BZR1_ORYSJ
ID BZR1_ORYSJ Reviewed; 298 AA.
AC Q7XI96; A0A0P0X7Z8; Q0D559;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Protein BZR1 homolog 1 {ECO:0000305};
DE Short=OsBZR1 {ECO:0000303|PubMed:17699623};
DE AltName: Full=Protein BRASSINAZOLE-RESISTANT 1 homolog 1 {ECO:0000305};
GN Name=BZR1 {ECO:0000303|PubMed:17699623};
GN OrderedLocusNames=Os07g0580500 {ECO:0000312|EMBL:BAT02328.1},
GN LOC_Os07g39220 {ECO:0000305};
GN ORFNames=OsJ_24880 {ECO:0000312|EMBL:EAZ40428.1}, P0453G03.22;
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=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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
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 [6]
RP FUNCTION, INTERACTION WITH GF14C, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP SER-156, AND MUTAGENESIS OF SER-156 AND PRO-206.
RX PubMed=17699623; DOI=10.1073/pnas.0706386104;
RA Bai M.Y., Zhang L.Y., Gampala S.S., Zhu S.W., Song W.Y., Chong K.,
RA Wang Z.Y.;
RT "Functions of OsBZR1 and 14-3-3 proteins in brassinosteroid signaling in
RT rice.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:13839-13844(2007).
RN [7]
RP FUNCTION.
RX PubMed=19220793; DOI=10.1111/j.1365-313x.2009.03825.x;
RA Tong H., Jin Y., Liu W., Li F., Fang J., Yin Y., Qian Q., Zhu L., Chu C.;
RT "DWARF AND LOW-TILLERING, a new member of the GRAS family, plays positive
RT roles in brassinosteroid signaling in rice.";
RL Plant J. 58:803-816(2009).
RN [8]
RP PHOSPHORYLATION.
RX PubMed=22685166; DOI=10.1105/tpc.112.097394;
RA Tong H., Liu L., Jin Y., Du L., Yin Y., Qian Q., Zhu L., Chu C.;
RT "DWARF AND LOW-TILLERING acts as a direct downstream target of a
RT GSK3/SHAGGY-like kinase to mediate brassinosteroid responses in rice.";
RL Plant Cell 24:2562-2577(2012).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=22570626; DOI=10.1371/journal.pgen.1002686;
RA Zhang C., Xu Y., Guo S., Zhu J., Huan Q., Liu H., Wang L., Luo G., Wang X.,
RA Chong K.;
RT "Dynamics of brassinosteroid response modulated by negative regulator LIC
RT in rice.";
RL PLoS Genet. 8:E1002686-E1002686(2012).
RN [10]
RP INTERACTION WITH SMOS1.
RX PubMed=28100707; DOI=10.1105/tpc.16.00611;
RA Qiao S., Sun S., Wang L., Wu Z., Li C., Li X., Wang T., Leng L., Tian W.,
RA Lu T., Wang X.;
RT "The RLA1/SMOS1 transcription factor functions with OsBZR1 to regulate
RT brassinosteroid signaling and rice architecture.";
RL Plant Cell 29:292-309(2017).
RN [11]
RP INTERACTION WITH PUB24, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=30920691; DOI=10.1111/tpj.14332;
RA Min H.J., Cui L.H., Oh T.R., Kim J.H., Kim T.W., Kim W.T.;
RT "OsBZR1 turnover mediated by OsSK22-regulated U-box E3 ligase OsPUB24 in
RT rice BR response.";
RL Plant J. 99:426-438(2019).
CC -!- FUNCTION: Positive brassinosteroid-signaling protein. Mediates
CC downstream brassinosteroid-regulated growth response and feedback
CC inhibition of brassinosteroid (BR) biosynthetic genes (PubMed:17699623,
CC PubMed:19220793). May act as transcriptional repressor by binding the
CC brassinosteroid-response element (BREE) (5'-CGTG(T/C)G-3') in the
CC promoter of DLT (AC Q9LWU9), another positive regulator of BR signaling
CC (PubMed:19220793). Acts as transcriptional repressor of LIC, a negative
CC regulator of BR signaling, by binding to the BRRE element of its
CC promoter. BZR1 and LIC play opposite roles in BR signaling and
CC regulation of leaf bending (PubMed:22570626).
CC {ECO:0000269|PubMed:17699623, ECO:0000269|PubMed:19220793,
CC ECO:0000269|PubMed:22570626}.
CC -!- SUBUNIT: Interacts with GF14C (PubMed:17699623). Interacts with PUB24
CC (PubMed:30920691). Interacts with SMOS1 (PubMed:28100707).
CC {ECO:0000269|PubMed:17699623, ECO:0000269|PubMed:28100707,
CC ECO:0000269|PubMed:30920691}.
