RSBZ1_ORYSJ
ID RSBZ1_ORYSJ Reviewed; 436 AA.
AC Q6ZLB0; Q9AR01;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=bZIP transcription factor RISBZ1 {ECO:0000305};
DE AltName: Full=Rice seed bZIP1 {ECO:0000305};
DE AltName: Full=bZIP transcription factor 58 {ECO:0000303|PubMed:18065552};
DE Short=OsbZIP58 {ECO:0000303|PubMed:18065552};
GN Name=RISBZ1 {ECO:0000303|PubMed:11133985};
GN Synonyms=BZIP58 {ECO:0000303|PubMed:18065552};
GN OrderedLocusNames=Os07g0182000 {ECO:0000312|EMBL:BAF20962.1},
GN LOC_Os07g08420 {ECO:0000305};
GN ORFNames=OJ1014_E09.42 {ECO:0000312|EMBL:BAC83055.1},
GN OsJ_23334 {ECO:0000312|EMBL:EEE66684.1};
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, HOMODIMERIZATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF HIS-3; ALA-6;
RP ASP-8; PRO-11; LEU-14; ALA-16; VAL-21 AND PRO-23.
RX PubMed=11133985; DOI=10.1074/jbc.m007405200;
RA Onodera Y., Suzuki A., Wu C.Y., Washida H., Takaiwa F.;
RT "A rice functional transcriptional activator, RISBZ1, responsible for
RT endosperm-specific expression of storage protein genes through GCN4
RT motif.";
RL J. Biol. Chem. 276:14139-14152(2001).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION.
RX PubMed=16798940; DOI=10.1104/pp.106.082826;
RA Yamamoto M.P., Onodera Y., Touno S.M., Takaiwa F.;
RT "Synergism between RPBF Dof and RISBZ1 bZIP activators in the regulation of
RT rice seed expression genes.";
RL Plant Physiol. 141:1694-1707(2006).
RN [7]
RP FUNCTION.
RX PubMed=18980953; DOI=10.1093/jxb/ern265;
RA Kawakatsu T., Yamamoto M.P., Hirose S., Yano M., Takaiwa F.;
RT "Characterization of a new rice glutelin gene GluD-1 expressed in the
RT starchy endosperm.";
RL J. Exp. Bot. 59:4233-4245(2008).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18065552; DOI=10.1104/pp.107.112821;
RA Nijhawan A., Jain M., Tyagi A.K., Khurana J.P.;
RT "Genomic survey and gene expression analysis of the basic leucine zipper
RT transcription factor family in rice.";
RL Plant Physiol. 146:333-350(2008).
RN [9]
RP FUNCTION, INTERACTION WITH DOF3/RPBF, AND SUBCELLULAR LOCATION.
RX PubMed=19473328; DOI=10.1111/j.1365-313x.2009.03925.x;
RA Kawakatsu T., Yamamoto M.P., Touno S.M., Yasuda H., Takaiwa F.;
RT "Compensation and interaction between RISBZ1 and RPBF during grain filling
RT in rice.";
RL Plant J. 59:908-920(2009).
RN [10]
RP FUNCTION.
RX PubMed=21037241; DOI=10.1093/pcp/pcq164;
RA Kawakatsu T., Takaiwa F.;
RT "Differences in transcriptional regulatory mechanisms functioning for free
RT lysine content and seed storage protein accumulation in rice grain.";
RL Plant Cell Physiol. 51:1964-1974(2010).
RN [11]
RP FUNCTION.
RX PubMed=23846875; DOI=10.1093/jxb/ert187;
RA Wang J.C., Xu H., Zhu Y., Liu Q.Q., Cai X.L.;
RT "OsbZIP58, a basic leucine zipper transcription factor, regulates starch
RT biosynthesis in rice endosperm.";
RL J. Exp. Bot. 64:3453-3466(2013).
CC -!- FUNCTION: Transcriptional activator that binds to the DNA specific
CC sequence 5'-TGAGTCA-3' found in seed storage protein gene promoters.
CC Involved in the endosperm-specific regulation of storage protein genes
CC (PubMed:15685292). Can activate the expression of genes encoding for
CC the seed storage proteins glutelin, prolamin, globulin and the allergen
CC RAG1. Functions synergistically with DOF3/RPBF to positively regulate
CC quantitatively many seed storage protein genes (PubMed:16798940,
CC PubMed:19473328). Functions synergistically with DOF3/RPBF to
CC positively regulate some metabolic enzymes, such as alanine
CC aminotransferase and pyruvate phosphate dikinase, that are expressed in
CC developing seeds (PubMed:16798940). Functions synergistically with
CC DOF3/RPBF to positively regulate genes that are key players in the
CC development of aleurone layers (PubMed:19473328). Functions
CC synergistically with DOF3/RPBF to positively regulate the glutelin
CC GLUD-1 gene in endosperm of developing seeds (PubMed:18980953). Can
CC activate the expression of the bifunctional lysine-degrading enzyme,
CC lysine ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH),
CC one of the key regulators determining free lysine content in plants
CC (PubMed:21037241). Functions as a key regulator of starch synthesis in
CC seeds, by direct binding to the promoters of starch-synthesizing genes,
CC such as AGPL3, WAXXY and SBE1 (PubMed:23846875).
