ID Q9EQC2_RAT Unreviewed; 111 AA. AC Q9EQC2; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 113. DE RecName: Full=Protein c-Fos {ECO:0000256|ARBA:ARBA00029563}; DE AltName: Full=Cellular oncogene fos {ECO:0000256|ARBA:ARBA00031103}; DE Flags: Fragment; 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:0000313|EMBL:AAG47951.1}; RN [1] {ECO:0000313|EMBL:AAG47951.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F344 {ECO:0000313|EMBL:AAG47951.1}; RC TISSUE=Brain {ECO:0000313|EMBL:AAG47951.1}; RA Feng Z., Kong L.-Y., Qi Q., Ho S.-L., Tiao N., Bing G., Han Y.; RT "Induction of unspliced C-FOS mRNA in rodent brain by kainic acid and RT lipopolysaccharide (LPS)."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. CC {ECO:0000256|ARBA:ARBA00007619}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF277645; AAG47951.1; -; Genomic_DNA. DR AlphaFoldDB; Q9EQC2; -. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. 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 CDD; cd14721; bZIP_Fos; 1. DR Gene3D; 1.20.5.170; -; 1. DR InterPro; IPR000837; AP-1. DR InterPro; IPR004827; bZIP. DR InterPro; IPR046347; bZIP_sf. DR PANTHER; PTHR23351; FOS TRANSCRIPTION FACTOR-RELATED; 1. DR PANTHER; PTHR23351:SF4; PROTEIN C-FOS; 1. DR Pfam; PF00170; bZIP_1; 1. DR PRINTS; PR00042; LEUZIPPRFOS. DR SMART; SM00338; BRLZ; 1. DR SUPFAM; SSF57959; Leucine zipper domain; 1. DR PROSITE; PS50217; BZIP; 1. DR PROSITE; PS00036; BZIP_BASIC; 1. PE 3: Inferred from homology; KW Nucleus {ECO:0000256|ARBA:ARBA00023242}. FT DOMAIN 3..66 FT /note="BZIP" FT /evidence="ECO:0000259|PROSITE:PS50217" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 89..111 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAG47951.1" FT NON_TER 111 FT /evidence="ECO:0000313|EMBL:AAG47951.1" SQ SEQUENCE 111 AA; 12705 MW; 655694096DAA6C4D CRC64; KREEKRRIRR ERNKMAAAKC RNRRRELTDT LQAETDQLED EKSALQTEIA NLLKEKEKLE FILAAHRPAC KIPNDLGFPE EMSVTSLDLT GGLPEATTPE SEEAFTLPLL N //