ID L5JX27_PTEAL Unreviewed; 537 AA.
AC L5JX27;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Early growth response protein {ECO:0000256|RuleBase:RU363046};
GN ORFNames=PAL_GLEAN10016817 {ECO:0000313|EMBL:ELK03046.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK03046.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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|ARBA:ARBA00004123, 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 EMBL; KB031114; ELK03046.1; -; Genomic_DNA.
DR RefSeq; XP_006923125.1; XM_006923063.2.
DR AlphaFoldDB; L5JX27; -.
DR STRING; 9402.L5JX27; -.
DR GeneID; 102892713; -.
DR KEGG; pale:102892713; -.
DR CTD; 1958; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; L5JX27; -.
DR OrthoDB; 2912670at2759; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
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:SF42; EARLY GROWTH RESPONSE PROTEIN 1; 1.
DR PANTHER; PTHR23235; KRUEPPEL-LIKE TRANSCRIPTION FACTOR; 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 Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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 Reference proteome {ECO:0000313|Proteomes:UP000010552};
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 332..361
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 362..389
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 390..417
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 57093 MW; 6B734943B7DF156C CRC64;
MAAAKAEMQL MSPLQISDPF GSFPHSPTMD NYPKLEEMML LSNGAPQFLS AAGAPEGSSG
GSNGSSGGGG GGSSSSSAFN PQGEAGEQPY EHLTSESFPD ISLNNEKVLV ETSYPSQTTR
LPPITYTGRF SLEPAPNSGN TLWPEPLFSL VSGLVSMTNP PATSSSAPSP AASSSSSASQ
SPPLSCAVQS SDSSPIYSAA PTFPTPNTDI FPEPQSQAYP GSAGTALQYP PPAYPAAKGS
FQVPMIPDYL FPQQQGDLGL GTPDQKPFQG LESRTQQPSL TPLSTIKAFA TQSGSQDLKA
LNTTYQSQLI KPSRMRKYPN RPSKTPPHER PYACPVESCD RRFSRSDELT RHIRIHTGQK
PFQCRICMRN FSRSDHLTTH IRTHTGEKPF ACDICGRKFA RSDERKRHTK IHLRQKDKKA
DKGVVASSAT PSLSSYSSPV ATSYTSPVTT SYPSSATTSY PSPVPTSYSS PGSSTYPSPV
HSGFPSPSVA TTYSSVPPAF PAQVSSFPSS SVTNSFSAST GLSDMTTTFS PRTIEIC
//
