ID   ATF7_MOUSE              Reviewed;         413 AA.
AC   Q8R0S1;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   24-JAN-2024, entry version 154.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX   PubMed=19893493; DOI=10.1038/emboj.2009.318;
RA   Maekawa T., Kim S., Nakai D., Makino C., Takagi T., Ogura H., Yamada K.,
RA   Chatton B., Ishii S.;
RT   "Social isolation stress induces ATF-7 phosphorylation and impairs
RT   silencing of the 5-HT 5B receptor gene.";
RL   EMBO J. 29:196-208(2010).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX   PubMed=29490055; DOI=10.1093/nar/gky155;
RA   Maekawa T., Liu B., Nakai D., Yoshida K., Nakamura K.I., Yasukawa M.,
RA   Koike M., Takubo K., Chatton B., Ishikawa F., Masutomi K., Ishii S.;
RT   "ATF7 mediates TNF-alpha-induced telomere shortening.";
RL   Nucleic Acids Res. 46:4487-4504(2018).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=31294895; DOI=10.1111/gtc.12713;
RA   Maekawa T., Liu B., Liu Y., Yoshida K., Muratani M., Chatton B., Ishii S.;
RT   "Stress-induced and ATF7-dependent epigenetic change influences cellular
RT   senescence.";
RL   Genes Cells 24:627-635(2019).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=30826729; DOI=10.1016/j.isci.2019.02.013;
RA   Liu Y., Maekawa T., Yoshida K., Muratani M., Chatton B., Ishii S.;
RT   "The Transcription Factor ATF7 Controls Adipocyte Differentiation and
RT   Thermogenic Gene Programming.";
RL   IScience 13:98-112(2019).
RN   [6]
RP   FUNCTION, PHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=31958521; DOI=10.1016/j.jcmgh.2020.01.005;
RA   Meijer B.J., Giugliano F.P., Baan B., van der Meer J.H.M., Meisner S.,
RA   van Roest M., Koelink P.J., de Boer R.J., Jones N., Breitwieser W.,
RA   van der Wel N.N., Wildenberg M.E., van den Brink G.R., Heijmans J.,
RA   Muncan V.;
RT   "ATF2 and ATF7 Are Critical Mediators of Intestinal Epithelial Repair.";
RL   Cell. Mol. Gastroenterol. Hepatol. 10:23-42(2020).
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 (PubMed:29490055).
CC       In absence of stress, contributes to the formation of heterochromatin
CC       and heterochromatin-like structure by recruiting histone H3K9 tri- and
CC       di-methyltransferases thus silencing the transcription of target genes
CC       such as Htr5b, STAT1 in adipocytes, or genes involved in innate
CC       immunity in macrophages and adipocytes (PubMed:19893493,
CC       PubMed:31294895, PubMed:30826729). Phosphorylation of ATF7 disrupts
CC       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 (PubMed:19893493). In response to TNF-alpha, which is
CC       induced by various stresses, phosphorylated ATF7 and telomerase are
CC       released from telomeres leading to telomere shortening
CC       (PubMed:29490055). Also plays a role in maintaining epithelial
CC       regenerative capacity and protecting against cell death during
CC       intestinal epithelial damage and repair (PubMed:31958521).
CC       {ECO:0000269|PubMed:19893493, ECO:0000269|PubMed:29490055,
CC       ECO:0000269|PubMed:30826729, ECO:0000269|PubMed:31294895,
CC       ECO:0000269|PubMed:31958521}.
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 the interaction potentiates the transactivation activity and is
CC       inhibited by ATF7 sumoylation. Interacts with TAF4; the interaction
CC       inhibits the TAF12-dependent transactivation. Interacts with MAPK9; the
CC       interaction does not phosphorylate ATF7 but acts as a docking site for
CC       ATF7-associated partners such as JUN. Interacts with Ku complex
CC       components XRCC6 and XRCC7. Interacts with TERT.
CC       {ECO:0000250|UniProtKB:P17544}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC       ECO:0000269|PubMed:19893493}. Nucleus, nucleoplasm
CC       {ECO:0000250|UniProtKB:P17544}. Chromosome, telomere
CC       {ECO:0000269|PubMed:29490055}. Note=Mainly nucleoplasmic. Restricted
CC       distribution to the perinuculear region. The sumoylated form locates to
CC       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       (PubMed:19893493, PubMed:29490055). Phosphorylated in proliferating
CC       colonic and small intestinal epithelial cells (PubMed:31958521).
CC       {ECO:0000250|UniProtKB:P17544, ECO:0000269|PubMed:19893493,
CC       ECO:0000269|PubMed:29490055, ECO:0000269|PubMed:31958521}.
