BZIP1_ARATH
ID BZIP1_ARATH Reviewed; 145 AA.
AC Q9FGX2;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Basic leucine zipper 1;
DE Short=AtbZIP1;
DE Short=bZIP protein 1;
GN Name=BZIP1; OrderedLocusNames=At5g49450; ORFNames=K7J8.13;
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 [MRNA].
RA Wang X., Droege-Laser W.;
RT "AtbZIP1, a transcription factor in Arabidopsis thaliana.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11906833; DOI=10.1016/s1360-1385(01)02223-3;
RA Jakoby M., Weisshaar B., Droege-Laser W., Vicente-Carbajosa J.,
RA Tiedemann J., Kroj T., Parcy F.;
RT "bZIP transcription factors in Arabidopsis.";
RL Trends Plant Sci. 7:106-111(2002).
RN [7]
RP INTERACTION WITH BZIP4; BZIP9; BZIP10; BZIP11; BZIP25; BZIP42; BZIP44;
RP BZIP58 AND BZIP63.
RX PubMed=16709202; DOI=10.1111/j.1365-313x.2006.02731.x;
RA Ehlert A., Weltmeier F., Wang X., Mayer C.S., Smeekens S.,
RA Vicente-Carbajosa J., Droege-Laser W.;
RT "Two-hybrid protein-protein interaction analysis in Arabidopsis
RT protoplasts: establishment of a heterodimerization map of group C and group
RT S bZIP transcription factors.";
RL Plant J. 46:890-900(2006).
RN [8]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION BY GLUCOSE AND
RP PSEUDOMONAS SYRINGAE.
RC STRAIN=cv. Columbia;
RX PubMed=18841482; DOI=10.1007/s11103-008-9410-9;
RA Weltmeier F., Rahmani F., Ehlert A., Dietrich K., Schuetze K., Wang X.,
RA Chaban C., Hanson J., Teige M., Harter K., Vicente-Carbajosa J.,
RA Smeekens S., Droege-Laser W.;
RT "Expression patterns within the Arabidopsis C/S1 bZIP transcription factor
RT network: availability of heterodimerization partners controls gene
RT expression during stress response and development.";
RL Plant Mol. Biol. 69:107-119(2009).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY GLUCOSE AND MANNOSE, TISSUE
RP SPECIFICITY, AND INTERACTION WITH ZFP7; BZIP10; BZIP11; BZIP25; BZIP44 AND
RP BZIP63.
RX PubMed=20080816; DOI=10.1093/mp/ssp115;
RA Kang S.G., Price J., Lin P.-C., Hong J.C., Jang J.-C.;
RT "The arabidopsis bZIP1 transcription factor is involved in sugar signaling,
RT protein networking, and DNA binding.";
RL Mol. Plant 3:361-373(2010).
RN [10]
RP FUNCTION, INTERACTION WITH BZIP53, AND INDUCTION BY STARVATION.
RX PubMed=21278122; DOI=10.1105/tpc.110.075390;
RA Dietrich K., Weltmeier F., Ehlert A., Weiste C., Stahl M., Harter K.,
RA Droege-Laser W.;
RT "Heterodimers of the Arabidopsis transcription factors bZIP1 and bZIP53
RT reprogram amino acid metabolism during low energy stress.";
RL Plant Cell 23:381-395(2011).
RN [11]
RP FUNCTION.
RX PubMed=24243147; DOI=10.1007/s11103-013-0154-9;
RA Kim W.C., Reca I.B., Kim Y., Park S., Thomashow M.F., Keegstra K.,
RA Han K.H.;
RT "Transcription factors that directly regulate the expression of CSLA9
RT encoding mannan synthase in Arabidopsis thaliana.";
RL Plant Mol. Biol. 84:577-587(2014).
RN [12]
RP INTERACTION WITH BZIP63.
RX PubMed=26263501; DOI=10.7554/elife.05828;
RA Mair A., Pedrotti L., Wurzinger B., Anrather D., Simeunovic A., Weiste C.,
RA Valerio C., Dietrich K., Kirchler T., Naegele T., Vicente Carbajosa J.,
RA Hanson J., Baena-Gonzalez E., Chaban C., Weckwerth W., Droege-Laser W.,
RA Teige M.;
RT "SnRK1-triggered switch of bZIP63 dimerization mediates the low-energy
RT response in plants.";
RL Elife 4:0-0(2015).
CC -!- FUNCTION: Transcription factor that binds to the C-box-like motif (5'-
CC TGCTGACGTCA-3') and G-box-like motif (5'-CCACGTGGCC-3'), ABRE elements,
CC of gene promoters involved in sugar signaling. Activated by low energy
CC stress both at transcriptional and post-transcriptional mechanisms.
CC Promotes dark-induced senescence and participates in the
CC transcriptional reprogramming of amino acid metabolism during the dark-
CC induced starvation response (PubMed:20080816, PubMed:21278122).
CC Transcription activator of the mannan synthase CSLA9. Recognizes and
CC binds to DNA-specific sequence of CSLA9 promoter (PubMed:24243147).
