BAZ2_CAEEL
ID BAZ2_CAEEL Reviewed; 1390 AA.
AC Q23590;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 4.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Bromodomain adjacent to zinc finger domain protein 2 {ECO:0000305};
GN Name=baz-2 {ECO:0000312|WormBase:ZK783.4};
GN Synonyms=flt-1 {ECO:0000312|WormBase:ZK783.4};
GN ORFNames=ZK783.4 {ECO:0000312|WormBase:ZK783.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SET-6, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=32103178; DOI=10.1038/s41586-020-2037-y;
RA Yuan J., Chang S.Y., Yin S.G., Liu Z.Y., Cheng X., Liu X.J., Jiang Q.,
RA Gao G., Lin D.Y., Kang X.L., Ye S.W., Chen Z., Yin J.A., Hao P., Jiang L.,
RA Cai S.Q.;
RT "Two conserved epigenetic regulators prevent healthy ageing.";
RL Nature 579:118-122(2020).
CC -!- FUNCTION: Chromatin reader protein, involved in positively modulating
CC the rate of age-related behavioral deterioration (PubMed:32103178).
CC Positively modulates the level of global trimethylated 'Lys-9' of
CC histone H3 (H3K9me3), but not of H3K9me2 or H3K9me1 (PubMed:32103178).
CC May repress the expression of mitochondrial function-related genes by
CC occupying their promoter regions, working in concert with histone
CC methyltransferase, set-6 (PubMed:32103178). Involved in modulation of
CC the mitochondrial unfolded protein response (UPR) (PubMed:32103178).
CC Negatively regulates expression of bas-1, a serotonin (5-HT) and
CC dopamine synthesizing enzyme (DOPA decarboxylase), with aging
CC (PubMed:32103178). Negatively modulates levels of endogenous 5-HT and
CC dopamine with aging (PubMed:32103178). Involved in modulating
CC longevity, probably as a result of enhanced stress resistance via
CC mechanisms related to dietary restriction and mitochondrial function
CC (PubMed:32103178). {ECO:0000269|PubMed:32103178}.
CC -!- SUBUNIT: Interacts with set-6. {ECO:0000269|PubMed:32103178}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32103178}. Chromosome
CC {ECO:0000269|PubMed:32103178}.
CC -!- TISSUE SPECIFICITY: Broadly expressed in the nervous system, including
CC head, body and tail neurons. {ECO:0000269|PubMed:32103178}.
CC -!- DEVELOPMENTAL STAGE: Expression increases with age.
CC {ECO:0000269|PubMed:32103178}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown prevents age-related
CC decline in the expression of bas-1, a serotonin (5-HT) and dopamine
CC synthesizing enzyme (DOPA decarboxylase) (PubMed:32103178). RNAi-
CC mediated knockdown improves behavioral performance in pharyngeal
CC pumping in aged worms (PubMed:32103178). {ECO:0000269|PubMed:32103178}.
CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX284603; CCD65251.2; -; Genomic_DNA.
DR RefSeq; NP_498673.3; NM_066272.4.
DR AlphaFoldDB; Q23590; -.
DR SMR; Q23590; -.
DR STRING; 6239.ZK783.4; -.
DR EPD; Q23590; -.
DR PaxDb; Q23590; -.
DR PeptideAtlas; Q23590; -.
DR EnsemblMetazoa; ZK783.4.1; ZK783.4.1; WBGene00001470.
DR GeneID; 176078; -.
DR KEGG; cel:CELE_ZK783.4; -.
DR UCSC; ZK783.4; c. elegans.
DR CTD; 176078; -.
DR WormBase; ZK783.4; CE47168; WBGene00001470; baz-2.
DR eggNOG; KOG1245; Eukaryota.
DR GeneTree; ENSGT00940000172329; -.
DR HOGENOM; CLU_255009_0_0_1; -.
DR InParanoid; Q23590; -.
DR OMA; GVEPTLC; -.
DR OrthoDB; 200493at2759; -.
