ID Q9EQL0_RAT Unreviewed; 271 AA. AC Q9EQL0; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 04-NOV-2026, entry version 167. DE RecName: Full=Cellular tumor antigen p53 {ECO:0000256|ARBA:ARBA00017135, ECO:0000256|RuleBase:RU003304}; GN Name=Tp53 {ECO:0000313|RGD:3889}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|EMBL:AAG35765.1}; RN [1] {ECO:0000313|EMBL:AAG35765.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Sprague-Dawley {ECO:0000313|EMBL:AAG35765.1}; RA Dell'Acqua G., Mann M.J., Mu H., Griese D.P., Ehsan A., Dzau V.; RT "p35/HAS."; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Multifunctional transcription factor that induces cell cycle CC arrest, DNA repair or apoptosis upon binding to its target DNA CC sequence. Acts as a tumor suppressor in many tumor types; induces CC growth arrest or apoptosis depending on the physiological circumstances CC and cell type. Negatively regulates cell division by controlling CC expression of a set of genes required for this process. One of the CC activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis CC induction seems to be mediated either by stimulation of BAX and FAS CC antigen expression, or by repression of Bcl-2 expression. CC {ECO:0000256|RuleBase:RU003304}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR602117-1, CC ECO:0000256|RuleBase:RU003304}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR602117-1, CC ECO:0000256|RuleBase:RU003304}; CC -!- SUBUNIT: Binds DNA as a homotetramer. {ECO:0000256|RuleBase:RU003304}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU003304}. CC Nucleus {ECO:0000256|RuleBase:RU003304}. Endoplasmic reticulum CC {ECO:0000256|ARBA:ARBA00004240}. Mitochondrion matrix CC {ECO:0000256|ARBA:ARBA00004305}. Nucleus, PML body CC {ECO:0000256|ARBA:ARBA00004322}. CC -!- SIMILARITY: Belongs to the p53 family. {ECO:0000256|ARBA:ARBA00006167, CC ECO:0000256|RuleBase:RU003304}. 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; AF209191; AAG35765.1; -; mRNA. DR AlphaFoldDB; Q9EQL0; -. DR SMR; Q9EQL0; -. DR RGD; 3889; Tp53. DR VEuPathDB; HostDB:ENSRNOG00000010756; -. DR HOGENOM; CLU_976476_0_0_1; -. DR Bgee; ENSRNOG00000010756; Expressed in thymus and 20 other cell types or tissues. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:InterPro. DR GO; GO:0006915; P:apoptotic process; IEA:InterPro. DR CDD; cd08367; P53; 1. DR FunFam; 2.60.40.720:FF:000003; Cellular tumor antigen p53; 1. DR Gene3D; 2.60.40.720; -; 1. DR Gene3D; 6.10.50.20; -; 1. DR InterPro; IPR008967; p53-like_TF_DNA-bd_sf. DR InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd_sf. DR InterPro; IPR057064; P53_central_site. DR InterPro; IPR011615; p53_DNA-bd. DR InterPro; IPR013872; p53_transactivation_domain. DR InterPro; IPR002117; p53_tumour_suppressor. DR PANTHER; PTHR11447; CELLULAR TUMOR ANTIGEN P53; 1. DR PANTHER; PTHR11447:SF6; CELLULAR TUMOR ANTIGEN P53; 1. DR Pfam; PF00870; P53; 1. DR Pfam; PF08563; P53_TAD; 1. DR PRINTS; PR00386; P53SUPPRESSR. DR SUPFAM; SSF49417; p53-like transcription factors; 1. DR PROSITE; PS00348; P53; 1. PE 2: Evidence at transcript level; KW Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|RuleBase:RU003304}; KW Apoptosis {ECO:0000256|ARBA:ARBA00022703, ECO:0000256|RuleBase:RU003304}; KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108}; KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|RuleBase:RU003304}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU003304}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU003304}; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824}; KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR602117-1}; KW Methylation {ECO:0000256|ARBA:ARBA00022481}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128}; KW Necrosis {ECO:0000256|ARBA:ARBA00022590}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU003304}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Repressor {ECO:0000256|ARBA:ARBA00022491}; KW Transcription {ECO:0000256|ARBA:ARBA00023163, KW ECO:0000256|RuleBase:RU003304}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, KW ECO:0000256|RuleBase:RU003304}; KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR602117-1}. FT DOMAIN 6..29 FT /note="p53 transactivation" FT /evidence="ECO:0000259|Pfam:PF08563" FT DOMAIN 98..259 FT /note="p53 DNA-binding" FT /evidence="ECO:0000259|Pfam:PF00870" FT REGION 65..90 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 77..90 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 174 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1" FT BINDING 177 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1" FT BINDING 236 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1" FT BINDING 240 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1" FT SITE 118 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|PIRSR:PIRSR602117-2" SQ SEQUENCE 271 AA; 29713 MW; 1C8687B74B9317D2 CRC64; MEDSQSDMSI ELPLSQETFS CLWKLLPPDD ILPTTATGSP NSMEDLFLPQ DVAELLEGPE EALQVSAPAA QEPGTEAPAP VAPASATPWP LSSSVPSQKT YQGNYGFHLG FLQSGTAKSV MCTYSISLNK LFCQLAKTCP VQLWVTSTPP PGTRVRAMAI YKKSQHMTEV VRRCPHHERC SDGDGLAPPQ HLIRVEGNPY AEYLDDRQTF RHSVVVPYEP PEVGSDYTTI HYKYMCNSSC MGGMNRRPIL TIITLEDSRS VGVSASRCSE S //