ATF7_MOUSE
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 03-AUG-2022, entry version 147.
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}.
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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.ENSMUSP00000104456; -.
DR iPTMnet; Q8R0S1; -.
DR EPD; Q8R0S1; -.
DR jPOST; Q8R0S1; -.
DR MaxQB; Q8R0S1; -.
DR PaxDb; Q8R0S1; -.
DR PRIDE; Q8R0S1; -.
DR ProteomicsDB; 265175; -.
DR Ensembl; ENSMUST00000108828; ENSMUSP00000104456; ENSMUSG00000099083.
DR Ensembl; ENSMUST00000169033; ENSMUSP00000130130; ENSMUSG00000099083.
DR UCSC; uc007xwo.1; mouse.
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 141 other tissues.
DR ExpressionAtlas; Q8R0S1; baseline and differential.
DR Genevisible; Q8R0S1; MM.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
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 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
