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Proto-oncogene c-Fos (Cellular oncogene fos) (Fragment)

 FOS_SHEEP               Reviewed;         195 AA.
O02761; O97787;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
28-MAR-2018, entry version 84.
RecName: Full=Proto-oncogene c-Fos;
AltName: Full=Cellular oncogene fos;
Flags: Fragment;
Name=FOS;
Ovis aries (Sheep).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Ovis.
NCBI_TaxID=9940;
[1]
NUCLEOTIDE SEQUENCE OF 1-96.
Mimmack M.L.;
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE OF 90-195.
Ing N.H., Bhattacharyya S.;
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Nuclear phosphoprotein which forms a tight but non-
covalently linked complex with the JUN/AP-1 transcription factor.
On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS
complex, at the AP1/SMAD-binding site to regulate TGF-beta-
mediated signaling. Has a critical function in regulating the
development of cells destined to form and maintain the skeleton.
It is thought to have an important role in signal transduction,
cell proliferation and differentiation (By similarity). In growing
cells, activates phospholipid synthesis, possibly by activating
CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and
association with the endoplasmic reticulum (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Heterodimer; with JUN (By similarity). Component of the
SMAD3/SMAD4/JUN/FOS complex required for synergistic TGF-beta-
mediated transcription at the AP1 promoter site. Interacts with
SMAD3; the interaction is weak even on TGF-beta activation.
Interacts with DSIPI; this interaction inhibits the binding of
active AP1 to its target DNA. Interacts with MAFB (By similarity).
Interacts with CDS1 and PI4K2A (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00978}. Endoplasmic reticulum {ECO:0000250}. Cytoplasm,
cytosol {ECO:0000250}. Note=In quiescent cells, present in very
small amounts in the cytosol. Following induction of cell growth,
first localizes to the endoplasmic reticulum and only later to the
nucleus. Localization at the endoplasmic reticulum requires Tyr-
dephosphorylation (By similarity). {ECO:0000250}.
-!- INDUCTION: Expression increases upon a variety of stimuli,
including growth factors, cytokines, neurotransmitters,
polypeptide hormones, stress and cell injury.
-!- PTM: Constitutively sumoylated with SUMO1, SUMO2 and SUMO3.
Desumoylated by SENP2. Sumoylation requires heterodimerization
with JUN and is enhanced by mitogen stimulation. Sumoylation
inhibits the AP-1 transcriptional activity and is, itself,
inhibited by Ras-activated phosphorylation on Thr-88 (By
similarity). {ECO:0000250}.
-!- PTM: In quiescent cells, the small amount of FOS present is
phosphorylated by SRC. This Tyr-phosphorylated form is cytosolic.
In growing cells, dephosphorylated by PTPN2. Dephosphorylation
leads to the association with endoplasmic reticulum membranes and
activation of phospholipid synthesis (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the bZIP family. Fos subfamily.
{ECO:0000305}.
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EMBL; Y15747; CAA75757.1; -; Genomic_DNA.
EMBL; U94719; AAB57839.1; -; mRNA.
UniGene; Oar.1016; -.
ProteinModelPortal; O02761; -.
SMR; O02761; -.
HOVERGEN; HBG005743; -.
Proteomes; UP000002356; Unplaced.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005667; C:transcription factor complex; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:DNA binding transcription factor activity; IEA:InterPro.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
InterPro; IPR000837; AP-1.
InterPro; IPR004827; bZIP.
InterPro; IPR029816; c-Fos/v-Fos.
PANTHER; PTHR23351; PTHR23351; 1.
PANTHER; PTHR23351:SF4; PTHR23351:SF4; 1.
Pfam; PF00170; bZIP_1; 1.
PRINTS; PR00042; LEUZIPPRFOS.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
2: Evidence at transcript level;
Complete proteome; Cytoplasm; DNA-binding; Endoplasmic reticulum;
Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene;
Reference proteome; Ubl conjugation.
CHAIN <1 >195 Proto-oncogene c-Fos.
/FTId=PRO_0000076470.
DOMAIN 1 56 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION <1 15 Basic motif; required for the activation
of phospholipid synthesis, but not for
CDS1-binding. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 21 49 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOD_RES 88 88 Phosphothreonine.
{ECO:0000250|UniProtKB:P01101}.
MOD_RES 181 181 Phosphothreonine; by MAPK1 and MAPK3.
{ECO:0000250|UniProtKB:P01100}.
MOD_RES 187 187 Phosphothreonine; by MAPK1 and MAPK3.
{ECO:0000250|UniProtKB:P01100}.
CROSSLNK 121 121 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 121 121 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P01100}.
NON_TER 1 1
NON_TER 195 195
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


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