P53_ICTPU
ID P53_ICTPU Reviewed; 376 AA.
AC O93379;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Cellular tumor antigen p53;
DE AltName: Full=Tumor suppressor p53;
GN Name=tp53; Synonyms=p53;
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9854815; DOI=10.1016/s0305-0491(98)10062-7;
RA Luft J.C., Bengten E., Clem L.W., Miller N.W., Wilson M.R.;
RT "Identification and characterization of the tumor suppressor p53 in channel
RT catfish (Ictalurus punctatus).";
RL Comp. Biochem. Physiol. 120B:675-682(1998).
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; AF074967; AAC26824.1; -; mRNA.
DR RefSeq; NP_001187005.1; NM_001200076.1.
DR AlphaFoldDB; O93379; -.
DR SMR; O93379; -.
DR STRING; 7998.ENSIPUP00000031919; -.
DR GeneID; 100304476; -.
DR KEGG; ipu:100304476; -.
DR CTD; 7157; -.
DR OrthoDB; 257530at2759; -.
DR Proteomes; UP000221080; Chromosome 28.
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..376
FT /note="Cellular tumor antigen p53"
FT /id="PRO_0000185719"
FT DNA_BIND 77..268
FT /evidence="ECO:0000250"
FT REGION 1..36
FT /note="Transcription activation (acidic)"
FT REGION 150..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..256
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 257..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..334
FT /note="Oligomerization"
FT REGION 342..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..372
FT /note="Basic (repression of DNA-binding)"
FT MOTIF 280..297
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 317..328
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT SITE 95
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 376 AA; 41989 MW; 1B89CD98DB3289F2 CRC64;
MEGNGERDTM MVEPPDSQEF AELWLRNLIV RDNSLWGKEE EIPDDLQEVP CDVLLSDMLQ
PQSSSSPPTS TVPVTSDYPG LLNFTLHFQE SSGTKSVTCT YSPDLNKLFC QLAKTCPVLM
AVSSSPPPGS VLRATAVYKR SEHVAEVVRR CPHHERSNDS SDGPAPPGHL LRVEGNSRAV
YQEDGNTQAH SVVVPYEPPQ VGSQSTTVLY NYMCNSSCMG GMNRRPILTI ITLETQDGHL
LGRRTFEVRV CACPGRDRKT EESNFKKQQE PKTSGKTLTK RSMKDPPSHP EASKKSKNSS
SDDEIYTLQV RGKERYEFLK KINDGLELSD VVPPADQEKY RQKLLSKTCR KERDGAAGEP
KRGKKRLVKE EKCDSD
