P53_CHICK
ID P53_CHICK Reviewed; 367 AA.
AC P10360;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Cellular tumor antigen p53;
DE AltName: Full=Tumor suppressor p53;
GN Name=TP53;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SPAFAS;
RX PubMed=3060861; DOI=10.1093/nar/16.23.11383;
RA Soussi T.;
RT "Nucleotide sequence of a cDNA encoding the chicken p53 nuclear
RT oncoprotein.";
RL Nucleic Acids Res. 16:11383-11383(1988).
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 -!- INTERACTION:
CC P10360; Q77Q71: R-LORF7; Xeno; NbExp=3; IntAct=EBI-10766704, EBI-10766689;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the p53 family. {ECO:0000305}.
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DR EMBL; X13057; CAA31456.1; -; mRNA.
DR PIR; S02193; S02193.
DR RefSeq; NP_990595.1; NM_205264.1.
DR AlphaFoldDB; P10360; -.
DR SMR; P10360; -.
DR BioGRID; 676460; 2.
DR IntAct; P10360; 1.
DR GeneID; 396200; -.
DR CTD; 7157; -.
DR VEuPathDB; HostDB:geneid_396200; -.
DR InParanoid; P10360; -.
DR PhylomeDB; P10360; -.
DR PRO; PR:P10360; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
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:0043065; P:positive regulation of apoptotic process; IMP:AgBase.
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 1: Evidence at protein 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..367
FT /note="Cellular tumor antigen p53"
FT /id="PRO_0000185716"
FT DNA_BIND 87..278
FT /evidence="ECO:0000250"
FT REGION 1..30
FT /note="Transcription activation (acidic)"
FT REGION 30..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..266
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 275..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..339
FT /note="Oligomerization"
FT REGION 333..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..364
FT /note="Basic (repression of DNA-binding)"
FT MOTIF 286..302
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 322..333
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 44..80
FT /note="Pro 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 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 228
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"
SQ SEQUENCE 367 AA; 40169 MW; FC37D0FCDF9195B6 CRC64;
MAEEMEPLLE PTEVFMDLWS MLPYSMQQLP LPEDHSNWQE LSPLEPSDPP PPPPPPPLPL
AAAAPPPLNP PTPPRAAPSP VVPSTEDYGG DFDFRVGFVE AGTAKSVTCT YSPVLNKVYC
RLAKPCPVQV RVGVAPPPGS SLRAVAVYKK SEHVAEVVRR CPHHERCGGG TDGLAPAQHL
IRVEGNPQAR YHDDETTKRH SVVVPYEPPE VGSDCTTVLY NFMCNSSCMG GMNRRPILTI
LTLEGPGGQL LGRRCFEVRV CACPGRDRKI EEENFRKRGG AGGVAKRAMS PPTEAPEPPK
KRVLNPDNEI FYLQVRGRRR YEMLKEINEA LQLAEGGSAP RPSKGRRVKV EGPQPSCGKK
LLQKGSD
