ATF3_MOUSE
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 03-AUG-2022, entry version 168.
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; 7.
DR IntAct; Q60765; 1.
DR STRING; 10090.ENSMUSP00000027941; -.
DR iPTMnet; Q60765; -.
DR PhosphoSitePlus; Q60765; -.
DR MaxQB; Q60765; -.
DR PaxDb; Q60765; -.
DR PRIDE; Q60765; -.
DR ProteomicsDB; 265174; -.
DR Antibodypedia; 658; 579 antibodies from 37 providers.
DR DNASU; 11910; -.
DR Ensembl; ENSMUST00000027941; ENSMUSP00000027941; ENSMUSG00000026628.
DR Ensembl; ENSMUST00000195117; ENSMUSP00000141492; ENSMUSG00000026628.
DR GeneID; 11910; -.
DR KEGG; mmu:11910; -.
DR UCSC; uc007ece.1; mouse.
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; PLEMSVM; -.
DR OrthoDB; 1457971at2759; -.
DR PhylomeDB; Q60765; -.
DR TreeFam; TF326301; -.
DR BioGRID-ORCS; 11910; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q60765; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q60765; protein.
DR Bgee; ENSMUSG00000026628; Expressed in endoderm of midgut and 175 other tissues.
DR ExpressionAtlas; Q60765; baseline and differential.
DR Genevisible; Q60765; MM.
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: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:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
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; ISO:MGI.
DR GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
DR InterPro; IPR000837; AP-1.
DR InterPro; IPR029812; ATF3.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR23351; PTHR23351; 1.
DR PANTHER; PTHR23351:SF23; PTHR23351:SF23; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR PRINTS; PR00042; LEUZIPPRFOS.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
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
