ATF7_PONAB
ID ATF7_PONAB Reviewed; 483 AA.
AC Q5R9C9;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Cyclic AMP-dependent transcription factor ATF-7;
DE Short=cAMP-dependent transcription factor ATF-7;
DE AltName: Full=Activating transcription factor 7;
DE AltName: Full=Transcription factor ATF-A;
GN Name=ATF7;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). In
CC absence of 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 (By similarity). In response to TNF-alpha, which is induced
CC by various stresses, phosphorylated ATF7 and telomerase are released
CC from telomeres leading to telomere shortening (By similarity). Plays
CC also a role in maintaining epithelial regenerative capacity and
CC protecting against cell death during intestinal epithelial damage and
CC repair (By similarity). {ECO:0000250|UniProtKB:P17544,
CC ECO:0000250|UniProtKB:Q8R0S1}.
CC -!- SUBUNIT: Homodimer; binds DNA as homodimer. Heterodimer;
CC heterodimerizes with other members of ATF family and with JUN family
CC members. Interacts with JNK2; the interaction does not phosphorylate
CC ATF7 but acts as a docking site for other ATF-associated partners such
CC as JUN family members. Interacts (via its transactivation domain) with
CC TAF12 (isoforms TAFII15 and TAFII20); the interaction potentiates the
CC transactivation activity (isoform TAFII20 only) and is inhibited by
CC ATF7 sumoylation. Interacts with TAF4; the interaction inhibits the
CC TAF12-dependent transactivation. Interacts with MAPK9; the interaction
CC does not phosphorylate ATF7 but acts as a docking site for ATF7-
CC associated partners such as JUN. Interacts with Ku complex components
CC XRCC6 and XRCC7. Interacts with TERT. {ECO:0000250|UniProtKB:P17544}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P17544}. Chromosome,
CC telomere {ECO:0000250|UniProtKB:P17544}. Note=Mainly nucleoplasmic.
CC Restricted distribution to the perinuculear region. The sumoylated form
CC locates to the nuclear peiphery. {ECO:0000250|UniProtKB:P17544}.
CC -!- PTM: On EGF stimulation, phosphorylated first on Thr-53 allowing
CC subsequent phosphorylation on Thr-51. This latter phosphorylation
CC prevents sumoylation, increases binding to TAF12 and enhances
CC transcriptional activity (By similarity). Social isolation stress as
CC well as TNF-alpha also induce the phosphorylation of ATF7.
CC Phosphorylated in proliferating colonic and small intestinal epithelial
CC cells (By similarity). {ECO:0000250|UniProtKB:P17544,
CC ECO:0000250|UniProtKB:Q8R0S1}.
CC -!- PTM: Sumoylation delays nuclear localization and inhibits
CC transactivation activity through preventing binding to TAF12. RANBP2
CC appears to be the specific E3 ligase. {ECO:0000250|UniProtKB:P17544}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; CR859460; CAH91631.1; -; mRNA.
DR RefSeq; NP_001125959.1; NM_001132487.1.
DR AlphaFoldDB; Q5R9C9; -.
DR SMR; Q5R9C9; -.
DR STRING; 9601.ENSPPYP00000005229; -.
DR GeneID; 100172894; -.
DR KEGG; pon:100172894; -.
DR CTD; 11016; -.
DR eggNOG; KOG1414; Eukaryota.
DR InParanoid; Q5R9C9; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Pfam; PF00170; bZIP_1; 1.
DR PIRSF; PIRSF003153; ATF2_CRE-BP1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SMART; SM00355; ZnF_C2H2; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR SUPFAM; SSF57959; SSF57959; 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 2: Evidence at transcript level;
KW Activator; Chromosome; DNA-binding; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Telomere; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..483
FT /note="Cyclic AMP-dependent transcription factor ATF-7"
FT /id="PRO_0000076594"
FT DOMAIN 332..395
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT ZN_FING 7..31
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..285
FT /note="Transactivation domain"
FT /evidence="ECO:0000250"
FT REGION 110..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..354
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 360..388
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 407..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphothreonine; by MAPK11"
FT /evidence="ECO:0000250|UniProtKB:P17544"
FT MOD_RES 53
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P17544"
FT MOD_RES 101
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P17544"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17544"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17544"
FT CROSSLNK 107
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P17544"
SQ SEQUENCE 483 AA; 51743 MW; D05D084FC73330D6 CRC64;
MGDDRPFVCN APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RTDSVIIADQ TPTPTRFLKN
CEEVGLFNEL ASSFEHEFKK AADEDEKKAA AGPLDMSLPS TPDIKIKEEE PVEVDSSPPD
SPASSPCSPP LKEKEVTPKP VLISTPTPTI VRPGSLPLHL GYDPLHPTLP SPTSVITQAP
PSNRQMGSPT GSLPLVMHLA NGQTMPVLPG PPVQMPSVIS LARPVSMVPN IPGIPGPPVN
SSGSISPSGH PIPSEAKMRL KATLTHQVSS INGGCGMVVG SASTMVTARP EQSQILIQHP
DAPSPAQPQV SPAQPTPSTG GRRRRTVDED PDERRQRFLE RNRAAASRCR QKRKLWVSSL
EKKAEELTSQ NIQLSNEVTL LRNEVAQLKQ LLLAHKDCPV TALQKKTQGY LESPKESSEP
TGSPAPVIQH SSATAPSNGL SVRSAAEAVA TSVLTQMASQ RTELSMPIQS HVIMTPQSQS
AGR
