EF100_ARATH
ID EF100_ARATH Reviewed; 268 AA.
AC O80337; Q93Z36; Q9SUK1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Ethylene-responsive transcription factor 1A;
DE Short=AtERF1A;
DE AltName: Full=Ethylene-responsive element-binding factor 1A;
DE Short=EREBP-1A;
GN Name=ERF1A; Synonyms=ERF-1, ERF100; OrderedLocusNames=At4g17500;
GN ORFNames=dl4785w, FCAALL.123;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-268, FUNCTION, AND INDUCTION.
RC STRAIN=cv. C24;
RX PubMed=10715325; DOI=10.2307/3870944;
RA Fujimoto S.Y., Ohta M., Usui A., Shinshi H., Ohme-Takagi M.;
RT "Arabidopsis ethylene responsive element binding factors act as
RT transcriptional activators or repressors of GCC box mediated gene
RT expression.";
RL Plant Cell 12:393-404(2000).
RN [6]
RP FUNCTION.
RX PubMed=9756931; DOI=10.1074/jbc.273.41.26857;
RA Hao D., Ohme-Takagi M., Sarai A.;
RT "Unique mode of GCC box recognition by the DNA-binding domain of ethylene-
RT responsive element-binding factor (ERF domain) in plant.";
RL J. Biol. Chem. 273:26857-26861(1998).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11950980; DOI=10.1104/pp.010862;
RA Onate-Sanchez L., Singh K.B.;
RT "Identification of Arabidopsis ethylene-responsive element binding factors
RT with distinct induction kinetics after pathogen infection.";
RL Plant Physiol. 128:1313-1322(2002).
RN [8]
RP STRUCTURE BY NMR OF 146-208.
RX PubMed=9736626; DOI=10.1093/emboj/17.18.5484;
RA Allen M.D., Yamasaki K., Ohme-Takagi M., Tateno M., Suzuki M.;
RT "A novel mode of DNA recognition by a beta-sheet revealed by the solution
RT structure of the GCC-box binding domain in complex with DNA.";
RL EMBO J. 17:5484-5496(1998).
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).
CC -!- FUNCTION: Acts as a transcriptional activator. Binds to the GCC-box
CC pathogenesis-related promoter element. Involved in the regulation of
CC gene expression by stress factors and by components of stress signal
CC transduction pathways. {ECO:0000269|PubMed:10715325,
CC ECO:0000269|PubMed:11950980, ECO:0000269|PubMed:9756931}.
CC -!- INTERACTION:
CC O80337; Q9FFR5: MBK23.15; NbExp=3; IntAct=EBI-25521413, EBI-25521402;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, mostly in flowers and
CC rosettes after ethylene treatment. {ECO:0000269|PubMed:11950980}.
CC -!- INDUCTION: Induced by Pseudomonas syringae tomato (both virulent and
CC avirulent avrRpt2 strains), independently of PAD4. Also induced by
CC methyl jasmonate (MeJA) independently of JAR1. Ethylene induction is
CC completely dependent on a functional ETHYLENE-INSENSITIVE2 (EIN2),
CC whereas induction by wounding does not need EIN2. Induction by
CC salicylic acid (SA) seems to be independent of PAD4 and NPR1.
CC Transcripts accumulate strongly in cycloheximide-treated plants, a
CC protein synthesis inhibitor. Seems to not be influenced by exogenous
CC abscisic acid (ABA), cold, heat, NaCl or drought stress.
CC {ECO:0000269|PubMed:10715325, ECO:0000269|PubMed:11950980}.
CC -!- DOMAIN: The AP2/ERF domain binds specifically to the 5'-GCCGCC-3'
CC motif. The affinity of this binding is higher if the seventh amino-acid
CC of this domain is basic (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AP2/ERF transcription factor family. ERF
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Two different genes At3g23240 and At4g17500 were assigned the
CC same gene name ERF1. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA32418.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB45963.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB78753.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z97343; CAB45963.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL161546; CAB78753.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CP002687; AEE83903.1; -; Genomic_DNA.
DR EMBL; AY058174; AAL25588.1; -; mRNA.
DR EMBL; AY062533; AAL32611.1; -; mRNA.
DR EMBL; BT002578; AAO00938.1; -; mRNA.
DR EMBL; AB008103; BAA32418.1; ALT_INIT; mRNA.
DR PIR; A85196; A85196.
DR PIR; T51988; T51988.
DR RefSeq; NP_567530.4; NM_117855.6.
DR PDB; 1GCC; NMR; -; A=146-208.
DR PDB; 2GCC; NMR; -; A=143-212.
DR PDB; 3GCC; NMR; -; A=143-212.
DR PDBsum; 1GCC; -.
DR PDBsum; 2GCC; -.
DR PDBsum; 3GCC; -.
DR AlphaFoldDB; O80337; -.
DR SMR; O80337; -.
DR BioGRID; 12757; 2.
DR IntAct; O80337; 1.
DR STRING; 3702.AT4G17500.1; -.
DR PaxDb; O80337; -.
DR PRIDE; O80337; -.
DR ProteomicsDB; 222067; -.
DR EnsemblPlants; AT4G17500.1; AT4G17500.1; AT4G17500.
DR GeneID; 827464; -.
DR Gramene; AT4G17500.1; AT4G17500.1; AT4G17500.
DR KEGG; ath:AT4G17500; -.
DR Araport; AT4G17500; -.
DR TAIR; locus:2129116; AT4G17500.
DR eggNOG; ENOG502QRIC; Eukaryota.
DR HOGENOM; CLU_058713_3_0_1; -.
DR InParanoid; O80337; -.
DR OMA; SGVEIKY; -.
DR OrthoDB; 1213926at2759; -.
DR PhylomeDB; O80337; -.
DR EvolutionaryTrace; O80337; -.
DR PRO; PR:O80337; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O80337; baseline and differential.
DR Genevisible; O80337; 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:0051301; P:cell division; IEP:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0010087; P:phloem or xylem histogenesis; IEP:TAIR.
DR GO; GO:0009624; P:response to nematode; 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; IPR044808; ERF_plant.
DR PANTHER; PTHR31190; PTHR31190; 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 3D-structure; Activator; DNA-binding; Ethylene signaling pathway; Nucleus;
KW Plant defense; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..268
FT /note="Ethylene-responsive transcription factor 1A"
FT /id="PRO_0000112542"
FT DNA_BIND 147..205
FT /note="AP2/ERF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00366"
FT REGION 215..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 221..237
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 220..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:1GCC"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:1GCC"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:1GCC"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:1GCC"
FT STRAND 170..180
FT /evidence="ECO:0007829|PDB:1GCC"
FT HELIX 181..196
FT /evidence="ECO:0007829|PDB:1GCC"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:3GCC"
SQ SEQUENCE 268 AA; 29190 MW; 0FB7839984E97B50 CRC64;
MSMTADSQSD YAFLESIRRH LLGESEPILS ESTASSVTQS CVTGQSIKPV YGRNPSFSKL
YPCFTESWGD LPLKENDSED MLVYGILNDA FHGGWEPSSS SSDEDRSSFP SVKIETPESF
AAVDSVPVKK EKTSPVSAAV TAAKGKHYRG VRQRPWGKFA AEIRDPAKNG ARVWLGTFET
AEDAALAYDR AAFRMRGSRA LLNFPLRVNS GEPDPVRIKS KRSSFSSSNE NGAPKKRRTV
AAGGGMDKGL TVKCEVVEVA RGDRLLVL
