BZR1_ARATH
ID BZR1_ARATH Reviewed; 336 AA.
AC Q8S307; Q8VZD2; Q9C9Q2;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Protein BRASSINAZOLE-RESISTANT 1 {ECO:0000303|PubMed:11970900};
DE AltName: Full=Protein BIN2 SUBSTRATE 2 {ECO:0000303|PubMed:12427989};
GN Name=BZR1 {ECO:0000303|PubMed:11970900};
GN Synonyms=BIS2 {ECO:0000303|PubMed:12427989};
GN OrderedLocusNames=At1g75080 {ECO:0000312|Araport:AT1G75080};
GN ORFNames=F9E10.7 {ECO:0000312|EMBL:AAG51929.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, MUTANT BZR1-1D, AND MUTAGENESIS OF PRO-234.
RX PubMed=11970900; DOI=10.1016/s1534-5807(02)00153-3;
RA Wang Z.-Y., Nakano T., Gendron J., He J., Chen M., Vafeados D., Yang Y.,
RA Fujioka S., Yoshida S., Asami T., Chory J.;
RT "Nuclear-localized BZR1 mediates brassinosteroid-induced growth and
RT feedback suppression of brassinosteroid biosynthesis.";
RL Dev. Cell 2:505-513(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION, SUBCELLULAR LOCATION, MUTANT PRO-234, AND INTERACTION WITH
RP BIN2.
RX PubMed=12427989; DOI=10.1104/pp.102.010918;
RA Zhao J., Peng P., Schmitz R.J., Decker A.D., Tax F.E., Li J.;
RT "Two putative BIN2 substrates are nuclear components of brassinosteroid
RT signaling.";
RL Plant Physiol. 130:1221-1229(2002).
RN [7]
RP PHOSPHORYLATION, AND INTERACTION WITH BIN2.
RX PubMed=12114546; DOI=10.1073/pnas.152342599;
RA He J.-X., Gendron J.M., Yang Y., Li J., Wang Z.-Y.;
RT "The GSK3-like kinase BIN2 phosphorylates and destabilizes BZR1, a positive
RT regulator of the brassinosteroid signaling pathway in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10185-10190(2002).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY BRASSINOSTEROID, AND
RP PHOSPHORYLATION IN RESPONSE TO BRASSINOSTEROID.
RX PubMed=15681342; DOI=10.1126/science.1107580;
RA He J.X., Gendron J.M., Sun Y., Gampala S.S., Gendron N., Sun C.Q.,
RA Wang Z.Y.;
RT "BZR1 is a transcriptional repressor with dual roles in brassinosteroid
RT homeostasis and growth responses.";
RL Science 307:1634-1638(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [10]
RP INTERACTION WITH B'ALPHA; B'BETA; B'ETA AND B'THETA.
RX PubMed=21258370; DOI=10.1038/ncb2151;
RA Tang W., Yuan M., Wang R., Yang Y., Wang C., Oses-Prieto J.A., Kim T.W.,
RA Zhou H.W., Deng Z., Gampala S.S., Gendron J.M., Jonassen E.M., Lillo C.,
RA DeLong A., Burlingame A.L., Sun Y., Wang Z.Y.;
RT "PP2A activates brassinosteroid-responsive gene expression and plant growth
RT by dephosphorylating BZR1.";
RL Nat. Cell Biol. 13:124-131(2011).
RN [11]
RP INTERACTION WITH SAUR50.
RX PubMed=23020777; DOI=10.1146/annurev-genet-102209-163450;
RA Wang Z.Y., Bai M.Y., Oh E., Zhu J.Y.;
RT "Brassinosteroid signaling network and regulation of photomorphogenesis.";
RL Annu. Rev. Genet. 46:701-724(2012).
RN [12]
RP PHOSPHORYLATION, AND INTERACTION WITH MKK5.
RX PubMed=24019147; DOI=10.1074/mcp.m113.029256;
RA Wang C., Shang J.X., Chen Q.X., Oses-Prieto J.A., Bai M.Y., Yang Y.,
RA Yuan M., Zhang Y.L., Mu C.C., Deng Z., Wei C.Q., Burlingame A.L.,
RA Wang Z.Y., Sun Y.;
RT "Identification of BZR1-interacting proteins as potential components of the
RT brassinosteroid signaling pathway in Arabidopsis through tandem affinity
RT purification.";
RL Mol. Cell. Proteomics 12:3653-3665(2013).
RN [13]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=22914576; DOI=10.1093/mp/sss070;
RA Huang H.-Y., Jiang W.-B., Hu Y.-W., Wu P., Zhu J.-Y., Liang W.-Q.,
RA Wang Z.-Y., Lin W.-H.;
RT "BR signal influences Arabidopsis ovule and seed number through regulating
RT related genes expression by BZR1.";
RL Mol. Plant 6:456-469(2013).
RN [14]
RP FUNCTION, AND INDUCTION BY ABSCISIC ACID.
