ID   FOS_CYPCA               Reviewed;         347 AA.
AC   P79702;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Protein c-Fos {ECO:0000305};
DE   AltName: Full=Cellular oncogene fos;
DE   AltName: Full=Transcription factor AP-1 subunit c-Fos {ECO:0000305};
GN   Name=fos;
OS   Cyprinus carpio (Common carp).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Cyprinus.
OX   NCBI_TaxID=7962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Chang M.S., Huang C.J.;
RT   "The cloning and sequence of carp c-fos cDNA.";
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Nuclear phosphoprotein which forms a tight but non-covalently
CC       linked complex with the JUN/AP-1 transcription factor. FOS has a
CC       critical function in regulating the development of cells destined to
CC       form and maintain the skeleton. It is thought to have an important role
CC       in signal transduction, cell proliferation and differentiation (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. {ECO:0000305}.
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DR   EMBL; U81505; AAB39938.1; -; mRNA.
DR   AlphaFoldDB; P79702; -.
DR   SMR; P79702; -.
DR   Proteomes; UP000694384; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005667; C:transcription regulator complex; IEA:InterPro.
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; IPR029816; c-Fos/v-Fos.
DR   PANTHER; PTHR23351; PTHR23351; 1.
DR   PANTHER; PTHR23351:SF4; PTHR23351:SF4; 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; Proto-oncogene; Reference proteome.
FT   CHAIN           1..347
FT                   /note="Protein c-Fos"
FT                   /id="PRO_0000076472"
FT   DOMAIN          113..176
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          72..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..135
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          141..169
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          323..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..121
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..347
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   347 AA;  37587 MW;  A8F8781044AB8CE1 CRC64;
     MMFTSLNADC DASSRCSTAS AAAESVACYP LNQTQKFTEL SVSSASFVPT VTAISSCPDL
     QWMVQPMVSS VAPSNGGARS YNPNPYPKMR VTGTKSPNSN KRARAEQLSP EEEEKKRVRR
     ERNKMAAAKC RNRRRELTDT LQAETDELED EKSALQNDIA NLLKEKERLE FILAAHKPIC
     KIPSSSVSPI PAASVPEIHS ITTSVVSTAN APVTTSSSSS LFSSTASTDS FGSTVEISDL
     EPTLEESLEL LAKAELETAR SVPDVDLSSS LYARDWESLY TPANNDLEPL CTPVVTRTPA
     CTTYTSSFTF TYPENDVFPS CGPVHRRGSS SNDQSSDSLN SPTLLTL