ID   P53_ORYLA               Reviewed;         352 AA.
AC   P79820; Q9PSU7; Q9PSU8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Cellular tumor antigen p53;
DE   AltName: Full=Tumor suppressor p53;
GN   Name=tp53; Synonyms=p53;
OS   Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=8090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=9161419; DOI=10.1016/s0378-1119(96)00841-4;
RA   Krause M.K., Rhodes L.D., van Beneden R.J.;
RT   "Cloning of the p53 tumor suppressor gene from the Japanese medaka (Oryzias
RT   latipes) and evaluation of mutational hotspots in MNNG-exposed fish.";
RL   Gene 189:101-106(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-91.
RC   STRAIN=Himedaka;
RA   Atkinson D.N., Gumerlock P.H., Wong J.T.Y., Hsieh D.P.H.;
RT   "Isolation of cDNAs encoding the p53 tumor suppressor gene in the Japanese
RT   Medaka (Oryzias latipes).";
RL   Submitted (MAY-1997) 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}.
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DR   EMBL; U57306; AAC60146.1; -; mRNA.
DR   EMBL; AF003949; AAD01195.1; -; mRNA.
DR   EMBL; AF003950; AAD01196.1; -; mRNA.
DR   RefSeq; NP_001098212.1; NM_001104742.1.
DR   RefSeq; XP_011485767.1; XM_011487465.1.
DR   AlphaFoldDB; P79820; -.
DR   SMR; P79820; -.
DR   STRING; 8090.ENSORLP00000008029; -.
DR   PRIDE; P79820; -.
DR   Ensembl; ENSORLT00000008032; ENSORLP00000008031; ENSORLG00000006390.
DR   Ensembl; ENSORLT00020015819; ENSORLP00020009441; ENSORLG00020010355.
DR   GeneID; 100049321; -.
DR   KEGG; ola:100049321; -.
DR   CTD; 7157; -.
DR   eggNOG; ENOG502QVY3; Eukaryota.
DR   GeneTree; ENSGT00950000183153; -.
DR   InParanoid; P79820; -.
DR   OrthoDB; 257530at2759; -.
DR   Proteomes; UP000001038; Chromosome 18.
DR   Proteomes; UP000265180; Chromosome 18.
DR   Proteomes; UP000265200; Unplaced.
DR   Bgee; ENSORLG00000006390; Expressed in animal zygote and 14 other tissues.
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:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
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   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; Reference proteome; Transcription;
KW   Transcription regulation; Tumor suppressor; Zinc.
FT   CHAIN           1..352
FT                   /note="Cellular tumor antigen p53"
FT                   /id="PRO_0000185721"
FT   DNA_BIND        87..273
FT                   /evidence="ECO:0000250"
FT   REGION          1..48
FT                   /note="Transcription activation (acidic)"
FT   REGION          254..261
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          262..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          302..331
FT                   /note="Oligomerization"
FT   REGION          330..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..350
FT                   /note="Basic (repression of DNA-binding)"
FT   MOTIF           276..291
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   MOTIF           316..327
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        338..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         161
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   SITE            105
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         351
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   VARIANT         91
FT                   /note="S -> T"
FT                   /evidence="ECO:0000269|Ref.2"
FT   CONFLICT        22
FT                   /note="Missing (in Ref. 1; AAC60146)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   352 AA;  39753 MW;  196868A66351BFF5 CRC64;
     MDPVPDLPES QGSFQELWET VSYPPLETLS LPTVNEPTGS WVATGDMFLL DQDLSGTFDD
     KIFDIPIEPV PTNEVNPPPT TVPVTTDYPG SYELELRFQK SGTAKSVTST YSETLNKLYC
     QLAKTSPIEV RVSKEPPKGA ILRATAVYKK TEHVADVVRR CPHHQNEDSV EHRSHLIRVE
     GSQLAQYFED PYTKRQSVTV PYEPPQPGSE MTTILLSYMC NSSCMGGMNR RPILTILTLE
     TEGLVLGRRC FEVRICACPG RDRKTEEESR QKTQPKKRKV TPNTSSSKRK KSHSSGEEED
     NREVFHFEVY GRERYEFLKK INDGLELLEK ESKSKNKDSG MVPSSGKKLK SN