FOSB_RAT
ID FOSB_RAT Reviewed; 338 AA.
AC D3ZLB7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Protein FosB {ECO:0000305};
DE AltName: Full=Transcription factor AP-1 subunit FosB {ECO:0000305};
GN Name=Fosb {ECO:0000312|RGD:1308198};
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 {ECO:0000312|Proteomes:UP000002494};
RN [1] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000312|EMBL:EDM08212.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|EMBL:EDM08212.1};
RX PubMed=15632090; DOI=10.1101/gr.2889405;
RA Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
RA Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
RA Istrail S., Li P., Sutton G.;
RT "Gene and alternative splicing annotation with AIR.";
RL Genome Res. 15:54-66(2005).
RN [3] {ECO:0000305}
RP TISSUE SPECIFICITY, INDUCTION BY ECS, AND PHOSPHORYLATION.
RX PubMed=16687504; DOI=10.1523/jneurosci.4970-05.2006;
RA Ulery P.G., Rudenko G., Nestler E.J.;
RT "Regulation of DeltaFosB stability by phosphorylation.";
RL J. Neurosci. 26:5131-5142(2006).
RN [4] {ECO:0000305}
RP TISSUE SPECIFICITY, AND INDUCTION BY NOVELTY EXPOSURE.
RX PubMed=26446228; DOI=10.1523/jneurosci.2083-15.2015;
RA Eagle A.L., Gajewski P.A., Yang M., Kechner M.E., Al Masraf B.S.,
RA Kennedy P.J., Wang H., Mazei-Robison M.S., Robison A.J.;
RT "Experience-Dependent Induction of Hippocampal DeltaFosB Controls
RT Learning.";
RL J. Neurosci. 35:13773-13783(2015).
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). {ECO:0000250|UniProtKB:P13346}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P13346}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (PubMed:16687504). Expressed in
CC pyramidal cells in CA1 and CA3, in the dentate gyrus and the nucleus
CC accumbens (at protein level) (PubMed:26446228).
CC {ECO:0000269|PubMed:16687504, ECO:0000269|PubMed:26446228}.
CC -!- INDUCTION: Induced by chronic electroconvulsive seizure (ECS) treatment
CC (PubMed:16687504). Induced in the hippocampus by novelty exposure and
CC spatial learning (PubMed:26446228). {ECO:0000269|PubMed:16687504,
CC ECO:0000269|PubMed:26446228}.
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; phosphorylation is induced by chronic
CC electroconvulsive seizure (ECS) treatment.
CC {ECO:0000269|PubMed:16687504}.
CC -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. {ECO:0000305}.
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DR EMBL; AABR07002674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473979; EDM08212.1; -; Genomic_DNA.
DR RefSeq; NP_001243438.1; NM_001256509.1.
DR AlphaFoldDB; D3ZLB7; -.
DR SMR; D3ZLB7; -.
DR STRING; 10116.ENSRNOP00000065427; -.
DR PaxDb; D3ZLB7; -.
DR Ensembl; ENSRNOT00000072149; ENSRNOP00000065427; ENSRNOG00000046667.
DR GeneID; 100360880; -.
DR KEGG; rno:100360880; -.
DR UCSC; RGD:2321278; rat.
DR CTD; 2354; -.
DR RGD; 1308198; Fosb.
DR eggNOG; KOG1414; Eukaryota.
DR GeneTree; ENSGT00940000160358; -.
DR HOGENOM; CLU_049742_0_0_1; -.
DR InParanoid; D3ZLB7; -.
DR OMA; QGMMQEV; -.
DR OrthoDB; 1221590at2759; -.
DR PhylomeDB; D3ZLB7; -.
DR TreeFam; TF326301; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000046667; Expressed in jejunum and 15 other tissues.
DR ExpressionAtlas; D3ZLB7; baseline and differential.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0071277; P:cellular response to calcium ion; ISO:RGD.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0045944; P:positive 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:0051591; P:response to cAMP; IEP:RGD.
DR GO; GO:0051412; P:response to corticosterone; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0043278; P:response to morphine; IEP:RGD.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:RGD.
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 1: Evidence at protein level;
KW Disulfide bond; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..338
FT /note="Protein FosB"
FT /id="PRO_0000454709"
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..179
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..276
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..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..269
FT /note="Pro 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-279 in JUND)"
FT /evidence="ECO:0000250|UniProtKB:P53539"
SQ SEQUENCE 338 AA; 35979 MW; DBB043A69B971C0E CRC64;
MFQAFPGDYD SGSRCSSSPS AESQYLSSVD SFGSPPTAAA SQECAGLGEM PGSFVPTVTA
ITTSQDLQWL VQPTLISSMA QSQGQPLASQ PPAVDPYDMP GTSYSTPGLS AYSTGGASGS
GGPSTSTSTS GPVSARPARA RPRRPREETL TPEEEEKRRV RRERNKLAAA KCRNRRRELT
DRLQAETDQL EEEKAELESE IAELQKEKER LEFVLVAHKP GCKIPYEEGP GPGPLAEVRD
LPGSTSAKED GFGWLLPPPP PPPLPFQSSR DAPPNLTASL FTHSEVQVLG DPFPVVSPSY
TSSFVLTCPE VSAFAGSQRT SGSEQPSDPL NSPSLLAL
