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Dehydration-responsive element-binding protein 1A (Protein DREB1A) (C-repeat/dehydration-responsive element-binding factor 3) (C-repeat-binding factor 3) (CRT/DRE-binding factor 3) (Cold resistance-related AP2 transcription factor)

 DRE1A_ARATH             Reviewed;         216 AA.
Q9M0L0; O65612; O82131; Q1ZZS0; Q2HII7; Q5QE70; Q5Y4C4; Q9SAZ3;
24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
24-MAY-2004, sequence version 2.
25-APR-2018, entry version 124.
RecName: Full=Dehydration-responsive element-binding protein 1A {ECO:0000303|PubMed:9707537};
Short=Protein DREB1A {ECO:0000303|PubMed:9707537};
AltName: Full=C-repeat/dehydration-responsive element-binding factor 3 {ECO:0000303|PubMed:9881163};
Short=C-repeat-binding factor 3 {ECO:0000303|PubMed:9881163};
Short=CRT/DRE-binding factor 3 {ECO:0000303|PubMed:9881163};
AltName: Full=Cold resistance-related AP2 transcription factor;
Name=DREB1A {ECO:0000303|PubMed:9707537};
Synonyms=CBF3 {ECO:0000303|PubMed:9881163}, CRAP2,
ERF072 {ECO:0000303|PubMed:16407444};
OrderedLocusNames=At4g25480 {ECO:0000312|Araport:AT4G25480};
ORFNames=M7J2.150 {ECO:0000312|EMBL:CAA18178.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
STRAIN=cv. Columbia;
PubMed=9707537; DOI=10.1105/tpc.10.8.1391;
Liu Q., Kasuga M., Sakuma Y., Abe H., Miura S.,
Yamaguchi-Shinozaki K., Shinozaki K.;
"Two transcription factors, DREB1 and DREB2, with an EREBP/AP2 DNA
binding domain separate two cellular signal transduction pathways in
drought- and low-temperature-responsive gene expression, respectively,
in Arabidopsis.";
Plant Cell 10:1391-1406(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
STRAIN=cv. Columbia;
PubMed=9735350; DOI=10.1006/bbrc.1998.9267;
Shinwari Z.K., Nakashima K., Miura S., Kasuga M., Seki M.,
Yamaguchi-Shinozaki K., Shinozaki K.;
"An Arabidopsis gene family encoding DRE/CRT binding proteins involved
in low-temperature -responsive gene expression.";
Biochem. Biophys. Res. Commun. 250:161-170(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=cv. Columbia, and cv. Landsberg erecta;
PubMed=9881163; DOI=10.1046/j.1365-313x.1998.00310.x;
Gilmour S.J., Zarka D.G., Stockinger E.J., Salazar M.P.,
Houghton J.M., Thomashow M.F.;
"Low temperature regulation of the Arabidopsis CBF family of AP2
transcriptional activators as an early step in cold-induced COR gene
expression.";
Plant J. 16:433-442(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND INDUCTION.
STRAIN=cv. Columbia;
PubMed=9952441; DOI=10.1104/pp.119.2.463;
Medina J., Bargues M., Terol J., Perez-Alonso M., Salinas J.;
"The Arabidopsis CBF gene family is composed of three genes encoding
AP2 domain-containing proteins whose expression is regulated by low
temperature but not by abscisic acid or dehydration.";
Plant Physiol. 119:463-470(1999).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND VARIANTS SER-2;
ILE-19 AND VAL-142.
STRAIN=cv. Cvi-1;
PubMed=16244146; DOI=10.1104/pp.105.068510;
Alonso-Blanco C., Gomez-Mena C., Llorente F., Koornneef M.,
Salinas J., Martinez-Zapater J.M.;
"Genetic and molecular analyses of natural variation indicate CBF2 as
a candidate gene for underlying a freezing tolerance quantitative
trait locus in Arabidopsis.";
Plant Physiol. 139:1304-1312(2005).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Zhou R.Y., Sun Z.X.;
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Aragao F.J.L., Morais A.T., Vieira L.S.;
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. HOG;
Huang C.-L., Wu Z.-Y., Zhang X.-H., Brunel D., Pelletier G.;
"The AP2 transcription factor related to cold resistance.";
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[10]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Shinn P., Chen H., Kim C.J., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
[12]
GENE FAMILY, FUNCTION, AND MUTAGENESIS OF VAL-63.
PubMed=11798174; DOI=10.1006/bbrc.2001.6299;
Sakuma Y., Liu Q., Dubouzet J.G., Abe H., Shinozaki K.,
Yamaguchi-Shinozaki K.;
"DNA-binding specificity of the ERF/AP2 domain of Arabidopsis DREBs,
transcription factors involved in dehydration- and cold-inducible gene
expression.";
Biochem. Biophys. Res. Commun. 290:998-1009(2002).
[13]
GENETIC REGULATION.
PubMed=12672693; DOI=10.1101/gad.1077503;
Chinnusamy V., Ohta M., Kanrar S., Lee B.-H., Hong X., Agarwal M.,
Zhu J.-K.;
"ICE1: a regulator of cold-induced transcriptome and freezing
tolerance in Arabidopsis.";
Genes Dev. 17:1043-1054(2003).
[14]
GENE FAMILY, AND NOMENCLATURE.
PubMed=16407444; DOI=10.1104/pp.105.073783;
Nakano T., Suzuki K., Fujimura T., Shinshi H.;
"Genome-wide analysis of the ERF gene family in Arabidopsis and
rice.";
Plant Physiol. 140:411-432(2006).
[15]
INTERACTION WITH GRF1; GRF3; GRF5; GRF6; GRF7; GRF9 AND GRF10, AND
REGULATION BY PROTEASOME.