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   -!- DISRUPTION PHENOTYPE: Mice exhibit abnormal behaviors and increased 5-
CC       HT receptor 5B (Htr5b) mRNA levels in the dorsal raphe nuclei
CC       (PubMed:19893493). They also exhibit reduced adipose tissue mass,
CC       showing a role for ATF7 in adipocyte differentiation (PubMed:30826729).
CC       They develop severe ulceration and inflammation associated with
CC       increased epithelial apoptosis on dextran-sulfate sodium (DSS) exposure
CC       and were less able to regenerate colonic crypts on irradiation
CC       (PubMed:31294895). When combined with loss of ATF2, mice show even more
CC       epithelial damage in response to DSS (PubMed:31958521). In addition,
CC       loss of ATF7 leads to telomere shortening and chromosome instability
CC       (PubMed:29490055). {ECO:0000269|PubMed:19893493,
CC       ECO:0000269|PubMed:29490055, ECO:0000269|PubMed:30826729,
CC       ECO:0000269|PubMed:31294895, ECO:0000269|PubMed:31958521}.
CC   -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC026483; AAH26483.1; -; mRNA.
DR   AlphaFoldDB; Q8R0S1; -.
DR   SMR; Q8R0S1; -.
DR   BioGRID; 230215; 3.
DR   IntAct; Q8R0S1; 1.
DR   MINT; Q8R0S1; -.
DR   STRING; 10090.ENSMUSP00000139181; -.
DR   iPTMnet; Q8R0S1; -.
DR   EPD; Q8R0S1; -.
DR   jPOST; Q8R0S1; -.
DR   MaxQB; Q8R0S1; -.
DR   PaxDb; 10090-ENSMUSP00000104456; -.
DR   ProteomicsDB; 265175; -.
DR   Pumba; Q8R0S1; -.
DR   Ensembl; ENSMUST00000108828.9; ENSMUSP00000104456.2; ENSMUSG00000099083.8.
DR   Ensembl; ENSMUST00000169033.8; ENSMUSP00000130130.2; ENSMUSG00000099083.8.
DR   UCSC; uc007xwo.1; mouse.
DR   AGR; MGI:2443472; -.
DR   MGI; MGI:2443472; Atf7.
DR   VEuPathDB; HostDB:ENSMUSG00000099083; -.
DR   eggNOG; KOG1414; Eukaryota.
DR   GeneTree; ENSGT00940000155261; -.
DR   HOGENOM; CLU_021564_0_0_1; -.
DR   InParanoid; Q8R0S1; -.
DR   PhylomeDB; Q8R0S1; -.
DR   ChiTaRS; Atf7; mouse.
DR   PRO; PR:Q8R0S1; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q8R0S1; Protein.
DR   Bgee; ENSMUSG00000099083; Expressed in embryonic brain and 144 other cell types or tissues.
DR   ExpressionAtlas; Q8R0S1; baseline and differential.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR   GO; GO:0035497; F:cAMP response element binding; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051019; F:mitogen-activated protein kinase binding; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR   GO; GO:0001223; F:transcription coactivator binding; ISO:MGI.
DR   GO; GO:0007507; P:heart development; IGI:MGI.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:MGI.
DR   GO; GO:0097284; P:hepatocyte apoptotic process; IGI:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR   GO; GO:0001889; P:liver development; IGI:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0038066; P:p38MAPK cascade; IGI:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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   SMART; SM00355; ZnF_C2H2; 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.
DR   Genevisible; Q8R0S1; MM.
PE   1: Evidence at protein 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..413
FT                   /note="Cyclic AMP-dependent transcription factor ATF-7"
FT                   /id="PRO_0000076593"
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          81..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..337
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   COMPBIAS        322..337
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   CROSSLNK        107
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000250|UniProtKB:P17544"
SQ   SEQUENCE   413 AA;  44608 MW;  AFF4D1A7BFE71AF3 CRC64;
     MGDDRPFVCS APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RTDSVIIADQ TPTPTRFLKN
     CEEVGLFNEL ASSFEHEFKK ASDDDEKKGA AGPLDMSLPS TPDIKIKEEE PVEVDSSPPD
     SPASSPCSPP LKEKEVTTKP VVISTPTPTI VRPGSLPLHL GYDPLHPTLP SPTSVITQAP
     PSNRQIGSPT GSLPLVMHLA NGQTMPMLPG PPVQMPSVIS LARPVSMVPN IPGIPGPPVN
     NSGSISPSGH PMPSEAKMRL KATLTHQVSS INGGCGMVVG TASTMVTARP EQNQILIQHP
     DAPSPAQPQV SPAQPTPSTG GRRRRTVDED PDERRQRFLE RNRAAASRCR QKRKLWVSSL
     EKKAEELTSQ NIQLSNEVTL LRNEVAQLKQ LLLAHKDCPV TALQKKTQGY LGK
//