FOS_PIG
ID FOS_PIG Reviewed; 380 AA.
AC O97930;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 127.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Pituitary anterior lobe;
RX PubMed=8793856; DOI=10.1016/0303-7207(96)03798-7;
RA Chung H.-O., Kato T., Kato Y.;
RT "Molecular cloning of c-jun and c-fos cDNAs from porcine anterior pituitary
RT and their involvement in gonadotropin-releasing hormone stimulation.";
RL Mol. Cell. Endocrinol. 119:75-82(1996).
RN [2]
RP ERRATUM OF PUBMED:8793856.
RX PubMed=8898353; DOI=10.1016/0303-7207(96)03902-0;
RA Chung H.-O., Kato T., Kato Y.;
RL Mol. Cell. Endocrinol. 122:113-114(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RA Reiner G., Heinricy J., Dzapo V.;
RT "The complete sequence of the porcine c-fos proto-oncogene.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 145-240.
RC STRAIN=Large white;
RA Mimmack M.L.;
RL Submitted (SEP-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 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-362 and Ser-374 by
CC MAPK1/2 and RSK1/2 leads to protein stabilization with phosphorylation
CC on Ser-374 being the major site for protein stabilization on NGF
CC stimulation. Phosphorylation on Ser-362 and Ser-374 primes further
CC phosphorylations on Thr-325 and Thr-331 through promoting docking of
CC MAPK to the DEF domain. Phosphorylation on Thr-232, induced by HA-RAS,
CC activates the transcriptional activity and antagonizes sumoylation.
CC Phosphorylation on Ser-362 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-232 (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; Y14808; CAB39278.1; -; Genomic_DNA.
DR EMBL; AJ132510; CAB40144.1; -; Genomic_DNA.
DR RefSeq; NP_001116585.1; NM_001123113.1.
DR AlphaFoldDB; O97930; -.
DR SMR; O97930; -.
DR STRING; 9823.ENSSSCP00000002583; -.
DR PaxDb; O97930; -.
DR PeptideAtlas; O97930; -.
DR GeneID; 100144486; -.
DR KEGG; ssc:100144486; -.
DR CTD; 2353; -.
DR eggNOG; KOG1414; Eukaryota.
DR HOGENOM; CLU_049742_2_0_1; -.
DR InParanoid; O97930; -.
DR OrthoDB; 1221590at2759; -.
DR TreeFam; TF326301; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; O97930; SS.
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; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IEA:InterPro.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 Cytoplasm; DNA-binding; Endoplasmic reticulum; Isopeptide bond; Nucleus;
KW Phosphoprotein; Proto-oncogene; Reference proteome; Ubl conjugation.
FT CHAIN 1..380
FT /note="Protein c-Fos"
FT /id="PRO_0000076468"
FT DOMAIN 137..200
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 115..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..159
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 165..193
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 354..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..380
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 232
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01101"
FT MOD_RES 325
FT /note="Phosphothreonine; by MAPK1 and MAPK3"
FT /evidence="ECO:0000250|UniProtKB:P01100"
FT MOD_RES 331
FT /note="Phosphothreonine; by MAPK1 and MAPK3"
FT /evidence="ECO:0000250|UniProtKB:P01100"
FT MOD_RES 362
FT /note="Phosphoserine; by MAPK1, MAPK3 and RPS6KA3"
FT /evidence="ECO:0000250|UniProtKB:P01100"
FT MOD_RES 374
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 128
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P01100"
FT CROSSLNK 265
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 265
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P01100"
FT CONFLICT 58
FT /note="V -> A (in Ref. 3; CAB40144)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="I -> T (in Ref. 3; CAB40144)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="A -> V (in Ref. 3; CAB40144)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="K -> N (in Ref. 3; CAB40144)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="A -> T (in Ref. 3; CAB40144)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 40674 MW; 33EEF3C4475599A8 CRC64;
MMFSGFNADY EASSSRCSSA SPAGDSLSYY HSPADSFSSM GSPVNAQDFC TDLAVSSVNF
IPTVTAISIS PDLQWLVQPT LVSSVAPSQT RAPHPYGVPT PSAGAYSRAG AVKTMPGGRA
QSIGRRGKVE QLSPEEEEKR RIRRERNKMA AAKCRNRRRE LTDTLQAETD QLEDEKSALQ
TEIANLLKEK EKLEFILAAH RPACKIPDDL GFPEEMSVAS LDLSGGLPEA ATPESEEAFT
LPLLNDPEPK PSVEPVKKVS SMELKAEPFD DFLFPASSRP GGSETARSVP DMDLSGSFYA
ADWEPLHGGS LGMGPMATEL EPLCTPVVTC TPSCTAYTSS FVFTYPEADS FPSCAAAHRK
GSSSNEPSSD SLSSPTLLAL
