BAZ2A_XENLA
ID BAZ2A_XENLA Reviewed; 1698 AA.
AC B7ZS37; Q6YI94;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Bromodomain adjacent to zinc finger domain protein 2A;
DE AltName: Full=Transcription termination factor I-interacting protein 5;
DE Short=TTF-I-interacting protein 5;
DE Short=Tip5;
GN Name=baz2a; Synonyms=tip5;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ruzov A., Meehan R.;
RT "Molecular cloning and expression analysis of chromatin remodelling factor
RT BAZ2A in Xenopus laevis.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential component of the NoRC (nucleolar remodeling
CC complex) complex, a complex that mediates silencing of a fraction of
CC rDNA by recruiting histone-modifying enzymes and DNA
CC methyltransferases, leading to heterochromatin formation and
CC transcriptional silencing. In the complex, it plays a central role by
CC being recruited to rDNA and by targeting chromatin modifying enzymes
CC such as HDAC1, leading to repress RNA polymerase I transcription.
CC Recruited to rDNA via its interaction with TTF1 and its ability to
CC recognize and bind histone H4 acetylated on 'Lys-16' (H4K16ac), leading
CC to deacetylation of H4K5ac, H4K8ac, H4K12ac but not H4K16ac.
CC Specifically binds pRNAs, 150-250 nucleotide RNAs that are
CC complementary in sequence to the rDNA promoter; pRNA-binding is
CC required for heterochromatin formation and rDNA silencing (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the NoRC complex, at least composed of
CC SMARCA5/SNF2H and BAZ2A/TIP5. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- DOMAIN: The MBD (methyl-CpG-binding) domain, also named TAM domain,
CC specifically recognizes and binds a conserved stem-loop structure the
CC association within pRNA. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000305}.
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DR EMBL; AY145834; AAN61105.1; -; mRNA.
DR EMBL; BC170384; AAI70384.1; -; mRNA.
DR EMBL; BC170386; AAI70386.1; -; mRNA.
DR RefSeq; NP_001082767.1; NM_001089298.1.
DR AlphaFoldDB; B7ZS37; -.
DR SMR; B7ZS37; -.
DR GeneID; 398712; -.
DR KEGG; xla:398712; -.
DR CTD; 398712; -.
DR Xenbase; XB-GENE-965905; baz2a.L.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 398712; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005677; C:chromatin silencing complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0033553; C:rDNA heterochromatin; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0006306; P:DNA methylation; ISS:UniProtKB.
DR GO; GO:0016575; P:histone deacetylation; ISS:UniProtKB.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; ISS:UniProtKB.
DR CDD; cd05503; Bromo_BAZ2A_B_like; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR037374; BAZ2A/B_Bromo.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR018501; DDT_dom.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR InterPro; IPR028940; TIP5.
DR InterPro; IPR028941; WHIM2_dom.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45915:SF5; PTHR45915:SF5; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF02791; DDT; 1.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF15613; WSD; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00571; DDT; 1.
DR SMART; SM00391; MBD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF54171; SSF54171; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS50982; MBD; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 2: Evidence at transcript level;
