BZP11_ARATH
ID BZP11_ARATH Reviewed; 159 AA.
AC O65683; P94060;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=bZIP transcription factor 11 {ECO:0000305};
DE Short=AtbZIP11 {ECO:0000303|PubMed:11906833};
DE AltName: Full=G-box-binding factor 6 {ECO:0000303|Ref.3};
DE AltName: Full=bZIP transcription factor ATB2 {ECO:0000303|PubMed:9620274};
GN Name=BZIP11 {ECO:0000303|PubMed:11906833};
GN Synonyms=ATB2 {ECO:0000303|PubMed:9620274}, GBF6 {ECO:0000303|Ref.3};
GN OrderedLocusNames=At4g34590;
GN ORFNames=T4L20.170 {ECO:0000312|EMBL:CAA18838.1};
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].
RC STRAIN=cv. Columbia;
RX PubMed=9380515; DOI=10.1093/nar/25.19.3904;
RA van Drunen C.M., Oosterling R.W., Keultjes G.M., Weisbeek P.J.,
RA van Driel R., Smeekens S.C.M.;
RT "Analysis of the chromatin domain organisation around the plastocyanin gene
RT reveals an MAR-specific sequence element in Arabidopsis thaliana.";
RL Nucleic Acids Res. 25:3904-3911(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION BY LIGHT.
RX PubMed=9620274; DOI=10.1023/a:1005964327725;
RA Rook F., Weisbeek P., Smeekens S.;
RT "The light-regulated Arabidopsis bZIP transcription factor gene ATB2
RT encodes a protein with an unusually long leucine zipper domain.";
RL Plant Mol. Biol. 37:171-178(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Jarillo J.A., Cashmore A.R.;
RT "GBF5 and GBF6: two bZIP proteins from Arabidopsis that belong to a new
RT subfamily of the GBF transcription factors.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [5]
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 [6]
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 [7]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9721683; DOI=10.1046/j.1365-313x.1998.00205.x;
RA Rook F., Gerrits N., Kortstee A., van Kampen M., Borrias M., Weisbeek P.,
RA Smeekens S.;
RT "Sucrose-specific signalling represses translation of the Arabidopsis ATB2
RT bZIP transcription factor gene.";
RL Plant J. 15:253-263(1998).
RN [8]
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 [9]
RP INDUCTION.
RX PubMed=15208401; DOI=10.1105/tpc.019349;
RA Wiese A., Elzinga N., Wobbes B., Smeekens S.;
RT "A conserved upstream open reading frame mediates sucrose-induced
RT repression of translation.";
RL Plant Cell 16:1717-1729(2004).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, 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 [11]
RP INTERACTION WITH BZIP1; 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 [12]
RP FUNCTION.
RX PubMed=18088315; DOI=10.1111/j.1365-313x.2007.03385.x;
RA Hanson J., Hanssen M., Wiese A., Hendriks M.M., Smeekens S.;
RT "The sucrose regulated transcription factor bZIP11 affects amino acid
RT metabolism by regulating the expression of ASPARAGINE SYNTHETASE1 and
RT PROLINE DEHYDROGENASE2.";
RL Plant J. 53:935-949(2008).
RN [13]
RP FUNCTION.
RX PubMed=21534971; DOI=10.1111/j.1469-8137.2011.03735.x;
RA Ma J., Hanssen M., Lundgren K., Hernandez L., Delatte T., Ehlert A.,
RA Liu C.M., Schluepmann H., Droege-Laser W., Moritz T., Smeekens S.,
RA Hanson J.;
RT "The sucrose-regulated Arabidopsis transcription factor bZIP11 reprograms
RT metabolism and regulates trehalose metabolism.";
RL New Phytol. 191:733-745(2011).
RN [14]
RP FUNCTION, AND INTERACTION WITH ADA2B.
RX PubMed=24861440; DOI=10.1038/ncomms4883;
RA Weiste C., Droege-Laser W.;
RT "The Arabidopsis transcription factor bZIP11 activates auxin-mediated
RT transcription by recruiting the histone acetylation machinery.";
RL Nat. Commun. 5:3883-3883(2014).
RN [15]
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 DNA sequence 5'-
CC ACTCAT-3' in target gene promoters. Promotes POX1/PRODH1 expression in
CC response to hypoosmolarity stress (PubMed:15047879). Positively
CC regulates the expression of ASN1 and POX2/PRODH2 genes, which are
CC involved in amino acid metabolism (PubMed:18088315). Regulates several
CC metabolic pathways such as myo-inositol, raffinose and trehalose.
CC Regulates several trehalose metabolism genes, including TRE1, TPP5 and
CC TPP6 (PubMed:21534971). Mediates recruitment of the histone acetylation
CC machinery to activate auxin-induced transcription. Interacts with ADA2B
CC adapter protein to promote ADA2B-mediated recruitment of SAGA-like
CC histone acetyltransferase complexes to specific auxin-responsive genes
CC (PubMed:24861440). {ECO:0000269|PubMed:15047879,
CC ECO:0000269|PubMed:18088315, ECO:0000269|PubMed:21534971,
CC ECO:0000269|PubMed:24861440}.
