DBP_RAT
ID DBP_RAT Reviewed; 325 AA.
AC P16443;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=D site-binding protein;
DE AltName: Full=Albumin D box-binding protein;
DE AltName: Full=Albumin D-element-binding protein;
DE AltName: Full=D site albumin promoter-binding protein 1;
GN Name=Dbp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=2331750; DOI=10.1016/0092-8674(90)90808-r;
RA Mueller C.R., Maire P., Schibler U.;
RT "DBP, a liver-enriched transcriptional activator, is expressed late in
RT ontogeny and its tissue specificity is determined posttranscriptionally.";
RL Cell 61:279-291(1990).
RN [2]
RP ERRATUM OF PUBMED:2331750, AND SEQUENCE REVISION.
RX PubMed=2040017;
RA Mueller C.R., Maire P., Schibler U.;
RL Cell 65:915-915(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
RP REVIEW.
RX PubMed=10508692; DOI=10.1016/s0959-437x(99)00009-x;
RA Brown S.A., Schibler U.;
RT "The ins and outs of circadian timekeeping.";
RL Curr. Opin. Genet. Dev. 9:588-594(1999).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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.
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 -!- DEVELOPMENTAL STAGE: Expressed late in ontogeny.
CC {ECO:0000269|PubMed:2331750}.
CC -!- SIMILARITY: Belongs to the bZIP family. PAR subfamily. {ECO:0000305}.
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DR EMBL; J03179; AAA41083.1; -; mRNA.
DR EMBL; BC087668; AAH87668.1; -; mRNA.
DR PIR; A34894; A34894.
DR RefSeq; NP_036675.1; NM_012543.3.
DR AlphaFoldDB; P16443; -.
DR SMR; P16443; -.
DR STRING; 10116.ENSRNOP00000028547; -.
DR iPTMnet; P16443; -.
DR PhosphoSitePlus; P16443; -.
DR PaxDb; P16443; -.
DR PRIDE; P16443; -.
DR Ensembl; ENSRNOT00000028546; ENSRNOP00000028547; ENSRNOG00000021027.
DR GeneID; 24309; -.
DR KEGG; rno:24309; -.
DR UCSC; RGD:2491; rat.
DR CTD; 1628; -.
DR RGD; 2491; Dbp.
DR eggNOG; KOG3119; Eukaryota.
DR GeneTree; ENSGT00940000162136; -.
DR HOGENOM; CLU_051922_0_0_1; -.
DR InParanoid; P16443; -.
DR OMA; PKEPASX; -.
DR OrthoDB; 1023460at2759; -.
DR PhylomeDB; P16443; -.
DR TreeFam; TF315869; -.
DR PRO; PR:P16443; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000021027; Expressed in skeletal muscle tissue and 20 other tissues.
DR ExpressionAtlas; P16443; baseline and differential.
DR Genevisible; P16443; RN.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:RGD.
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:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0007623; P:circadian rhythm; IEA:InterPro.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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_0000076509"
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..255
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:22673903"
SQ SEQUENCE 325 AA; 34436 MW; D9B2A53FF18455B2 CRC64;
MARPLSDRTP GPLLLGGPAG APPGGGALLG LRSLLQGNSK PKEPASCLLK EKERKATLPS
APVPGPVLET AGPADAPTGA 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