KW Bromodomain; Chromatin regulator; Coiled coil; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Repressor; RNA-binding; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1698
FT /note="Bromodomain adjacent to zinc finger domain protein
FT 2A"
FT /id="PRO_0000383149"
FT DOMAIN 418..489
FT /note="MBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00338"
FT DOMAIN 701..766
FT /note="DDT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00063"
FT DOMAIN 1602..1672
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DNA_BIND 541..553
FT /note="A.T hook 1"
FT DNA_BIND 541..553
FT /note="A.T hook 2"
FT DNA_BIND 1204..1216
FT /note="A.T hook 3"
FT ZN_FING 1476..1526
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 240..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1549..1587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 579..638
FT /evidence="ECO:0000255"
FT COMPBIAS 610..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1549..1563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 653
FT /note="L -> Q (in Ref. 1; AAN61105)"
FT /evidence="ECO:0000305"
FT CONFLICT 661
FT /note="E -> K (in Ref. 1; AAN61105)"
FT /evidence="ECO:0000305"
FT CONFLICT 741
FT /note="N -> K (in Ref. 1; AAN61105)"
FT /evidence="ECO:0000305"
FT CONFLICT 806
FT /note="E -> Q (in Ref. 1; AAN61105)"
FT /evidence="ECO:0000305"
FT CONFLICT 966
FT /note="D -> Y (in Ref. 1; AAN61105)"
FT /evidence="ECO:0000305"
FT CONFLICT 1210
FT /note="R -> P (in Ref. 1; AAN61105)"
FT /evidence="ECO:0000305"
FT CONFLICT 1268
FT /note="H -> Y (in Ref. 1; AAN61105)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1698 AA; 192095 MW; 4D58AB30632A88AE CRC64;
METQNHLSCT GQTPLTNASG LKLLPQSVEP VYTNSTLTSF SQHGKVLNYD LPVNGLISPS
LSNNAHGTLL SNEHITHNSA SNNFDYLWKK PKSSVHKDSH VSNQFLVNGS TCPITNGPSI
KRSPQETLGN CTSNQTASFN VSSHSVCSPN EANVKMVTAA NGAHYGFYEA SLPVSVSASN
MQSVSGDNLV KERTVEENEA GATEERNHTP ELAEALEPSD TQTDLNICEY KESVLDPVIQ
STPNPLLPPD VSNLDDPSQL PSQLGDSHLL NEDSLEPFGA DLIQDPISST MYDLEELEVG
STKQKDPQLD TSSLDCPTYS LSAAFPLVAE DTNDSSVLFN ASSASPVLGD SVMQESASEM
GEDPEGSKAE EPVSGPENVS QDEMTIENTS PEPCVAAEHE EEELEPGEVK GTISRRRIAT
PEQVCFPLQH GWRREVRIKK GSHRWQGETW YYAPCGKRMK QFPEVIKYLS KNAGPFVRRE
HFSFSPRMPV GDFYEERNTA EGLQWVLLNS EEIPSRIIAI TGKRGRPRNL EKAKAKEQKA
KRGRGRPPKV KMIDLLSKAD AKLLRKLENQ DILSDSEKVQ LCKLKKKMRR KARNQEAKLE
AAKKLKEIKE KEEKKQKIQK AKNQEKAKNQ EKKRTRRQPK QKAPVVQKPD RKLLAQQRRL
EERKRQQFIL EELKKPTEDM CLPDHQQLPD FPCVPGLFLP SCAFSDCLTT VEFLHSYGKV
LGLDEAKDIP SLCTLQEGLF NVGDSLGEVQ DLLVKLLQAA MINPGLPPYC QSLKILGEKV
SEIVLSRENV SEPLRIFLEA YGGDIELCDS LRSHPFQAHA PHIKTAILAF IVNELNASSL
IISEIDKTLE NMSHYRKHKW IIEGKIRRLK FALSKRKSSE ESQITTTEVS LRRRSERNAE
ENDELDSIDE SAIQKDYVQE EVDIPPSTSV VELERQIEKL TKRQMFFRKK ILGSSQRLRT
VCLGQDRYRR CYWMLPHLGG IFIEGLPESA EPTEEAALGN DIEASSVKTE DKSFGSLCKT
SGHPRNSTAE PEQNSTSCHC SDSKDKEPSG VTDQFPNSVP LTNNQQDLSQ SVFLSWLTKN
QTSIMDSTVL TPESSPPHSE STPIISSEAT EKPEQWLPLI SRTPCRNHNQ GLSTHSSNRL
SPPSPTAATS VKQVNEFTEE AQTFATSLPS NSTPCHVCYN SGKSSTASHE ITLTSNILHD
SEKEKRRGRR PSKLLKQIEQ KYYNQLIERP IPAGVRQKWW WIKDPAMLES LLKALHPRGI
REKTLHKHLT KHLQHLKEMC ARPASDALFK FTPVDGHRVS QETLDRWSVT DLTFQVDLSA
LQWVEDLEQR VMLSDLQQRG WSPSAPDSVR TDLKYYEHQL EPADDITVKV KREDCRLYRE
SSNPLDLAVL RILCLEENVE RKYLKEPLWL FSEVQHEKVV ITNPEDPLST TEIEYSITSR
LRLWRQTVER CRSAAQLSLC LQQLERSIAW ERSLNKVTCL YCRKGDNDEL LLLCDSCDRG
CHTYCHRPRM NEIPEGDWFC PTCISLQSES EFLRSSGSSK RIRKCTVRFT EDSPSKPSRR
REHPTASQFS PGESPASKKR RMGTRSQSPD LTFCEIILME LESHEDAWPF LEPVNPRLVP
GYRKIIKNPM DFSTMRHKLL NGNYSRCEEF AEDAELIFSN CQLFNEDESD VGKAGLILKK
FYDARWEEFS QERNQISL
