ID   Q3TZR9_MOUSE            Unreviewed;       483 AA.
AC   Q3TZR9;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Cyclic AMP-dependent transcription factor ATF-7 {ECO:0000256|PIRNR:PIRNR003153};
GN   Name=Atf7 {ECO:0000313|Ensembl:ENSMUSP00000139181.2};
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 {ECO:0000313|EMBL:BAE34138.1};
RN   [1] {ECO:0000313|EMBL:BAE34138.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD {ECO:0000313|EMBL:BAE34138.1};
RC   TISSUE=Activated spleen {ECO:0000313|EMBL:BAE34138.1};
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2] {ECO:0000313|EMBL:BAE34138.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD {ECO:0000313|EMBL:BAE34138.1};
RC   TISSUE=Activated spleen {ECO:0000313|EMBL:BAE34138.1};
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT   full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [3] {ECO:0000313|EMBL:BAE34138.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD {ECO:0000313|EMBL:BAE34138.1};
RC   TISSUE=Activated spleen {ECO:0000313|EMBL:BAE34138.1};
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA   Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA   Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA   Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA   Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA   Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT   pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [4] {ECO:0000313|EMBL:BAE34138.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD {ECO:0000313|EMBL:BAE34138.1};
RC   TISSUE=Activated spleen {ECO:0000313|EMBL:BAE34138.1};
RX   PubMed=11217851; DOI=10.1038/35055500;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [5] {ECO:0000313|EMBL:BAE34138.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD {ECO:0000313|EMBL:BAE34138.1};
RC   TISSUE=Activated spleen {ECO:0000313|EMBL:BAE34138.1};
RX   PubMed=12466851; DOI=10.1038/nature01266;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [6] {ECO:0000313|EMBL:BAE34138.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD {ECO:0000313|EMBL:BAE34138.1};
RC   TISSUE=Activated spleen {ECO:0000313|EMBL:BAE34138.1};
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F.,
RA   Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M.,
RA   Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K.,
RA   Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T.,
RA   Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:BAE34138.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD {ECO:0000313|EMBL:BAE34138.1};
RC   TISSUE=Activated spleen {ECO:0000313|EMBL:BAE34138.1};
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [8] {ECO:0000313|EMBL:BAE34138.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD {ECO:0000313|EMBL:BAE34138.1};
RC   TISSUE=Activated spleen {ECO:0000313|EMBL:BAE34138.1};
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [9] {ECO:0007829|PubMed:17242355}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10] {ECO:0000313|Ensembl:ENSMUSP00000139181.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000139181.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [11] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [12] {ECO:0000313|Ensembl:ENSMUSP00000139181.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000139181.2};
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   EMBL; AK157628; BAE34138.1; -; mRNA.
DR   RefSeq; NP_001296995.1; NM_001310066.1.
DR   RefSeq; NP_001296996.1; NM_001310067.1.
DR   ProteomicsDB; 335205; -.
DR   DNASU; 223922; -.
DR   Ensembl; ENSMUST00000184485.8; ENSMUSP00000139308.2; ENSMUSG00000099083.8.
DR   Ensembl; ENSMUST00000184616.8; ENSMUSP00000139181.2; ENSMUSG00000099083.8.
DR   GeneID; 223922; -.
DR   KEGG; mmu:223922; -.
DR   UCSC; uc007xwm.1; mouse.
DR   CTD; 11016; -.
DR   MGI; MGI:2443472; Atf7.
DR   VEuPathDB; HostDB:ENSMUSG00000099083; -.
DR   GeneTree; ENSGT00940000155261; -.
DR   OMA; TELSMPM; -.
DR   OrthoDB; 1361169at2759; -.
DR   BioGRID-ORCS; 223922; 4 hits in 62 CRISPR screens.
DR   ChiTaRS; Atf7; mouse.
DR   Proteomes; UP000000589; Chromosome 15.
DR   Bgee; ENSMUSG00000099083; Expressed in embryonic brain and 144 other cell types or tissues.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051019; F:mitogen-activated protein kinase binding; IEA:Ensembl.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:Ensembl.
DR   GO; GO:0001223; F:transcription coactivator binding; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
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.
PE   1: Evidence at protein level;
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   Proteomics identification {ECO:0007829|EPD:Q3TZR9,
KW   ECO:0007829|MaxQB:Q3TZR9};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
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          332..395
FT                   /note="BZIP"
FT                   /evidence="ECO:0000259|PROSITE:PS50217"
FT   REGION          81..140
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          409..441
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   COILED          357..391
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        322..345
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   483 AA;  51780 MW;  4DF10D373FE376C8 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 LESPKESSEP
     TGSPAPVIQH SSASAPSNGL SVRSAAEAVA TSVLTQMASQ RTELSMPIQS HVIMTPQSQS
     AGR
//