STRAIN=cv. Columbia;
PubMed=28344081; DOI=10.1016/j.molcel.2017.02.016;
Liu Z., Jia Y., Ding Y., Shi Y., Li Z., Guo Y., Gong Z., Yang S.;
"Plasma membrane CRPK1-mediated phosphorylation of 14-3-3 proteins
induces their nuclear import to fine-tune CBF signaling during cold
response.";
Mol. Cell 66:117-128(2017).
-!- FUNCTION: Transcriptional activator that binds specifically to the
DNA sequence 5'-[AG]CCGAC-3'. Binding to the C-repeat/DRE element
mediates cold-inducible transcription. CBF/DREB1 factors play a
key role in freezing tolerance and cold acclimation.
{ECO:0000269|PubMed:11798174, ECO:0000269|PubMed:16244146}.
-!- SUBUNIT: Interacts with 14-3-3 proteins GRF1, GRF3, GRF5, GRF6,
GRF7, GRF9 and GRF10 in the nucleus upon freezing.
{ECO:0000269|PubMed:28344081}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- INDUCTION: By cold stress. Positively regulated by the
transcription factor ICE1. Subject to degradation by the 26S
proteasome pathway in freezing conditions (PubMed:28344081).
{ECO:0000269|PubMed:28344081, ECO:0000269|PubMed:9707537,
ECO:0000269|PubMed:9735350, ECO:0000269|PubMed:9952441}.
-!- SIMILARITY: Belongs to the AP2/ERF transcription factor family.
ERF subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=ABD72616.1; Type=Erroneous termination; Positions=152; Note=Translated as Glu.; Evidence={ECO:0000305};
Sequence=CAA18178.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAB81358.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AB007787; BAA33791.1; -; mRNA.
EMBL; AB013815; BAA33434.1; -; Genomic_DNA.
EMBL; AF074602; AAD15977.1; -; mRNA.
EMBL; AF076155; AAC99370.1; -; Genomic_DNA.
EMBL; AF062924; AAC78646.1; -; Genomic_DNA.
EMBL; AY667247; AAV80414.1; -; Genomic_DNA.
EMBL; AY691904; AAU93686.1; -; Genomic_DNA.
EMBL; DQ372533; ABD14412.1; -; Genomic_DNA.
EMBL; DQ415923; ABD72616.1; ALT_SEQ; Genomic_DNA.
EMBL; AL022197; CAA18178.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161563; CAB81358.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002687; AEE85065.1; -; Genomic_DNA.
EMBL; BT024594; ABD42992.1; -; mRNA.
PIR; D85294; D85294.
PIR; JE0297; JE0297.
PIR; T05799; T05799.
PIR; T51830; T51830.
RefSeq; NP_567720.1; NM_118680.2.
UniGene; At.231; -.
ProteinModelPortal; Q9M0L0; -.
SMR; Q9M0L0; -.
BioGrid; 13939; 3.
STRING; 3702.AT4G25480.1; -.
PaxDb; Q9M0L0; -.
EnsemblPlants; AT4G25480.1; AT4G25480.1; AT4G25480.
GeneID; 828652; -.
Gramene; AT4G25480.1; AT4G25480.1; AT4G25480.
KEGG; ath:AT4G25480; -.
Araport; AT4G25480; -.
TAIR; locus:2131849; AT4G25480.
eggNOG; ENOG410IVY9; Eukaryota.
eggNOG; ENOG410YK37; LUCA.
InParanoid; Q9M0L0; -.
KO; K09286; -.
OMA; MNMEEAT; -.
OrthoDB; EOG09360N5C; -.
PhylomeDB; Q9M0L0; -.
PRO; PR:Q9M0L0; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q9M0L0; baseline and differential.
Genevisible; Q9M0L0; AT.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:DNA binding transcription factor activity; IDA:TAIR.
GO; GO:0009631; P:cold acclimation; IMP:TAIR.
GO; GO:0009409; P:response to cold; IDA:TAIR.
GO; GO:0009414; P:response to water deprivation; IDA:TAIR.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00018; AP2; 1.
Gene3D; 3.30.730.10; -; 1.
InterPro; IPR001471; AP2/ERF_dom.
InterPro; IPR036955; AP2/ERF_dom_sf.
InterPro; IPR016177; DNA-bd_dom_sf.
Pfam; PF00847; AP2; 1.
PRINTS; PR00367; ETHRSPELEMNT.
SMART; SM00380; AP2; 1.
SUPFAM; SSF54171; SSF54171; 1.
PROSITE; PS51032; AP2_ERF; 1.
1: Evidence at protein level;
Activator; Complete proteome; DNA-binding; Nucleus; Polymorphism;
Reference proteome; Stress response; Transcription;
Transcription regulation.
CHAIN 1 216 Dehydration-responsive element-binding
protein 1A.
/FTId=PRO_0000112528.
DNA_BIND 50 107 AP2/ERF. {ECO:0000255|PROSITE-
ProRule:PRU00366}.
MOTIF 35 47 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 205 210 Poly-Asp.
VARIANT 2 2 N -> S (in strain: cv. Cvi-1).
{ECO:0000269|PubMed:16244146}.
VARIANT 19 19 V -> I (in strain: cv. Cvi-1).
{ECO:0000269|PubMed:16244146}.
VARIANT 142 142 A -> V (in strain: cv. Cvi-1).
{ECO:0000269|PubMed:16244146}.
MUTAGEN 63 63 V->A: Affects the binding to the CRT/DRE
cis-element.
{ECO:0000269|PubMed:11798174}.
CONFLICT 146 146 H -> Y (in Ref. 2; BAA33434, 6; AAU93686
and 7; ABD14412). {ECO:0000305}.
CONFLICT 193 193 L -> P (in Ref. 8; ABD72616).
{ECO:0000305}.
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


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