ID   DBP_BOVIN               Reviewed;         325 AA.
AC   Q32PF6;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   03-AUG-2022, entry version 98.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the bZIP family. PAR subfamily. {ECO:0000305}.
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DR   EMBL; BC108134; AAI08135.2; -; mRNA.
DR   RefSeq; NP_001032522.1; NM_001037445.1.
DR   AlphaFoldDB; Q32PF6; -.
DR   SMR; Q32PF6; -.
DR   STRING; 9913.ENSBTAP00000008883; -.
DR   PaxDb; Q32PF6; -.
DR   PRIDE; Q32PF6; -.
DR   Ensembl; ENSBTAT00000008883; ENSBTAP00000008883; ENSBTAG00000006754.
DR   GeneID; 503577; -.
DR   KEGG; bta:503577; -.
DR   CTD; 1628; -.
DR   VEuPathDB; HostDB:ENSBTAG00000006754; -.
DR   VGNC; VGNC:27894; DBP.
DR   eggNOG; KOG3119; Eukaryota.
DR   GeneTree; ENSGT00940000162136; -.
DR   HOGENOM; CLU_051922_0_0_1; -.
DR   InParanoid; Q32PF6; -.
DR   OMA; PKEPASX; -.
DR   OrthoDB; 1023460at2759; -.
DR   TreeFam; TF315869; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000006754; Expressed in retina and 107 other tissues.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
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:0007623; P:circadian rhythm; IEA:InterPro.
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   2: Evidence at transcript 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_0000226720"
FT   DOMAIN          255..318
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          124..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          212..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        221..255
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         86
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q10586"
SQ   SEQUENCE   325 AA;  34322 MW;  59C3A8D4F54D00CB CRC64;
     MARPVSERTP APLLLGGPTG APPGGGALLG LRSLLQGTSK PKEPTSCLLK EKERKASPPA
     ATVPGPGLET AGPADASAGA VVGGGSPRGR PGAAPGPGLL APLLWERTLP FGDVEYVDLD
     AFLLEHGLPP SPPPPGGPSP APSPVRTPAP SPRPGSCGSA SPRSSPGHAP ARAALGAAGG
     HRAGLTSRDT PSPVDPDTVE VLMTFEPDPA DLALSSIPGH ETFDPRRHRF SEEELKPQPI
     MKKARKIQVP EEQKDEKYWS RRYKNNEAAK RSRDARRLKE NQISVRAAFL EKENALLRQE
     VVAVRQELSH YRAVLSRYQA QHGAL