ERF5_TOBAC
ID ERF5_TOBAC Reviewed; 291 AA.
AC Q40478;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Ethylene-responsive transcription factor 5;
DE AltName: Full=Ethylene-responsive element-binding factor 4;
DE Short=EREBP-4;
DE AltName: Full=Ethylene-responsive element-binding factor 5 homolog;
DE AltName: Full=NtERF4;
GN Name=ERF5; Synonyms=ERF-4, ERF4;
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).
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 mediated by ethylene, that seems to depend on a
CC protein kinase/phosphatase cascade, and to be influenced by methyl-
CC jasmonate. {ECO:0000269|PubMed:10652129, ECO:0000269|PubMed:10792818,
CC ECO:0000269|PubMed:7756828, ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366,
CC ECO:0000269|PubMed:10792818}.
CC -!- TISSUE SPECIFICITY: Expressed in roots. Not expressed in cell culture.
CC {ECO:0000269|PubMed:11440157, ECO:0000269|PubMed:7756828}.
CC -!- INDUCTION: Strongly induced by ethephon (ethylene-releasing compound)
CC in buds and in leaves. Also strongly induced by cycloheximide,
CC mechanical stimuli. Wounding leads to a both local and systemic
CC expression, independently of ethylene, and through a de-novo-protein-
CC synthesis-independent regulation. Wound induction is reduced by methyl-
CC jasmonate. Induction by purified xylanase from Trichoderma viride (TvX)
CC and another elicitor from Phytophthora infestans (PiE), that appears to
CC be mediated by a protein kinase cascade, and to be negatively regulated
CC by protein phosphatases. {ECO:0000269|PubMed:10652129,
CC ECO:0000269|PubMed:12090623, ECO:0000269|PubMed:7756828,
CC 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 -!- SIMILARITY: Belongs to the ethylene-response factor family. Class 3
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Was named ERF4 but it corresponds to Arabidopsis ERF5.
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; D38125; BAA07323.1; -; mRNA.
DR PIR; T02434; T02434.
DR RefSeq; NP_001312428.1; NM_001325499.1.
DR AlphaFoldDB; Q40478; -.
DR SMR; Q40478; -.
DR PRIDE; Q40478; -.
DR GeneID; 107790518; -.
DR KEGG; nta:107790518; -.
DR OMA; CWASVWD; -.
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 2: Evidence at transcript level;
KW Activator; DNA-binding; Ethylene signaling pathway; Nucleus; Plant defense;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..291
FT /note="Ethylene-responsive transcription factor 5"
FT /id="PRO_0000112565"
FT DNA_BIND 144..202
FT /note="AP2/ERF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00366"
SQ SEQUENCE 291 AA; 32878 MW; 13E7ED8C819D5F48 CRC64;
MASPQENCTT LDLIRQHLLD DNVFMEHYCP QPILYSQSSS SSESLNSIAS ELNNETFSFE
PTLKYADTAQ SSNLDISSFF NNSKTEFDSF EFETKPNVSA ARISSNSPKQ TSFKERKPSL
NIAIPMKQQE VVQKVEVVPT EKKHYRGVRQ RPWGKFAAEI RDPNRKGTRV WLGTFDTAIE
AAKAYDRAAF KLRGSKAIVN FPLEVANFKQ QDNEILQPAN SGRKRMRETE NEEIVIKKEV
KREERVPAAA APLTPSSWSA IWEGEDGKGI FEVPPLSPLS PHMAYSQLVM I