ID   ATF1_MOUSE              Reviewed;         269 AA.
AC   P81269;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   27-MAR-2024, entry version 181.
DE   RecName: Full=Cyclic AMP-dependent transcription factor ATF-1;
DE            Short=cAMP-dependent transcription factor ATF-1;
DE   AltName: Full=Activating transcription factor 1;
DE   AltName: Full=TCR-ATF1;
GN   Name=Atf1;
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], AND SUBCELLULAR LOCATION.
RX   PubMed=1531847;
RA   Lee M.-R., Chung C.-S., Liou M.-L., Wu M., Li W.-F., Hsueh Y.-P.,
RA   Lai M.-Z.;
RT   "Isolation and characterization of nuclear proteins that bind to T cell
RT   receptor V beta decamer motif.";
RL   J. Immunol. 148:1906-1912(1992).
RN   [2]
RP   PHOSPHORYLATION AT SER-63.
RX   PubMed=18690222; DOI=10.1038/ni.1644;
RA   Ananieva O., Darragh J., Johansen C., Carr J.M., McIlrath J., Park J.M.,
RA   Wingate A., Monk C.E., Toth R., Santos S.G., Iversen L., Arthur J.S.;
RT   "The kinases MSK1 and MSK2 act as negative regulators of Toll-like receptor
RT   signaling.";
RL   Nat. Immunol. 9:1028-1036(2008).
CC   -!- FUNCTION: Binds the cAMP response element (CRE) (consensus: 5'-
CC       GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular
CC       promoters. Binds to the Tax-responsive element (TRE) of HTLV-I.
CC       Mediates PKA-induced stimulation of CRE-reporter genes. Represses the
CC       expression of FTH1 and other antioxidant detoxification genes. Triggers
CC       cell proliferation and transformation (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds DNA as a dimer. Interacts with HIPK2 and CDK3. Interacts
CC       with MOTS-c, a peptide produced by the mitochondrially encoded 12S rRNA
CC       MT-RNR1; the interaction occurs in the nucleus following metabolic
CC       stress. {ECO:0000250|UniProtKB:P18846}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1531847}.
CC   -!- PTM: Phosphorylated at Ser-196 by HIPK2 in response to genotoxic
CC       stress. This phosphorylation promotes transcription repression of FTH1
CC       and other antioxidant detoxification genes. The CDK3-mediated
CC       phosphorylation at Ser-63 promotes its transactivation and
CC       transcriptional activities (By similarity). Phosphorylated at Ser-63 by
CC       RPS6KA4 and RPS6KA5 in response to mitogenic or stress stimuli.
CC       {ECO:0000250, ECO:0000269|PubMed:18690222}.
CC   -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
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DR   EMBL; M63725; AAA40395.1; -; mRNA.
DR   CCDS; CCDS27832.1; -.
DR   PIR; A46490; A46490.
DR   RefSeq; NP_031523.3; NM_007497.3.
DR   RefSeq; XP_006520414.1; XM_006520351.3.
DR   RefSeq; XP_006520415.1; XM_006520352.3.
DR   AlphaFoldDB; P81269; -.
DR   BioGRID; 198232; 2.
DR   ComplexPortal; CPX-7; bZIP transcription factor complex, Atf1-Atf4.
DR   IntAct; P81269; 2.
DR   STRING; 10090.ENSMUSP00000023769; -.
DR   GlyGen; P81269; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; P81269; -.
DR   PhosphoSitePlus; P81269; -.
DR   MaxQB; P81269; -.
DR   PaxDb; 10090-ENSMUSP00000023769; -.
DR   PeptideAtlas; P81269; -.
DR   ProteomicsDB; 265141; -.
DR   Pumba; P81269; -.
DR   Antibodypedia; 4260; 794 antibodies from 43 providers.
DR   DNASU; 11908; -.
DR   Ensembl; ENSMUST00000023769.11; ENSMUSP00000023769.5; ENSMUSG00000023027.14.
DR   GeneID; 11908; -.
DR   KEGG; mmu:11908; -.
