EGR1_XENTR
ID EGR1_XENTR Reviewed; 498 AA.
AC A4II20; Q6F2L9;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Early growth response protein 1 {ECO:0000250|UniProtKB:P08046};
DE Short=EGR-1 {ECO:0000250|UniProtKB:P08046};
GN Name=egr1 {ECO:0000312|EMBL:AAI35807.1}; Synonyms=egr {ECO:0000303|Ref.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAT71995.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Qin S., Dors M., Johnson E., Bloom S., Hood L., Rowen L.;
RT "Sequence of Xenopus tropicalis development genes.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAT71995.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tadpole {ECO:0000312|EMBL:AAI35807.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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 a 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:0000255}.
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DR EMBL; AC146894; AAT71995.1; -; Genomic_DNA.
DR EMBL; BC135806; AAI35807.1; -; mRNA.
DR RefSeq; NP_001090830.1; NM_001097361.1.
DR AlphaFoldDB; A4II20; -.
DR BMRB; A4II20; -.
DR SMR; A4II20; -.
DR STRING; 8364.ENSXETP00000047681; -.
DR PaxDb; A4II20; -.
DR DNASU; 100038164; -.
DR Ensembl; ENSXETT00000047681; ENSXETP00000047681; ENSXETG00000006697.
DR GeneID; 100038164; -.
DR KEGG; xtr:100038164; -.
DR CTD; 1958; -.
DR Xenbase; XB-GENE-853412; egr1.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; A4II20; -.
DR OMA; QAMESRT; -.
DR OrthoDB; 1318335at2759; -.
DR TreeFam; TF318980; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000006697; Expressed in brain and 19 other tissues.
DR ExpressionAtlas; A4II20; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR InterPro; IPR021839; EGR1_C.
DR InterPro; IPR021849; EGR_N.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF11914; DUF3432; 1.
DR Pfam; PF11928; DUF3446; 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; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 2: Evidence at transcript level;
KW Activator; Biological rhythms; Cytoplasm; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..498
FT /note="Early growth response protein 1"
FT /id="PRO_0000386429"
FT ZN_FING 307..331
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 337..359
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 365..387
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 137..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 305
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 316
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08046"
FT SITE 320
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08046"
FT SITE 326
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 344
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08046"
FT SITE 348
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 372
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 376
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 382
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT CONFLICT 148
FT /note="P -> PS (in Ref. 2; AAI35807)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 498 AA; 53997 MW; F0A812624C004C74 CRC64;
MAAAKTDMLV SPLQISDPFS SFPHSPTMDN YPKLEEMMLL NPGAPQFLGA AVPEGSGFNS
PVEGSEQFDH LAADAFSDMS LSGEKAVIES SYANQSARLP SLTYTGRFSL EPAPNSSNTL
WPEPLFSLVS GLVGMANASP SSAPSSSPSS SSSSSQSPPL SCSVQSNDSS PIYSAAPTFP
NSSPELFPDQ SPQPFQNAST ASIPYPPPAY PVSKTTFQVP MIPDYLFPQQ QGDVSLVSAD
QKPFQAMESR TQQPSLTPLS TIKAFATQTS QDLKTINSTY QSQIIKPSRM RKYPNRPSKT
PPHERPYACP VESCDRRFSR SDELTRHIRI HTGQKPFQCR ICMRNFSRSD HLTTHIRTHT
GEKPFACDIC GRKFARSDER KRHTKIHLRQ KDKKADKATP VSVASPVSSY SPSASTSYPS
PVPTSYSSPV SSAYPSPVHS SFPSPTTAVT YPSVTSTFQT HGITSFPSSI VTNSFSSPVS
SALSDMSITY SPRTIEIC
