FOSL1_RAT
ID FOSL1_RAT Reviewed; 275 AA.
AC P10158; Q4V8K7;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Fos-related antigen 1;
DE Short=FRA-1;
GN Name=Fosl1; Synonyms=Fra1;
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 INDUCTION BY SERUM.
RX PubMed=3133553; DOI=10.1128/mcb.8.5.2063-2069.1988;
RA Cohen D.R., Curran T.;
RT "fra-1: a serum-inducible, cellular immediate-early gene that encodes a
RT fos-related antigen.";
RL Mol. Cell. Biol. 8:2063-2069(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-43.
RC STRAIN=Sprague-Dawley;
RX PubMed=7791782; DOI=10.1128/mcb.15.7.3748;
RA Bergers G., Graninger P., Braselmann S., Wrighton C., Busslinger M.;
RT "Transcriptional activation of the fra-1 gene by AP-1 is mediated by
RT regulatory sequences in the first intron.";
RL Mol. Cell. Biol. 15:3748-3758(1995).
CC -!- SUBUNIT: Heterodimer (By similarity). Interacts with the BAF
CC multiprotein chromatin-remodeling complex subunits SMARCB1 and SMARCD1
CC (By similarity). Interacts with ARID1A and JUN (By similarity).
CC {ECO:0000250|UniProtKB:P47930, ECO:0000250|UniProtKB:P48755}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51145}.
CC -!- INDUCTION: By serum. {ECO:0000269|PubMed:3133553}.
CC -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. {ECO:0000305}.
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DR EMBL; M19651; AAA41171.1; -; mRNA.
DR EMBL; BC097342; AAH97342.1; -; mRNA.
DR EMBL; U24154; AAA82045.1; -; Genomic_DNA.
DR PIR; A27722; TVRTFR.
DR RefSeq; NP_037085.1; NM_012953.1.
DR AlphaFoldDB; P10158; -.
DR SMR; P10158; -.
DR CORUM; P10158; -.
DR DIP; DIP-1071N; -.
DR STRING; 10116.ENSRNOP00000027891; -.
DR iPTMnet; P10158; -.
DR PhosphoSitePlus; P10158; -.
DR PaxDb; P10158; -.
DR Ensembl; ENSRNOT00000027891; ENSRNOP00000027891; ENSRNOG00000020552.
DR GeneID; 25445; -.
DR KEGG; rno:25445; -.
DR UCSC; RGD:2627; rat.
DR CTD; 8061; -.
DR RGD; 2627; Fosl1.
DR eggNOG; KOG1414; Eukaryota.
DR GeneTree; ENSGT00940000160034; -.
DR HOGENOM; CLU_049742_2_1_1; -.
DR InParanoid; P10158; -.
DR OMA; LEPADSC; -.
DR OrthoDB; 1221590at2759; -.
DR PhylomeDB; P10158; -.
DR TreeFam; TF326301; -.
DR PRO; PR:P10158; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020552; Expressed in skeletal muscle tissue and 16 other tissues.
DR Genevisible; P10158; RN.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0042734; C:presynaptic membrane; IDA:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IDA:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
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; IDA:NTNU_SB.
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:0031668; P:cellular response to extracellular stimulus; ISO:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0007612; P:learning; IEP:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0060674; P:placenta blood vessel development; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:RGD.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:RGD.
DR GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; ISO:RGD.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
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:0034097; P:response to cytokine; IEP:RGD.
DR GO; GO:0009629; P:response to gravity; IEP:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; 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:0007296; P:vitellogenesis; ISO:RGD.
DR InterPro; IPR000837; AP-1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR029815; Fra1.
DR PANTHER; PTHR23351; PTHR23351; 1.
DR PANTHER; PTHR23351:SF6; PTHR23351:SF6; 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 2: Evidence at transcript level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..275
FT /note="Fos-related antigen 1"
FT /id="PRO_0000076481"
FT DOMAIN 107..170
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..129
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 135..163
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 171..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..87
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15407"
SQ SEQUENCE 275 AA; 30115 MW; 103726AD5D1FAB2F CRC64;
MYRDFGEPGP SSGAGSAYGR PAQPQQAQTQ TVQQQKFHLV PSINAVSGSQ ELQWMVQPHF
LGPSGYPRPL TYPQYSPPQP RPGVIRALGP PPGVRRRPCE QISPEEEERR RVRRERNKLA
AAKCRNRRKE LTDFLQAETD KLEDEKSGLQ REIEELQKQK ERLELVLEAH RPICKIPEED
KKDTGGTSST SGAGSPPGPC RPVPCISLSP GPVLEPEALH TPTLMTTPSL TPFTPSLVFT
YPSTPEPCSS AHRKSSSSSG DPSSDPLGSP TLLAL