DR   UCSC; uc007xqs.1; mouse.
DR   AGR; MGI:1298366; -.
DR   CTD; 466; -.
DR   MGI; MGI:1298366; Atf1.
DR   VEuPathDB; HostDB:ENSMUSG00000023027; -.
DR   eggNOG; KOG3584; Eukaryota.
DR   GeneTree; ENSGT00940000158200; -.
DR   HOGENOM; CLU_042675_1_0_1; -.
DR   InParanoid; P81269; -.
DR   OMA; THISHIA; -.
DR   OrthoDB; 3137625at2759; -.
DR   PhylomeDB; P81269; -.
DR   TreeFam; TF106464; -.
DR   Reactome; R-MMU-199920; CREB phosphorylation.
DR   BioGRID-ORCS; 11908; 3 hits in 81 CRISPR screens.
DR   ChiTaRS; Atf1; mouse.
DR   PRO; PR:P81269; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; P81269; Protein.
DR   Bgee; ENSMUSG00000023027; Expressed in cumulus cell and 268 other cell types or tissues.
DR   ExpressionAtlas; P81269; baseline and differential.
DR   GO; GO:1990590; C:ATF1-ATF4 transcription factor complex; IDA:ParkinsonsUK-UCL.
DR   GO; GO:1990589; C:ATF4-CREB1 transcription factor complex; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR   GO; GO:0005667; C:transcription regulator complex; IDA: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:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0019933; P:cAMP-mediated signaling; ISO:MGI.
DR   GO; GO:0140928; P:inhibition of non-skeletal tissue mineralization; ISO:MGI.
DR   GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR   GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0032025; P:response to cobalt ion; IEA:Ensembl.
DR   GO; GO:0010035; P:response to inorganic substance; IMP:MGI.
DR   GO; GO:0014074; P:response to purine-containing compound; ISO:MGI.
DR   CDD; cd14690; bZIP_CREB1; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR003102; CREB1-like_pKID.
DR   InterPro; IPR001630; Leuzip_CREB.
DR   PANTHER; PTHR45879; CYCLIC AMP RESPONSE ELEMENT-BINDING PROTEIN B; 1.
DR   PANTHER; PTHR45879:SF2; CYCLIC AMP-DEPENDENT TRANSCRIPTION FACTOR ATF-1; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   Pfam; PF02173; pKID; 1.
DR   PRINTS; PR00041; LEUZIPPRCREB.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
DR   PROSITE; PS50953; KID; 1.
DR   Genevisible; P81269; MM.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..269
FT                   /note="Cyclic AMP-dependent transcription factor ATF-1"
FT                   /id="PRO_0000076576"
FT   DOMAIN          31..90
FT                   /note="KID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00312"
FT   DOMAIN          211..269
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          213..237
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          239..260
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   COMPBIAS        8..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         63
FT                   /note="Phosphoserine; by CaMK1, CDK3, RPS6KA4 and RPS6KA5"
FT                   /evidence="ECO:0000305|PubMed:18690222"
FT   MOD_RES         196
FT                   /note="Phosphoserine; by HIPK2"
FT                   /evidence="ECO:0000250|UniProtKB:P18846,
FT                   ECO:0000255|PROSITE-ProRule:PRU00312"
FT   CROSSLNK        206
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P18846"
SQ   SEQUENCE   269 AA;  29238 MW;  9885265159D64A0C CRC64;
     MEDSHKSNTT ETASQPGSTV AGPHVSQIVH QVSSLSESEE SQDSSDSIGS SQKAHGILAR
     RPSYRKILKD LSSEDTRGRK GEGENPSISA ITSMSVPAPI YQTSSGQYIA IAPNGALQLA
     SPSTDGVQAL QTLTMTNSSS TQQGTILQYA QTSDGQQILV PSNQVVVQTA SGDMQTYQIR
     TTPSATSLPQ TVVMTSPVTL ASQTTKTDDP QLRREIRLMK NREAARECRR KKKEYVKCLE
     NRVAVLENQN KTLIEELKTL KDLYSHKSV
//