DRE1B_ARATH
ID DRE1B_ARATH Reviewed; 213 AA.
AC P93835; O65611; Q5QE71;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Dehydration-responsive element-binding protein 1B {ECO:0000303|PubMed:9707537};
DE Short=Protein DREB1B {ECO:0000303|PubMed:9707537};
DE AltName: Full=C-repeat/dehydration-responsive element-binding factor 1 {ECO:0000303|PubMed:9023378};
DE Short=C-repeat-binding factor 1 {ECO:0000303|PubMed:9023378};
DE Short=CRT/DRE-binding factor 1 {ECO:0000303|PubMed:9023378};
GN Name=DREB1B {ECO:0000303|PubMed:9707537};
GN Synonyms=CBF1 {ECO:0000303|PubMed:9023378},
GN ERF029 {ECO:0000303|PubMed:16407444};
GN OrderedLocusNames=At4g25490 {ECO:0000312|Araport:AT4G25490};
GN ORFNames=M7J2.140 {ECO:0000312|EMBL:CAA18177.1};
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].
RC STRAIN=cv. Columbia;
RX PubMed=9023378; DOI=10.1073/pnas.94.3.1035;
RA Stockinger E.J., Gilmour S.J., Thomashow M.F.;
RT "Arabidopsis thaliana CBF1 encodes an AP2 domain-containing transcriptional
RT activator that binds to the C-repeat/DRE, a cis-acting DNA regulatory
RT element that stimulates transcription in response to low temperature and
RT water deficit.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:1035-1040(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9707537; DOI=10.2307/3870648;
RA Liu Q., Kasuga M., Sakuma Y., Abe H., Miura S., Yamaguchi-Shinozaki K.,
RA Shinozaki K.;
RT "Two transcription factors, DREB1 and DREB2, with an EREBP/AP2 DNA binding
RT domain separate two cellular signal transduction pathways in drought- and
RT low-temperature-responsive gene expression, respectively, in Arabidopsis.";
RL Plant Cell 10:1391-1406(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=9735350; DOI=10.1006/bbrc.1998.9267;
RA Shinwari Z.K., Nakashima K., Miura S., Kasuga M., Seki M.,
RA Yamaguchi-Shinozaki K., Shinozaki K.;
RT "An Arabidopsis gene family encoding DRE/CRT binding proteins involved in
RT low-temperature -responsive gene expression.";
RL Biochem. Biophys. Res. Commun. 250:161-170(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9881163; DOI=10.1046/j.1365-313x.1998.00310.x;
RA Gilmour S.J., Zarka D.G., Stockinger E.J., Salazar M.P., Houghton J.M.,
RA Thomashow M.F.;
RT "Low temperature regulation of the Arabidopsis CBF family of AP2
RT transcriptional activators as an early step in cold-induced COR gene
RT expression.";
RL Plant J. 16:433-442(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND VARIANTS LYS-127 AND
RP SER-178.
RC STRAIN=cv. Cvi-1;
RX PubMed=16244146; DOI=10.1104/pp.105.068510;
RA Alonso-Blanco C., Gomez-Mena C., Llorente F., Koornneef M., Salinas J.,
RA Martinez-Zapater J.M.;
RT "Genetic and molecular analyses of natural variation indicate CBF2 as a
RT candidate gene for underlying a freezing tolerance quantitative trait locus
RT in Arabidopsis.";
RL Plant Physiol. 139:1304-1312(2005).
RN [6]
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 [7]
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 [8]
RP GENE FAMILY, AND FUNCTION.
RX PubMed=11798174; DOI=10.1006/bbrc.2001.6299;
RA Sakuma Y., Liu Q., Dubouzet J.G., Abe H., Shinozaki K.,
RA Yamaguchi-Shinozaki K.;
RT "DNA-binding specificity of the ERF/AP2 domain of Arabidopsis DREBs,
RT transcription factors involved in dehydration- and cold-inducible gene
RT expression.";
RL Biochem. Biophys. Res. Commun. 290:998-1009(2002).
RN [9]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16407444; DOI=10.1104/pp.105.073783;
RA Nakano T., Suzuki K., Fujimura T., Shinshi H.;
RT "Genome-wide analysis of the ERF gene family in Arabidopsis and rice.";
RL Plant Physiol. 140:411-432(2006).
RN [10]
RP INTERACTION WITH GRF1; GRF3; GRF5; GRF6; GRF7; GRF9 AND GRF10, AND
RP REGULATION BY PROTEASOME.
RC STRAIN=cv. Columbia;
RX PubMed=28344081; DOI=10.1016/j.molcel.2017.02.016;
RA Liu Z., Jia Y., Ding Y., Shi Y., Li Z., Guo Y., Gong Z., Yang S.;
RT "Plasma membrane CRPK1-mediated phosphorylation of 14-3-3 proteins induces
RT their nuclear import to fine-tune CBF signaling during cold response.";
RL Mol. Cell 66:117-128(2017).
