ID   FOS_TETFL               Reviewed;         374 AA.
AC   Q91496;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 80.
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   Tetraodon fluviatilis (Green pufferfish) (Chelonodon fluviatilis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=47145;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Chang M.S., Chang G.D., Huang F.L., Huang C.J., Lo T.B.;
RL   Submitted (APR-1996) 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; U53520; AAB07359.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q91496; -.
DR   SMR; Q91496; -.
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   3: Inferred from homology;
KW   DNA-binding; Nucleus; Phosphoprotein; Proto-oncogene.
FT   CHAIN           1..374
FT                   /note="Protein c-Fos"
FT                   /id="PRO_0000076474"
FT   DOMAIN          120..183
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          78..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..142
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          148..176
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          355..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..128
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   374 AA;  40526 MW;  4DE2CB426D9FEEB9 CRC64;
     MMFTSFNAEC DSSSRCSASP SDNVYYPSPA GSYSSMGSPQ SQDLTDLTAS SASFVPTVTA
     ISTSPDLQWM VQPLVSSVAP SRRAHPYSPS PSYKRTVMRS GASKPHAKRG RVEQTTPEEE
     EKKRIRRERN KQAAAKCRNR RRELTDSLQA ETDQLEAEKS SLQNDIANLL KEKERLEFIL
     AAHQPICKIP SQMDSDFPVV SMSPVHAYLS TAASTQPQTS VPEATTVTSS HSTFTSTSNS
     IFGSNSDSLL STATVSDSVV KMTDLESSVL EESLDLLAKT EVETVEVPDV NLSSSLYTAQ
     DWEPLHATIG SSDFEPLCTP VVTCTPACTT ITSSFVFTFP EAETFPTCCV AHRRGSNSND
     QSSDSLSSPT LLAL