DRE2A_ARATH
ID DRE2A_ARATH Reviewed; 335 AA.
AC O82132; Q5Y4C5;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 158.
DE RecName: Full=Dehydration-responsive element-binding protein 2A {ECO:0000303|PubMed:10809011, ECO:0000303|PubMed:9707537};
DE Short=Protein DREB2A {ECO:0000303|PubMed:10809011, ECO:0000303|PubMed:9707537};
GN Name=DREB2A {ECO:0000303|PubMed:10809011, ECO:0000303|PubMed:9707537};
GN Synonyms=ERF045 {ECO:0000303|PubMed:16407444};
GN OrderedLocusNames=At5g05410 {ECO:0000312|Araport:AT5G05410};
GN ORFNames=K18I23.22 {ECO:0000312|EMBL:BAB09984.1};
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], TISSUE SPECIFICITY, 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], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10809011; DOI=10.1023/a:1006321900483;
RA Nakashima K., Shinwari Z.K., Sakuma Y., Seki M., Miura S., Shinozaki K.,
RA Yamaguchi-Shinozaki K.;
RT "Organization and expression of two Arabidopsis DREB2 genes encoding DRE-
RT binding proteins involved in dehydration- and high-salinity-responsive gene
RT expression.";
RL Plant Mol. Biol. 42:657-665(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-167.
RA Zhou R.Y., Sun Z.X.;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP GENE FAMILY, FUNCTION, INDUCTION, AND MUTAGENESIS OF VAL-91 AND GLU-96.
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 [8]
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 [9]
RP INTERACTION WITH DRIP1 AND DRIP2, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=18552202; DOI=10.1105/tpc.107.057380;
RA Qin F., Sakuma Y., Tran L.-S.H., Maruyama K., Kidokoro S., Fujita Y.,
RA Fujita M., Umezawa T., Sawano Y., Miyazono K., Tanokura M., Shinozaki K.,
RA Yamaguchi-Shinozaki K.;
RT "Arabidopsis DREB2A-interacting proteins function as RING E3 ligases and
RT negatively regulate plant drought stress-responsive gene expression.";
RL Plant Cell 20:1693-1707(2008).
RN [10]
RP INTERACTION WITH MED25.
RX PubMed=21536906; DOI=10.1073/pnas.1002981108;
RA Elfving N., Davoine C., Benlloch R., Blomberg J., Braennstroem K.,
RA Mueller D., Nilsson A., Ulfstedt M., Ronne H., Wingsle G., Nilsson O.,
RA Bjoerklund S.;
RT "The Arabidopsis thaliana Med25 mediator subunit integrates environmental
RT cues to control plant development.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:8245-8250(2011).
RN [11]
RP FUNCTION, INTERACTION WITH DPB3-1, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=25490919; DOI=10.1105/tpc.114.132928;
RA Sato H., Mizoi J., Tanaka H., Maruyama K., Qin F., Osakabe Y., Morimoto K.,
RA Ohori T., Kusakabe K., Nagata M., Shinozaki K., Yamaguchi-Shinozaki K.;
RT "Arabidopsis DPB3-1, a DREB2A interactor, specifically enhances heat
RT stress-induced gene expression by forming a heat stress-specific
RT transcriptional complex with NF-Y subunits.";
RL Plant Cell 26:4954-4973(2014).
CC -!- FUNCTION: Transcriptional activator that binds specifically to the DNA
CC sequence 5'-[AG]CCGAC-3' (PubMed:11798174). Binding to the C-repeat/DRE
CC element mediates high salinity- and dehydration-inducible transcription
CC (PubMed:11798174). Promotes the expression of heat stress-inducible
CC genes by contributing to the formation of a heat stress-specific
CC transcriptional complex with NF-Y subunits (e.g. DPB3-1, NF-YA2 and NF-
CC YB3) at the promoter of target genes, thus promoting heat tolerance
CC (PubMed:25490919). {ECO:0000269|PubMed:11798174,
CC ECO:0000269|PubMed:25490919}.
CC -!- SUBUNIT: Interacts with MED25 (PubMed:18552202, PubMed:21536906). Binds
CC to DPB3-1 in the nucleus during heat-stress (PubMed:25490919).
CC {ECO:0000269|PubMed:18552202, ECO:0000269|PubMed:21536906,
CC ECO:0000269|PubMed:25490919}.
