAAGGG GEDGGERLEL RELLGGGGEE
VEVGYEALRL VLDYLYSGRV GDLPKAACLC VDEDCAHVGC HPAVAFMAQV LFAASTFQVA
ELTNLFQRRL LDVLDKVEVD NLLLILSVAN LCNKSCMKLL ERCLDMVVRS NLDMITLEKS
LPPDVIKQII DARLSLGLIS PENKGFPNKH VRRIHRALDS DDVELVRMLL TEGQTNLDDA
FALHYAVEHC DSKITTELLD LALADVNHRN PRGYTVLHIA ARRREPKIIV SLLTKGARPA
DVTFDGRKAV QISKRLTKQG DYFGVTEEGK PSPKDRLCIE ILEQAERRDP QLGEASVSLA
MAGESLRGRL LYLENRVALA RIMFPMEARV AMDIAQVDGT LEFNLGSGAN PPPERQRTTV
DLNESPFIMK EEHLARMTAL SKTVELGKRF FPRCSNVLDK IMDDETDPVS LGRDTSAEKR
KRFHDLQDVL QKAFHEDKEE NDRSGLSSSS SSTSIGAIRP RR
