ID A0A2K6FGG6_PROCO Unreviewed; 475 AA.
AC A0A2K6FGG6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Cyclic AMP-dependent transcription factor ATF-7 {ECO:0000256|PIRNR:PIRNR003153};
GN Name=ATF7 {ECO:0000313|Ensembl:ENSPCOP00000013078.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000013078.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000013078.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A2K6FGG6; -.
DR Ensembl; ENSPCOT00000023681.1; ENSPCOP00000013078.1; ENSPCOG00000018139.1.
DR GeneTree; ENSGT00940000155261; -.
DR Proteomes; UP000233160; 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 InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR016378; TF_CRE-BP1-typ.
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; SSF57959; Leucine zipper domain; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR003153};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW Transcription {ECO:0000256|PIRNR:PIRNR003153};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR003153}.
FT DOMAIN 324..387
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 75..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 349..383
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 314..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 50861 MW; 415CC2B4B954177A CRC64;
AGNPRPSTRF TNEDHLAVHK HKHEMTLKFG PARTDSVIIA DQTPTPTRFL KNCEEVGLFN
ELASSFEHEF KKAADEDEKK ASAGPLDMSL PSTPDVKIKE EEPVEVDSSP PDSPASSPCS
PPLKEKEVAP KPVVISTPTP TIVRPGSLPL HLGYDPLHPT LPSPTSVITQ APPSNRQMGS
PTGSLPLVMH LANGQTMPVL PGPPVQMPSV ISLARPVSMV PNIPGIPGPP VNSSGSISPS
GHPIPSEAKM RLKATLTHQV SSINGGCGMV VGTASTMVTA RPEQSQILIQ HPDAPSPAQP
QVSPAQPTPS TGGRRRRTVD EDPDERRQRF LERNRAAASR CRQKRKLWVS SLEKKAEELT
SQNIQLSNEV TLLRNEVAQL KQLLLAHKDC PVTALQKKTQ GYLESPKESS EPTGSPAPVI
QHSSATVPSN GLSVRSAAEA VATSVLTQMA SQRTEVSMPI QSHVIMTPQS QSAGR
//
