BZP29_ARATH
ID BZP29_ARATH Reviewed; 547 AA.
AC Q8H1F0; Q8RXK4; Q9T0J7;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=bZIP transcription factor 29 {ECO:0000303|PubMed:11906833};
DE Short=AtbZIP29 {ECO:0000303|PubMed:11906833};
DE AltName: Full=Protein DRINK ME-LIKE {ECO:0000303|PubMed:27402171};
GN Name=BZIP29 {ECO:0000303|PubMed:11906833};
GN Synonyms=DKML {ECO:0000303|PubMed:27402171};
GN OrderedLocusNames=At4g38900 {ECO:0000312|Araport:AT4G38900};
GN ORFNames=F19H22.5 {ECO:0000312|EMBL:AEE86989.1};
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 [MRNA] (ISOFORM 2), 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 [2]
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 [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] (ISOFORM 1).
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 FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25093810; DOI=10.1371/journal.pone.0103930;
RA Tsugama D., Liu S., Takano T.;
RT "Analysis of functions of VIP1 and its close homologs in osmosensory
RT responses of Arabidopsis thaliana.";
RL PLoS ONE 9:e103930-e103930(2014).
RN [6]
RP FUNCTION, HOMODIMERIZATION, AND TISSUE SPECIFICITY.
RX PubMed=27660483; DOI=10.1093/jxb/erw347;
RA Van Leene J., Blomme J., Kulkarni S.R., Cannoot B., De Winne N.,
RA Eeckhout D., Persiau G., Van De Slijke E., Vercruysse L.,
RA Vanden Bossche R., Heyndrickx K.S., Vanneste S., Goossens A., Gevaert K.,
RA Vandepoele K., Gonzalez N., Inze D., De Jaeger G.;
RT "Functional characterization of the Arabidopsis transcription factor bZIP29
RT reveals its role in leaf and root development.";
RL J. Exp. Bot. 67:5825-5840(2016).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27402171; DOI=10.1111/tpj.13264;
RA Lozano-Sotomayor P., Chavez Montes R.A., Silvestre-Vano M.,
RA Herrera-Ubaldo H., Greco R., Pablo-Villa J., Galliani B.M.,
RA Diaz-Ramirez D., Weemen M., Boutilier K., Pereira A., Colombo L.,
RA Madueno F., Marsch-Martinez N., de Folter S.;
RT "Altered expression of the bZIP transcription factor DRINK ME affects
RT growth and reproductive development in Arabidopsis thaliana.";
RL Plant J. 88:437-451(2016).
RN [8]
RP FUNCTION.
RX PubMed=26923089; DOI=10.1111/ppl.12439;
RA Ben Daniel B.H., Cattan E., Wachtel C., Avrahami D., Glick Y., Malichy A.,
RA Gerber D., Miller G.;
RT "Identification of novel transcriptional regulators of Zat12 using
RT comprehensive yeast one-hybrid screens.";
RL Physiol. Plantarum 157:422-441(2016).
CC -!- FUNCTION: Transcription factor that acts as a repressor of reproductive
CC development, meristem size and plant growth (PubMed:27402171).
CC Regulates meristem size, cell size and cell number during plant
CC development (PubMed:27660483). Binds to the promoters of the cell cycle
CC regulators CYCB1-2 and SMR4, and genes involved in cell wall
CC organization, such as XTH9, EXPA1 and EXPA3 (PubMed:27660483).
CC Possesses transactivation activity in yeast (PubMed:25093810).
CC Possesses transactivation activity in plant protoplasts
CC (PubMed:27660483). Plays a role in abiotic stress response by binding
CC to the 5'-CAGCTG-3' DNA sequence found in the promoters of MYB44 and
CC TRX8 (PubMed:27660483). Plays a role in osmosensory response by binding
CC to the 5'-AGCTGT/G-3' DNA sequence found in the promoters of the
CC hypoosmolarity-responsive genes CYP707A1 and CYP707A3 (PubMed:25093810,
CC PubMed:27660483). Binds to the 5'-AGCTGT-3' DNA sequence found in the
CC promoter of the ZAT1 gene in response to abiotic stresses, such as
CC oxidative stress, high-light, osmotic shock, salt and heat stresses
CC (PubMed:26923089). {ECO:0000269|PubMed:25093810,
CC ECO:0000269|PubMed:26923089, ECO:0000269|PubMed:27402171,
CC ECO:0000269|PubMed:27660483}.
CC -!- SUBUNIT: Forms homodimers. {ECO:0000269|PubMed:27660483}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25093810}. Nucleus
CC {ECO:0000269|PubMed:25093810}. Note=Transiently accumulates in the
CC nucleus when cells are exposed to hypoosmotic conditions.
CC {ECO:0000269|PubMed:25093810}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8H1F0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8H1F0-2; Sequence=VSP_060767;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers
CC (PubMed:25093810). Expressed in the root tips, lateral root primordia,
CC and guard cells of leaves, hypocotyls and anthers (PubMed:27660483).
