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ERF1_SOLLC
ID   ERF1_SOLLC              Reviewed;         244 AA.
AC   Q84XB3;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Ethylene-responsive transcription factor 1;
DE            Short=LeERF1;
DE   AltName: Full=ERF1-like protein;
DE   AltName: Full=Ethylene-responsive element-binding factor 1;
DE            Short=EREBP-1;
GN   Name=ERF1; Synonyms=ERF-1;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION, AND DOMAIN.
RC   STRAIN=cv. MicroTom;
RX   PubMed=12935902; DOI=10.1016/s0014-5793(03)00757-9;
RA   Tournier B., Sanchez-Ballesta M.T., Jones B., Pesquet E., Regad F.,
RA   Latche A., Pech J.-C., Bouzayen M.;
RT   "New members of the tomato ERF family show specific expression pattern and
RT   diverse DNA-binding capacity to the GCC box element.";
RL   FEBS Lett. 550:149-154(2003).
CC   -!- FUNCTION: Involved in the regulation of gene expression during fruit
CC       ripening, by stress factors and by components of stress signal
CC       transduction pathways. Transcription factor that binds to the GCC-box
CC       pathogenesis-related promoter element. Probably acts as a
CC       transcriptional activator and may be involved in disease resistance
CC       pathways (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Present in stems. {ECO:0000269|PubMed:12935902}.
CC   -!- INDUCTION: Strong induction by ethylene and by wounding.
CC       {ECO:0000269|PubMed:12935902}.
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}.
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DR   EMBL; AY192367; AAO34703.1; -; mRNA.
DR   AlphaFoldDB; Q84XB3; -.
DR   SMR; Q84XB3; -.
DR   STRING; 4081.Solyc03g093610.1.1; -.
DR   PaxDb; Q84XB3; -.
DR   PRIDE; Q84XB3; -.
DR   eggNOG; ENOG502QRIC; Eukaryota.
DR   InParanoid; Q84XB3; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; Q84XB3; baseline and differential.
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   GO; GO:0009835; P:fruit ripening; 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; Fruit ripening;
KW   Nucleus; Plant defense; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..244
FT                   /note="Ethylene-responsive transcription factor 1"
FT                   /id="PRO_0000112544"
FT   DNA_BIND        106..164
FT                   /note="AP2/ERF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00366"
FT   REGION          186..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..212
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   244 AA;  27085 MW;  D090818A6CE5B833 CRC64;
     MYQLPTSTEL TFFPAEFPVY CRSSSFSSLM PCLTESWGDL PLKVNDSEDM VIYGFLQDAF
     SIGWTPSNLT SEEVKLEPRE EIEPAMSTSV SPPTVAPAAL QPKGRHYRGV RQRPWGKFAA
     EIRDPAKNGA RVWLGTYESA EEAALAYGKA AFRMRGTKAL LNFPHRIGLN EPEPVRVTVK
     RRLSESASSS VSSASESGSP KRRRKGVAAK QAELEVESRG PNVMKVGCQM FQLASSYWLV
     KIWS
 
 
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