DR PhylomeDB; Q23590; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001470; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0000785; C:chromatin; IMP:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051574; P:positive regulation of histone H3-K9 methylation; IMP: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; IPR028942; WHIM1_dom.
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 Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF15612; WHIM1; 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; 2.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF54171; SSF54171; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
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 1: Evidence at protein level;
KW Bromodomain; Chromosome; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1390
FT /note="Bromodomain adjacent to zinc finger domain protein
FT 2"
FT /id="PRO_0000452176"
FT DOMAIN 323..395
FT /note="MBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00338"
FT DOMAIN 524..588
FT /note="DDT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00063"
FT DOMAIN 1290..1360
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT ZN_FING 1100..1149
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 30..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1390 AA; 156593 MW; 5D05420388A61B3B CRC64;
MSDNSSNQFL LLLAAAQQQQ QQQLLQQQLA KIQKATASSP SKSTNGTSAS TSAVPSTSGT
SSSQNEAAQL QNLAKMQQIQ QLAQFGALMA AQKKQQEKAA ADKAKEKEKE KQKAAAAAAA
AAAKASASTS SASAIPGLSP EMLAAWQQAI QMQALQQMMM TPQKSQMEEA IKKMMDMAKK
KPAGVASTSS ASTSSSTPST SSASITSSNN NAANNAASNM MNNVMWQLVA AQMQQKQQQQ
QKDTQKKADQ AKKAKELAKQ QQKEQDVKNK QQEEILKFLM AQHQLNHQKK HEKKQADAAA
LAAKVLAAHR AALESDSPEE GKKTNEAMLR LPLQLGWRRQ TCVRSIASAG VKGDVSYFAP
CGKKLSTYSE VVRYLTKNSI HYITRDNFLF NTKLVIGEFI VPKQTEADET QQEREFAMFT
EDDINKELTR LNVLKFVPKI QASTSNGVHE DDIKMSKIEE PDEPLDPSEL NDEFTEELVH
SQIMSNGVDE CKIREREADD LLVNINDVRH LPDFSRIGNQ CLSSQGFADA LMVHEFVQNF
GHVLGIDLEI APKLESLCAG LDGDANHAEQ TLQLTRQLLR LALEFPGMGN EKRFGQGGGE
MGLDRENFSE VMRLFLIDKG KRGEELSQPL LTCNFLSISP EQKASILAFL CDELVCSRNV
VTEIDKNLDE ISRLKGEKWM REGKARALRS ARSKKKNDEK VVVVKEEQNH ESDSEPPTRP
DTPKKATVAP PTVVSVSPVS AAQQQQRKFT PGLGQCEVLT EQEESMSLQQ MDSLIGDLHQ
EAQNINQKIH DTGLKIRSFP FGTDRFHRNY WMLAHTDKVI IESLATTSVN NPACNANEYA
SKDPPTLEQR VPGACETIDL DVIACVEDLV DDVVLLRAKA DKKTRKRYRR IENHMKRGWW
TMQNRDCVES LRSCMLSRGI RERALHRLLT KPWFLNELKF GTITIEPVGE KSDLELVRRQ
GWTRLNTAID KLQCHLKMSD VSKPLPSITP FETQKPIVVP PTMALAQIVK DDMAWKVIDE
EVDGQELDET IIRQKIIETA DMVQPKFWRP KFQKLEDQDT CQLFEDWKSY VSTEAQTTSQ
LMVALQTLEG MIMWERSSRE ALCQICKSMD GDEMLVCDGC ESGCHMECFR PRMTKVPEGD
WFCQRCREEK SGRPMCMFCS RETGNLHQCQ RCAYHVHQEC SQDGPKEAIN PETFICGHCQ
EMKQMRFVKR LILRSESEER ELEDDNHAEN GENTKNGHMN GMNGAIAIGV HNQQNGVKGN
LKRKLEVPSI GGLPKNMNKE LCQLMLDELV VQANALPFLE PVNPKLVPGY KMIISKPMDL
KTIRQKNEKL IYETPEDFAE DIELMFANCR QFNIDHSEIG RAGISLHKFF QKRWKQLKYN
FTKRLRRLHR
