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Database: UniProt
Entry: A0A384B6J4_BALAS
LinkDB: A0A384B6J4_BALAS
Original site: A0A384B6J4_BALAS 
ID   A0A384B6J4_BALAS        Unreviewed;       676 AA.
AC   A0A384B6J4;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Tumor protein 63 (p63) {ECO:0000256|RuleBase:RU003304};
GN   Name=TP63 {ECO:0000313|RefSeq:XP_007195280.1};
OS   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007195280.1};
RN   [1] {ECO:0000313|RefSeq:XP_007195280.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007195280.1};
RG   RefSeq;
RL   Submitted (JAN-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   RefSeq; XP_007195280.1; XM_007195218.2.
DR   AlphaFoldDB; A0A384B6J4; -.
DR   GeneID; 103005802; -.
DR   CTD; 8626; -.
DR   OrthoDB; 2902631at2759; -.
DR   Proteomes; UP000261681; Unplaced.
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:UP000261681};
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          537..603
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|SMART:SM00454"
FT   REGION          123..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          351..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..385
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         244
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT   BINDING         247
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT   BINDING         308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT   BINDING         312
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
SQ   SEQUENCE   676 AA;  76318 MW;  5D921D921C023718 CRC64;
     MNFETSRCAT LQYCPDPYIQ RFVETPAHFS WKESYYRSTM SQSTQTSEFL SPEVFQHIWD
     FLEQPICSVQ PIDLNFVDEP SENGATNKIE ISMDCIRMQD SELSDPMWPQ YTNLGLLNSM
     DQQIQNGSSS TSPYNTDHAQ NSVTAPSPYA QPSSTFDALS PSPAIPSNTD YPGPHSFDVS
     FQQSSTAKSA TWTYSTELKK LYCQIAKTCP IQIKVMTPPP QGAVIRAMPV YKKAEHVTEV
     VKRCPNHELS REFNEGQIAP PSHLIRVEGN SHAQYVEDPI TGRQSVLVPY EPPQVGTEFT
     TVLYNFMCNS SCVGGMNRRP ILIIVTLETR DGQVLGRRCF EARICACPGR DRKADEDSIR
     KQQVSDSTKN GDAFRQNTHG IQMTSIKKRR SPDDELLYLP VRGRETYEML LKIKESLELM
     QYLPQHTIET YRQQQQQQHQ HLLQKQTSMQ SQSSYGNSSP PLNKMNSMNK LPSVSQLINP
     QQRNALTPTT IPDGMGANIP MMGTHMPMAG DMNGLSPTQA LPPPLSMPST SHCTPPPPYP
     TDCSLVSFLA RLGCSSCLDY FTTQGLTTIY QIEHYSMDDL ASLKIPEQFR HAIWKGILDH
     RQLHDFSSPP HLLRTPSGAS TVSVGSSETR GERVIDAVRF TLRQTISFPP RDEWNDFNFD
     MDARRNKQQR IKEEGE
//
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