FOS_FELCA
ID FOS_FELCA Reviewed; 381 AA.
AC Q8HZP6; Q2PZG4;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
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 Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12654520; DOI=10.1016/s0169-328x(03)00031-7;
RA Van der Gucht E., Massie A., De Klerck B., Peeters K., Winters K.,
RA Gerets H.H., Clerens S., Vandesande F., Arckens L.;
RT "Molecular cloning and differential expression of the cat immediate early
RT gene c-fos.";
RL Brain Res. Mol. Brain Res. 111:198-210(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Visual cortex;
RA Weiler E.;
RT "Determination of evolutionary relationships of mammalia using cFOS.";
RL Submitted (NOV-2005) 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 dephosphorylation at Tyr-10 and Tyr-30
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated in the C-terminal upon stimulation by nerve growth
CC factor (NGF) and epidermal growth factor (EGF). Phosphorylated, in
CC vitro, by MAPK and RSK1. Phosphorylation on both Ser-363 and Ser-375 by
CC MAPK1/2 and RSK1/2 leads to protein stabilization with phosphorylation
CC on Ser-375 being the major site for protein stabilization on NGF
CC stimulation. Phosphorylation on Ser-363 and Ser-375 primes further
CC phosphorylations on Thr-326 and Thr-332 through promoting docking of
CC MAPK to the DEF domain. Phosphorylation on Thr-233, induced by HA-RAS,
CC activates the transcriptional activity and antagonizes sumoylation.
CC Phosphorylation on Ser-363 by RSK2 in osteoblasts contributes to
CC osteoblast transformation (By similarity). {ECO:0000250}.
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-233 (By similarity). {ECO:0000250}.
CC -!- PTM: In quiescent cells, the small amount of FOS present is
CC phosphorylated at Tyr-10 and Tyr-30 by SRC. This Tyr-phosphorylated
CC form is cytosolic. In growing cells, dephosphorylated by PTPN2.
CC Dephosphorylation leads to the association with endoplasmic reticulum
CC membranes and activation of phospholipid synthesis (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. {ECO:0000305}.
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DR EMBL; AF540379; AAN16394.1; -; mRNA.
DR EMBL; DQ288168; ABC00779.1; -; Genomic_DNA.
DR RefSeq; NP_001009341.1; NM_001009341.1.
DR AlphaFoldDB; Q8HZP6; -.
DR SMR; Q8HZP6; -.
DR STRING; 9685.ENSFCAP00000021643; -.
DR Ensembl; ENSFCAT00000056629; ENSFCAP00000046194; ENSFCAG00000025370.
DR GeneID; 493935; -.
DR KEGG; fca:493935; -.
DR CTD; 2353; -.
DR VGNC; VGNC:62329; FOS.
DR eggNOG; KOG1414; Eukaryota.
DR GeneTree; ENSGT00940000159276; -.
DR HOGENOM; CLU_049742_2_0_1; -.
DR InParanoid; Q8HZP6; -.
DR OMA; FTYPEAE; -.
DR OrthoDB; 1221590at2759; -.
DR Proteomes; UP000011712; Chromosome B3.
DR Bgee; ENSFCAG00000025370; Expressed in zone of skin and 11 other tissues.
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 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..381
FT /note="Protein c-Fos"
FT /id="PRO_0000076464"
FT DOMAIN 138..201
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 120..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..160
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 166..194
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 355..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P01100"
FT MOD_RES 30
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P01100"
FT MOD_RES 233
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01101"
FT MOD_RES 326
FT /note="Phosphothreonine; by MAPK1 and MAPK3"
FT /evidence="ECO:0000250|UniProtKB:P01100"
FT MOD_RES 332
FT /note="Phosphothreonine; by MAPK1 and MAPK3"
FT /evidence="ECO:0000250|UniProtKB:P01100"
FT MOD_RES 363
FT /note="Phosphoserine; by MAPK1, MAPK3 and RPS6KA3"
FT /evidence="ECO:0000250|UniProtKB:P01100"
FT MOD_RES 375
FT /note="Phosphoserine; by MAPK1 and MAPK3"
FT /evidence="ECO:0000250|UniProtKB:P01100"
FT CROSSLNK 113
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P01100"
FT CROSSLNK 129
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P01100"
FT CROSSLNK 266
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 266
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P01100"
SQ SEQUENCE 381 AA; 40721 MW; 33BBB87633489B8A CRC64;
MMFSGFNADY EASSSRCSSA SPAGDNLSYY HSPADSFSSM GSPVNAQDFC TDLAVSSANF
IPTVTAISTS PDLQWLVQPT LVSSVAPSQT RAPHPYGVPA PSAGAYSRAG VVKTVTAGGR
AQSIGRRGKV EQLSPEEEEK RRIRRERNKM AAAKCRNRRR ELTDTLQAET DQLEDEKSAL
QTEIANLLKE KEKLEFILAA HRPACKIPDD LGFPEEMSVA SLDLSGGLPE AATPESEEAF
TLPLLNDPEP KPSVEPVKSI SSMELKAEPF DDFLFPASSR PSGSETARSV PDMDLSGSFY
AADWEPLHGG SLGMGPMATE LEPLCTPVVT CTPSCTTYTS SFVFTYPEAD SFPSCGAAHR
KGSSSNEPSS DSLSSPTLLA L
