DRE1A_ARATH
ID DRE1A_ARATH Reviewed; 216 AA.
AC Q9M0L0; O65612; O82131; Q1ZZS0; Q2HII7; Q5QE70; Q5Y4C4; Q9SAZ3;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Dehydration-responsive element-binding protein 1A {ECO:0000303|PubMed:9707537};
DE Short=Protein DREB1A {ECO:0000303|PubMed:9707537};
DE AltName: Full=C-repeat/dehydration-responsive element-binding factor 3 {ECO:0000303|PubMed:9881163};
DE Short=C-repeat-binding factor 3 {ECO:0000303|PubMed:9881163};
DE Short=CRT/DRE-binding factor 3 {ECO:0000303|PubMed:9881163};
DE AltName: Full=Cold resistance-related AP2 transcription factor;
GN Name=DREB1A {ECO:0000303|PubMed:9707537};
GN Synonyms=CBF3 {ECO:0000303|PubMed:9881163}, CRAP2,
GN ERF072 {ECO:0000303|PubMed:16407444};
GN OrderedLocusNames=At4g25480 {ECO:0000312|Araport:AT4G25480};
GN ORFNames=M7J2.150 {ECO:0000312|EMBL:CAA18178.1};
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], AND INDUCTION.
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. Columbia, and 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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=9952441; DOI=10.1104/pp.119.2.463;
RA Medina J., Bargues M., Terol J., Perez-Alonso M., Salinas J.;
RT "The Arabidopsis CBF gene family is composed of three genes encoding AP2
RT domain-containing proteins whose expression is regulated by low temperature
RT but not by abscisic acid or dehydration.";
RL Plant Physiol. 119:463-470(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND VARIANTS SER-2; ILE-19 AND
RP VAL-142.
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 [GENOMIC DNA].
RA Zhou R.Y., Sun Z.X.;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Aragao F.J.L., Morais A.T., Vieira L.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. HOG;
RA Huang C.-L., Wu Z.-Y., Zhang X.-H., Brunel D., Pelletier G.;
RT "The AP2 transcription factor related to cold resistance.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [9]
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 [10]
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 [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP GENE FAMILY, FUNCTION, AND MUTAGENESIS OF VAL-63.
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 [13]
RP GENETIC REGULATION.
RX PubMed=12672693; DOI=10.1101/gad.1077503;
RA Chinnusamy V., Ohta M., Kanrar S., Lee B.-H., Hong X., Agarwal M.,
RA Zhu J.-K.;
RT "ICE1: a regulator of cold-induced transcriptome and freezing tolerance in
RT Arabidopsis.";
RL Genes Dev. 17:1043-1054(2003).
RN [14]
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 [15]
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:0000305}.
CC -!- INDUCTION: By cold stress. Positively regulated by the transcription
CC factor ICE1. Subject to degradation by the 26S proteasome pathway in
CC freezing conditions (PubMed:28344081). {ECO:0000269|PubMed:28344081,
CC ECO:0000269|PubMed:9707537, ECO:0000269|PubMed:9735350,
CC ECO:0000269|PubMed:9952441}.
CC -!- SIMILARITY: Belongs to the AP2/ERF transcription factor family. ERF
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD72616.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA18178.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81358.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB007787; BAA33791.1; -; mRNA.
DR EMBL; AB013815; BAA33434.1; -; Genomic_DNA.
DR EMBL; AF074602; AAD15977.1; -; mRNA.
DR EMBL; AF076155; AAC99370.1; -; Genomic_DNA.
DR EMBL; AF062924; AAC78646.1; -; Genomic_DNA.
DR EMBL; AY667247; AAV80414.1; -; Genomic_DNA.
DR EMBL; AY691904; AAU93686.1; -; Genomic_DNA.
DR EMBL; DQ372533; ABD14412.1; -; Genomic_DNA.
DR EMBL; DQ415923; ABD72616.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL022197; CAA18178.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161563; CAB81358.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85065.1; -; Genomic_DNA.
DR EMBL; BT024594; ABD42992.1; -; mRNA.
DR PIR; D85294; D85294.
DR PIR; JE0297; JE0297.
DR PIR; T05799; T05799.
DR PIR; T51830; T51830.
DR RefSeq; NP_567720.1; NM_118680.2.
DR AlphaFoldDB; Q9M0L0; -.
DR SMR; Q9M0L0; -.
DR BioGRID; 13939; 6.
DR STRING; 3702.AT4G25480.1; -.
DR PaxDb; Q9M0L0; -.
DR PRIDE; Q9M0L0; -.
DR EnsemblPlants; AT4G25480.1; AT4G25480.1; AT4G25480.
DR GeneID; 828652; -.
DR Gramene; AT4G25480.1; AT4G25480.1; AT4G25480.
DR KEGG; ath:AT4G25480; -.
DR Araport; AT4G25480; -.
DR TAIR; locus:2131849; AT4G25480.
DR eggNOG; ENOG502QQ5M; Eukaryota.
DR HOGENOM; CLU_063331_1_0_1; -.
DR InParanoid; Q9M0L0; -.
DR OMA; AFQDEMC; -.
DR OrthoDB; 1352198at2759; -.
DR PhylomeDB; Q9M0L0; -.
DR PRO; PR:Q9M0L0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0L0; baseline and differential.
DR Genevisible; Q9M0L0; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IPI:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0009631; P:cold acclimation; IMP:TAIR.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:TAIR.
DR GO; GO:0009409; P:response to cold; IDA:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IDA: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..216
FT /note="Dehydration-responsive element-binding protein 1A"
FT /id="PRO_0000112528"
FT DNA_BIND 50..107
FT /note="AP2/ERF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00366"
FT MOTIF 35..47
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT VARIANT 2
FT /note="N -> S (in strain: cv. Cvi-1)"
FT /evidence="ECO:0000269|PubMed:16244146"
FT VARIANT 19
FT /note="V -> I (in strain: cv. Cvi-1)"
FT /evidence="ECO:0000269|PubMed:16244146"
FT VARIANT 142
FT /note="A -> V (in strain: cv. Cvi-1)"
FT /evidence="ECO:0000269|PubMed:16244146"
FT MUTAGEN 63
FT /note="V->A: Affects the binding to the CRT/DRE cis-
FT element."
FT /evidence="ECO:0000269|PubMed:11798174"
FT CONFLICT 146
FT /note="H -> Y (in Ref. 2; BAA33434, 6; AAU93686 and 7;
FT ABD14412)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="L -> P (in Ref. 8; ABD72616)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 24236 MW; C625E2D0FAE0FFFB CRC64;
MNSFSAFSEM FGSDYESSVS SGGDYIPTLA SSCPKKPAGR KKFRETRHPI YRGVRRRNSG
KWVCEVREPN KKTRIWLGTF QTAEMAARAH DVAALALRGR SACLNFADSA WRLRIPESTC
AKDIQKAAAE AALAFQDEMC DATTDHGFDM EETLVEAIYT AEQSENAFYM HDEAMFEMPS
LLANMAEGML LPLPSVQWNH NHEVDGDDDD VSLWSY
