ID   D4AA88_RAT              Unreviewed;       684 AA.
AC   D4AA88;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=Tumor protein p73 {ECO:0000256|RuleBase:RU003304};
GN   Name=Tp73 {ECO:0000313|Ensembl:ENSRNOP00000052265.2,
GN   ECO:0000313|RGD:1307083};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000052265.2, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000052265.2, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000052265.2,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000052265.2}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000052265.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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: 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   RefSeq; NP_001102166.1; NM_001108696.1.
DR   AlphaFoldDB; D4AA88; -.
DR   SMR; D4AA88; -.
DR   STRING; 10116.ENSRNOP00000052265; -.
DR   PaxDb; 10116-ENSRNOP00000052265; -.
DR   Ensembl; ENSRNOT00000055398.3; ENSRNOP00000052265.2; ENSRNOG00000024707.6.
DR   GeneID; 362675; -.
DR   KEGG; rno:362675; -.
DR   UCSC; RGD:1307083; rat.
DR   AGR; RGD:1307083; -.
DR   CTD; 7161; -.
DR   RGD; 1307083; Tp73.
DR   eggNOG; ENOG502QQ48; Eukaryota.
DR   GeneTree; ENSGT00950000183153; -.
DR   HOGENOM; CLU_019621_1_1_1; -.
DR   OMA; KMSQPTA; -.
DR   OrthoDB; 2902631at2759; -.
DR   TreeFam; TF106101; -.
DR   Reactome; R-RNO-6804759; Regulation of TP53 Activity through Association with Co-factors.
DR   Reactome; R-RNO-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000024707; Expressed in lung and 4 other cell types or tissues.
DR   GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR   GO; GO:0000785; C:chromatin; IDA:RGD.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; ISO:RGD.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:RGD.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0097371; F:MDM2/MDM4 family protein binding; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0002039; F:p53 binding; ISO:RGD.
DR   GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR   GO; GO:0001222; F:transcription corepressor binding; ISO:RGD.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0033326; P:cerebrospinal fluid secretion; ISO:RGD.
DR   GO; GO:0048546; P:digestive tract morphogenesis; ISO:RGD.
DR   GO; GO:0006974; P:DNA damage response; ISO:RGD.
DR   GO; GO:0030900; P:forebrain development; ISO:RGD.
DR   GO; GO:0021766; P:hippocampus development; ISO:RGD.
DR   GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR   GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:RGD.
DR   GO; GO:0001822; P:kidney development; IEP:RGD.
DR   GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; ISO:RGD.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:RGD.
DR   GO; GO:0048666; P:neuron development; ISO:RGD.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR   GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:RGD.
DR   GO; GO:0045793; P:positive regulation of cell size; ISO:RGD.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:RGD.
DR   GO; GO:1902167; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:RGD.
DR   GO; GO:1901248; P:positive regulation of lung ciliated cell differentiation; ISO:RGD.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:RGD.
DR   GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IMP:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR   GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR   GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR   GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; ISO:RGD.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR   CDD; cd08367; P53; 1.
DR   CDD; cd09571; SAM_tumor-p73; 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; 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   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   Cell cycle {ECO:0000256|RuleBase:RU003304};
KW   Cytoplasm {ECO:0000256|RuleBase:RU003304};
KW   DNA-binding {ECO:0000256|RuleBase:RU003304};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602117-1}; Nucleus {ECO:0000256|RuleBase:RU003304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Transcription {ECO:0000256|RuleBase:RU003304};
KW   Transcription regulation {ECO:0000256|RuleBase:RU003304};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR602117-1}.
FT   BINDING         239
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT   BINDING         242
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT   BINDING         303
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT   BINDING         307
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
SQ   SEQUENCE   684 AA;  74579 MW;  5DD54931B07B269B CRC64;
     MSSPRQLDAY ATALPLQATG PPAPLPKSTD PSRAQVQPRM SNGVGEMAQS SSSSSSSSTF
     EHLWSSLEPD STYFDLPQPS QGNSEATGSE ESNMDVFHLQ GMTSSVMAQF NLLSSAMDQM
     GSRAAPASPY TPEHAASAPT HSPYAQPSST FDTMSPAPVI PSNTDYPGPH HFEVTFQQSS
     TAKSATWTYS PLLKKLYCQI AKTCPIQIKV STPPPPGTAI RAMPVYKKAE HVTDIVKRCP
     NHELGRDFNE GQSAPASHLI RVEGNNLSQY VDDPVTGRQS VVVPYEPPQV GTEFTTILYN
     FMCNSSCVGG MNRRPILVII TLETRDGQVL GRRSFEGRIC ACPGRDRKAD EDHYREQQAL
     NESTTKNGAA SKRAFKQSPP AIPALGTNVK KRRHGDEDMF YMHVRGRENF EILMKVKESL
     ELMELVPQPL VDSYRQQQQQ QLLQRPSHLQ PPSYGPVLSP MNKVHGGVNK LPSVNQLVGQ
     PPPHSSAAGP NLGSMGSGIL NSHSHSMPAN GEMNGGHSSQ TMVSGSHCTP PPPYHADPSL
     VSFLTGLGCP NCIECFTSQG LQSIYHLQNL TIEDLGALKI PDQYRMTIWR GLQDLKQSHD
     CGQQLLRSSS NAATISIGGS GELQRQRVME AVHFRVRHTI TIPNRGGAGG VTGPDEWADF
     GFDLPDCKSR KQPIKEEFTE TESH
//