EGR1_TAEGU
ID EGR1_TAEGU Reviewed; 193 AA.
AC O73693;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Early growth response protein 1;
DE Short=EGR-1;
DE AltName: Full=Zinc finger protein ZENK {ECO:0000303|PubMed:9501495};
DE Flags: Fragment;
GN Name=EGR1; Synonyms=ZENK {ECO:0000303|PubMed:9501495};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9501495; DOI=10.1093/oxfordjournals.molbev.a025925;
RA Long K.D., Salbaum J.M.;
RT "Evolutionary conservation of the immediate-early gene ZENK.";
RL Mol. Biol. Evol. 15:284-292(1998).
CC -!- FUNCTION: Transcriptional regulator. Recognizes and binds to the DNA
CC sequence 5'-GCG(T/G)GGGCG-3'(EGR-site) in the promoter region of target
CC genes (By similarity). Binds double-stranded target DNA, irrespective
CC of the cytosine methylation status (By similarity). Regulates the
CC transcription of numerous target genes, and thereby plays an important
CC role in regulating the response to growth factors, DNA damage, and
CC ischemia. Plays a role in the regulation of cell survival,
CC proliferation and cell death. Mediates responses to ischemia and
CC hypoxia; regulates the expression of proteins that are involved in
CC inflammatory processes (By similarity). Plays role in regulating the
CC expression of circadian clock genes (By similarity).
CC {ECO:0000250|UniProtKB:P08046, ECO:0000250|UniProtKB:P18146}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P18146}. Cytoplasm
CC {ECO:0000250|UniProtKB:P18146}.
CC -!- DOMAIN: Binds to DNA motifs with the sequence 5'-GCG(T/G)GGGCG-3' via
CC its C2H2-type zinc fingers. The first, most N-terminal zinc finger
CC binds to the 3'-GCG motif, the middle zinc finger interacts with the
CC central TGG motif, and the C-terminal zinc finger binds to the 5'-GCG
CC motif. Binds double-stranded target DNA, irrespective of the cytosine
CC methylation status. Has reduced affinity for target DNA where the
CC cytosines have been oxidized to 5-hydroxymethylcytosine. Does not bind
CC target DNA where the cytosines have been oxidized to 5-formylcytosine
CC or 5-carboxylcytosine. {ECO:0000250|UniProtKB:P18146}.
CC -!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AF026084; AAC12268.1; -; Genomic_DNA.
DR AlphaFoldDB; O73693; -.
DR BMRB; O73693; -.
DR SMR; O73693; -.
DR STRING; 59729.ENSTGUP00000000002; -.
DR InParanoid; O73693; -.
DR Proteomes; UP000007754; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISA:AgBase.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISA:AgBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISA:AgBase.
DR GO; GO:0010385; F:double-stranded methylated DNA binding; ISS:UniProtKB.
DR GO; GO:0044729; F:hemi-methylated DNA-binding; ISS:UniProtKB.
DR GO; GO:0035035; F:histone acetyltransferase binding; ISA:AgBase.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISA:AgBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISA:AgBase.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISA:AgBase.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0098759; P:cellular response to interleukin-8; ISS:AgBase.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; ISA:AgBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0033233; P:regulation of protein sumoylation; ISA:AgBase.
DR GO; GO:0010996; P:response to auditory stimulus; IDA:AgBase.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISA:AgBase.
DR InterPro; IPR021839; EGR1_C.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF11914; DUF3432; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 3: Inferred from homology;
KW Activator; Biological rhythms; Cytoplasm; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN <1..193
FT /note="Early growth response protein 1"
FT /id="PRO_0000047114"
FT ZN_FING <1..18
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 24..46
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 52..74
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 65..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 3
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08046"
FT SITE 7
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08046"
FT SITE 13
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 31
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08046"
FT SITE 35
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 59
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 63
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 69
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT NON_TER 1
SQ SEQUENCE 193 AA; 21278 MW; FD26489CA2615E96 CRC64;
CDRRFSRSDE LTRHIRIHTG QKPFQCRICM RNFSRSDHLT THIRTHTGEK PFACDICGRK
FARSDERKRH TKIHLRQKDK KVEKAAPAST ASPIPAYSSS VTTSYPSSIT TTYPSPVRTA
YSSPAPSSYP SPVHTTFPSP SIATTYPSGT ATFQTQVATS FSSPGVANNF SSQVTSALSD
INSAFSPRTI EIC