CC -!- INTERACTION:
CC Q7XI96; Q6ZKC0: GF14C; NbExp=3; IntAct=EBI-15652208, EBI-628537;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17699623,
CC ECO:0000269|PubMed:30920691}. Cytoplasm {ECO:0000269|PubMed:17699623,
CC ECO:0000269|PubMed:30920691}. Note=Brassinosteroid promotes nuclear
CC localization, and binding to GF14C is required for cytoplasmic
CC retention and efficient inhibition of BZR1 when brassinosteroid levels
CC are low. {ECO:0000269|PubMed:17699623}.
CC -!- INDUCTION: Down-regulated by 24-epibrassinolide.
CC {ECO:0000269|PubMed:22570626}.
CC -!- PTM: Phosphorylated on serine and threonine residues by GSK2
CC (PubMed:22685166). Dephosphorylated during response to brassinosteroid
CC (PubMed:17699623, PubMed:22685166). {ECO:0000269|PubMed:17699623,
CC ECO:0000269|PubMed:22685166}.
CC -!- PTM: Ubiquitinated by PUB24 (PubMed:30920691). Ubiquitination leads to
CC its subsequent degradation by the 26S proteasome, thus reducing
CC sensitivity to brassinosteroid signaling (PubMed:30920691).
CC {ECO:0000269|PubMed:30920691}.
CC -!- MISCELLANEOUS: Plants silencing BZR1 are dwarf with erect leaves, and
CC have reduced brassinosteroid sensitivity and altered expression of
CC brassinosteroid-responsive genes. {ECO:0000269|PubMed:17699623}.
CC -!- SIMILARITY: Belongs to the BZR/LAT61 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF22014.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP004276; BAC79822.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF22014.2; ALT_INIT; Genomic_DNA.
DR EMBL; AP014963; BAT02328.1; -; Genomic_DNA.
DR EMBL; CM000144; EAZ40428.1; -; Genomic_DNA.
DR EMBL; AK106748; BAG97818.1; -; mRNA.
DR RefSeq; XP_015645123.1; XM_015789637.1.
DR AlphaFoldDB; Q7XI96; -.
DR SMR; Q7XI96; -.
DR DIP; DIP-46484N; -.
DR IntAct; Q7XI96; 8.
DR STRING; 4530.OS07T0580500-01; -.
DR iPTMnet; Q7XI96; -.
DR PaxDb; Q7XI96; -.
DR PRIDE; Q7XI96; -.
DR EnsemblPlants; Os07t0580500-01; Os07t0580500-01; Os07g0580500.
DR GeneID; 4343719; -.
DR Gramene; Os07t0580500-01; Os07t0580500-01; Os07g0580500.
DR KEGG; osa:4343719; -.
DR eggNOG; ENOG502QS1Z; Eukaryota.
DR HOGENOM; CLU_036256_0_0_1; -.
DR InParanoid; Q7XI96; -.
DR OMA; GCKPPPG; -.
DR OrthoDB; 1120557at2759; -.
DR PlantReactome; R-OSA-5632095; Brassinosteroid signaling.
DR PlantReactome; R-OSA-5679411; Gibberellin signaling.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR Genevisible; Q7XI96; OS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0009741; P:response to brassinosteroid; IMP:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR008540; BES1_N.
DR InterPro; IPR033264; BZR.
DR PANTHER; PTHR31506; PTHR31506; 1.
DR Pfam; PF05687; BES1_N; 1.
PE 1: Evidence at protein level;
KW Brassinosteroid signaling pathway; Cytoplasm; DNA-binding;
KW Growth regulation; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..298
FT /note="Protein BZR1 homolog 1"
FT /id="PRO_0000429108"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 10..91
FT /note="Required for DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 71..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..224
FT /note="PEST-like"
FT COMPBIAS 89..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:17699623"
FT MUTAGEN 156
FT /note="S->G: Abolishes interaction with GF14C; increases
FT nuclear localization and activity."
FT /evidence="ECO:0000269|PubMed:17699623"
FT MUTAGEN 206
FT /note="P->L: Increases lamina joint bending."
FT /evidence="ECO:0000269|PubMed:17699623"
SQ SEQUENCE 298 AA; 31909 MW; 407B51633EF06C80 CRC64;
MTSGAAAAGR TPTWKERENN KRRERRRRAI AAKIFTGLRA LGNYNLPKHC DNNEVLKALC
REAGWVVEDD GTTYRKGCKP PPSSAGGASV GMSPCSSTQL LSAPSSSFPS PVPSYHASPA
SSSFPSPSRI DNPSASCLLP FLRGLPNLPP LRVSSSAPVT PPLSSPTASR PPKIRKPDWD
VDPFRHPFFA VSAPASPTRG RRLEHPDTIP ECDESDVSTV DSGRWISFQM ATTAPTSPTY
NLVNPGASTS NSMEIEGTAG RGGAEFEFDK GRVTPWEGER IHEVAAEELE LTLGVGAK
