ID   ATF3_MOUSE              Reviewed;         181 AA.
AC   Q60765;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=Cyclic AMP-dependent transcription factor ATF-3;
DE            Short=cAMP-dependent transcription factor ATF-3;
DE   AltName: Full=Activating transcription factor 3;
DE   AltName: Full=Transcription factor LRG-21 {ECO:0000303|PubMed:8960123};
GN   Name=Atf3 {ECO:0000303|PubMed:11916968, ECO:0000312|MGI:MGI:109384};
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 [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Macrophage;
RX   PubMed=8960123; DOI=10.1016/s0161-5890(96)00043-0;
RA   Drysdale B.E., Howard D.L., Johnson R.J.;
RT   "Identification of a lipopolysaccharide inducible transcription factor in
RT   murine macrophages.";
RL   Mol. Immunol. 33:989-998(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland, and Osteoblast;
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   [3]
RP   FUNCTION.
RX   PubMed=11916968; DOI=10.1074/jbc.m200727200;
RA   Allen-Jennings A.E., Hartman M.G., Kociba G.J., Hai T.;
RT   "The roles of ATF3 in liver dysfunction and the regulation of
RT   phosphoenolpyruvate carboxykinase gene expression.";
RL   J. Biol. Chem. 277:20020-20025(2002).
RN   [4]
RP   INDUCTION.
RX   PubMed=22242125; DOI=10.1371/journal.pone.0029498;
RA   Alter J., Bengal E.;
RT   "Stress-induced C/EBP homology protein (CHOP) represses MyoD transcription
RT   to delay myoblast differentiation.";
RL   PLoS ONE 6:E29498-E29498(2011).
CC   -!- FUNCTION: This protein binds the cAMP response element (CRE)
CC       (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral
CC       and cellular promoters (PubMed:11916968). Represses transcription from
CC       promoters with ATF sites (PubMed:11916968). It may repress
CC       transcription by stabilizing the binding of inhibitory cofactors at the
CC       promoter (By similarity). {ECO:0000250|UniProtKB:P18847,
CC       ECO:0000269|PubMed:11916968}.
CC   -!- SUBUNIT: Binds DNA as a homodimer or a heterodimer. Interacts with
CC       KAT5; promoting KAT5 autoacetylation and KAT5 deubiquitination by USP7.
CC       {ECO:0000250|UniProtKB:P18847}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P18847,
CC       ECO:0000255|PROSITE-ProRule:PRU00978}.
CC   -!- INDUCTION: By stress. {ECO:0000269|PubMed:22242125}.
CC   -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
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DR   EMBL; U19118; AAB48941.1; -; mRNA.
DR   EMBL; BC019946; AAH19946.1; -; mRNA.
DR   EMBL; BC064799; AAH64799.1; -; mRNA.
DR   CCDS; CCDS15616.1; -.
DR   RefSeq; NP_031524.2; NM_007498.3.
DR   AlphaFoldDB; Q60765; -.
DR   SMR; Q60765; -.
DR   BioGRID; 198234; 9.
DR   IntAct; Q60765; 1.
DR   STRING; 10090.ENSMUSP00000027941; -.
DR   iPTMnet; Q60765; -.
DR   PhosphoSitePlus; Q60765; -.
DR   MaxQB; Q60765; -.
DR   PaxDb; 10090-ENSMUSP00000027941; -.
DR   ProteomicsDB; 265174; -.
DR   Antibodypedia; 658; 637 antibodies from 37 providers.
DR   DNASU; 11910; -.
DR   Ensembl; ENSMUST00000027941.14; ENSMUSP00000027941.9; ENSMUSG00000026628.14.
DR   Ensembl; ENSMUST00000195117.2; ENSMUSP00000141492.2; ENSMUSG00000026628.14.
DR   GeneID; 11910; -.
DR   KEGG; mmu:11910; -.
DR   UCSC; uc007ece.1; mouse.
DR   AGR; MGI:109384; -.
DR   CTD; 467; -.
DR   MGI; MGI:109384; Atf3.
DR   VEuPathDB; HostDB:ENSMUSG00000026628; -.
DR   eggNOG; KOG1414; Eukaryota.
DR   GeneTree; ENSGT00940000156376; -.
DR   HOGENOM; CLU_088612_0_2_1; -.
DR   InParanoid; Q60765; -.
DR   OMA; ACMNTER; -.
DR   OrthoDB; 5354319at2759; -.
DR   PhylomeDB; Q60765; -.
DR   TreeFam; TF326301; -.
DR   BioGRID-ORCS; 11910; 1 hit in 79 CRISPR screens.
DR   PRO; PR:Q60765; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q60765; Protein.
DR   Bgee; ENSMUSG00000026628; Expressed in endoderm of midgut and 178 other cell types or tissues.
DR   ExpressionAtlas; Q60765; baseline and differential.
DR   GO; GO:1990622; C:CHOP-ATF3 complex; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
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; IDA:NTNU_SB.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0000977; F:RNA polymerase II transcription 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:0034198; P:cellular response to amino acid starvation; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0006094; P:gluconeogenesis; IDA:MGI.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:MGI.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:CACAO.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:ParkinsonsUK-UCL.
DR   GO; GO:1903984; P:positive regulation of TRAIL-activated apoptotic signaling pathway; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:ParkinsonsUK-UCL.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0010033; P:response to organic substance; IDA:MGI.
DR   GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
DR   CDD; cd14722; bZIP_ATF3; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   InterPro; IPR000837; AP-1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   PANTHER; PTHR23351:SF23; CYCLIC AMP-DEPENDENT TRANSCRIPTION FACTOR ATF-3; 1.
DR   PANTHER; PTHR23351; FOS TRANSCRIPTION FACTOR-RELATED; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   PRINTS; PR00042; LEUZIPPRFOS.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
DR   Genevisible; Q60765; MM.
PE   2: Evidence at transcript level;
KW   DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW   Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..181
FT                   /note="Cyclic AMP-dependent transcription factor ATF-3"
FT                   /id="PRO_0000076582"
FT   DOMAIN          86..149
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          73..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..110
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          114..142
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   COMPBIAS        79..93
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         162
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P18847"
FT   CROSSLNK        78
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P18847"
FT   CROSSLNK        175
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P18847"
SQ   SEQUENCE   181 AA;  20722 MW;  D641C8C6D14A457D CRC64;
     MMLQHPGQVS ASEVSATAIV PCLSPPGSLV FEDFANLTPF VKEELRFAIQ NKHLCHRMSS
     ALESVTVNNR PLEMSVTKSE AAPEEDERKR RRRERNKIAA AKCRNKKKEK TECLQKESEK
     LESVNAELKA QIEELKNEKQ HLIYMLNLHR PTCIVRAQNG RTPEDERNLF IQQIKEGTLQ
     S
//