FOSB_CANLF
ID FOSB_CANLF Reviewed; 338 AA.
AC Q9TUB3;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Protein FosB {ECO:0000305};
DE AltName: Full=Transcription factor AP-1 subunit FosB {ECO:0000305};
GN Name=FOSB;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sapsari;
RA Myeong H.K., Park C.K.;
RT "Genomic sequence of the canine fosB gene.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Heterodimerizes with proteins of the JUN family to form an
CC AP-1 transcription factor complex, thereby enhancing their DNA binding
CC activity to an AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing
CC their transcriptional activity (By similarity). Exhibits
CC transactivation activity in vitro (By similarity). As part of the AP-1
CC complex, facilitates enhancer selection together with cell-type-
CC specific transcription factors by collaboratively binding to
CC nucleosomal enhancers and recruiting the SWI/SNF (BAF) chromatin
CC remodeling complex to establish accessible chromatin (By similarity).
CC Together with JUN, plays a role in activation-induced cell death of T
CC cells by binding to the AP-1 promoter site of FASLG/CD95L, and inducing
CC its transcription in response to activation of the TCR/CD3 signaling
CC pathway (By similarity). Involved in the display of nurturing behavior
CC towards newborns (By similarity). May play a role in neurogenesis in
CC the hippocampus and in learning and memory-related tasks by regulating
CC the expression of various genes involved in neurogenesis, depression
CC and epilepsy (By similarity). Implicated in behavioral responses
CC related to morphine reward and spatial memory (By similarity).
CC {ECO:0000250|UniProtKB:P13346, ECO:0000250|UniProtKB:P53539}.
CC -!- SUBUNIT: Heterodimer; binds to DNA as heterodimer (By similarity).
CC Component of an AP-1 transcription factor complex; composed of FOS-JUN
CC heterodimers (By similarity). As part of the AP-1 transcription factor
CC complex, forms heterodimers with JUN, JUNB or JUND, thereby binding to
CC the AP-1 consensus sequence and stimulating transcription (By
CC similarity). Interacts with the BAF multiprotein chromatin-remodeling
CC complex subunits SMARCB1 and SMARCD1 (By similarity). Interacts with
CC ARID1A and JUN (By similarity). {ECO:0000250|UniProtKB:P13346}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P13346}.
CC -!- DOMAIN: Binds DNA via bZIP domain; DNA-binding is under control of
CC cellular redox homeostasis (in vitro) (By similarity). To enable DNA
CC binding, the bZIP domain must undergo a conformational rearrangement
CC which requires the reduction of the interchain disulfide bond between
CC FosB and JunD (in vitro) (By similarity). The bZIP domain is able to
CC form homomeric oligomers via formation of interchain disulfide bonds
CC under non-reducing conditions (in vitro) (By similarity). Under
CC reducing conditions, the disulfide-bonded homomeric species dissociates
CC into monomers (in vitro) (By similarity).
CC {ECO:0000250|UniProtKB:P53539}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:D3ZLB7}.
CC -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. {ECO:0000305}.
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DR EMBL; AF095857; AAF01350.1; -; Genomic_DNA.
DR RefSeq; NP_001013866.1; NM_001013844.1.
DR AlphaFoldDB; Q9TUB3; -.
DR SMR; Q9TUB3; -.
DR STRING; 9615.ENSCAFP00000051752; -.
DR PaxDb; Q9TUB3; -.
DR GeneID; 484445; -.
DR KEGG; cfa:484445; -.
DR CTD; 2354; -.
DR eggNOG; KOG1414; Eukaryota.
DR InParanoid; Q9TUB3; -.
DR OrthoDB; 1221590at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR InterPro; IPR000837; AP-1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR029813; FosB.
DR PANTHER; PTHR23351; PTHR23351; 1.
DR PANTHER; PTHR23351:SF3; PTHR23351:SF3; 1.
DR Pfam; PF00170; bZIP_1; 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 3: Inferred from homology;
KW Disulfide bond; DNA-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..338
FT /note="Protein FosB"
FT /id="PRO_0000076475"
FT DOMAIN 155..218
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..182
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 183..211
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 222..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13346"
FT DISULFID 172
FT /note="Interchain (with C-285 in JUND)"
FT /evidence="ECO:0000250|UniProtKB:P53539"
SQ SEQUENCE 338 AA; 35924 MW; CDD2800870FE197A CRC64;
MFQAFPGDYD SGSRCSSSPS AESQYLSSVD SFGSPPTAAA SQECAGLGEM PGSFVPTVTA
ITTSQDLQWL VQPTLISSMA QSQGQPLASQ PPAVDPYDMP GTSYSTPGMS GYSSGGASGS
GGPSTSGTTS GPGPARPARA RLRRPREETL TPEEEEKRRV RRERNKLAAA KCRNRRRELT
DRLQAETDQL EEEKAELESE IAELQKEKER LEFVLVAHKP GCKIPYEEGP GPGPLAEVRD
LPGSASTKED GFSWLLPPPP APPLPFQTSQ DAAPNLTASL FTHSEVQVLG DPFPVVNPSY
TSSFVLTCPE VSAFAGTQRP SGSDQPTDPL NSPSLLAL
