ID A0A3B3ULL0_9TELE Unreviewed; 690 AA.
AC A0A3B3ULL0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Tumor protein p73 {ECO:0000256|RuleBase:RU003304};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000013554.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000013554.1}
RP IDENTIFICATION.
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|ARBA:ARBA00024672}.
CC -!- FUNCTION: Participates in the apoptotic response to DNA damage.
CC Isoforms containing the transactivation domain are pro-apoptotic,
CC isoforms lacking the domain are anti-apoptotic and block the function
CC of p53 and transactivating p73 isoforms. May be a tumor suppressor
CC protein. {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|ARBA:ARBA00011393}.
CC -!- SUBUNIT: Found in a complex with p53/TP53 and CABLES1.
CC {ECO:0000256|RuleBase:RU003304}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU003304}.
CC Nucleus {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 AlphaFoldDB; A0A3B3ULL0; -.
DR Ensembl; ENSPLAT00000021602.1; ENSPLAP00000013554.1; ENSPLAG00000017124.1.
DR GeneTree; ENSGT00950000183153; -.
DR Proteomes; UP000261500; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 CDD; cd09571; SAM_tumor-p73; 1.
DR Gene3D; 2.60.40.720; -; 2.
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; IPR037612; Tumour-p73_SAM.
DR PANTHER; PTHR11447; CELLULAR TUMOR ANTIGEN P53; 1.
DR PANTHER; PTHR11447:SF21; TUMOR PROTEIN P73; 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; 2.
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 Cell cycle {ECO:0000256|RuleBase:RU003304};
KW Cytoplasm {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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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 516..582
FT /note="SAM"
FT /evidence="ECO:0000259|SMART:SM00454"
FT REGION 21..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
SQ SEQUENCE 690 AA; 76099 MW; 6BD5CC0C8E6065A5 CRC64;
MYYVKKKSQY NLLSSSMESL GSRATSASPY SSENTSSSAV PTPSPYSQPN STFEGLSPTP
AIPSNTDYPG PHAFQVSFQQ SSTAKSATWT SQYNLLSSSM ESLGSRATSA SPYSSENTSS
SAVPTPSPYS QPNSTFEGLS PTPAIPSNTD YPGPHAFQVS FQQSSTAKSA TWTYSPLLKK
LYCQIAKTCP IQIKVSSSPP HGSIIRAMPV YKKAEHVTEV VKRCPNHELG REFNDGQTAP
ASHLIRVEGN NLCQYVDDQV TGRQSVFVPY EAPQVGTEFT TILYNFMCNS SCVGGMNRRP
ILIIITLETR DGQVLGRRSF EGRICACPGR DRKADEDHFR EQQALNDSVA KNGSANKRNF
KQSPPNISSP HINIRKRRHG EEEIYYIPVR GRENFELLMK IKDSLELVEL VPQPLVDSYR
QQTQQQLLQR PNHIASPSSY SPLSNMNKMH SHSGLGKTQS LNQMVGHQPQ QHPNANPTIT
HMGPSMLNSN HMQGNGDMNS GHSSQNIVSA SHCSPPPYNP DPSLVSFLTS LGCQNFIEYF
TSQGLQSVYH LQTLTMEDLG ALKIPEQSRL AIWRGLQDMK QGAVHQLPNS THHHEYHGQQ
LLRSSSNMAA SAMAAIGAAG GELQRQRVME AVHFRVRHTI TIPNRPGVVG PSGMTPAPDE
WADFGFDMPD CKESRSKHSI KEEFMESDVH
//
