ID A0A337SKN0_FELCA Unreviewed; 636 AA.
AC A0A337SKN0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Tumor protein 63 (p63) {ECO:0000256|RuleBase:RU003304};
GN Name=TP63 {ECO:0000313|Ensembl:ENSFCAP00000046138.1,
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:ENSFCAP00000046138.1, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000046138.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000046138.1,
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:ENSFCAP00000046138.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000046138.1,
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:ENSFCAP00000046138.1}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000046138.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Acts as a sequence specific DNA binding transcriptional
CC activator or repressor. The isoforms contain a varying set of
CC transactivation and auto-regulating transactivation inhibiting domains
CC thus showing an isoform specific activity. May be required in
CC conjunction with TP73/p73 for initiation of p53/TP53 dependent
CC apoptosis in response to genotoxic insults and the presence of
CC activated oncogenes. {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. Isoform composition of the
CC tetramer may determine transactivation activity.
CC {ECO:0000256|RuleBase:RU003304}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU003304}.
CC -!- SIMILARITY: Belongs to the p53 family. {ECO:0000256|ARBA:ARBA00006167,
CC ECO:0000256|RuleBase:RU003304}.
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DR EMBL; AANG04001816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A337SKN0; -.
DR Ensembl; ENSFCAT00000054873.2; ENSFCAP00000046138.1; ENSFCAG00000000790.6.
DR VGNC; VGNC:66467; TP63.
DR GeneTree; ENSGT00950000183153; -.
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:0051262; P:protein tetramerization; IEA:InterPro.
DR CDD; cd08367; P53; 1.
DR CDD; cd09572; SAM_tumor-p63; 1.
DR Gene3D; 2.60.40.720; -; 1.
DR Gene3D; 4.10.170.10; p53-like tetramerisation domain; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 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 InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR037611; Tumor-p63_SAM.
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 Pfam; PF07647; SAM_2; 1.
DR PRINTS; PR00386; P53SUPPRESSR.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47719; p53 tetramerization domain; 1.
DR SUPFAM; SSF49417; p53-like transcription factors; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 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 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 497..563
FT /note="SAM"
FT /evidence="ECO:0000259|SMART:SM00454"
FT REGION 79..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT BINDING 203
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 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
SQ SEQUENCE 636 AA; 71321 MW; F5408BADFE0E5730 CRC64;
MYRERKRERD LSSVIFLVDS YCQGLRGGGG VGKILEPEER TAALINLTAN MLYLENNAQT
QFSEPQYTNL GLLNSMDQQI QNGSSSTSPY NTDHAQNSVT APSPYAQPSS TFDALSPSPA
IPSNTDYPGP HSFDVSFQQS STAKSATWTY STELKKLYCQ IAKTCPIQIK VMTPPPQGAV
IRAMPVYKKA EHVTEVVKRC PNHELSREFN EGQIAPPSHL IRVEGNSHAQ YVEDPITGRQ
SVLVPYEPPQ VGTEFTTVLY NFMCNSSCVG GMNRRPILII VTLETRDGQV LGRRCFEARI
CACPGRDRKA DEDSIRKQQV SDSAKNGDGT KRPFRQNTHG IQMTSIKKRR SPDDELLYLP
VRGRETYEML LKIKESLELM QYLPQHTIET YRQQQQQQHQ HLLQKQTSMQ TQSSYGNSSP
PLNKMNSMNK LPSVSQLINP QQRNALTPTT IPDGMGANIP MMGTHMPMAG DMNGLSPTQA
LPPPLSMPST SHCTPPPPYP TDCSLVSFLA RLGCSSCLDY FTTQGLTTIY QIEHYSMDDL
ASLKIPEQFR HAIWKGILDH RQLHDFSSPP HLLRTPSGAS TVSVGSSETR GERVIDAVRF
TLRQTISFPP RDEWNDFNFD MDARRNKQQR IKEEGE
//
