P53_ONCMY
ID P53_ONCMY Reviewed; 396 AA.
AC P25035;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Cellular tumor antigen p53;
DE AltName: Full=Tumor suppressor p53;
GN Name=tp53; Synonyms=p53;
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1339362; DOI=10.1016/0378-1119(92)90383-z;
RA de Fromentel C.C., Padkel F., Chapus A., Baney C., May P., Soussi T.;
RT "Rainbow trout p53: cDNA cloning and biochemical characterization.";
RL Gene 112:241-245(1992).
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; M75145; AAA49605.1; -; mRNA.
DR PIR; JH0631; JH0631.
DR RefSeq; NP_001118164.1; NM_001124692.1.
DR AlphaFoldDB; P25035; -.
DR SMR; P25035; -.
DR GeneID; 100136737; -.
DR KEGG; omy:100136737; -.
DR CTD; 7157; -.
DR OrthoDB; 257530at2759; -.
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:0043066; P:negative regulation of apoptotic process; IMP:AgBase.
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..396
FT /note="Cellular tumor antigen p53"
FT /id="PRO_0000185720"
FT DNA_BIND 90..281
FT /evidence="ECO:0000250"
FT REGION 1..44
FT /note="Transcription activation (acidic)"
FT REGION 63..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..269
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 301..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..356
FT /note="Oligomerization"
FT REGION 369..392
FT /note="Basic (repression of DNA-binding)"
FT MOTIF 297..317
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 339..350
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 64..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT SITE 108
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 396 AA; 43966 MW; 8422250765545A1C CRC64;
MADLAENVSL PLSQESFEDL WKMNLNLVAV QPPETESWVG YDNFMMEAPL QVEFDPSLFE
VSATEPAPQP SISTLDTGSP PTSTVPTTSD YPGALGFQLR FLQSSTAKSV TCTYSPDLNK
LFCQLAKTCP VQIVVDHPPP PGAVVRALAI YKKLSDVADV VRRCPHHQST SENNEGPAPR
GHLVRVEGNQ RSEYMEDGNT LRHSVLVPYE PPQVGSECTT VLYNFMCNSS CMGGMNRRPI
LTIITLETQE GQLLGRRSFE VRVCACPGRD RKTEEINLKK QQETTLETKT KPAQGIKRAM
KEASLPAPQP GASKKTKSSP AVSDDEIYTL QIRGKEKYEM LKKFNDSLEL SELVPVADAD
KYRQKCLTKR VAKRDFGVGP KKRKKLLVKE EKSDSD
