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Database: UniProt
Entry: A0A3M0J8E0_HIRRU
LinkDB: A0A3M0J8E0_HIRRU
Original site: A0A3M0J8E0_HIRRU 
ID   A0A3M0J8E0_HIRRU        Unreviewed;       510 AA.
AC   A0A3M0J8E0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Early growth response protein {ECO:0000256|RuleBase:RU363046};
GN   ORFNames=DUI87_26583 {ECO:0000313|EMBL:RMB96520.1};
OS   Hirundo rustica rustica.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC   Hirundo.
OX   NCBI_TaxID=333673 {ECO:0000313|EMBL:RMB96520.1, ECO:0000313|Proteomes:UP000269221};
RN   [1] {ECO:0000313|EMBL:RMB96520.1, ECO:0000313|Proteomes:UP000269221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Chelidonia {ECO:0000313|EMBL:RMB96520.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:RMB96520.1};
RA   Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA   Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT   "A high quality draft genome assembly of the barn swallow (H. rustica
RT   rustica).";
RL   Submitted (JUL-2018) 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. 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RMB96520.1}.
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DR   EMBL; QRBI01000172; RMB96520.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M0J8E0; -.
DR   STRING; 333673.A0A3M0J8E0; -.
DR   Proteomes; UP000269221; 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:UP000269221};
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          311..340
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          341..368
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          369..396
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          45..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          142..204
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          382..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..201
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..424
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   510 AA;  55325 MW;  552125A9AD01E33B CRC64;
     MAAAKAEMQL LPPLQISDPF GAFPHSPPSM DTHYPKLEEM MLLSGGGPQF LAPPGAPESA
     GFGAAGEPGE QHFEHLAADT FPEISLNNEK TLPETSYPNQ TTRLPPITYT GRFSLEPASN
     SSNPLWPEPL FSLVSGLVSM ANAPQTSTTP TSSSPSSSQS SPLSCSVQAS ENNPIYSAAP
     TFPNSTSDIF PESQTQPFPN PSGAPIQYPP PAYPTAKANF QVPMIPDYLF PQQQGELSLV
     PADQKPFPAL ETRAQQPSLT PLSTIKAFAT QTGSQELKTL NTNYQSQLIK PSRMRKYPNR
     PSKTPPHERP YACPVESCDR RFSRSDELTR HIRIHTGQKP FQCRICMRNF SRSDHLTTHI
     RTHTGEKPFA CDICGRKFAR SDERKRHTKI HLRQKDKKVE KAAPASTASP IPAYSSSVTT
     SYPSSIATTY PSPVRTAYSS PAPSSYPSPT HTTFPSPSIA TTYPSGTAAF QTQVATSFSS
     PGVANNFSSQ VTSALSDVNS AFSPRTIEIC
//
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