CC -!- FUNCTION: Transcriptional activator that binds specifically to the DNA
CC sequence 5'-[AG]CCGAC-3'. Binding to the C-repeat/DRE element mediates
CC cold-inducible transcription. CBF/DREB1 factors play a key role in
CC freezing tolerance and cold acclimation. {ECO:0000269|PubMed:11798174,
CC ECO:0000269|PubMed:16244146}.
CC -!- SUBUNIT: Interacts with 14-3-3 proteins GRF1, GRF3, GRF5, GRF6, GRF7,
CC GRF9 and GRF10 in the nucleus upon freezing.
CC {ECO:0000269|PubMed:28344081}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366}.
CC -!- INDUCTION: By cold stress (PubMed:9735350). Subject to degradation by
CC the 26S proteasome pathway in freezing conditions (PubMed:28344081).
CC {ECO:0000269|PubMed:28344081, ECO:0000269|PubMed:9735350}.
CC -!- SIMILARITY: Belongs to the AP2/ERF transcription factor family. ERF
CC subfamily. {ECO:0000305}.
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DR EMBL; U77378; AAC49662.1; -; mRNA.
DR EMBL; AB007788; BAA33792.1; -; mRNA.
DR EMBL; AB013816; BAA33435.1; -; Genomic_DNA.
DR EMBL; AF076155; AAC99369.1; -; Genomic_DNA.
DR EMBL; AY667247; AAV80413.1; -; Genomic_DNA.
DR EMBL; AL022197; CAA18177.1; -; Genomic_DNA.
DR EMBL; AL161563; CAB81359.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85066.1; -; Genomic_DNA.
DR PIR; JE0298; JE0298.
DR RefSeq; NP_567721.1; NM_118681.4.
DR AlphaFoldDB; P93835; -.
DR SMR; P93835; -.
DR BioGRID; 13940; 7.
DR IntAct; P93835; 4.
DR STRING; 3702.AT4G25490.1; -.
DR PaxDb; P93835; -.
DR PRIDE; P93835; -.
DR EnsemblPlants; AT4G25490.1; AT4G25490.1; AT4G25490.
DR GeneID; 828653; -.
DR Gramene; AT4G25490.1; AT4G25490.1; AT4G25490.
DR KEGG; ath:AT4G25490; -.
DR Araport; AT4G25490; -.
DR TAIR; locus:2131854; AT4G25490.
DR eggNOG; ENOG502QQ5M; Eukaryota.
DR HOGENOM; CLU_063331_1_0_1; -.
DR InParanoid; P93835; -.
DR OMA; EPFALDC; -.
DR OrthoDB; 1352198at2759; -.
DR PhylomeDB; P93835; -.
DR PRO; PR:P93835; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P93835; baseline and differential.
DR Genevisible; P93835; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0009631; P:cold acclimation; IMP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR CDD; cd00018; AP2; 1.
DR Gene3D; 3.30.730.10; -; 1.
DR InterPro; IPR001471; AP2/ERF_dom.
DR InterPro; IPR036955; AP2/ERF_dom_sf.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR045277; DRE1A-I.
DR PANTHER; PTHR31839; PTHR31839; 1.
DR Pfam; PF00847; AP2; 1.
DR PRINTS; PR00367; ETHRSPELEMNT.
DR SMART; SM00380; AP2; 1.
DR SUPFAM; SSF54171; SSF54171; 1.
DR PROSITE; PS51032; AP2_ERF; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Nucleus; Reference proteome; Stress response;
KW Transcription; Transcription regulation.
FT CHAIN 1..213
FT /note="Dehydration-responsive element-binding protein 1B"
FT /id="PRO_0000112529"
FT DNA_BIND 47..104
FT /note="AP2/ERF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00366"
FT MOTIF 32..44
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT VARIANT 127
FT /note="E -> K (in strain: cv. Cvi-1)"
FT /evidence="ECO:0000269|PubMed:16244146"
FT VARIANT 178
FT /note="T -> S (in strain: cv. Cvi-1)"
FT /evidence="ECO:0000269|PubMed:16244146"
FT CONFLICT 143
FT /note="N -> D (in Ref. 1; AAC49662, 4; AAC99369 and 5;
FT AAV80413)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 213 AA; 23830 MW; ED1B79183C3D34C3 CRC64;
MNSFSAFSEM FGSDYEPQGG DYCPTLATSC PKKPAGRKKF RETRHPIYRG VRQRNSGKWV
SEVREPNKKT RIWLGTFQTA EMAARAHDVA ALALRGRSAC LNFADSAWRL RIPESTCAKD
IQKAAAEAAL AFQDETCDTT TTNHGLDMEE TMVEAIYTPE QSEGAFYMDE ETMFGMPTLL
DNMAEGMLLP PPSVQWNHNY DGEGDGDVSL WSY
