EGR1_BOVIN
ID EGR1_BOVIN Reviewed; 540 AA.
AC Q29W20;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Early growth response protein 1;
DE Short=EGR-1;
GN Name=EGR1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovarian follicle;
RA Sayasith K., Sirois J.;
RT "Characterization of bovine early growth response 1.";
RL Submitted (FEB-2005) 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. Activates expression of p53/TP53 and
CC TGFB1, and thereby helps prevent tumor formation. Required for normal
CC progress through mitosis and normal proliferation of hepatocytes after
CC partial hepatectomy. Mediates responses to ischemia and hypoxia;
CC regulates the expression of proteins such as IL1B and CXCL2 that are
CC involved in inflammatory processes and development of tissue damage
CC after ischemia. Regulates biosynthesis of luteinizing hormone (LHB) in
CC the pituitary (By similarity). Regulates the amplitude of the
CC expression rhythms of clock genes: ARNTL/BMAL1, PER2 and NR1D1 in the
CC liver via the activation of PER1 (clock repressor) transcription.
CC Regulates the rhythmic expression of core-clock gene ARNTL/BMAL1 in the
CC suprachiasmatic nucleus (SCN) (By similarity).
CC {ECO:0000250|UniProtKB:P08046, ECO:0000250|UniProtKB:P18146}.
CC -!- SUBUNIT: Interacts with SNAI1 and SP1 upon 12-O-tetradecanoylphorbol-
CC 13-acetate (TPA) induction. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY924307; AAY16442.1; -; mRNA.
DR RefSeq; NP_001039340.1; NM_001045875.1.
DR AlphaFoldDB; Q29W20; -.
DR SMR; Q29W20; -.
DR STRING; 9913.ENSBTAP00000013284; -.
DR iPTMnet; Q29W20; -.
DR PaxDb; Q29W20; -.
DR GeneID; 407125; -.
DR KEGG; bta:407125; -.
DR CTD; 1958; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q29W20; -.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000009136; Unplaced.
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:0071504; P:cellular response to heparin; ISS:UniProtKB.
DR GO; GO:0098759; P:cellular response to interleukin-8; ISS:UniProtKB.
DR GO; GO:0071506; P:cellular response to mycophenolic acid; ISS:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0060086; P:circadian temperature homeostasis; ISS:UniProtKB.
DR GO; GO:0044849; P:estrous cycle; ISS:UniProtKB.
DR GO; GO:0072110; P:glomerular mesangial cell proliferation; ISS:UniProtKB.
DR GO; GO:0045475; P:locomotor rhythm; ISS:UniProtKB.
DR GO; GO:0032722; P:positive regulation of chemokine production; ISS:UniProtKB.
DR GO; GO:0072303; P:positive regulation of glomerular metanephric mesangial cell proliferation; ISS:UniProtKB.
DR GO; GO:0046886; P:positive regulation of hormone biosynthetic process; ISS:UniProtKB.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; 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:2000182; P:regulation of progesterone biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR GO; GO:0002931; P:response to ischemia; 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; 2.
DR Pfam; PF11928; DUF3446; 1.
DR Pfam; PF00096; zf-C2H2; 2.
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 2: Evidence at transcript level;
KW Activator; Biological rhythms; Cytoplasm; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..540
FT /note="Early growth response protein 1"
FT /id="PRO_0000244380"
FT ZN_FING 337..361
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 366..388
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 394..416
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 335
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 346
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08046"
FT SITE 350
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08046"
FT SITE 356
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 373
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08046"
FT SITE 377
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 401
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 405
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 411
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT CROSSLNK 304
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P18146"
SQ SEQUENCE 540 AA; 57115 MW; C16D470B244B34AB CRC64;
MAAAKAEMQL MSPLQISDPF GSFPHSPTMD NYPKLEEMML SNGAPQFLGA AGAPEGSSGS
SSGSSGGGGG GGGGSSSSNS NSSSAFNPQG EASEQPYEHL TAESFPDISL NNEKVLVETS
YPSQTTRLPP ITYTGRFSLE PAPNSGNTLW PEPLFSLVSG LVSMTNPPAT SSSASSPAAS
SSASQSPPLS CAVQSNDSSP IYSAAPTFPT PNTDIFPEPQ GQAFPGSAGP ALQYPPPAYP
GAKGGFQVPM IPDYLFPQQQ GDLGLGTPDQ KPFQGLESRT QQPSLTPLST IKAFATQSGS
QDLKALNSTY QSQLIKPSRM RKYPNRPSKT PPHERPYACP VESCDRRFSR SDELTRHIRI
HTGQKPQCRI SMRNFSRSDH LTTHIRTHTG EKPFACDICG RKFARSDERK RHTKIHLRQK
DKKADKSAAS AATSSLPSYP SPVATSYPSP ATTSYPSPAT TSYPSPVPTS YSSPGSSTYP
SPVHNGFPSP SVATTYSSVP PAFPTQVSSF PSSAVTNSFS ASTGLSDMTT TFSPRTIEIC
