P53_XIPHE
ID P53_XIPHE Reviewed; 342 AA.
AC O57538;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Cellular tumor antigen p53;
DE AltName: Full=Tumor suppressor p53;
GN Name=tp53; Synonyms=p53;
OS Xiphophorus helleri (Green swordtail).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8084;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Rio Sarabia;
RX PubMed=9661661; DOI=10.1016/s0378-1119(98)00144-9;
RA Kazianis S., Gan L., Della Coletta L., Santi B., Morizot D.C., Nairn R.S.;
RT "Cloning and comparative sequence analysis of TP53 in xiphophorus fish
RT hybrid melanoma models.";
RL Gene 212:31-38(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; AF043946; AAC31133.1; -; mRNA.
DR AlphaFoldDB; O57538; -.
DR SMR; O57538; -.
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: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: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; IPR013872; p53_transactivation_domain.
DR InterPro; IPR002117; p53_tumour_suppressor.
DR PANTHER; PTHR11447; PTHR11447; 1.
DR Pfam; PF00870; P53; 1.
DR Pfam; PF08563; P53_TAD; 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..342
FT /note="Cellular tumor antigen p53"
FT /id="PRO_0000185725"
FT DNA_BIND 68..255
FT /evidence="ECO:0000250"
FT REGION 1..35
FT /note="Transcription activation (acidic)"
FT REGION 236..243
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 244..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..317
FT /note="Oligomerization"
FT REGION 318..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..336
FT /note="Basic (repression of DNA-binding)"
FT MOTIF 261..278
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 302..313
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 244..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT SITE 86
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 342 AA; 37948 MW; 87E4AE8CFAEE333D CRC64;
MEEADLTLPL SQDTFHDLWN NVFLSTENES LAPPEGLLSQ NMDFWEDPET MQETKNVPTA
PTVPAISNYA GEHGFNLEFN DSGTAKSVTS TYSVKLGKLF CQLAKTTPIG VLVKEEPPQG
AVIRATSVYK KTEHVGEVVK RCPHHQSEDL SDNKSHLIRV EGSQLAQYFE DPNTRRHSVT
VPYERPQLGS EMTTILLSFM CNSSCMGGMN RRPILTILTL ETTEGEVLGR RCFEVRVCAC
PGRDRKTEEG NLEKSGTKQT KKRKSAPAPD TSTAKKSKSA SSGEDEDKEI YTLSIRGRNR
YLWFKSLNDG LELMDKTGPK IKQEIPAPSS GKRLLKGGSD SD
