ID A0A2I2UUR1_FELCA Unreviewed; 504 AA.
AC A0A2I2UUR1;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Cellular tumor antigen p53 {ECO:0000256|RuleBase:RU003304};
GN Name=TP63 {ECO:0000313|Ensembl:ENSFCAP00000036259.1,
GN ECO:0000313|VGNC:VGNC:66467};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000036259.1, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000036259.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000036259.1,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000036259.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000036259.1,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000036259.1}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000036259.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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. {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. {ECO:0000256|RuleBase:RU003304}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm
CC {ECO:0000256|RuleBase:RU003304}. Nucleus
CC {ECO:0000256|RuleBase:RU003304}.
CC -!- SIMILARITY: Belongs to the p53 family. {ECO:0000256|ARBA:ARBA00006167,
CC ECO:0000256|RuleBase:RU003304}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AANG04001816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003991847.1; XM_003991798.3.
DR AlphaFoldDB; A0A2I2UUR1; -.
DR Ensembl; ENSFCAT00000041529.3; ENSFCAP00000036259.1; ENSFCAG00000000790.6.
DR GeneID; 101095124; -.
DR CTD; 8626; -.
DR VGNC; VGNC:66467; TP63.
DR GeneTree; ENSGT00950000183153; -.
DR OrthoDB; 2902631at2759; -.
DR Proteomes; UP000011712; Chromosome C2.
DR Bgee; ENSFCAG00000000790; Expressed in zone of skin and 5 other cell types or tissues.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
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; p53-like tetramerisation domain; 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 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 PRINTS; PR00386; P53SUPPRESSR.
DR SUPFAM; SSF47719; p53 tetramerization domain; 1.
DR SUPFAM; SSF49417; p53-like transcription factors; 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 Cell cycle {ECO:0000256|RuleBase:RU003304};
KW Cytoplasm {ECO:0000256|RuleBase:RU003304};
KW DNA-binding {ECO:0000256|RuleBase:RU003304};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602117-1}; Nucleus {ECO:0000256|RuleBase:RU003304};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
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 185..374
FT /note="p53 DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF00870"
FT DOMAIN 408..448
FT /note="p53 tetramerisation"
FT /evidence="ECO:0000259|Pfam:PF07710"
FT REGION 140..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
SQ SEQUENCE 504 AA; 57624 MW; 191982A83497D181 CRC64;
MLYNCSPLVD CQRELEEMNC ETSRCATLQY CPDPYIQRFV ETPAHFSWKE SYYRSTMSQS
TQTSEFLSPE VFQHIWDFLE QPICSVQPID LNFVDEPSEN GARNKIEISM DCIRMQDSDL
SDPMWPQYTN LGLLNSMDQQ IQNGSSSTSP YNTDHAQNSV TAPSPYAQPS STFDALSPSP
AIPSNTDYPG PHSFDVSFQQ SSTAKSATWT YSTELKKLYC QIAKTCPIQI KVMTPPPQGA
VIRAMPVYKK AEHVTEVVKR CPNHELSREF NEGQIAPPSH LIRVEGNSHA QYVEDPITGR
QSVLVPYEPP QVGTEFTTVL YNFMCNSSCV GGMNRRPILI IVTLETRDGQ VLGRRCFEAR
ICACPGRDRK ADEDSIRKQQ VSDSAKNGDG TKRPFRQNTH GIQMTSIKKR RSPDDELLYL
PVRGRETYEM LLKIKESLEL MQYLPQHTIE TYRQQQQQQH QHLLQKHLLS ACFRNELVEP
RRETPKQSDV FFRHSSPPNR SVYP
//