ID   FOS_TAKRU               Reviewed;         376 AA.
AC   P53450;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 108.
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   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8643637; DOI=10.1073/pnas.93.4.1366;
RA   Trower M.K., Orton S.M., Purvis I.J., Sanseau P., Riley J.,
RA   Christodoulou C., Burt D., See C.G., Elgar G., Sherrington R., Rogaev E.I.,
RA   St George-Hyslop P.H., Brenner S., Dykes C.W.;
RT   "Conservation of synteny between the genome of the pufferfish (Fugu
RT   rubripes) and the region on human chromosome 14 (14q24.3) associated with
RT   familial Alzheimer disease (AD3 locus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:1366-1369(1996).
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}.
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; U40757; AAC59778.1; -; Genomic_DNA.
DR   RefSeq; XP_003971716.1; XM_003971667.2.
DR   AlphaFoldDB; P53450; -.
DR   SMR; P53450; -.
DR   STRING; 31033.ENSTRUP00000026703; -.
DR   Ensembl; ENSTRUT00000092218; ENSTRUP00000074379; ENSTRUG00000010579.
DR   eggNOG; KOG1414; Eukaryota.
DR   GeneTree; ENSGT00940000159276; -.
DR   InParanoid; P53450; -.
DR   OrthoDB; 1221590at2759; -.
DR   Proteomes; UP000005226; Chromosome 16.
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; Reference proteome.
FT   CHAIN           1..376
FT                   /note="Protein c-Fos"
FT                   /id="PRO_0000076473"
FT   DOMAIN          121..184
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          81..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          123..143
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          149..177
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          354..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..129
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..161
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   376 AA;  40826 MW;  BFC28534431DB491 CRC64;
     MMFTSFNAEC DSSSRCSASP VGDNLYYPSP AGSYSSMGSP QSQDFTDLTA SSASFIPTVT
     AISTSPDLQW MVQPLISSVA PSHRAHPYSP SPSYKRTVMR SAASKAHGKR SRVEQTTPEE
     EEKKRIRRER NKQAAAKCRN RRRELTDTLQ AETDQLEDEK SSLQNDIANL LKEKERLEFI
     LAAHQPICKI PSQMDTDFSV VSMSPVHACL STTVSTQLQT SIPEATTVTS SHSTFTSTSN
     SIFSGSSDSL LSTATVSNSV VKMTDLDSSV LEESLDLLAK TEAETARSVP DVNLSNSLFA
     AQDWEPLHAT ISSSDFEPLC TPVVTCTPAC TTLTSSFVFT FPEAETFPTC GVAHRRRSNS
     NDQSSDSLSS PTLLAL