EGR1B_XENLA
ID EGR1B_XENLA Reviewed; 475 AA.
AC Q6NTY6;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Early growth response protein 1-B;
DE Short=EGR-1-B;
GN Name=egr1-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|EMBL:AAH68816.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula {ECO:0000312|EMBL:AAH68816.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2004) 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; BC068816; AAH68816.1; -; mRNA.
DR RefSeq; NP_001084566.1; NM_001091097.1.
DR AlphaFoldDB; Q6NTY6; -.
DR SMR; Q6NTY6; -.
DR DNASU; 414518; -.
DR GeneID; 414518; -.
DR KEGG; xla:414518; -.
DR CTD; 414518; -.
DR Xenbase; XB-GENE-6252570; egr1.S.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 414518; Expressed in brain and 17 other tissues.
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: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: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: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..475
FT /note="Early growth response protein 1-B"
FT /id="PRO_0000386428"
FT ZN_FING 284..308
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 314..336
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 342..364
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 109..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 282
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 293
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08046"
FT SITE 297
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08046"
FT SITE 303
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 321
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08046"
FT SITE 325
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 349
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 353
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 359
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
SQ SEQUENCE 475 AA; 51906 MW; 324B69090A9F9C7F CRC64;
MALAKTDMLV SPLQISDPFS SFPHSPTMDN YPKLDGAEQF DHHAADAFSE MSLSNEKAVL
ESSYANHTTR LPSLTYTGRF SLEPAPNSSN TLWPEPLFSL VSGLVGMANV SSSSAPSSSP
SSSSSSSSSS SSQSPPLSCS VQSNESSPIY SAAPTFPNSS PEMFPDHSPQ PFQNASTASI
PYPPPAYPVS KTTFQVPMIP DYLFPQQQGD VSLVSADQKP FQAMENRTQQ PSLTPLSTIK
AFATQTSQDL KTINSTYQSQ IIKPSRMRKY PNRPSKTPPH ERPYACPVES CDRRFSRSDE
LTRHIRIHTG QKPFQCRICM RNFSRSDHLT THIRTHTGEK PFACDICGRK FARSDERKRH
TKIHLRQKDK KADKATPVSI ASPVSAYSPS ASTSYPSPVP TSYSSPVSSC YPSPVHSSFP
SPTTAVTYPS VTSTFQTQCI TSFPSSIVTN SYSSPVSSAL SDMSVTYSPR TIEIC