CC {ECO:0000269|PubMed:20080816, ECO:0000269|PubMed:21278122,
CC ECO:0000269|PubMed:24243147}.
CC -!- SUBUNIT: Interacts with ZFP7, BZIP4, BZIP9, BZIP10, BZIP11, BZIP25,
CC BZIP42, BZIP44, BZIP53, BZIP58 and BZIP63.
CC {ECO:0000269|PubMed:16709202, ECO:0000269|PubMed:20080816,
CC ECO:0000269|PubMed:21278122, ECO:0000269|PubMed:26263501}.
CC -!- INTERACTION:
CC Q9FGX2; O22763: BZIP10; NbExp=3; IntAct=EBI-942623, EBI-942648;
CC Q9FGX2; O65683: BZIP11; NbExp=5; IntAct=EBI-942623, EBI-942769;
CC Q9FGX2; Q9M1G6: BZIP25; NbExp=6; IntAct=EBI-942623, EBI-942696;
CC Q9FGX2; C0Z2L5: BZIP44; NbExp=5; IntAct=EBI-942623, EBI-942804;
CC Q9FGX2; B9DGI8: BZIP63; NbExp=4; IntAct=EBI-942623, EBI-942713;
CC Q9FGX2; Q9FUD3: BZIP9; NbExp=3; IntAct=EBI-942623, EBI-942633;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- TISSUE SPECIFICITY: Expressed in both shoots, including young leaves,
CC stipulae and trichomes (except in cotyledons and hypocotyl), and roots,
CC including vascular tissues (e.g. in both the phloem and the xylem).
CC Present in seeds and pollen. Restricted to vasculatures and roots in
CC the presence of sucrose or glucose. {ECO:0000269|PubMed:18841482,
CC ECO:0000269|PubMed:20080816}.
CC -!- DEVELOPMENTAL STAGE: Expressed in seeds during late stage of
CC development. {ECO:0000269|PubMed:18841482}.
CC -!- INDUCTION: Reversibly repressed by glucose and mannose. Slowly induced
CC by Pseudomonas syringae. Induced in roots upon cold and salt stress but
CC then repressed in leaves. Promoted by low energy stress and dark-
CC induced starvation. {ECO:0000269|PubMed:18841482,
CC ECO:0000269|PubMed:20080816, ECO:0000269|PubMed:21278122}.
CC -!- DISRUPTION PHENOTYPE: Reduced requirement for exogenous sugar for
CC seedling growth and higher rates of true leaf development.
CC {ECO:0000269|PubMed:20080816}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; AF400618; AAK94022.1; -; mRNA.
DR EMBL; AB023034; BAB09915.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95813.1; -; Genomic_DNA.
DR EMBL; AY136307; AAM96973.1; -; mRNA.
DR EMBL; BT000400; AAN15719.1; -; mRNA.
DR EMBL; AY088207; AAM65749.1; -; mRNA.
DR RefSeq; NP_199756.1; NM_124322.3.
DR AlphaFoldDB; Q9FGX2; -.
DR SMR; Q9FGX2; -.
DR BioGRID; 20251; 18.
DR IntAct; Q9FGX2; 21.
DR STRING; 3702.AT5G49450.1; -.
DR iPTMnet; Q9FGX2; -.
DR PaxDb; Q9FGX2; -.
DR PRIDE; Q9FGX2; -.
DR ProteomicsDB; 240255; -.
DR EnsemblPlants; AT5G49450.1; AT5G49450.1; AT5G49450.
DR GeneID; 835005; -.
DR Gramene; AT5G49450.1; AT5G49450.1; AT5G49450.
DR KEGG; ath:AT5G49450; -.
DR Araport; AT5G49450; -.
DR TAIR; locus:2157999; AT5G49450.
DR eggNOG; ENOG502R7IP; Eukaryota.
DR HOGENOM; CLU_1779969_0_0_1; -.
DR InParanoid; Q9FGX2; -.
DR OMA; LMEDTIH; -.
DR OrthoDB; 1494953at2759; -.
DR PhylomeDB; Q9FGX2; -.
DR PRO; PR:Q9FGX2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGX2; baseline and differential.
DR Genevisible; Q9FGX2; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IPI:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0009901; P:anther dehiscence; IMP:TAIR.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; IEP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0010182; P:sugar mediated signaling pathway; IMP:UniProtKB.
DR CDD; cd14702; bZIP_plant_GBF1; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR045314; bZIP_plant_GBF1.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF07716; bZIP_2; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..145
FT /note="Basic leucine zipper 1"
FT /id="PRO_0000416557"
FT DOMAIN 14..77
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 16..37
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 46..53
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
SQ SEQUENCE 145 AA; 16224 MW; 5137A1CCE8638C0A CRC64;
MANAEKTSSG SDIDEKKRKR KLSNRESARR SRLKKQKLME DTIHEISSLE RRIKENSERC
RAVKQRLDSV ETENAGLRSE KIWLSSYVSD LENMIATTSL TLTQSGGGDC VDDQNANAGI
AVGDCRRTPW KLSCGSLQPM ASFKT
