BZP53_ARATH
ID BZP53_ARATH Reviewed; 146 AA.
AC Q9LZP8;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=bZIP transcription factor 53 {ECO:0000303|PubMed:11906833};
DE Short=AtbZIP53 {ECO:0000303|PubMed:11906833};
GN Name=BZIP53 {ECO:0000303|PubMed:11906833};
GN OrderedLocusNames=At3g62420 {ECO:0000312|EMBL:AEE80350.1};
GN ORFNames=T12C14.120 {ECO:0000312|EMBL:CAB82956.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang X., Droege-Laser W.;
RT "AtbZIP53, 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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 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 [6]
RP FUNCTION, AND INDUCTION BY HYPOOSMOLARITY.
RC STRAIN=cv. Columbia;
RX PubMed=15047879; DOI=10.1093/pcp/pch036;
RA Satoh R., Fujita Y., Nakashima K., Shinozaki K., Yamaguchi-Shinozaki K.;
RT "A novel subgroup of bZIP proteins functions as transcriptional activators
RT in hypoosmolarity-responsive expression of the ProDH gene in Arabidopsis.";
RL Plant Cell Physiol. 45:309-317(2004).
RN [7]
RP FUNCTION, MUTAGENESIS OF LEU-51 AND ALA-72, INTERACTION WITH BZIP9; BZIP10;
RP BZIP25 AND BZIP63, INDUCTION BY HYPOOSMOLARITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=16810321; DOI=10.1038/sj.emboj.7601206;
RA Weltmeier F., Ehlert A., Mayer C.S., Dietrich K., Wang X., Schuetze K.,
RA Alonso R., Harter K., Vicente-Carbajosa J., Droege-Laser W.;
RT "Combinatorial control of Arabidopsis proline dehydrogenase transcription
RT by specific heterodimerisation of bZIP transcription factors.";
RL EMBO J. 25:3133-3143(2006).
RN [8]
RP INTERACTION WITH BZIP9; BZIP10; BZIP25 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 [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INTERACTION WITH BZIP10 AND BZIP25.
RC STRAIN=cv. Columbia;
RX PubMed=19531597; DOI=10.1105/tpc.108.062968;
RA Alonso R., Onate-Sanchez L., Weltmeier F., Ehlert A., Diaz I., Dietrich K.,
RA Vicente-Carbajosa J., Droege-Laser W.;
RT "A pivotal role of the basic leucine zipper transcription factor bZIP53 in
RT the regulation of Arabidopsis seed maturation gene expression based on
RT heterodimerization and protein complex formation.";
RL Plant Cell 21:1747-1761(2009).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH BZIP1, AND INDUCTION BY
RP 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=25108460; DOI=10.1007/s11103-014-0234-5;
RA Ji X., Wang L., Nie X., He L., Zang D., Liu Y., Zhang B., Wang Y.;
RT "A novel method to identify the DNA motifs recognized by a defined
RT transcription factor.";
RL Plant Mol. Biol. 86:367-380(2014).
CC -!- FUNCTION: Transcription activator that binds DNA to the C-box-like
CC motif (5'-TGCTGACGTCA-3'), ABRE elements, G-box-like motif (5'-
CC CCACGTGGCC-3'), DOF (5'-AAAG-3'), I-box (5'-GATAA-3'), BS1 (5'-AGCGGG-
CC 3'), MY3 (5'-CGACG-3'), 5'-CAGTGCGC-3' and 5'-ACTCAT-3' sequence in
CC target gene promoters (PubMed:15047879, PubMed:16810321,
CC PubMed:19531597, PubMed:21278122, PubMed:25108460). DNA-binding and
CC subsequent transcription activation is triggered by heterodimerization
CC with other bZIP proteins (e.g. BZIP1, BZIP10 and BZIP25)
CC (PubMed:16810321, PubMed:19531597, PubMed:21278122). Promotes
CC POX1/PRODH1 expression in response to hypoosmolarity stress
CC (PubMed:15047879, PubMed:16810321). Transcriptional activator of seed
CC maturation (MAT) genes (e.g. AT2S2), including seed storage protein
CC (SSP) and late embryogenesis abundant (LEA) genes (PubMed:19531597).
CC Activated by low energy stress both by transcriptional and post-
CC transcriptional mechanisms. Promotes dark-induced senescence and
CC participates in the transcriptional reprogramming of amino acid
CC metabolism during the dark-induced starvation response, especially when
CC heterodimerized with BZIP1, by triggering accumulation of specific
CC proteins including ASN1 and POX1/PRODH1 (PubMed:21278122).
CC {ECO:0000269|PubMed:15047879, ECO:0000269|PubMed:16810321,
CC ECO:0000269|PubMed:19531597, ECO:0000269|PubMed:21278122,
CC ECO:0000269|PubMed:25108460}.
CC -!- SUBUNIT: Forms heterodimers with other bZIP proteins such as BZIP1,
CC BZIP9, BZIP10, BZIP25 and BZIP63 (PubMed:16810321, PubMed:16709202,
CC PubMed:19531597, PubMed:21278122). BZIP heterodimers form complexes
CC with ABI3 that enhance G-box element-binding to increase the expression
CC of seed maturation (MAT) genes (PubMed:19531597).