RC STRAIN=cv. Columbia;
RX PubMed=33324437; DOI=10.3389/fpls.2020.596835;
RA Wu J., Yan M., Zhang D., Zhou D., Yamaguchi N., Ito T.;
RT "Histone demethylases coordinate the antagonistic interaction between
RT abscisic acid and brassinosteroid signaling in Arabidopsis.";
RL Front. Plant Sci. 11:596835-596835(2020).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF 21-104 IN COMPLEX WITH DNA, AND
RP HOMODIMERIZATION.
RX PubMed=30287951; DOI=10.1038/s41477-018-0255-1;
RA Nosaki S., Miyakawa T., Xu Y., Nakamura A., Hirabayashi K., Asami T.,
RA Nakano T., Tanokura M.;
RT "Structural basis for brassinosteroid response by BIL1/BZR1.";
RL Nat. Plants 4:771-776(2018).
CC -!- FUNCTION: Transcriptional repressor that binds to the brassinosteroid
CC (BR) response element (BRRE) 5'-CGTG(T/C)G-3' in gene promoter.
CC Regulates positively the brassinosteroid-signaling pathway
CC (PubMed:33324437). Mediates downstream growth responses and negative
CC feedback regulation of brassinosteroid biosynthesis. Promotes growth.
CC Modulates ovule initiation and development by monitoring the expression
CC of genes related to ovule development (e.g. HLL, ANT, and AP2).
CC Regulates negatively the abscisic acid (ABA) signaling pathway during
CC the post-germination stage (PubMed:33324437).
CC {ECO:0000269|PubMed:15681342, ECO:0000269|PubMed:22914576,
CC ECO:0000269|PubMed:33324437}.
CC -!- SUBUNIT: Homodimer (PubMed:30287951). Interacts with BIN2 through its
CC C-terminal fragment (PubMed:12427989, PubMed:12114546). Interacts with
CC MKK5 (PubMed:24019147). Interacts with SAUR50 (PubMed:23020777).
CC Interacts with B'ALPHA, B'BETA, B'ETA and B'THETA (PubMed:21258370).
CC {ECO:0000269|PubMed:12114546, ECO:0000269|PubMed:12427989,
CC ECO:0000269|PubMed:21258370, ECO:0000269|PubMed:23020777,
CC ECO:0000269|PubMed:24019147, ECO:0000269|PubMed:30287951}.
CC -!- INTERACTION:
CC Q8S307; Q9FIW5: ANAC094; NbExp=3; IntAct=EBI-1803261, EBI-25522986;
CC Q8S307; Q39011: ASK7; NbExp=2; IntAct=EBI-1803261, EBI-1798250;
CC Q8S307; Q94C33: At3g51180; NbExp=3; IntAct=EBI-1803261, EBI-4438678;
CC Q8S307; Q9FIK2: At5g47790; NbExp=3; IntAct=EBI-1803261, EBI-25523851;
CC Q8S307; Q38897: BEL1; NbExp=3; IntAct=EBI-1803261, EBI-1153783;
CC Q8S307; Q9LQT8: GAI; NbExp=9; IntAct=EBI-1803261, EBI-963606;
CC Q8S307; P48349: GRF6; NbExp=5; IntAct=EBI-1803261, EBI-1633785;
CC Q8S307; Q9FPE8: HHO3; NbExp=3; IntAct=EBI-1803261, EBI-2298866;
CC Q8S307; Q9LSI4: MGH6.1; NbExp=3; IntAct=EBI-1803261, EBI-15198743;
CC Q8S307; Q9LK95: MYB21; NbExp=3; IntAct=EBI-1803261, EBI-15197631;
CC Q8S307; Q8GZM7: PIF1; NbExp=2; IntAct=EBI-1803261, EBI-630400;
CC Q8S307; Q8W2F3: PIF4; NbExp=4; IntAct=EBI-1803261, EBI-625716;
CC Q8S307; Q9SLH3: RGA; NbExp=8; IntAct=EBI-1803261, EBI-963624;
CC Q8S307; Q9C8Y3: RGL1; NbExp=3; IntAct=EBI-1803261, EBI-963647;
CC Q8S307; Q9S7W5: TCP13; NbExp=4; IntAct=EBI-1803261, EBI-4424877;
CC Q8S307; Q9C9L2: TCP15; NbExp=6; IntAct=EBI-1803261, EBI-4426144;
CC Q8S307; Q9M1U4: TCP16; NbExp=3; IntAct=EBI-1803261, EBI-15198627;
CC Q8S307; Q9FTA2: TCP21; NbExp=5; IntAct=EBI-1803261, EBI-4426168;
CC Q8S307; Q9MAH8: TCP3; NbExp=3; IntAct=EBI-1803261, EBI-25522447;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11970900,
CC ECO:0000269|PubMed:12427989}.
CC -!- TISSUE SPECIFICITY: Accumulates in the growing region of the hypocotyl.
CC {ECO:0000269|PubMed:11970900}.
CC -!- INDUCTION: By brassinosteroid (BR) (PubMed:15681342). Up-regulated in
CC response to abscisic acid (ABA) via epigenetic regulation on repressive
CC histone marks (H3K27me3) mediated by JMJ30 and JMJ32 (PubMed:33324437).
