FOS_SHEEP
ID FOS_SHEEP Reviewed; 195 AA.
AC O02761; O97787;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 93.
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};
DE Flags: Fragment;
GN Name=FOS;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE OF 1-96.
RA Mimmack M.L.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE OF 90-195.
RA Ing N.H., Bhattacharyya S.;
RL Submitted (MAR-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. On TGF-beta
CC activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex, at the
CC AP1/SMAD-binding site to regulate TGF-beta-mediated signaling. 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). In growing cells, activates phospholipid synthesis,
CC possibly by activating CDS1 and PI4K2A. This activity requires Tyr-
CC dephosphorylation and association with the endoplasmic reticulum (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer; with JUN (By similarity). Component of the
CC SMAD3/SMAD4/JUN/FOS complex required for synergistic TGF-beta-mediated
CC transcription at the AP1-binding site (By similarity). Interacts with
CC SMAD3; the interaction is weak even on TGF-beta activation (By
CC similarity). Interacts with MAFB (By similarity). Interacts with DSIPI;
CC this interaction inhibits the binding of active AP1 to its target DNA
CC (By similarity). Interacts with CDS1 and PI4K2A (By similarity).
CC Interacts (via bZIP domain and leucine-zipper region) with the
CC multiprotein chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF)
CC subunits SMARCB1, SMARCC2 and SMARCD1 (By similarity). Interacts (via
CC bZIP domain and leucine-zipper region) with ARID1A (By similarity).
CC {ECO:0000250|UniProtKB:P01100, ECO:0000250|UniProtKB:P01101,
CC ECO:0000250|UniProtKB:P12841}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC Endoplasmic reticulum {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.
CC Note=In quiescent cells, present in very small amounts in the cytosol.
CC Following induction of cell growth, first localizes to the endoplasmic
CC reticulum and only later to the nucleus. Localization at the
CC endoplasmic reticulum requires Tyr-dephosphorylation (By similarity).
CC {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: Constitutively sumoylated with SUMO1, SUMO2 and SUMO3.
CC Desumoylated by SENP2. Sumoylation requires heterodimerization with JUN
CC and is enhanced by mitogen stimulation. Sumoylation inhibits the AP-1
CC transcriptional activity and is, itself, inhibited by Ras-activated
CC phosphorylation on Thr-88 (By similarity). {ECO:0000250}.
CC -!- PTM: In quiescent cells, the small amount of FOS present is
CC phosphorylated by SRC. This Tyr-phosphorylated form is cytosolic. In
CC growing cells, dephosphorylated by PTPN2. Dephosphorylation leads to
CC the association with endoplasmic reticulum membranes and activation of
CC phospholipid synthesis (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. {ECO:0000305}.
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DR EMBL; Y15747; CAA75757.1; -; Genomic_DNA.
DR EMBL; U94719; AAB57839.1; -; mRNA.
DR AlphaFoldDB; O02761; -.
DR SMR; O02761; -.
DR STRING; 9940.ENSOARP00000001873; -.
DR eggNOG; KOG1414; Eukaryota.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
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.
PE 2: Evidence at transcript level;
KW Cytoplasm; DNA-binding; Endoplasmic reticulum; Isopeptide bond; Nucleus;
KW Phosphoprotein; Proto-oncogene; Reference proteome; Ubl conjugation.
FT CHAIN <1..>195
FT /note="Protein c-Fos"
FT /id="PRO_0000076470"
FT DOMAIN 1..56
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION <1..15
FT /note="Basic motif; required for the activation of
FT phospholipid synthesis, but not for CDS1-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 21..49
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 80..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 88
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01101"
FT MOD_RES 181
FT /note="Phosphothreonine; by MAPK1 and MAPK3"
FT /evidence="ECO:0000250|UniProtKB:P01100"
FT MOD_RES 187
FT /note="Phosphothreonine; by MAPK1 and MAPK3"
FT /evidence="ECO:0000250|UniProtKB:P01100"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P01100"
FT NON_TER 1
FT NON_TER 195
SQ SEQUENCE 195 AA; 21255 MW; 7ED1084BA002848B CRC64;
ERNKMAAAKC RNRRRELTDT LQAETDQLED EKSALQTEIA NLLKEKEKLE FILAAHRPAC
KIPDDLGFPE EMSVASLDLS GGLPEAATPE SEEAFTLPLL NDPEPKPSLE PVKSISNVEL
KAEPFDDFLF PASSRPSGSE TSRSVPDVDL SGSFYAADWE PLHSNSLGMG PMVTELEPLC
TPVVTCTPGC TTYTS
