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Database: UniProt
Entry: A0A091VW97_OPIHO
LinkDB: A0A091VW97_OPIHO
Original site: A0A091VW97_OPIHO 
ID   A0A091VW97_OPIHO        Unreviewed;       680 AA.
AC   A0A091VW97;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   28-JUN-2023, entry version 40.
DE   RecName: Full=Tumor protein 63 (p63) {ECO:0000256|RuleBase:RU003304};
GN   ORFNames=N306_14128 {ECO:0000313|EMBL:KFR06798.1};
OS   Opisthocomus hoazin (Hoatzin) (Phasianus hoazin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae;
OC   Opisthocomus.
OX   NCBI_TaxID=30419 {ECO:0000313|EMBL:KFR06798.1, ECO:0000313|Proteomes:UP000053605};
RN   [1] {ECO:0000313|EMBL:KFR06798.1, ECO:0000313|Proteomes:UP000053605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N306 {ECO:0000313|EMBL:KFR06798.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       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; KK734351; KFR06798.1; -; Genomic_DNA.
DR   RefSeq; XP_009929967.1; XM_009931665.1.
DR   AlphaFoldDB; A0A091VW97; -.
DR   STRING; 30419.A0A091VW97; -.
DR   GeneID; 104326847; -.
DR   KEGG; oha:104326847; -.
DR   CTD; 8626; -.
DR   OrthoDB; 2902631at2759; -.
DR   PhylomeDB; A0A091VW97; -.
DR   Proteomes; UP000053605; Unassembled WGS sequence.
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602117-1}; Nucleus {ECO:0000256|RuleBase:RU003304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053605};
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          541..607
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..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          436..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          481..500
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..389
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        481..498
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   680 AA;  76842 MW;  2FCBF3385D8573F3 CRC64;
     MNFEPAPFTT LQYYPEPCIQ RFVETPSHFS WKETYYRSAM SQSSQPREFL SPEVLQHIWD
     FLEQPICSVQ PIDLNFIDDP SENGPTNKIE ISMDCVRVQD TELNDPMWPQ YTNLGLLNSM
     DQQIQNGSSS TSPYNTEHAQ NSVTAPSPYA QPSSTFDALS PSPAIPSNTD YPGPHSFDVS
     FQQSSTAKSA TWTYSTELKK LYCQIAKTCP IQIKVMTPPP QGAVIRAMPV YKKAEHVTEV
     VKRCPNHELS REFNEGQIAP PSHLIRVEGN SHAQYVEDPI TGRQSVLVPY EPPQVGTEFT
     TVLYNFMCNS SCVGGMNRRP ILIIVTLETR DGQVLGRRCF EARICACPGR DRKADEDSIR
     KQQVSDSTKN GDGTKRPFRQ GTHGIQMTSI KKRRSPDDEL LYLPVRGRET YEMLLKIKES
     LELMQYLPQH TIETYRQQQQ QQHQHLLQKQ TSMQSQSSYG SNSPPLSKMN SMNKLPSVSQ
     LINPQQRNAL TPTTIPDGMG TNIPMMGTHM AMTSDMNGLS PTQALPPPLS MPSTSHCTPP
     PPYPTDCSIV SFLARLGCSS CVDYFTTQGL TTIYQIEHYS MDDLVSLKIP EQFRHAIWKG
     ILDHRQLHDF SSPPHLLRTP SGASTVSVGS SETRGERVID AVRFTLRQTI SFPPRDEWND
     FNFDMDARRN KQQRIKEEGE
//
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