GenomeNet

Database: UniProt
Entry: A0A3Q1HNT1_ANATE
LinkDB: A0A3Q1HNT1_ANATE
Original site: A0A3Q1HNT1_ANATE 
ID   A0A3Q1HNT1_ANATE        Unreviewed;       511 AA.
AC   A0A3Q1HNT1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Early growth response protein {ECO:0000256|RuleBase:RU363046};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000009270.1, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000009270.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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|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   AlphaFoldDB; A0A3Q1HNT1; -.
DR   STRING; 64144.ENSATEP00000009270; -.
DR   Ensembl; ENSATET00000009430.2; ENSATEP00000009270.1; ENSATEG00000006524.2.
DR   GeneTree; ENSGT00940000165075; -.
DR   InParanoid; A0A3Q1HNT1; -.
DR   OMA; NFQVPMI; -.
DR   OrthoDB; 2912670at2759; -.
DR   Proteomes; UP000265040; 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:0060059; P:embryonic retina morphogenesis in camera-type eye; IEA:Ensembl.
DR   GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IEA:Ensembl.
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:UP000265040};
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          313..342
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          343..370
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          371..398
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          132..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..207
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   511 AA;  54959 MW;  7476E9461DEE0F42 CRC64;
     MAAAKTEMIL PTLQISEPLS FPHSPMDNYP KLEEVMMLNP AGTPFLTASA PEGAGFGSGE
     PGEQYDHLAG DTLPDIPFNC EKPVSEQTYS TQRLPPISYT GRFTLEPATT CSNSLWAEPI
     LGLFTNIMGS VAPSSSSSSG AAQTTSSSSS SASSSSTSSS STSSSQSSSL SSSIHHSEPN
     PIYSAAPTYS SPNSDIFPDQ GQAFPTSAGA VQYPPPAYPN GKSCSTSFPV PMIPDYLFPQ
     QQGEISLVPP DQKPFQSQSS QPSLTPLSTI KAFATQTGSQ DLKSVYQSQL IKPSRMRKYP
     TRPSKTPPHE RPYACPVETC DRRFSRSDEL TRHIRIHTGQ KPFQCRICMR NFSRSDHLTT
     HIRTHTGEKP FACEICGRKF ARSDERKRHT KIHLRQKDKK AEKAGAVVVT AAPVSTASPA
     SSYPSPITSY PSPVSSYPSP VTSCYSSPVH TSYPSPSVAT TYPSVSMSST FQSQVASSFP
     SSVGSNIYSS PVPTPLSDMQ TTLSPRTIEI C
//
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