位置:首页 > 蛋白库 > ERF2_TOBAC
ERF2_TOBAC
ID   ERF2_TOBAC              Reviewed;         233 AA.
AC   Q40479;
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 2;
DE            Short=NtERF2;
DE   AltName: Full=Ethylene-responsive element-binding factor 2;
DE            Short=EREBP-2;
GN   Name=ERF2; Synonyms=ERF-2;
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   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 and may be involved in
CC       disease resistance pathways. Binds to the GCC-box pathogenesis-related
CC       promoter element. Involved in the regulation of gene expression by
CC       stress factors and by components of stress signal transduction pathways
CC       mediated by ethylene, that seems to depend on a protein kinase cascade,
CC       and to be influenced by methyl-jasmonate. {ECO:0000269|PubMed:10652129,
CC       ECO:0000269|PubMed:10792818, ECO:0000269|PubMed:7756828,
CC       ECO:0000269|Ref.2}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366,
CC       ECO:0000269|PubMed:10792818}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots and at low levels in buds and
CC       leaves. Not expressed in cell culture. {ECO:0000269|PubMed:7756828}.
CC   -!- INDUCTION: Induced by ethephon (ethylene-releasing compound) in buds
CC       and to a lower extent in leaves. Strongly induced by cycloheximide and
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 both protein kinases and 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   -!- SIMILARITY: Belongs to the ethylene-response factor family. Class 1
CC       subfamily. {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; D38126; BAA07324.1; -; mRNA.
DR   PIR; T02590; T02590.
DR   RefSeq; NP_001311965.1; NM_001325036.1.
DR   AlphaFoldDB; Q40479; -.
DR   SMR; Q40479; -.
DR   STRING; 4097.Q40479; -.
DR   GeneID; 107769743; -.
DR   KEGG; nta:107769743; -.
DR   OMA; WGDLPFK; -.
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   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   2: Evidence at transcript level;
KW   Activator; DNA-binding; Ethylene signaling pathway; Nucleus; Plant defense;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..233
FT                   /note="Ethylene-responsive transcription factor 2"
FT                   /id="PRO_0000112548"
FT   DNA_BIND        98..156
FT                   /note="AP2/ERF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00366"
FT   REGION          164..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..189
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   233 AA;  25563 MW;  6CD16783582C0CB5 CRC64;
     MYQPISTELP PTSFSSLMPC LTDTWGDLPL KVDDSEDMVI YGLLSDALTA GWTPFNLTST
     EIKAEPREEI EPATIPVPSV APPAETTTAQ AVVPKGRHYR GVRQRPWGKF AAEIRDPAKN
     GARVWLGTYE TAEEAALAYD KAAYRMRGSK ALLNFPHRIG LNEPEPVRLT AKRRSPEPAS
     SSISSALENG SPKRRRKAVA AKKAELEVQS RSNAMQVGCQ MEQFPVGEQL LVS
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024