ID A0A3B3TDA2_9TELE Unreviewed; 479 AA.
AC A0A3B3TDA2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Early growth response protein {ECO:0000256|RuleBase:RU363046};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000041227.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000041227.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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. Binds double-stranded target DNA, irrespective of the cytosine
CC methylation status. Regulates the transcription of numerous target
CC genes, and thereby plays an important role in regulating the response
CC to growth factors, DNA damage, and ischemia. Plays a role in the
CC regulation of cell survival, proliferation and cell death.
CC {ECO:0000256|RuleBase:RU363046}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|RuleBase:RU363046}.
CC -!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein family.
CC {ECO:0000256|ARBA:ARBA00005682, ECO:0000256|RuleBase:RU363046}.
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DR AlphaFoldDB; A0A3B3TDA2; -.
DR STRING; 1676925.ENSPKIP00000041227; -.
DR Ensembl; ENSPKIT00000022260.1; ENSPKIP00000041227.1; ENSPKIG00000017864.1.
DR GeneTree; ENSGT00940000165075; -.
DR OrthoDB; 2912670at2759; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
DR InterPro; IPR021839; EGR1_C.
DR InterPro; IPR021849; EGR_N.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23235; KRUEPPEL-LIKE TRANSCRIPTION FACTOR; 1.
DR PANTHER; PTHR23235:SF60; STRIPE, ISOFORM D; 1.
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; beta-beta-alpha zinc fingers; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|RuleBase:RU363046};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU363046};
KW Metal-binding {ECO:0000256|RuleBase:RU363046};
KW Nucleus {ECO:0000256|RuleBase:RU363046};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|RuleBase:RU363046};
KW Transcription regulation {ECO:0000256|RuleBase:RU363046};
KW Zinc {ECO:0000256|RuleBase:RU363046};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042,
KW ECO:0000256|RuleBase:RU363046}.
FT DOMAIN 293..322
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 323..350
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 351..378
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 265..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 479 AA; 51571 MW; AF3FE2731AA3DB18 CRC64;
MCAAKTEMLL PTLQISEPLS FPQSPMDSYP KLEDIMLLHS AGTPFLAASA PEGAGFGTGD
PGEQYDHLAG DTLPDIAVSY EKSFVEQSYP SQRLPPLSYT GRFTLEPTAT CGGSLCPEPL
LSLVSGLMGI SNPSASSSST SSVSSSCQAN MSCSAHHGES NPIYSAAPTQ AASNSNLLPE
HSQAFPSPTG CAIPYPPPAY AGGKTTSFPV PIIPDYLFPQ QQTDSSLVPP DQKPFQSQSG
QLCLTPLSTI RAFASQTGSQ DLKCVEQSQV TKPRQVRKYP NRTSKTPPHE RPYACPVESC
SRRFSRSDEL TRHIRIHTGQ KPFQCRICMR NFSRSDHLTT HIRTHTGEKP FACDVCGRKF
ARSDERKRHT KIHLRQKEKK VEKVVGPVSM PSPASSYPSP VTSYPSPVSS YPSPVPSCYA
SPVHSSYPTQ SAATAYPSGT FSTQVAATFP STLPTALYSP PVNSPDGQST VSPRTTDIC
//
