ID A0A1S3FFI4_DIPOR Unreviewed; 393 AA.
AC A0A1S3FFI4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Cellular tumor antigen p53 {ECO:0000256|RuleBase:RU003304};
GN Name=Tp63 {ECO:0000313|RefSeq:XP_012874804.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012874804.1};
RN [1] {ECO:0000313|RefSeq:XP_012874804.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012874804.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 {ECO:0000256|RuleBase:RU003304}.
CC Nucleus {ECO:0000256|RuleBase:RU003304}.
CC -!- SIMILARITY: Belongs to the p53 family. {ECO:0000256|ARBA:ARBA00006167,
CC ECO:0000256|RuleBase:RU003304}.
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DR RefSeq; XP_012874804.1; XM_013019350.1.
DR AlphaFoldDB; A0A1S3FFI4; -.
DR GeneID; 105987920; -.
DR CTD; 8626; -.
DR OrthoDB; 2902631at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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:0051262; P:protein tetramerization; IEA:InterPro.
DR CDD; cd08367; P53; 1.
DR Gene3D; 2.60.40.720; -; 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; IPR036674; p53_tetramer_sf.
DR InterPro; IPR010991; p53_tetrameristn.
DR InterPro; IPR002117; p53_tumour_suppressor.
DR PANTHER; PTHR11447; CELLULAR TUMOR ANTIGEN P53; 1.
DR PANTHER; PTHR11447:SF8; TUMOR PROTEIN 63; 1.
DR Pfam; PF00870; P53; 1.
DR Pfam; PF07710; P53_tetramer; 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 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|RuleBase:RU003304};
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703, ECO:0000256|RuleBase:RU003304};
KW Cell cycle {ECO:0000256|RuleBase:RU003304};
KW Cytoplasm {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}; Nucleus {ECO:0000256|RuleBase:RU003304};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Transcription {ECO:0000256|RuleBase:RU003304};
KW Transcription regulation {ECO:0000256|RuleBase:RU003304};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR602117-1}.
FT DOMAIN 74..263
FT /note="p53 DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF00870"
FT DOMAIN 297..337
FT /note="p53 tetramerisation"
FT /evidence="ECO:0000259|Pfam:PF07710"
FT REGION 29..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
SQ SEQUENCE 393 AA; 44655 MW; A102AB8635125C2E CRC64;
MHFLKNNSKT QLSFPQYTNL GLLNSMDQQI QNGSSSTSPY NTDHAQNSVT APSPYAQPSS
TFDALSPSPA IPSNTDYPGP HSFDVSFQQS STAKSATWTY STELKKLYCQ IAKTCPIQIK
VMTPPPQGAV IRAMPVYKKA EHVTEVVKRC PNHELSREFN EGQMAPPSHL IRVEGNSHAQ
YVEDPITGRQ SVLVPYEPPQ VGTEFTTVLY NFMCNSSCVG GMNRRPILII VTLETRDGQV
LGRRCFEARI CACPGRDRKA DEDSIRKQQV SDSTKNGDGT KRPFRQNTHG IQMTSIKKRR
SPDDELLYLP VRGRETYEML LKIKESLELM QYLPQHTIET YRQQQQQQHQ HLLQKHLLSA
CFRNELVEPR RETPKQSDIF FRHSNPPNQS VYP
//
