ID   BANP_DANRE              Reviewed;         508 AA.
AC   Q502P7;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Protein BANP;
GN   Name=banp; ORFNames=zgc:111954;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-binding protein which may repress cyclin D1 transcription
CC       by recruiting HDAC1 to its promoter, thereby diminishing H3K9ac,
CC       H3S10ph and H4K8ac levels. Promotes TP53 activation, which causes cell
CC       cycle arrest (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:Q8VBU8}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the BANP/SMAR1 family. {ECO:0000305}.
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DR   EMBL; BC095613; AAH95613.1; -; mRNA.
DR   RefSeq; NP_001018468.1; NM_001020632.1.
DR   AlphaFoldDB; Q502P7; -.
DR   SMR; Q502P7; -.
DR   STRING; 7955.ENSDARP00000023623; -.
DR   PaxDb; Q502P7; -.
DR   GeneID; 553659; -.
DR   KEGG; dre:553659; -.
DR   CTD; 54971; -.
DR   ZFIN; ZDB-GENE-050522-54; banp.
DR   eggNOG; ENOG502QRIF; Eukaryota.
DR   InParanoid; Q502P7; -.
DR   OrthoDB; 1401911at2759; -.
DR   PhylomeDB; Q502P7; -.
DR   Reactome; R-DRE-6804759; Regulation of TP53 Activity through Association with Co-factors.
DR   PRO; PR:Q502P7; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IBA:GO_Central.
DR   GO; GO:0034504; P:protein localization to nucleus; IBA:GO_Central.
DR   InterPro; IPR042343; BANP.
DR   InterPro; IPR018379; BEN_domain.
DR   PANTHER; PTHR16243; PTHR16243; 1.
DR   Pfam; PF10523; BEN; 1.
DR   SMART; SM01025; BEN; 1.
DR   PROSITE; PS51457; BEN; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Chromatin regulator; Coiled coil; DNA-binding; Nucleus;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..508
FT                   /note="Protein BANP"
FT                   /id="PRO_0000297912"
FT   DOMAIN          223..319
FT                   /note="BEN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00784"
FT   REGION          132..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          168..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          326..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          65..90
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        180..198
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   508 AA;  55463 MW;  9BA86D95DF43E59F CRC64;
     MMSEQGLVEI VQIAVADLNH EGHQTDVLEN NEDSDQPGRK RARIEISQET SIKSMLISIS
     QAICQRLDSM EAKLQVLEVT CRGLVEKLDT VMGKNQSTTQ VPMVSGSPFG ATQTCDKVRC
     VVPQTNVIVS GDRAKTEETS PRTSDSLENL LSNTVGRGRQ KTIVLKVPVQ EEIQDDQESG
     SETSDSVSNS GQPQNNNNVT LITLNSEEDY PTGTWLGDEN NPEMRVRCPV SPADMLHIST
     NCRTAEKMAL TLLDYLFHRE VQAVSNLSGQ GKHGKKQLDP LMIYGIRCHL FFKFAITESD
     WYRIKQSIDS KCRTAWRRKQ RGQSLAVKSF SRRTPASQSS SDGVSAAETS AIETSTQQAL
     HYALAGATQQ VQIHRIGEDG QVQVIPQGHL HIAQVPQGEQ VQITQDSEGN LQIHQVHVGQ
     DGQVNVLRGP QLIAVASTDG TGGVDASPLQ ANDIQVQYVQ LGTVTDHTGA VQAEALTPAL
     QAEMDVKEAI QLQQAENGEV VQIQMPGT