P53_BARBU
ID P53_BARBU Reviewed; 369 AA.
AC Q9W678;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cellular tumor antigen p53;
DE AltName: Full=Tumor suppressor p53;
GN Name=tp53; Synonyms=p53;
OS Barbus barbus (Barbel) (Cyprinus barbus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Barbinae; Barbus.
OX NCBI_TaxID=40830;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bhaskaran A., May D., Rand-Weaver M., Tyler C.R.;
RT "Evolutionary conservancy of p53 gene sequences in fish.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the p53 family. {ECO:0000305}.
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DR EMBL; AF071570; AAD34212.1; -; mRNA.
DR AlphaFoldDB; Q9W678; -.
DR SMR; Q9W678; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:InterPro.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
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:0060429; P:epithelium development; IEA:UniProt.
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 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 2: Evidence at transcript level;
KW Activator; Apoptosis; Cell cycle; Cytoplasm; DNA-binding; Metal-binding;
KW Nucleus; Phosphoprotein; Transcription; Transcription regulation;
KW Tumor suppressor; Zinc.
FT CHAIN 1..369
FT /note="Cellular tumor antigen p53"
FT /id="PRO_0000185717"
FT DNA_BIND 66..256
FT /evidence="ECO:0000250"
FT REGION 1..28
FT /note="Transcription activation (acidic)"
FT REGION 237..244
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 246..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..329
FT /note="Oligomerization"
FT REGION 318..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..365
FT /note="Basic (repression of DNA-binding)"
FT MOTIF 270..289
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 312..323
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 246..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT SITE 84
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 369 AA; 41234 MW; 0BE2CF2CEA74C304 CRC64;
MAESQEFAEL WERNLISTQE AGTCWELIND EYLPSSFDPN IFDNVLTEQP QPSTSPPTAS
VPVATDYPGE HGFKLGFPQS GTAKSVTCTY SSDLNKLFCQ LAKTCPVQMV VNVAPPQGSV
IRATAIYKKS EHVAEVVRRC PHHERTPDGD GLAPAAHLIR VEGNSRALYR EDDVNSRHSV
VVPYEVPQLG SEFTTVLYNF MCNSSCMGGM NRRPILTIIS LETHDGQLLG RRSFEVRVCA
CPGRDRKTEE SNFRKDQETK TLDKIPSANK RSLTKDSTSS VPRPEGSKKA KLSGSSDEEI
YTLQVRGKER YEMLKKINDS LELSDVVPPS EMDRYRQKLL TKGKKKDGQT PEPKRGKKLM
VKDEKSDSD
