EGR1_DANRE
ID EGR1_DANRE Reviewed; 511 AA.
AC P26632;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Early growth response protein 1;
DE Short=EGR-1;
DE AltName: Full=Zinc finger protein Krox-24;
GN Name=egr1; Synonyms=krox24;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=7945937; DOI=10.1089/dna.1994.13.1047;
RA Drummond I.A., Rohwer-Nutter P., Sukhatme V.P.;
RT "The zebrafish egr1 gene encodes a highly conserved, zinc-finger
RT transcriptional regulator.";
RL DNA Cell Biol. 13:1047-1055(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 315-376.
RX PubMed=1930167; DOI=10.1016/0006-291x(91)91702-e;
RA Lanfear J., Jowett T., Holland P.W.;
RT "Cloning of fish zinc-finger genes related to Krox-20 and Krox-24.";
RL Biochem. Biophys. Res. Commun. 179:1220-1224(1991).
CC -!- FUNCTION: Transcriptional regulator (PubMed:7945937). Recognizes and
CC binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'(EGR-site) in the promoter
CC region of target genes (By similarity). Binds double-stranded target
CC DNA, irrespective of the cytosine methylation status (By similarity).
CC Regulates the transcription of numerous target genes, and thereby plays
CC an important role in regulating the response to growth factors, DNA
CC damage, and 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 ECO:0000269|PubMed:7945937}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P18146}. Cytoplasm
CC {ECO:0000250|UniProtKB:P18146}.
CC -!- TISSUE SPECIFICITY: Detected in muscle and brain.
CC {ECO:0000269|PubMed:7945937}.
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; U12895; AAA63651.1; -; Genomic_DNA.
DR EMBL; M81109; AAA50035.1; -; Genomic_DNA.
DR PIR; I50114; I50114.
DR PIR; PQ0233; PQ0233.
DR RefSeq; NP_571323.1; NM_131248.1.
DR AlphaFoldDB; P26632; -.
DR SMR; P26632; -.
DR STRING; 7955.ENSDARP00000054459; -.
DR PaxDb; P26632; -.
DR Ensembl; ENSDART00000054460; ENSDARP00000054459; ENSDARG00000037421.
DR Ensembl; ENSDART00000183884; ENSDARP00000151657; ENSDARG00000115563.
DR GeneID; 30498; -.
DR KEGG; dre:30498; -.
DR CTD; 1958; -.
DR ZFIN; ZDB-GENE-980526-320; egr1.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000165075; -.
DR HOGENOM; CLU_043235_2_0_1; -.
DR InParanoid; P26632; -.
DR OMA; NFQVPMI; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P26632; -.
DR TreeFam; TF318980; -.
DR PRO; PR:P26632; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 14.
DR Bgee; ENSDARG00000037421; Expressed in granulocyte and 19 other tissues.
DR ExpressionAtlas; P26632; baseline.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; 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:0043010; P:camera-type eye development; IMP:ZFIN.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IMP:ZFIN.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IMP:ZFIN.
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 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..511
FT /note="Early growth response protein 1"
FT /id="PRO_0000047116"
FT ZN_FING 311..335
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 341..363
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 369..391
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 133..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 309
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 320
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08046"
FT SITE 324
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08046"
FT SITE 330
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 348
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08046"
FT SITE 352
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 380
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 386
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT CONFLICT 317
FT /note="T -> S (in Ref. 2; AAA50035)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="R -> S (in Ref. 2; AAA50035)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="S -> R (in Ref. 2; AAA50035)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="E -> D (in Ref. 2; AAA50035)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 511 AA; 55140 MW; 411C31E6F4AA10BF CRC64;
MAAAKTEMLL PALQISDPLS FPHSPTDNYP KLEEMIMLNS AGTPFLNATA PEGAVFGSGE
PGEQFDHLAG DTLSEISMEK PLSDQTYSTQ RLPPISYTGR FTLEPATNCS NSLWAEPLFS
LVSGLVGINP PPASIPSSTS QATHPSSSST SSIPSSSSSS TSSASLSCSV HQSEPNPIYS
AAPTYSSASP DIFPESGPNF STTVGTSLQY SSSTYPSAKT CNPSFSVPMI PDYLFTQQQS
EISLVPPDQK PIQTQAGQQP ALTPLHTIKA FATQTGSQDL KSVYQSQLIK PSRMRKYPNR
PSKTPPHERP YACPVETCDR RFSRSDELTR HIRIHTGQKP FQCRICMRNF SRSDHLTTHI
RTHTGEKPFA CEICGRKFAR SDERKRHTKI HMRQKDKKAE KGATAAVQSS VSNISISASS
PVSSYPSPIT SYPSPVSSFP SPVNSCYSSP VHTSYPSPSI ATTYPSATST FQTQVATSFP
TSVASNIYSS PVTTPLPDMQ SALSPRTADI C
