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Database: UniProt
Entry: A0A226MN96_CALSU
LinkDB: A0A226MN96_CALSU
Original site: A0A226MN96_CALSU 
ID   A0A226MN96_CALSU        Unreviewed;       675 AA.
AC   A0A226MN96;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Tumor protein p73 {ECO:0000256|RuleBase:RU003304};
GN   ORFNames=ASZ78_009825 {ECO:0000313|EMBL:OXB56610.1};
OS   Callipepla squamata (Scaled quail).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC   Callipepla.
OX   NCBI_TaxID=9009 {ECO:0000313|EMBL:OXB56610.1, ECO:0000313|Proteomes:UP000198323};
RN   [1] {ECO:0000313|EMBL:OXB56610.1, ECO:0000313|Proteomes:UP000198323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texas {ECO:0000313|EMBL:OXB56610.1,
RC   ECO:0000313|Proteomes:UP000198323};
RC   TISSUE=Leg muscle {ECO:0000313|EMBL:OXB56610.1};
RA   Oldeschulte D.L., Halley Y.A., Bhattarai E.K., Brashear W.A., Hill J.,
RA   Metz R.P., Johnson C.D., Rollins D., Peterson M.J., Bickhart D.M.,
RA   Decker J.E., Seabury C.M.;
RT   "Disparate Historic Effective Population Sizes Predicted by Modern Levels
RT   of Genome Diversity for the Scaled Quail (Callipepla squamata) and the
RT   Northern Bobwhite (Colinus virginianus): Inferences from First and Second
RT   Generation Draft Genome Assemblies for Sympatric New World Quail.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OXB56610.1}.
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DR   EMBL; MCFN01000630; OXB56610.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A226MN96; -.
DR   STRING; 9009.A0A226MN96; -.
DR   Proteomes; UP000198323; Unassembled WGS sequence.
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; -; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602117-1}; Nucleus {ECO:0000256|RuleBase:RU003304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198323};
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          528..594
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|SMART:SM00454"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          95..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          359..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..132
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..375
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..454
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..490
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..524
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         220
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT   BINDING         223
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602117-1"
FT   BINDING         284
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"
SQ   SEQUENCE   675 AA;  74793 MW;  E2E248CDF15BA62D CRC64;
     MESSTEAGVI YPLSDSPSVK MSQSSPADES TTFEHLWSTL APDSTYFDLS PSSHTGSNEV
     SNRTEVTMDV FQMRGMNDSV MSQFNLLNNS MDQSIGSRAA STSPYSSEHT SNVPTHSPYS
     QPSSTFDAMS PAPVIPSNTD YPGPHHFEVT FQQSSTAKSA TWTLSLLLQY SPLLKKLYCQ
     IAKTCPIQIK VSSPPPPGTI IRAMPVYKKA EHVTEVVKRC PNHELGRDFN DGQSAPASHL
     IRVEGNNLSQ YVDDPVTGRQ SVMVPYEPPQ VGTEFTTILY NFMCNSSCVG GMNRRPILII
     ITLETRDERP WQKQIHQFLS PPSGQVLGRR SFEGRICACP GRDRKADEDH YREQQALNEN
     AAKNGNANKR TFKQSPQAIP ALGPGVKKRR HGEEEMYYVP VRGRENFEIL MKIKESLELV
     ELVPQQLVDS YRQQQQQLLQ RQNQLQTPSS YGPVLSPMNK VHGGGINKLP SVNQLVGQPA
     QHSSSSAPSL GPMGPGMLNS HPMQPNGEMN GGHSSQSMVS GSHCTPPPPY NPDPSLVSFL
     TGLGCPNCID YFTSQGLQNI YHLQNLSIED LGALKIPEQY RMIIWRGLQE LKQSHDYGAQ
     QLIRSSSNAS TISIGSSGEL QRQRVMEAVH FRVRHTITIP NRGAADEWAD FGFDLPDCKS
     RKQSIKEEFT EGEIN
//
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