CC {ECO:0000269|PubMed:15681342, ECO:0000269|PubMed:33324437}.
CC -!- PTM: Phosphorylated by BIN2 and MKK5 in response to brassinosteroid
CC (BR). Dephosphorylation level is consistent with ovule and seed number.
CC {ECO:0000269|PubMed:12114546, ECO:0000269|PubMed:12427989,
CC ECO:0000269|PubMed:15681342, ECO:0000269|PubMed:22914576,
CC ECO:0000269|PubMed:24019147}.
CC -!- DISRUPTION PHENOTYPE: In bzr1-1D, weak dwarf phenotype with reduced
CC hypocotyl and petiole lengths and dark green curled leaves when light-
CC grown. Increased cell elongation in the dark. Hypersensitive to
CC brassinosteroid (BR). {ECO:0000269|PubMed:15681342}.
CC -!- MISCELLANEOUS: Phosphorylation by BIN2 increases protein degradation
CC and/or interferes with the nuclear localization.
CC -!- SIMILARITY: Belongs to the BZR/LAT61 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51929.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF494338; AAM18490.1; -; Genomic_DNA.
DR EMBL; AC013258; AAG51929.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35669.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35670.1; -; Genomic_DNA.
DR EMBL; AY065049; AAL57684.1; -; mRNA.
DR EMBL; AY093747; AAM10371.1; -; mRNA.
DR EMBL; AY087257; AAM64812.1; -; mRNA.
DR PIR; G96780; G96780.
DR RefSeq; NP_565099.1; NM_106164.3.
DR RefSeq; NP_974145.1; NM_202416.1.
DR PDB; 5ZD4; X-ray; 2.17 A; A/B/C/D=21-104.
DR PDBsum; 5ZD4; -.
DR AlphaFoldDB; Q8S307; -.
DR SMR; Q8S307; -.
DR BioGRID; 29064; 82.
DR DIP; DIP-47078N; -.
DR IntAct; Q8S307; 39.
DR STRING; 3702.AT1G75080.2; -.
DR iPTMnet; Q8S307; -.
DR PaxDb; Q8S307; -.
DR PRIDE; Q8S307; -.
DR ProteomicsDB; 240258; -.
DR EnsemblPlants; AT1G75080.1; AT1G75080.1; AT1G75080.
DR EnsemblPlants; AT1G75080.2; AT1G75080.2; AT1G75080.
DR GeneID; 843845; -.
DR Gramene; AT1G75080.1; AT1G75080.1; AT1G75080.
DR Gramene; AT1G75080.2; AT1G75080.2; AT1G75080.
DR KEGG; ath:AT1G75080; -.
DR Araport; AT1G75080; -.
DR TAIR; locus:2037279; AT1G75080.
DR eggNOG; ENOG502QUKX; Eukaryota.
DR HOGENOM; CLU_036256_0_0_1; -.
DR InParanoid; Q8S307; -.
DR OMA; GQWMNFQ; -.
DR OrthoDB; 1078944at2759; -.
DR PhylomeDB; Q8S307; -.
DR PRO; PR:Q8S307; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8S307; baseline and differential.
DR Genevisible; Q8S307; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0048481; P:plant ovule development; IMP:TAIR.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0048316; P:seed development; IMP:TAIR.
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 3D-structure; Brassinosteroid signaling pathway; DNA-binding;
KW Growth regulation; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..336
FT /note="Protein BRASSINAZOLE-RESISTANT 1"
FT /id="PRO_0000113271"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 21..104
FT /note="Required for DNA-binding"
FT REGION 102..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..252
FT /note="PEST-like"
FT COMPBIAS 23..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 177
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LN63"
FT MUTAGEN 234
FT /note="P->L: In bzr1-1D; insensitive to brassinazole;
FT increased stability of the protein but no effect on its
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:11970900"
FT CONFLICT 180
FT /note="V -> L (in Ref. 4; AAL57684/AAM10371)"
FT /evidence="ECO:0000305"
FT HELIX 27..54
FT /evidence="ECO:0007829|PDB:5ZD4"
FT HELIX 65..75
FT /evidence="ECO:0007829|PDB:5ZD4"
SQ SEQUENCE 336 AA; 36486 MW; 2CE6D6647D72C012 CRC64;
MTSDGATSTS AAAAAAAAAA ARRKPSWRER ENNRRRERRR RAVAAKIYTG LRAQGDYNLP
KHCDNNEVLK ALCVEAGWVV EEDGTTYRKG CKPLPGEIAG TSSRVTPYSS QNQSPLSSAF
QSPIPSYQVS PSSSSFPSPS RGEPNNNMSS TFFPFLRNGG IPSSLPSLRI SNSCPVTPPV
SSPTSKNPKP LPNWESIAKQ SMAIAKQSMA SFNYPFYAVS APASPTHRHQ FHTPATIPEC
DESDSSTVDS GHWISFQKFA QQQPFSASMV PTSPTFNLVK PAPQQMSPNT AAFQEIGQSS
EFKFENSQVK PWEGERIHDV GMEDLELTLG NGKARG
