ID A0A3Q1H9A7_ANATE Unreviewed; 473 AA.
AC A0A3Q1H9A7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Cyclic AMP-dependent transcription factor ATF-7 {ECO:0000256|PIRNR:PIRNR003153};
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:ENSATEP00000001398.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000001398.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Stress-responsive chromatin regulator that plays a role in
CC various biological processes including innate immunological memory,
CC adipocyte differentiation or telomerase regulation. In absence of
CC stress, contributes to the formation of heterochromatin and
CC heterochromatin-like structure by recruiting histone H3K9 tri- and di-
CC methyltransferases thus silencing the transcription of target genes
CC such as STAT1 in adipocytes, or genes involved in innate immunity in
CC macrophages and adipocytes. Stress induces ATF7 phosphorylation that
CC disrupts interactions with histone methyltransferase and enhances the
CC association with coactivators containing histone acetyltransferase
CC and/or histone demethylase, leading to disruption of the
CC heterochromatin-like structure and subsequently transcriptional
CC activation. In response to TNF-alpha, which is induced by various
CC stresses, phosphorylated ATF7 and telomerase are released from
CC telomeres leading to telomere shortening.
CC {ECO:0000256|PIRNR:PIRNR003153}.
CC -!- SUBUNIT: Homodimer; binds DNA as homodimer. Heterodimer;
CC heterodimerizes with other members of ATF family and with JUN family
CC members. {ECO:0000256|PIRNR:PIRNR003153}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR003153}.
CC -!- SIMILARITY: Belongs to the bZIP family.
CC {ECO:0000256|PIRNR:PIRNR003153}.
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DR AlphaFoldDB; A0A3Q1H9A7; -.
DR STRING; 64144.ENSATEP00000001398; -.
DR Ensembl; ENSATET00000001420.2; ENSATEP00000001398.2; ENSATEG00000000979.2.
DR GeneTree; ENSGT00940000155261; -.
DR InParanoid; A0A3Q1H9A7; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd14687; bZIP_ATF2; 1.
DR CDD; cd12192; GCN4_cent; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR016378; TF_CRE-BP1-typ.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR19304:SF10; CYCLIC AMP-DEPENDENT TRANSCRIPTION FACTOR ATF-7; 1.
DR PANTHER; PTHR19304; CYCLIC-AMP RESPONSE ELEMENT BINDING PROTEIN; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR PIRSF; PIRSF003153; ATF2_CRE-BP1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|PIRNR:PIRNR003153};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|PIRNR:PIRNR003153};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR003153};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Transcription {ECO:0000256|PIRNR:PIRNR003153};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR003153};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 7..31
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 321..384
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 81..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 346..380
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 161..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 473 AA; 50398 MW; 8F7E0547E2B1B6E2 CRC64;
MGDDRPFVCT APGCGQRFTN EDHLSVHKHK HEMTLKFGPA RTDSVIIADQ TPTPTRFLKN
CEEVGLFNEL ASSFEQEFCK AQEDERTKHP AALLQTPSEL KNEDEGPLEV DSTPPGSPDS
SSSMSDDSRD SRVRIKPSSA PTPTIVRPGS LPLHMSNDPL HPTLPSPTSV ITQAPPSNRQ
LGSPTSSYPL MRHLPNGQTV PLLPSPVQLT SVISVARAVN TVPNIPGIPG PPVGGASSGS
SSPSGYSLHS ETKMRLKAAL THQSPGAQDG AGGSIPAVPQ RQEYSQQPTQ NSDAPSPAQP
QVSPAQPTGG RRRRASEMDP DERRQRFLER NRAAASRCRQ KRKLWVNSLE KKAEDLANMN
VSLTNEVTLL RNEVAQLKQL LLAHKDCPVT VMQKKAAFLE ETSRETSAEP ISSPAAVIQH
GPSPPASASS PVATINGLSV RAAEAVAMSV LAGMGSGQPG GVVMATQSQS APR
//
