BZP30_ARATH
ID BZP30_ARATH Reviewed; 519 AA.
AC Q9SIG8; A0A178VTL1;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 166.
DE RecName: Full=bZIP transcription factor 30 {ECO:0000303|PubMed:11906833};
DE Short=AtbZIP30 {ECO:0000303|PubMed:11906833};
DE AltName: Full=Protein DRINK ME {ECO:0000303|PubMed:27402171};
GN Name=BZIP30 {ECO:0000303|PubMed:11906833};
GN Synonyms=DKM {ECO:0000303|PubMed:27402171};
GN OrderedLocusNames=At2g21230 {ECO:0000312|Araport:AT2G21230};
GN ORFNames=F7O24.5 {ECO:0000312|EMBL:AAD24827.1};
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], 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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP FUNCTION, INTERACTION WITH WUS; HEC1; KNAT1; KNAT2; HAT1; BEL1 AND NGA1,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, 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).
CC -!- FUNCTION: Transcription factor that acts as a repressor of reproductive
CC development, meristem size and plant growth (PubMed:27402171). Acts as
CC a transcriptional repressor in inflorescence tissues (PubMed:27402171).
CC Interacts with well known regulators of meristem and gynoecium
CC development such as WUS, HEC1, KNAT1, KNAT2, HAT1, BEL1 and NGA1
CC (PubMed:27402171). Acts as positive regulator of JAG and OFP1
CC expression in developing gynoecia (PubMed:27402171).
CC {ECO:0000269|PubMed:27402171}.
CC -!- SUBUNIT: Interacts with WUS, HEC1, KNAT1, KNAT2, HAT1, BEL1, and NGA1.
CC {ECO:0000269|PubMed:27402171}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27402171}.
CC -!- TISSUE SPECIFICITY: Expressed in inflorescence meristem, floral organ
CC primordia, gynoecia, ovules and carpel margin meristem.
CC {ECO:0000269|PubMed:27402171}.
CC -!- DISRUPTION PHENOTYPE: Increased size of rosette leaves, increased plant
CC height, increased number of floral buds and increased length of
CC siliques. {ECO:0000269|PubMed:27402171}.
CC -!- MISCELLANEOUS: Plants overexpressing BZIP29 exhibit altered
CC reproductive development, such as a reduction in the number of floral
CC buds, reduction in ovule production with underdeveloped transmitting
CC tract and altered or aborted development of ovules.
CC {ECO:0000269|PubMed:27402171}.
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DR EMBL; AF401298; AAK84221.1; -; mRNA.
DR EMBL; AC007142; AAD24827.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07142.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61685.1; -; Genomic_DNA.
DR EMBL; AY054497; AAK96688.1; -; mRNA.
DR EMBL; AY093268; AAM13267.1; -; mRNA.
DR PIR; G84598; G84598.
DR RefSeq; NP_001323888.1; NM_001335736.1.
DR RefSeq; NP_179719.1; NM_127695.3.
DR AlphaFoldDB; Q9SIG8; -.
DR SMR; Q9SIG8; -.
DR IntAct; Q9SIG8; 9.
DR MetOSite; Q9SIG8; -.
DR PRIDE; Q9SIG8; -.
DR ProteomicsDB; 181629; -.
DR EnsemblPlants; AT2G21230.1; AT2G21230.1; AT2G21230.
DR EnsemblPlants; AT2G21230.4; AT2G21230.4; AT2G21230.
DR GeneID; 816660; -.
DR Gramene; AT2G21230.1; AT2G21230.1; AT2G21230.
DR Gramene; AT2G21230.4; AT2G21230.4; AT2G21230.
DR KEGG; ath:AT2G21230; -.
DR Araport; AT2G21230; -.
DR PhylomeDB; Q9SIG8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIG8; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0090567; P:reproductive shoot system development; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Activator; Coiled coil; DNA-binding; Growth regulation; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..519
FT /note="bZIP transcription factor 30"
FT /id="PRO_0000451165"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..393
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 398..433
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 465..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 386..460
FT /evidence="ECO:0000255"
FT COMPBIAS 7..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..65
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 519 AA; 56326 MW; 504EBE5C4626B4DC CRC64;
MGGGGDTTDT NMMQRVNSSS GTSSSSIPKH NLHLNPALIR SHHHFRHPFT GAPPPPIPPI
SPYSQIPATL QPRHSRSMSQ PSSFFSFDSL PPLNPSAPSV SVSVEEKTGA GFSPSLPPSP
FTMCHSSSSR NAGDGENLPP RKSHRRSNSD VTFGFSSMMS QNQKSPPLSS LERSISGEDT
SDWSNLVKKE PREGFYKGRK PEVEAAMDDV FTAYMNLDNI DVLNSFGGED GKNGNENVEE
MESSRGSGTK KTNGGSSSDS EGDSSASGNV KVALSSSSSG VKRRAGGDIA PTGRHYRSVS
MDSCFMGKLN FGDESSLKLP PSSSAKVSPT NSGEGNSSAY SVEFGNSEFT AAEMKKIAAD
EKLAEIVMAD PKRVKRILAN RVSAARSKER KTRYMAELEH KVQTLQTEAT TLSAQLTHLQ
RDSMGLTNQN SELKFRLQAM EQQAQLRDAL SEKLNEEVQR LKLVIGEPNR RQSGSSSSES
KMSLNPEMFQ QLSISQLQHQ QMQHSNQCST MKAKHTSND