CC {ECO:0000269|PubMed:16709202, ECO:0000269|PubMed:16810321,
CC ECO:0000269|PubMed:19531597, ECO:0000269|PubMed:21278122}.
CC -!- INTERACTION:
CC Q9LZP8; O22763: BZIP10; NbExp=8; IntAct=EBI-942845, EBI-942648;
CC Q9LZP8; O65683: BZIP11; NbExp=3; IntAct=EBI-942845, EBI-942769;
CC Q9LZP8; Q9SI15: BZIP2; NbExp=3; IntAct=EBI-942845, EBI-942735;
CC Q9LZP8; Q9M1G6: BZIP25; NbExp=6; IntAct=EBI-942845, EBI-942696;
CC Q9LZP8; C0Z2L5: BZIP44; NbExp=3; IntAct=EBI-942845, EBI-942804;
CC Q9LZP8; B9DGI8: BZIP63; NbExp=8; IntAct=EBI-942845, EBI-942713;
CC Q9LZP8; Q9FUD3: BZIP9; NbExp=5; IntAct=EBI-942845, EBI-942633;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:16810321}.
CC -!- TISSUE SPECIFICITY: Expressed in developing seeds.
CC {ECO:0000269|PubMed:19531597}.
CC -!- DEVELOPMENTAL STAGE: In developing seeds, accumulates in embryo
CC cotyledons during late maturation, from the torpedo to the green
CC cotyledon stages. Also present in endosperm.
CC {ECO:0000269|PubMed:19531597}.
CC -!- INDUCTION: By hypoosmolarity (PubMed:15047879, PubMed:16810321).
CC Accumulates during dark-induced starvation (PubMed:21278122).
CC {ECO:0000269|PubMed:15047879, ECO:0000269|PubMed:16810321,
CC ECO:0000269|PubMed:21278122}.
CC -!- DISRUPTION PHENOTYPE: Reduced seed maturation (MAT) genes expression
CC (PubMed:19531597). Slight reduction in the dark-induced activation of
CC POX1/PRODH1 transcript accumulation (PubMed:21278122).
CC {ECO:0000269|PubMed:19531597, ECO:0000269|PubMed:21278122}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; AF400620; AAK94024.1; -; mRNA.
DR EMBL; AL162507; CAB82956.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80350.1; -; Genomic_DNA.
DR EMBL; AY050923; AAK93600.1; -; mRNA.
DR EMBL; AY091421; AAM14360.1; -; mRNA.
DR PIR; T48034; T48034.
DR RefSeq; NP_191801.1; NM_116107.2.
DR AlphaFoldDB; Q9LZP8; -.
DR SMR; Q9LZP8; -.
DR IntAct; Q9LZP8; 15.
DR MINT; Q9LZP8; -.
DR STRING; 3702.AT3G62420.1; -.
DR PaxDb; Q9LZP8; -.
DR PRIDE; Q9LZP8; -.
DR EnsemblPlants; AT3G62420.1; AT3G62420.1; AT3G62420.
DR GeneID; 825415; -.
DR Gramene; AT3G62420.1; AT3G62420.1; AT3G62420.
DR KEGG; ath:AT3G62420; -.
DR Araport; AT3G62420; -.
DR TAIR; locus:2096024; AT3G62420.
DR eggNOG; ENOG502S1GC; Eukaryota.
DR HOGENOM; CLU_112634_1_1_1; -.
DR InParanoid; Q9LZP8; -.
DR OMA; MKKQKQM; -.
DR OrthoDB; 1416695at2759; -.
DR PhylomeDB; Q9LZP8; -.
DR PRO; PR:Q9LZP8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LZP8; baseline and differential.
DR Genevisible; Q9LZP8; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IEP:UniProtKB.
DR GO; GO:0006971; P:hypotonic response; IDA:UniProtKB.
DR GO; GO:2000693; P:positive regulation of seed maturation; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA: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; PF00170; bZIP_1; 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; Seed storage protein;
KW Storage protein; Stress response; Transcription; Transcription regulation.
FT CHAIN 1..146
FT /note="bZIP transcription factor 53"
FT /id="PRO_0000434615"
FT DOMAIN 23..86
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 25..46
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 51..65
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT MOTIF 26..33
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 51
FT /note="L->P: Impaired heterodimerization with bZIP
FT proteins; when associated with P-72."
FT /evidence="ECO:0000269|PubMed:16810321"
FT MUTAGEN 72
FT /note="A->P: Impaired heterodimerization with bZIP
FT proteins; when associated with P-51."
FT /evidence="ECO:0000269|PubMed:16810321"
SQ SEQUENCE 146 AA; 16805 MW; 3DC0F19D229597EB CRC64;
MGSLQMQTSP ESDNDPRYAT VTDERKRKRM ISNRESARRS RMRKQKQLGD LINEVTLLKN
DNAKITEQVD EASKKYIEME SKNNVLRAQA SELTDRLRSL NSVLEMVEEI SGQALDIPEI
PESMQNPWQM PCPMQPIRAS ADMFDC
