P53_PLAFE
ID P53_PLAFE Reviewed; 366 AA.
AC O12946;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cellular tumor antigen p53;
DE AltName: Full=Tumor suppressor p53;
GN Name=tp53; Synonyms=p53;
OS Platichthys flesus (European flounder) (Pleuronectes flesus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Pleuronectidae;
OC Platichthys.
OX NCBI_TaxID=8260;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9972298; DOI=10.1016/s0305-0491(98)10133-5;
RA Cachot J., Galgani F., Vincent F.;
RT "cDNA cloning and expression analysis of flounder p53 tumour suppressor
RT gene.";
RL Comp. Biochem. Physiol. 121B:235-242(1998).
CC -!- FUNCTION: Acts as a tumor suppressor in many tumor types; induces
CC growth arrest or apoptosis depending on the physiological circumstances
CC and cell type. Involved in cell cycle regulation as a trans-activator
CC that acts to negatively regulate cell division by controlling a set of
CC genes required for this process. One of the activated genes is an
CC inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be
CC mediated either by stimulation of BAX and FAS antigen expression, or by
CC repression of Bcl-2 expression (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Binds DNA as a homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the p53 family. {ECO:0000305}.
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DR EMBL; Y08919; CAA70123.1; -; mRNA.
DR AlphaFoldDB; O12946; -.
DR SMR; O12946; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR CDD; cd08367; P53; 1.
DR Gene3D; 2.60.40.720; -; 1.
DR Gene3D; 4.10.170.10; -; 1.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd_sf.
DR InterPro; IPR011615; p53_DNA-bd.
DR InterPro; IPR036674; p53_tetramer_sf.
DR InterPro; IPR010991; p53_tetrameristn.
DR InterPro; IPR002117; p53_tumour_suppressor.
DR PANTHER; PTHR11447; PTHR11447; 1.
DR Pfam; PF00870; P53; 1.
DR Pfam; PF07710; P53_tetramer; 1.
DR PRINTS; PR00386; P53SUPPRESSR.
DR SUPFAM; SSF47719; SSF47719; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR PROSITE; PS00348; P53; 1.
PE 2: Evidence at transcript level;
KW Activator; Apoptosis; Cell cycle; Cytoplasm; DNA-binding; Metal-binding;
KW Nucleus; Phosphoprotein; Transcription; Transcription regulation;
KW Tumor suppressor; Zinc.
FT CHAIN 1..366
FT /note="Cellular tumor antigen p53"
FT /id="PRO_0000185722"
FT DNA_BIND 80..267
FT /evidence="ECO:0000250"
FT REGION 1..41
FT /note="Transcription activation (acidic)"
FT REGION 248..255
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 255..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..336
FT /note="Oligomerization"
FT REGION 332..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..362
FT /note="Basic (repression of DNA-binding)"
FT MOTIF 275..295
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 319..330
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 266..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT SITE 98
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 366 AA; 40619 MW; 40DE4CA20B22BB88 CRC64;
MMDEQGLDGM QILPGSQDSF SELWASVQTP SIATIAEEFD DHLGNLLQNG FDMNLFELPP
EMVAKDSVTP PSSTVPVVTD YPGEYGFQLR FQKSGTAKSV TSTFSELLKK LYCQLAKTSP
VEVLLSKEPP QGAVLRATAV YKKTEHVADV VRRCPHHQTE DTAEHRSHLI RLEGSQRALY
FEDPHTKRQS VTVPYEPPQL GSETTAILLS FMCNSSCMGG MNRRQILTIL TLETPDGLVL
GRRCFEVRVC ACPGRDRKTD EESSTKTPNG PKQTKKRKQA PSNSAPHTTT VMKSKSSSSA
EEEDKEVFTV LVKGRERYEI IKKINEAFEG AAEKEKAKNK VAVKQELPVP SSGKRLVQRG
ERSDSD
