ERF4_TOBAC
ID ERF4_TOBAC Reviewed; 225 AA.
AC Q40477;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Ethylene-responsive transcription factor 4;
DE AltName: Full=Ethylene-responsive element-binding factor 3;
DE Short=EREBP-3;
DE AltName: Full=Ethylene-responsive element-binding factor 4 homolog;
DE AltName: Full=NtERF3;
GN Name=ERF4; Synonyms=ERF-3, ERF3;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Bright Yellow 4; TISSUE=Leaf;
RX PubMed=7756828; DOI=10.2307/3869993;
RA Ohme-Takagi M., Shinshi H.;
RT "Ethylene-inducible DNA binding proteins that interact with an ethylene
RT responsive element.";
RL Plant Cell 7:173-182(1995).
RN [2]
RP FUNCTION, AND INDUCTION.
RX DOI=10.1046/j.1365-313x.1998.00243.x;
RA Suzuki K., Suzuki N., Ohme-Takagi M., Shinshi H.;
RT "Immediate early induction of mRNAs for ethylene-responsive transcription
RT factors in tobacco leaf strips after cutting.";
RL Plant J. 15:657-665(1998).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=10652129; DOI=10.1046/j.1365-313x.1999.00634.x;
RA Yamamoto S., Suzuki K., Shinshi H.;
RT "Elicitor-responsive, ethylene-independent activation of GCC box-mediated
RT transcription that is regulated by both protein phosphorylation and
RT dephosphorylation in cultured tobacco cells.";
RL Plant J. 20:571-579(1999).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10792818; DOI=10.1046/j.1365-313x.2000.00709.x;
RA Ohta M., Ohme-Takagi M., Shinshi H.;
RT "Three ethylene-responsive transcription factors in tobacco with distinct
RT transactivation functions.";
RL Plant J. 22:29-38(2000).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=11440157; DOI=10.1271/bbb.65.1270;
RA Koyama T., Kitajima S., Sato F.;
RT "Expression of PR-5d and ERF genes in cultured tobacco cells and their NaCl
RT stress-response.";
RL Biosci. Biotechnol. Biochem. 65:1270-1273(2001).
RN [6]
RP INDUCTION.
RX PubMed=12090623; DOI=10.1023/a:1015553232309;
RA Nishiuchi T., Suzuki K., Kitajima S., Sato F., Shinshi H.;
RT "Wounding activates immediate early transcription of genes for ERFs in
RT tobacco plants.";
RL Plant Mol. Biol. 49:473-482(2002).
RN [7]
RP FUNCTION, PROBABLE UBIQUITINATION, AND INTERACTION WITH UBC2.
RX PubMed=12654868; DOI=10.1093/jxb/erg136;
RA Koyama T., Okada T., Kitajima S., Ohme-Takagi M., Shinshi H., Sato F.;
RT "Isolation of tobacco ubiquitin-conjugating enzyme cDNA in a yeast two-
RT hybrid system with tobacco ERF3 as bait and its characterization of
RT specific interaction.";
RL J. Exp. Bot. 54:1175-1181(2003).
CC -!- FUNCTION: Acts as a transcriptional repressor. 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 mediated by ethylene, that seems to depend on a
CC protein kinase/phosphatase cascade, and to be influenced by methyl-
CC jasmonate. May regulate other AtERFs (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:10652129, ECO:0000269|PubMed:10792818,
CC ECO:0000269|PubMed:12654868, ECO:0000269|PubMed:7756828,
CC ECO:0000269|Ref.2}.
CC -!- SUBUNIT: Interacts with UBC2. {ECO:0000269|PubMed:12654868}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366,
CC ECO:0000269|PubMed:10792818}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, in cultured cells and at low
CC levels in buds and leaves. Highly expressed in cell culture, especially
CC during the exponential phase. {ECO:0000269|PubMed:11440157,
CC ECO:0000269|PubMed:7756828}.
CC -!- INDUCTION: Strongly induced by ethephon (ethylene-releasing compound)
CC in buds and to lower extent in leaves. Strongly induced by
CC cycloheximide and mechanical stimuli. Wounding leads to a both local
CC and systemical transient expression, independently of ethylene, and
CC through a de-novo-protein-synthesis-independent regulation. Not
CC influenced by methyl-jasmonate. Induction by purified xylanase from
CC Trichoderma viride (TvX) and another elicitor from Phytophthora
CC infestans (PiE), that appears to be mediated by a protein kinase
CC cascade, and to be negatively regulated by protein phosphatases.
CC {ECO:0000269|PubMed:10652129, ECO:0000269|PubMed:12090623,
CC ECO:0000269|PubMed:7756828, ECO:0000269|Ref.2}.
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 -!- DOMAIN: Contains a slightly degenerated ERF-associated amphiphilic
CC repression (EAR) motif, which may be involved in the activity of
CC transcriptional repression. {ECO:0000250}.
CC -!- PTM: Probably negatively regulated by UBC2, that targets it to the
CC ubiquitin proteasome pathway after ubiquitination and leads it to
CC proteolysis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ethylene-response factor family. Class 2
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Was named ERF3 but it corresponds to Arabidopsis ERF4.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D38124; BAA07322.1; -; mRNA.
DR PIR; T02433; T02433.
DR RefSeq; NP_001312182.1; NM_001325253.1.
DR AlphaFoldDB; Q40477; -.
DR SMR; Q40477; -.
DR GeneID; 107778042; -.
DR KEGG; nta:107778042; -.
DR OMA; LAPPMEF; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
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 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 DNA-binding; Ethylene signaling pathway; Nucleus; Plant defense;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..225
FT /note="Ethylene-responsive transcription factor 4"
FT /id="PRO_0000112556"
FT DNA_BIND 26..83
FT /note="AP2/ERF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00366"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..196
FT /note="Interaction with UBC2"
FT /evidence="ECO:0000269|PubMed:12654868"
FT MOTIF 215..221
FT /note="EAR-like (transcriptional repression)"
FT /evidence="ECO:0000255"
FT COMPBIAS 81..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 225 AA; 24262 MW; BFF148E5B0B4EFAE CRC64;
MAVKNKVSNG NLKGGNVKTD GVKEVHYRGV RKRPWGRYAA EIRDPGKKSR VWLGTFDTAE
EAAKAYDTAA REFRGPKAKT NFPSPTENQS PSHSSTVESS SGENGVHAPP HAPLELDLTR
RLGSVAADGG DNCRRSGEVG YPIFHQQPTV AVLPNGQPVL LFDSLWRAGV VNRPQPYHVT
PMGFNGVNAG VGPTVSDSSS AVEENQYDGK RGIDLDLNLA PPMEF
