ID   DBP_MOUSE               Reviewed;         325 AA.
AC   Q60925; Q8VCX3;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   24-JAN-2024, entry version 177.
DE   RecName: Full=D site-binding protein;
DE   AltName: Full=Albumin D box-binding protein;
DE   AltName: Full=Albumin D-element-binding protein;
GN   Name=Dbp;
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 [GENOMIC DNA].
RC   STRAIN=129/Sv; TISSUE=Liver;
RA   Lee Y.H., Oguchi H., Gonzalez F.J.;
RL   Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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   CIRCADIAN INDUCTION.
RX   PubMed=8617210; DOI=10.1002/j.1460-2075.1996.tb00365.x;
RA   Fonjallaz P., Ossipow V., Wanner G., Schibler U.;
RT   "The two PAR leucine zipper proteins, TEF and DBP, display similar
RT   circadian and tissue-specific expression, but have different target
RT   promoter preferences.";
RL   EMBO J. 15:351-362(1996).
RN   [4]
RP   INVOLVEMENT IN EPILEPSY.
RX   PubMed=15175240; DOI=10.1101/gad.301404;
RA   Gachon F., Fonjallaz P., Damiola F., Gos P., Kodama T., Zakany J.,
RA   Duboule D., Petit B., Tafti M., Schibler U.;
RT   "The loss of circadian PAR bZip transcription factors results in
RT   epilepsy.";
RL   Genes Dev. 18:1397-1412(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver, and Pancreas;
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).
CC   -!- FUNCTION: This transcriptional activator recognizes and binds to the
CC       sequence 5'-RTTAYGTAAY-3' found in the promoter of genes such as
CC       albumin, CYP2A4 and CYP2A5. It is not essential for circadian rhythm
CC       generation, but modulates important clock output genes. May be a direct
CC       target for regulation by the circadian pacemaker component clock. May
CC       affect circadian period and sleep regulation (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Binds DNA as a homodimer or a heterodimer. Can form a
CC       heterodimer with TEF (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed in the suprachiasmatic nuclei (SCN) and
CC       in most peripheral tissues, with a strong circadian rhythmicity.
CC   -!- INDUCTION: Accumulates according to a robust circadian rhythm in liver
CC       and kidney. In liver nuclei, the amplitude of daily oscillation has
CC       been estimated to be >50-fold, and 2-fold in the brain.
CC   -!- MISCELLANEOUS: Mice deficient for all three PAR bZIP proteins (DBP, HLF
CC       and TEF) display a dramatically shortened life span and are highly
CC       susceptible to generalized spontaneous and audiogenic epilepsies (due
CC       for example to the noise of a vacuum cleaner) that are frequently
CC       lethal. The down-regulation of pyridoxal kinase (Pdxk) expression in
CC       these mice may participate in this seizure phenotype.
CC   -!- SIMILARITY: Belongs to the bZIP family. PAR subfamily. {ECO:0000305}.
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DR   EMBL; U29762; AAA73924.1; -; Genomic_DNA.
DR   EMBL; BC018323; AAH18323.1; -; mRNA.
DR   CCDS; CCDS21260.1; -.
DR   RefSeq; NP_058670.2; NM_016974.3.
DR   AlphaFoldDB; Q60925; -.
DR   SMR; Q60925; -.
DR   BioGRID; 199060; 7.
DR   IntAct; Q60925; 4.
DR   STRING; 10090.ENSMUSP00000079693; -.
DR   iPTMnet; Q60925; -.
DR   PhosphoSitePlus; Q60925; -.
DR   SwissPalm; Q60925; -.
DR   PaxDb; 10090-ENSMUSP00000079693; -.
DR   ProteomicsDB; 279158; -.
DR   Antibodypedia; 18372; 137 antibodies from 22 providers.
DR   DNASU; 13170; -.
DR   Ensembl; ENSMUST00000080885.12; ENSMUSP00000079693.4; ENSMUSG00000059824.13.
DR   GeneID; 13170; -.
DR   KEGG; mmu:13170; -.
DR   UCSC; uc009gws.2; mouse.
DR   AGR; MGI:94866; -.
DR   CTD; 1628; -.
DR   MGI; MGI:94866; Dbp.
DR   VEuPathDB; HostDB:ENSMUSG00000059824; -.
DR   eggNOG; KOG3119; Eukaryota.
DR   GeneTree; ENSGT00940000162136; -.
DR   HOGENOM; CLU_051922_0_0_1; -.
DR   InParanoid; Q60925; -.
DR   OMA; WERTLPY; -.
DR   OrthoDB; 5354784at2759; -.
DR   PhylomeDB; Q60925; -.
DR   TreeFam; TF315869; -.
DR   BioGRID-ORCS; 13170; 2 hits in 82 CRISPR screens.
DR   PRO; PR:Q60925; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q60925; Protein.
DR   Bgee; ENSMUSG00000059824; Expressed in pigmented layer of retina and 249 other cell types or tissues.
DR   ExpressionAtlas; Q60925; baseline and differential.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO: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; IBA:GO_Central.
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:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0007623; P:circadian rhythm; TAS:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; TAS:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd14695; bZIP_HLF; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR040223; PAR_bZIP.
DR   PANTHER; PTHR11988:SF7; D SITE-BINDING PROTEIN; 1.
DR   PANTHER; PTHR11988; THYROTROPH EMBRYONIC FACTOR RELATED; 1.
DR   Pfam; PF07716; bZIP_2; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   Genevisible; Q60925; MM.
PE   1: Evidence at protein level;
KW   Activator; Biological rhythms; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..325
FT                   /note="D site-binding protein"
FT                   /id="PRO_0000076508"
FT   DOMAIN          255..318
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          124..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          257..279
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          283..297
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   COMPBIAS        127..151
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         86
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        60
FT                   /note="S -> T (in Ref. 1; AAA73924)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        109
FT                   /note="L -> F (in Ref. 1; AAA73924)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   325 AA;  34380 MW;  B2B2A3E091845A16 CRC64;
     MARPLSDRTP GPLLLGGPAG APPGGGALLG LRSLLQGNSK PKEPASCLLK EKERKATLPS
     APVPGPGLET AGPADAPSGA VSGGGSPRGR SGPVAGPSLF APLLWERTLP FGDVEYVDLD
     AFLLEHGLPP SPPPPGGLSP APSPARTPAP SPGPGSCSSS SPRSSPGHAP ARATLGAAGG
     HRAGLTSRDT PSPVDPDTVE VLMTFEPDPA DLALSSIPGH ETFDPRRHRF SEEELKPQPI
     MKKARKVQVP EEQKDEKYWS RRYKNNEAAK RSRDARRLKE NQISVRAAFL EKENALLRQE
     VVAVRQELSH YRAVLSRYQA QHGTL
//