CC {ECO:0000269|PubMed:15685292, ECO:0000269|PubMed:16798940,
CC ECO:0000269|PubMed:18980953, ECO:0000269|PubMed:19473328,
CC ECO:0000269|PubMed:21037241, ECO:0000269|PubMed:23846875}.
CC -!- SUBUNIT: Homodimer. Forms heterodimers with RISBZ2/BZP33 and
CC RISBZ3/BZP20 (PubMed:11133985). Interacts with DOF3/RPBF
CC (PubMed:19473328). {ECO:0000269|PubMed:11133985,
CC ECO:0000269|PubMed:19473328}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:19473328}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in seeds. Expressed in
CC aleurone and subaleurone layers of maturing seeds, but not in the
CC embryo tissues. {ECO:0000269|PubMed:11133985}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing seeds from 5 to 20 days
CC after flowering (DAF). {ECO:0000269|PubMed:11133985}.
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DR EMBL; AB053472; BAB39173.1; -; mRNA.
DR EMBL; AB053475; BAB39176.1; -; Genomic_DNA.
DR EMBL; AP003800; BAC83055.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF20962.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT00329.1; -; Genomic_DNA.
DR EMBL; CM000144; EEE66684.1; -; Genomic_DNA.
DR RefSeq; XP_015645416.1; XM_015789930.1.
DR AlphaFoldDB; Q6ZLB0; -.
DR SMR; Q6ZLB0; -.
DR STRING; 4530.OS07T0182000-01; -.
DR PaxDb; Q6ZLB0; -.
DR PRIDE; Q6ZLB0; -.
DR EnsemblPlants; Os07t0182000-01; Os07t0182000-01; Os07g0182000.
DR GeneID; 4342570; -.
DR Gramene; Os07t0182000-01; Os07t0182000-01; Os07g0182000.
DR KEGG; osa:4342570; -.
DR eggNOG; ENOG502QS0A; Eukaryota.
DR HOGENOM; CLU_037575_1_1_1; -.
DR InParanoid; Q6ZLB0; -.
DR OMA; EAMGNMI; -.
DR OrthoDB; 1008484at2759; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0010581; P:regulation of starch biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR020983; Basic_leucine-zipper_C.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF12498; bZIP_C; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..436
FT /note="bZIP transcription factor RISBZ1"
FT /id="PRO_0000441222"
FT DOMAIN 236..299
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..27
FT /note="Required for transactivation activity"
FT /evidence="ECO:0000269|PubMed:11133985"
FT REGION 182..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..257
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 264..278
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 182..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 3
FT /note="H->R: Loss of transactivation activity."
FT /evidence="ECO:0000269|PubMed:11133985"
FT MUTAGEN 6
FT /note="A->S: Loss of transactivation activity."
FT /evidence="ECO:0000269|PubMed:11133985"
FT MUTAGEN 8
FT /note="D->E: Slight decrease of transactivation activity."
FT /evidence="ECO:0000269|PubMed:11133985"
FT MUTAGEN 11
FT /note="P->S: Loss of transactivation activity."
FT /evidence="ECO:0000269|PubMed:11133985"
FT MUTAGEN 14
FT /note="L->F: Loss of transactivation activity."
FT /evidence="ECO:0000269|PubMed:11133985"
FT MUTAGEN 16
FT /note="A->V: Loss of transactivation activity."
FT /evidence="ECO:0000269|PubMed:11133985"
FT MUTAGEN 21
FT /note="V->P: Loss of transactivation activity."
FT /evidence="ECO:0000269|PubMed:11133985"
FT MUTAGEN 23
FT /note="P->S: Loss of transactivation activity."
FT /evidence="ECO:0000269|PubMed:11133985"
SQ SEQUENCE 436 AA; 46491 MW; 7C0F08A4040E3960 CRC64;
MEHVFAVDEI PDPLWAPPPP VQPAAAAGVD DVGAVSGGGL LERCPSGWNL ERFLEELDGV
PAPAASPDGA AIYPSPMPAA AAEAAARWSR GYGDREAVGV MPMPAAALPA APASAAMDPV
EYNAMLKRKL DEDLATVAMW RASGAIHSES PLGNKTSLSI VGSILSSQKC IEGNGILVQT
KLSPGPNGGS GPYVNQNTDA HAKQATSGSS REPSPSEDDD MEGDAEAMGN MILDEEDKVK
KRKESNRESA RRSRSRKAAR LKDLEEQVSL LRVENSSLLR RLADANQKYS AAAIDNRVLM
ADIEALRAKV RMAEESVKMV TGARQLHQAI PDMQSPLNVN SDASVPIQNN NPMNYFSNAN
NAGVNSFMHQ VSPAFQIVDS VEKIDPTDPV QLQQQQMASL QHLQNRACGG GASSNEYTAW
GSSLMDANEL VNMELQ
