P53_TETMU
ID P53_TETMU Reviewed; 367 AA.
AC Q9W679;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Cellular tumor antigen p53;
DE AltName: Full=Tumor suppressor p53;
GN Name=tp53; Synonyms=p53;
OS Tetraodon miurus (Congo puffer).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=94908;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RA Bhaskaran A., May D., Rand-Weaver M., Tyler C.R.;
RT "Evolutionary conservancy of p53 gene sequences in fish.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
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}.
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; AF071571; AAD34213.1; -; mRNA.
DR AlphaFoldDB; Q9W679; -.
DR SMR; Q9W679; -.
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; IPR013872; p53_transactivation_domain.
DR InterPro; IPR002117; p53_tumour_suppressor.
DR PANTHER; PTHR11447; PTHR11447; 1.
DR Pfam; PF00870; P53; 1.
DR Pfam; PF08563; P53_TAD; 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..367
FT /note="Cellular tumor antigen p53"
FT /id="PRO_0000185723"
FT DNA_BIND 86..273
FT /evidence="ECO:0000250"
FT REGION 1..47
FT /note="Transcription activation (acidic)"
FT REGION 254..261
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 262..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..337
FT /note="Oligomerization"
FT REGION 332..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..363
FT /note="Basic (repression of DNA-binding)"
FT MOTIF 282..300
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 322..333
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 262..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT SITE 104
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 367 AA; 41267 MW; ACC10EEE2F5F9CFD CRC64;
MEEENISLPL SQDTFQDLWD NVSAPPISTI QTAALENEAW PAERQMNMMC NFMDSTFNEA
LFNLLPEPPS RDGANSSSPT VPVTTDYPGE YGFKLRFQKS GTAKSVTSTY SEILNKLYCQ
LAKTSLVEVL LGKDPPMGAV LRATAIYKKT EHVAEVVRRC PHHQNEDSAE HRSHLIRMEG
SERAQYFEHP HTKRQSVTVP YEPPQLGSEF TTILLSFMCN SSCMGGMNRR PILTILTLET
QEGIVLGRRC FEVRVCACPG RDRKTEETNS TKMQNDAKDA KKRKSVPTPD STTIKKSKTA
SSAEEDNNEV YTLQIRGRKR YEMLKKINDG LDLLENKPKS KATHRPDGPI PPSGKRLLHR
GEKSDSD