CC -!- SUBUNIT: Forms heterodimers with BZIP1, BZIP9, BZIP10, BZIP25 and
CC BZIP63 (PubMed:16709202). Interacts with ADA2B (PubMed:24861440).
CC {ECO:0000269|PubMed:16709202, ECO:0000269|PubMed:24861440,
CC ECO:0000269|PubMed:26263501}.
CC -!- INTERACTION:
CC O65683; Q9FGX2: BZIP1; NbExp=5; IntAct=EBI-942769, EBI-942623;
CC O65683; O22763: BZIP10; NbExp=3; IntAct=EBI-942769, EBI-942648;
CC O65683; Q9M1G6: BZIP25; NbExp=6; IntAct=EBI-942769, EBI-942696;
CC O65683; Q9LZP8: BZIP53; NbExp=3; IntAct=EBI-942769, EBI-942845;
CC O65683; B9DGI8: BZIP63; NbExp=4; IntAct=EBI-942769, EBI-942713;
CC O65683; Q9FUD3: BZIP9; NbExp=3; IntAct=EBI-942769, EBI-942633;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:15047879}.
CC -!- TISSUE SPECIFICITY: Highly expressed in stems and flowers
CC (PubMed:9620274). Expressed in root tips, cotyledons, leaf vasculature,
CC embryos, apical parts of siliques and funiculi (PubMed:9721683).
CC {ECO:0000269|PubMed:9620274, ECO:0000269|PubMed:9721683}.
CC -!- INDUCTION: By light (PubMed:9620274). Induced by hypoosmolarity
CC (PubMed:15047879). Repressed by sucrose (at protein level)
CC (PubMed:9721683, PubMed:15208401). {ECO:0000269|PubMed:15047879,
CC ECO:0000269|PubMed:15208401, ECO:0000269|PubMed:9620274,
CC ECO:0000269|PubMed:9721683}.
CC -!- MISCELLANEOUS: A highly conserved upstream open reading frame (uORF)
CC coding for 42 amino acids is essential for the BZIP11 sucrose-induced
CC repression of translation (SIRT) (PubMed:15208401). Plants over-
CC expressing BZIP11 show severe alterations of plant growth and
CC development, reduced seed set and viability (PubMed:18088315).
CC {ECO:0000269|PubMed:15208401, ECO:0000269|PubMed:18088315}.
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DR EMBL; Z82043; CAB04795.1; -; Genomic_DNA.
DR EMBL; AF053940; AAG17475.1; -; mRNA.
DR EMBL; X99747; CAA68078.1; -; Genomic_DNA.
DR EMBL; AL023094; CAA18838.1; -; Genomic_DNA.
DR EMBL; AL161585; CAB80176.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86397.1; -; Genomic_DNA.
DR EMBL; AY063979; AAL36335.1; -; mRNA.
DR EMBL; AY096396; AAM20036.1; -; mRNA.
DR PIR; T05279; T05279.
DR RefSeq; NP_195185.1; NM_119625.3.
DR AlphaFoldDB; O65683; -.
DR SMR; O65683; -.
DR IntAct; O65683; 11.
DR MINT; O65683; -.
DR STRING; 3702.AT4G34590.1; -.
DR PaxDb; O65683; -.
DR PRIDE; O65683; -.
DR EnsemblPlants; AT4G34590.1; AT4G34590.1; AT4G34590.
DR GeneID; 829611; -.
DR Gramene; AT4G34590.1; AT4G34590.1; AT4G34590.
DR KEGG; ath:AT4G34590; -.
DR Araport; AT4G34590; -.
DR TAIR; locus:2139584; AT4G34590.
DR eggNOG; ENOG502S0BS; Eukaryota.
DR HOGENOM; CLU_112634_1_0_1; -.
DR InParanoid; O65683; -.
DR OMA; ASADMFH; -.
DR OrthoDB; 1624574at2759; -.
DR PhylomeDB; O65683; -.
DR PRO; PR:O65683; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65683; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0017148; P:negative regulation of translation; IMP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0009744; P:response to sucrose; IEP:TAIR.
DR GO; GO:0080149; P:sucrose induced translational repression; IMP:TAIR.
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 DNA-binding; Nucleus; Reference proteome; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..159
FT /note="bZIP transcription factor 11"
FT /id="PRO_0000436840"
FT DOMAIN 25..88
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 27..48
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 53..67
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 112
FT /note="S -> SN (in Ref. 1; CAB04795, 3; CAA68078 and 2;
FT AAG17475)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 159 AA; 18035 MW; 8A355CF86660E169 CRC64;
MESSSSGTTS STIQTSSGSE ESLMEQRKRK RMLSNRESAR RSRMKKQKLL DDLTAQVNHL
KKENTEIVTS VSITTQHYLT VEAENSVLRA QLDELNHRLQ SLNDIIEFLD SSNNNNNNNM
GMCSNPLVGL ECDDFFVNQM NMSYIMNQPL MASSDALMY
