ID A0A2K6KGG2_RHIBE Unreviewed; 561 AA.
AC A0A2K6KGG2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Tumor protein 63 (p63) {ECO:0000256|RuleBase:RU003304};
GN Name=TP63 {ECO:0000313|Ensembl:ENSRBIP00000010363.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000010363.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000010363.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000010363.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Acts as a sequence specific DNA binding transcriptional
CC activator or repressor. The isoforms contain a varying set of
CC transactivation and auto-regulating transactivation inhibiting domains
CC thus showing an isoform specific activity. May be required in
CC conjunction with TP73/p73 for initiation of p53/TP53 dependent
CC apoptosis in response to genotoxic insults and the presence of
CC activated oncogenes. {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. Isoform composition of the
CC tetramer may determine transactivation activity.
CC {ECO:0000256|RuleBase:RU003304}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC 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 AlphaFoldDB; A0A2K6KGG2; -.
DR Ensembl; ENSRBIT00000033991.1; ENSRBIP00000010363.1; ENSRBIG00000028344.1.
DR GeneTree; ENSGT00950000183153; -.
DR Proteomes; UP000233180; Unplaced.
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:0045893; P:positive regulation of DNA-templated transcription; IEA:UniProt.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR CDD; cd08367; P53; 1.
DR CDD; cd09572; SAM_tumor-p63; 1.
DR Gene3D; 2.60.40.720; -; 2.
DR Gene3D; 4.10.170.10; p53-like tetramerisation domain; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 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 InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR037611; Tumor-p63_SAM.
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 Pfam; PF07647; SAM_2; 1.
DR PRINTS; PR00386; P53SUPPRESSR.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47719; p53 tetramerization domain; 1.
DR SUPFAM; SSF49417; p53-like transcription factors; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 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 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:UP000233180};
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 422..488
FT /note="SAM"
FT /evidence="ECO:0000259|SMART:SM00454"
FT REGION 28..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
SQ SEQUENCE 561 AA; 62935 MW; D8271461B12745DC CRC64;
MLGQRLYLSD SNTPQYTNLG LLNSMDQQIQ NGSSSTSPYN TDHAQNSVTA PSPYAQPSST
FDALSPSPAI PSNTDYPGPH SFDVSFQQSS TAKSATWTYS TELKKLYCQI AKTCPIQIKV
MTPPPQGAVI RAMPVYKKAE HVTEVVKRCP NHELSREFNE GQHSVGVLLF SPCFQVGTEF
TTVLYNFMCN SSCVGGMNRR PILIIVTLET RDGQVLGRRC FEARICACPG RDRKADEDSI
RKQQVSDSTK NGDGTKRPFR QNTHGIQMTS IKKRRSPDDE LLYLPVRGRE TYEMLLKIKE
SLELMQYLPQ HTIETYRQQQ QQQHQHLLQK QTSIQSQSSY GNSSPPLNKM NSMNKLPSVS
QLINPQQRNA LTPTTIPDGM GANIPMMGTH MPMAGDMNGL SPTQALPPPL SMPSTSHCTP
PPPYPTDCSI VSFLARLGCS SCLDYFTTQG LTTIYQIEHY SMDDLASLKI PEQFRHAIWK
GILDHRQLHE FSSPSHLLRT PSSASTVSVG SSETRGERVI DAVRFTLRQT ISFPPRDEWN
DFNFDMDARR NKQQRIKEEG E
//
