FOS_CHICK
ID FOS_CHICK Reviewed; 367 AA.
AC P11939;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 123.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3330781;
RA Moelders H., Jenuwein T., Adamkiewicz J., Mueller R.;
RT "Isolation and structural analysis of a biologically active chicken c-fos
RT cDNA: identification of evolutionarily conserved domains in fos protein.";
RL Oncogene 1:377-385(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3316710; DOI=10.1128/jvi.61.12.4012-4018.1987;
RA Fujiwara K.T., Ashida K., Nishina H., Iba H., Miyajima N., Nishizawa M.,
RA Kawai S.;
RT "The chicken c-fos gene: cloning and nucleotide sequence analysis.";
RL J. Virol. 61:4012-4018(1987).
RN [3]
RP INTERACTION WITH MAFB.
RX PubMed=7935473; DOI=10.1128/mcb.14.11.7581-7591.1994;
RA Kataoka K., Fujiwara K.T., Noda M., Nishizawa M.;
RT "MafB,a new Maf family transcription activator that can associate with Maf
RT and Fos but not with Jun.";
RL Mol. Cell. Biol. 14:7581-7591(1994).
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. In
CC growing cells, may activate phospholipid synthesis (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer. Interacts with MAFB.
CC {ECO:0000269|PubMed:7935473}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Endoplasmic reticulum {ECO:0000250}.
CC Cytoplasm, cytosol {ECO:0000250}. Note=In quiescent cells, may be
CC present in very small amounts in the cytosol. Following induction of
CC cell growth, first localizes to the endoplasmic reticulum and later to
CC the nucleus (By similarity). {ECO:0000250}.
CC -!- INDUCTION: Expression increases upon a variety of stimuli, including
CC growth factors, cytokines, neurotransmitters, polypeptide hormones,
CC stress and cell injury.
CC -!- PTM: May be Tyr-phosphorylated in quiescent cells and dephosphorylated
CC upon cell growth induction. {ECO:0000250}.
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; M37000; AAA48670.1; -; mRNA.
DR EMBL; M18043; AAA76823.1; -; Genomic_DNA.
DR PIR; A28368; TVCHFS.
DR RefSeq; NP_990839.1; NM_205508.1.
DR AlphaFoldDB; P11939; -.
DR SMR; P11939; -.
DR STRING; 9031.ENSGALP00000041340; -.
DR Ensembl; ENSGALT00000043488; ENSGALP00000041340; ENSGALG00000028037.
DR GeneID; 396512; -.
DR KEGG; gga:396512; -.
DR CTD; 2353; -.
DR VEuPathDB; HostDB:geneid_396512; -.
DR GeneTree; ENSGT00940000159276; -.
DR InParanoid; P11939; -.
DR OMA; FTYPEAE; -.
DR OrthoDB; 1221590at2759; -.
DR PhylomeDB; P11939; -.
DR PRO; PR:P11939; -.
DR Proteomes; UP000000539; Chromosome 5.
DR Bgee; ENSGALG00000028037; Expressed in spermatocyte and 13 other tissues.
DR ExpressionAtlas; P11939; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032993; C:protein-DNA complex; IEA:Ensembl.
DR GO; GO:0035976; C:transcription factor AP-1 complex; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0070412; F:R-SMAD binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0001221; F:transcription coregulator binding; IEA:Ensembl.
DR GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
DR GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
DR GO; GO:0031668; P:cellular response to extracellular stimulus; IEA:Ensembl.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; IEA:Ensembl.
DR GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035994; P:response to muscle stretch; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
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 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Endoplasmic reticulum; Nucleus; Phosphoprotein;
KW Proto-oncogene; Reference proteome.
FT CHAIN 1..367
FT /note="Protein c-Fos"
FT /id="PRO_0000076471"
FT DOMAIN 136..199
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..158
FT /note="Basic motif; required for the activation of
FT phospholipid synthesis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 164..192
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 343..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250"
FT MOD_RES 30
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250"
SQ SEQUENCE 367 AA; 39005 MW; CB7F2BF658713599 CRC64;
MMYQGFAGEY EAPSSRCSSA SPAGDSLTYY PSPADSFSSM GSPVNSQDFC TDLAVSSANF
VPTVTAISTS PDLQWLVQPT LISSVAPSQN RGHPYGVPAP APPAAYSRPA VLKAPGGRGQ
SIGRRGKVEQ LSPEEEEKRR IRRERNKMAA AKCRNRRREL TDTLQAETDQ LEEEKSALQA
EIANLLKEKE KLEFILAAHR PACKMPEELR FSEELAAATA LDLGAPSPAA AEEAFALPLM
TEAPPAVPPK EPSGSGLELK AEPFDELLFS AGPREASRSV PDMDLPGASS FYASDWEPLG
AGSGGELEPL CTPVVTCTPC PSTYTSTFVF TYPEADAFPS CAAAHRKGSS SNEPSSDSLS
SPTLLAL