CC {ECO:0000269|PubMed:25093810, ECO:0000269|PubMed:27660483}.
CC -!- DISRUPTION PHENOTYPE: Increased size of rosette leaves, increased plant
CC height and increased length of siliques. {ECO:0000269|PubMed:27402171}.
CC -!- MISCELLANEOUS: Plants lines expressing a bZIP29-SRDX dominant-negative
CC repressor under a constitutive 35S promoter are seedling lethal.
CC {ECO:0000269|PubMed:27660483}.
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DR EMBL; AF401297; AAK84220.1; -; mRNA.
DR EMBL; AL035656; CAB38624.1; -; Genomic_DNA.
DR EMBL; AL161594; CAB80553.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86988.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86989.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86990.1; -; Genomic_DNA.
DR EMBL; AY080839; AAL87314.1; -; mRNA.
DR EMBL; AY150435; AAN12977.1; -; mRNA.
DR PIR; T06089; T06089.
DR RefSeq; NP_001031810.1; NM_001036733.4. [Q8H1F0-1]
DR RefSeq; NP_195601.1; NM_120050.4. [Q8H1F0-2]
DR RefSeq; NP_849520.1; NM_179189.4. [Q8H1F0-1]
DR AlphaFoldDB; Q8H1F0; -.
DR SMR; Q8H1F0; -.
DR IntAct; Q8H1F0; 8.
DR STRING; 3702.AT4G38900.1; -.
DR PRIDE; Q8H1F0; -.
DR EnsemblPlants; AT4G38900.1; AT4G38900.1; AT4G38900. [Q8H1F0-2]
DR EnsemblPlants; AT4G38900.2; AT4G38900.2; AT4G38900. [Q8H1F0-1]
DR EnsemblPlants; AT4G38900.3; AT4G38900.3; AT4G38900. [Q8H1F0-1]
DR GeneID; 830045; -.
DR Gramene; AT4G38900.1; AT4G38900.1; AT4G38900. [Q8H1F0-2]
DR Gramene; AT4G38900.2; AT4G38900.2; AT4G38900. [Q8H1F0-1]
DR Gramene; AT4G38900.3; AT4G38900.3; AT4G38900. [Q8H1F0-1]
DR KEGG; ath:AT4G38900; -.
DR Araport; AT4G38900; -.
DR TAIR; locus:2141826; AT4G38900.
DR eggNOG; ENOG502QRIA; Eukaryota.
DR HOGENOM; CLU_026205_4_1_1; -.
DR OMA; FRGQMRQ; -.
DR OrthoDB; 1209347at2759; -.
DR PhylomeDB; Q8H1F0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8H1F0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0042803; F:protein homodimerization 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:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0090567; P:reproductive shoot system development; IMP:TAIR.
DR CDD; cd14703; bZIP_plant_RF2; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR044759; bZIP_RF2.
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.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Cytoplasm; DNA-binding;
KW Growth regulation; Nucleus; Reference proteome; Stress response;
KW Transcription; Transcription regulation.
FT CHAIN 1..547
FT /note="bZIP transcription factor 29"
FT /id="PRO_0000451164"
FT DOMAIN 394..457
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..417
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 422..457
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 517..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 416..469
FT /evidence="ECO:0000255"
FT COMPBIAS 11..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 399
FT /note="K -> KRNDPLF (in isoform 2)"
FT /id="VSP_060767"
FT CONFLICT 217
FT /note="E -> K (in Ref. 4; AAL87314)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 547 AA; 60414 MW; E8277485A231C07B CRC64;
MGDTEKCNSD MIQRLHSSFG TTSSSIPKNP ISQLDLNPNF IRSSAPQFSK PFSDSGKRIG
VPPSHPNLIP PTSPFSQIPT TRQPGSHNFN PGGANHSRSM SQPNSFFSFD SLPPLSPSPF
RDHDVSMEDR DSGVFNSNHS LPPSPFTRCN STSSSSLRVG ESLPPRKSHR RSNSDIPSGF
NSMPLIPPRP LERSFSGGEC ADWSKSNPFV KKESSCEREG VGEREAMDDL FSAYMNLENI
DVLNSSEADD SKNGNENRDD MESSRASGTK TNGSDTEGES SSVNESANNN MNSSGEKRES
VKRRAAGGDI APTTRHYRSV SVDSCFMEKL SFGDESLKPP PSPGSMSRKV SPTNSVDGNS
GAAFSIEFNN GEFTAAEMKK IMANDKLAEM AMSDPKRVKR ILANRQSAAR SKERKMRYIV
ELEHKVQTLQ TEATTLSAQL TLLQRDMMGL TNQNNELKFR LQAMEQQARL RDALNEALNG
EVQRLKLAIG ESSQNESERS KMQSLNAEMF QQLNISQLRQ QPQQMQQQSH QQNHQNGTMA
TKSESNE
