ID   BATF3_RAT               Reviewed;         133 AA.
AC   P97876;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Basic leucine zipper transcriptional factor ATF-like 3;
DE            Short=B-ATF-3;
DE   AltName: Full=Jun dimerization protein 1;
DE            Short=JDP-1;
GN   Name=Batf3; Synonyms=Jdp1;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND INTERACTION WITH
RP   JUN.
RX   PubMed=9154808; DOI=10.1128/mcb.17.6.3094;
RA   Aronheim A., Zandi E., Hennemann H., Elledge S.J., Karin M.;
RT   "Isolation of an AP-1 repressor by a novel method for detecting protein-
RT   protein interactions.";
RL   Mol. Cell. Biol. 17:3094-3102(1997).
CC   -!- FUNCTION: AP-1 family transcription factor that controls the
CC       differentiation of CD8(+) thymic conventional dendritic cells in the
CC       immune system. Acts via the formation of a heterodimer with JUN family
CC       proteins that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3' and
CC       regulates expression of target genes. Required for development of CD8-
CC       alpha(+) classical dendritic cells (cDCs) and related CD103(+)
CC       dendritic cells that cross-present antigens to CD8 T-cells and produce
CC       interleukin-12 (IL12) in response to pathogens (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer; heterodimerizes with JUN family proteins.
CC       Interacts with JUN. {ECO:0000269|PubMed:9154808}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:9154808}.
CC   -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR   EMBL; U53450; AAB49921.1; -; Genomic_DNA.
DR   RefSeq; NP_068637.1; NM_021865.1.
DR   AlphaFoldDB; P97876; -.
DR   SMR; P97876; -.
DR   BioGRID; 248847; 1.
DR   STRING; 10116.ENSRNOP00000004962; -.
DR   PaxDb; P97876; -.
DR   GeneID; 60462; -.
DR   KEGG; rno:60462; -.
DR   CTD; 55509; -.
DR   RGD; 620501; Batf3.
DR   eggNOG; KOG1414; Eukaryota.
DR   InParanoid; P97876; -.
DR   OrthoDB; 1440552at2759; -.
DR   PhylomeDB; P97876; -.
DR   PRO; PR:P97876; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; TAS:RGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; TAS:RGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR   GO; GO:0097028; P:dendritic cell differentiation; ISS:UniProtKB.
DR   GO; GO:0043011; P:myeloid dendritic cell differentiation; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0009615; P:response to virus; ISS:UniProtKB.
DR   InterPro; IPR000837; AP-1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR029818; p21SNFT.
DR   PANTHER; PTHR23351; PTHR23351; 1.
DR   PANTHER; PTHR23351:SF13; PTHR23351:SF13; 1.
DR   Pfam; PF07716; bZIP_2; 1.
DR   PRINTS; PR00042; LEUZIPPRFOS.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..133
FT                   /note="Basic leucine zipper transcriptional factor ATF-like
FT                   3"
FT                   /id="PRO_0000326108"
FT   DOMAIN          28..91
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          30..55
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          56..84
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..68
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NR55"
FT   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NR55"
SQ   SEQUENCE   133 AA;  15129 MW;  0A38C37121EB06F2 CRC64;
     MSQGPPAGGV LQSSVAAPGN QPQSPKDDDR KVRRREKNRV AAQRSRKKQT QKSDKLHEEH
     ESLEQENSVL RREIAKLKEE LRHLTEALKE HEKMCPLLLC PMNFVQLRPD PVASWSAHDA
     PDHPSFIWLG TLV