CC -!- INTERACTION:
CC O82132; A0SVK0: DOG1; NbExp=3; IntAct=EBI-1786840, EBI-25512274;
CC O82132; Q9M9Y4: DRIP1; NbExp=4; IntAct=EBI-1786840, EBI-1786858;
CC O82132; Q9FWY7: IMPA6; NbExp=3; IntAct=EBI-1786840, EBI-4431755;
CC O82132; Q7XYY2-1: MED25; NbExp=3; IntAct=EBI-1786840, EBI-15924435;
CC O82132; Q8RY59: RCD1; NbExp=3; IntAct=EBI-1786840, EBI-2118043;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366,
CC ECO:0000269|PubMed:18552202, ECO:0000269|PubMed:25490919}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O82132-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed preferentially in roots and stems, and at
CC a lower level in leaves. {ECO:0000269|PubMed:10809011,
CC ECO:0000269|PubMed:9707537}.
CC -!- INDUCTION: By high-salt and drought stresses.
CC {ECO:0000269|PubMed:10809011, ECO:0000269|PubMed:11798174,
CC ECO:0000269|PubMed:9707537}.
CC -!- PTM: Ubiquitinated by DRIP1 and DRIP2. Ubiquitination probably leads to
CC its subsequent degradation, thus negatively regulating response to
CC drought. {ECO:0000269|PubMed:18552202}.
CC -!- SIMILARITY: Belongs to the AP2/ERF transcription factor family. ERF
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAU93685.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB007790; BAA33794.1; -; mRNA.
DR EMBL; AB016570; BAA36705.1; -; Genomic_DNA.
DR EMBL; AB010692; BAB09984.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90870.1; -; Genomic_DNA.
DR EMBL; AY063972; AAL36328.1; -; mRNA.
DR EMBL; AY691903; AAU93685.1; ALT_SEQ; Genomic_DNA.
DR PIR; T51833; T51833.
DR RefSeq; NP_196160.1; NM_120623.3. [O82132-1]
DR PDB; 5OAP; NMR; -; A=255-272.
DR PDBsum; 5OAP; -.
DR AlphaFoldDB; O82132; -.
DR SMR; O82132; -.
DR BioGRID; 15703; 11.
DR DIP; DIP-40571N; -.
DR IntAct; O82132; 33.
DR STRING; 3702.AT5G05410.1; -.
DR PaxDb; O82132; -.
DR EnsemblPlants; AT5G05410.1; AT5G05410.1; AT5G05410. [O82132-1]
DR GeneID; 830424; -.
DR Gramene; AT5G05410.1; AT5G05410.1; AT5G05410. [O82132-1]
DR KEGG; ath:AT5G05410; -.
DR Araport; AT5G05410; -.
DR TAIR; locus:2153504; AT5G05410.
DR eggNOG; ENOG502QTBU; Eukaryota.
DR InParanoid; O82132; -.
DR OMA; NGAYTHE; -.
DR OrthoDB; 1404403at2759; -.
DR PhylomeDB; O82132; -.
DR PRO; PR:O82132; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O82132; baseline and differential.
DR Genevisible; O82132; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0010286; P:heat acclimation; IEP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0009408; P:response to heat; IDA:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:TAIR.
DR GO; GO:0010224; P:response to UV-B; IGI:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR CDD; cd00018; AP2; 1.
DR DisProt; DP02209; -.
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 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 3D-structure; Activator; Alternative splicing; DNA-binding; Nucleus;
KW Reference proteome; Stress response; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..335
FT /note="Dehydration-responsive element-binding protein 2A"
FT /id="PRO_0000112534"
FT DNA_BIND 78..135
FT /note="AP2/ERF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00366"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 19..55
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 12..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 91
FT /note="V->A: Affects the binding to the CRT/DRE cis-
FT element."
FT /evidence="ECO:0000269|PubMed:11798174"
FT MUTAGEN 96
FT /note="E->D: Affects the binding to the CRT/DRE cis-
FT element."
FT /evidence="ECO:0000269|PubMed:11798174"
FT CONFLICT 162
FT /note="V -> M (in Ref. 6; AAU93685)"
FT /evidence="ECO:0000305"
FT HELIX 261..270
FT /evidence="ECO:0007829|PDB:5OAP"
SQ SEQUENCE 335 AA; 37703 MW; 9742CE579CC7314C CRC64;
MAVYDQSGDR NRTQIDTSRK RKSRSRGDGT TVAERLKRWK EYNETVEEVS TKKRKVPAKG
SKKGCMKGKG GPENSRCSFR GVRQRIWGKW VAEIREPNRG SRLWLGTFPT AQEAASAYDE
AAKAMYGPLA RLNFPRSDAS EVTSTSSQSE VCTVETPGCV HVKTEDPDCE SKPFSGGVEP
MYCLENGAEE MKRGVKADKH WLSEFEHNYW SDILKEKEKQ KEQGIVETCQ QQQQDSLSVA
DYGWPNDVDQ SHLDSSDMFD VDELLRDLNG DDVFAGLNQD RYPGNSVANG SYRPESQQSG
FDPLQSLNYG IPPFQLEGKD GNGFFDDLSY LDLEN
