DBP_MOUSE
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 03-AUG-2022, entry version 169.
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; Q60925; -.
DR PRIDE; Q60925; -.
DR ProteomicsDB; 279158; -.
DR Antibodypedia; 18372; 120 antibodies from 22 providers.
DR DNASU; 13170; -.
DR Ensembl; ENSMUST00000080885; ENSMUSP00000079693; ENSMUSG00000059824.
DR GeneID; 13170; -.
DR KEGG; mmu:13170; -.
DR UCSC; uc009gws.2; mouse.
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; PKEPASX; -.
DR OrthoDB; 1023460at2759; -.
DR PhylomeDB; Q60925; -.
DR TreeFam; TF315869; -.
DR BioGRID-ORCS; 13170; 2 hits in 77 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 247 other tissues.
DR ExpressionAtlas; Q60925; baseline and differential.
DR Genevisible; Q60925; MM.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:MGI.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR029830; DBP.
DR InterPro; IPR040223; PAR_bZIP.
DR PANTHER; PTHR11988; PTHR11988; 1.
DR PANTHER; PTHR11988:SF7; PTHR11988:SF7; 1.
DR Pfam; PF07716; bZIP_2; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
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
