ID   E3U906_MACMU            Unreviewed;       393 AA.
AC   E3U906; G7NIG9;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Cellular tumor antigen p53 {ECO:0000256|ARBA:ARBA00017135, ECO:0000256|RuleBase:RU003304};
GN   Name=TP53 {ECO:0000313|EMBL:ADO78765.1};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|EMBL:ADO78765.1};
RN   [1] {ECO:0000313|EMBL:ADO78765.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23516500;
RA   Diehl W.E., Johnson W.E., Hunter E.;
RT   "Elevated Rate of Fixation of Endogenous Retroviral Elements in Haplorhini
RT   TRIM5 and TRIM22 Genomic Sequences: Impact on Transcriptional Regulation.";
RL   PLoS ONE 8:E58532-E58532(2013).
RN   [2] {ECO:0000313|EMBL:AFH28962.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Testis {ECO:0000313|EMBL:AFI34822.1}, and Thymus
RC   {ECO:0000313|EMBL:AFH28962.1};
RX   PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA   Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA   Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA   Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA   Yorke J.A., Norgren R.B.Jr.;
RT   "A new rhesus macaque assembly and annotation for next-generation
RT   sequencing analyses.";
RL   Biol. Direct 9:20-20(2014).
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. {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, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm
CC       {ECO:0000256|RuleBase:RU003304}. Nucleus
CC       {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}.
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DR   EMBL; HM104190; ADO78765.1; -; mRNA.
DR   EMBL; HM104191; ADO78766.1; -; mRNA.
DR   EMBL; JU472158; AFH28962.1; -; mRNA.
DR   EMBL; JU472159; AFH28963.1; -; mRNA.
DR   EMBL; JU472160; AFH28964.1; -; mRNA.
DR   EMBL; JV044751; AFI34822.1; -; mRNA.
DR   RefSeq; NP_001040616.1; NM_001047151.2.
DR   AlphaFoldDB; E3U906; -.
DR   SMR; E3U906; -.
DR   GeneID; 716170; -.
DR   KEGG; mcc:716170; -.
DR   CTD; 7157; -.
DR   HOGENOM; CLU_019621_0_0_1; -.
DR   OrthoDB; 2902631at2759; -.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0045893; P:positive regulation of DNA-templated transcription; IEA:UniProt.
DR   GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   CDD; cd08367; P53; 1.
DR   Gene3D; 2.60.40.720; -; 1.
DR   Gene3D; 6.10.50.20; -; 1.
DR   Gene3D; 4.10.170.10; p53-like tetramerisation domain; 1.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd_sf.
DR   InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd_sf.
DR   InterPro; IPR011615; p53_DNA-bd.
DR   InterPro; IPR040926; p53_TAD2.
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; 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   Pfam; PF07710; P53_tetramer; 1.
DR   Pfam; PF18521; TAD2; 1.
DR   PRINTS; PR00386; P53SUPPRESSR.
DR   SUPFAM; SSF47719; p53 tetramerization domain; 1.
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|RuleBase:RU003304};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602117-1}; Necrosis {ECO:0000256|ARBA:ARBA00022590};
KW   Nucleus {ECO:0000256|RuleBase:RU003304};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Transcription {ECO:0000256|RuleBase:RU003304};
KW   Transcription regulation {ECO:0000256|RuleBase:RU003304};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR602117-1}.
FT   DOMAIN          6..30
FT                   /note="p53 transactivation"
FT                   /evidence="ECO:0000259|Pfam:PF08563"
FT   DOMAIN          35..59
FT                   /note="Cellular tumor antigen p53 transactivation"
FT                   /evidence="ECO:0000259|Pfam:PF18521"
FT   DOMAIN          100..288
FT                   /note="p53 DNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00870"
FT   DOMAIN          319..357
FT                   /note="p53 tetramerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07710"
FT   REGION          48..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..92
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..380
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         176
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT   BINDING         238
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT   BINDING         242
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
SQ   SEQUENCE   393 AA;  43655 MW;  E212E5E4FE650103 CRC64;
     MEEPQSDPSI EPPLSQETFS DLWKLLPENN VLSPLPSQAV DDLMLSPDDL AQWLTEDPGP
     DEAPRMSEAA PPMAPTPAAP TPAAPAPAPS WPLSSSVPSQ KTYHGSYGFR LGFLHSGTAK
     SVTCTYSPDL NKMFCQLAKT CPVQLWVDST PPPGSRVRAM AIYKQSQHMT EVVRRCPHHE
     RCSDSDGLAP PQHLIRVEGN LRVEYSDDRN TFRHSVVVPY EPPEVGSDCT TIHYNYMCNS
     SCMGGMNRRP ILTIITLEDS SGNLLGRNSF EVRVCACPGR DRRTEEENFR KKGEPCHQLP
     PGSTKRALPN NTSSSPQPKK KPLDGEYFTL QIRGRERFEM FRELNEALEL KDAQAGKEPA
     GSRAHSSHLK SKKGQSTSRH KKFMFKTEGP DSD
//