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 27-MAR-2024, entry version 92.
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 Proteomes; UP000694427; Unplaced.
DR Proteomes; UP000694700; Unplaced.
DR Proteomes; UP000694701; Unplaced.
DR Proteomes; UP001155660; Genome assembly.
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 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 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
//
