ID   FOSX_MSVFR              Reviewed;         244 AA.
AC   P29176;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Transforming protein v-Fos/v-Fox;
GN   Name=FOS-FOX;
OS   FBR murine osteosarcoma virus (FBR-MSV) (Finkel-Biskis-Reilly murine
OS   osteosarcoma virus).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX   NCBI_TaxID=353765;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6203215; DOI=10.1016/0042-6822(84)90133-8;
RA   van Beveren C., Enami S., Curran T., Verma I.M.;
RT   "FBR murine osteosarcoma virus. II. Nucleotide sequence of the provirus
RT   reveals that the genome contains sequences acquired from two cellular
RT   genes.";
RL   Virology 135:229-243(1984).
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000305}.
CC   -!- MISCELLANEOUS: This protein is synthesized as a Gag-Fos-Fox
CC       polyprotein.
CC   -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA46573.1; Type=Erroneous initiation; Evidence={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; K02712; AAA46573.1; ALT_INIT; Genomic_DNA.
DR   PIR; B23244; TVMVFB.
DR   SMR; P29176; -.
DR   Proteomes; UP000237129; Chromosome.
DR   GO; GO:0042025; C:host cell 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.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Host nucleus; Oncogene.
FT   CHAIN           1..244
FT                   /note="Transforming protein v-Fos/v-Fox"
FT                   /id="PRO_0000076461"
FT   DOMAIN          113..176
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..236
FT                   /note="Transforming protein v-Fos"
FT   REGION          115..135
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          141..169
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          237..244
FT                   /note="Transforming protein v-Fox"
SQ   SEQUENCE   244 AA;  26622 MW;  95C904B66B0EB270 CRC64;
     DSLSYYHSPA DSFSSMGSPV NTQDFCADLS VSSANFIPTE TAISTSPDLQ WLVQPTLVSS
     VAPSQTRAPH PYGLPTQSAG AYARAGMVKT VSGGRAQSIG RRGKVEQLSP EEEVKRRIRR
     ERNKMAAAKC RNRRRELTDT LQAETDQLED EKSALQTEIA NLLKEKEKLE FILAAHRPAC
     KIPDDLGFPE EMSVASLDLT GGLLPLLNDP EPKPSLEPVK SSFDDFLFPA SSGHSGFISM
     AGWQ