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DRE1C_ARATH
ID   DRE1C_ARATH             Reviewed;         216 AA.
AC   Q9SYS6; O65613; O82776; Q08A88; Q5QE69;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Dehydration-responsive element-binding protein 1C;
DE            Short=Protein DREB1C;
DE   AltName: Full=C-repeat/dehydration-responsive element-binding factor 2;
DE            Short=C-repeat-binding factor 2;
DE            Short=CRT/DRE-binding factor 2;
GN   Name=DREB1C; Synonyms=CBF2, ERF030; OrderedLocusNames=At4g25470;
GN   ORFNames=M7J2.161;
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=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=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 VARIANT THR-49.
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [9]
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   [10]
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).
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   -!- INTERACTION:
CC       Q9SYS6; Q6NM52: At4g15770; NbExp=3; IntAct=EBI-15198565, EBI-25516637;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves and roots.
CC       {ECO:0000269|PubMed:9735350}.
CC   -!- INDUCTION: By cold stress. {ECO:0000269|PubMed:9735350,
CC       ECO:0000269|PubMed:9952441}.
CC   -!- SIMILARITY: Belongs to the AP2/ERF transcription factor family. ERF
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AB007789; BAA33793.1; -; mRNA.
DR   EMBL; AB013817; BAA33436.1; -; Genomic_DNA.
DR   EMBL; AF074601; AAD15976.1; -; mRNA.
DR   EMBL; AF076155; AAC99371.1; -; Genomic_DNA.
DR   EMBL; AF062925; AAC78647.1; -; Genomic_DNA.
DR   EMBL; AY667247; AAV80415.1; -; Genomic_DNA.
DR   EMBL; AL022197; CAB51470.1; -; Genomic_DNA.
DR   EMBL; AL161563; CAB81357.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85064.1; -; Genomic_DNA.
DR   EMBL; BT028991; ABI93900.1; -; mRNA.
DR   PIR; JE0299; JE0299.
DR   RefSeq; NP_567719.1; NM_118679.2.
DR   AlphaFoldDB; Q9SYS6; -.
DR   SMR; Q9SYS6; -.
DR   BioGRID; 13938; 4.
DR   IntAct; Q9SYS6; 4.
DR   STRING; 3702.AT4G25470.1; -.
DR   PaxDb; Q9SYS6; -.
DR   PRIDE; Q9SYS6; -.
DR   EnsemblPlants; AT4G25470.1; AT4G25470.1; AT4G25470.
DR   GeneID; 828651; -.
DR   Gramene; AT4G25470.1; AT4G25470.1; AT4G25470.
DR   KEGG; ath:AT4G25470; -.
DR   Araport; AT4G25470; -.
DR   TAIR; locus:2131834; AT4G25470.
DR   eggNOG; ENOG502QQ5M; Eukaryota.
DR   HOGENOM; CLU_063331_1_0_1; -.
DR   InParanoid; Q9SYS6; -.
DR   OMA; CVEMEGS; -.
DR   OrthoDB; 1352198at2759; -.
DR   PhylomeDB; Q9SYS6; -.
DR   PRO; PR:Q9SYS6; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SYS6; baseline and differential.
DR   Genevisible; Q9SYS6; AT.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS: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: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..216
FT                   /note="Dehydration-responsive element-binding protein 1C"
FT                   /id="PRO_0000112530"
FT   DNA_BIND        50..107
FT                   /note="AP2/ERF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00366"
FT   REGION          15..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           35..47
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   VARIANT         49
FT                   /note="P -> T (in strain: cv. Cvi-1)"
FT                   /evidence="ECO:0000269|PubMed:16244146"
FT   CONFLICT        4
FT                   /note="F -> C (in Ref. 3; AAC99371)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   216 AA;  24264 MW;  BE3A4824A678B968 CRC64;
     MNSFSAFSEM FGSDYESPVS SGGDYSPKLA TSCPKKPAGR KKFRETRHPI YRGVRQRNSG
     KWVCELREPN KKTRIWLGTF QTAEMAARAH DVAAIALRGR SACLNFADSA WRLRIPESTC
     AKEIQKAAAE AALNFQDEMC HMTTDAHGLD MEETLVEAIY TPEQSQDAFY MDEEAMLGMS
     SLLDNMAEGM LLPSPSVQWN YNFDVEGDDD VSLWSY
 
 
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