MBTD1_XENTR
ID MBTD1_XENTR Reviewed; 651 AA.
AC Q6DIN3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=MBT domain-containing protein 1 {ECO:0000305};
GN Name=mbtd1 {ECO:0000250|UniProtKB:Q05BQ5};
GN ORFNames=TTpA012c17.1 {ECO:0000303|Ref.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tadpole;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Chromatin reader component of the NuA4 histone
CC acetyltransferase complex, a multiprotein complex involved in
CC transcriptional activation of select genes principally by acetylation
CC of nucleosomal histones H4 and H2A. The NuA4 complex plays a direct
CC role in repair of DNA double-strand breaks (DSBs) by promoting
CC homologous recombination (HR). MBTD1 specifically recognizes and binds
CC monomethylated and dimethylated 'Lys-20' on histone H4 (H4K20me1 and
CC H4K20me2, respectively). In the NuA4 complex, MBTD1 promotes
CC recruitment of the complex to H4K20me marks by competing with TP53BP1
CC for binding to H4K20me. Following recruitment to H4K20me at DNA breaks,
CC the NuA4 complex catalyzes acetylation of 'Lys-15' on histone H2A
CC (H2AK15), blocking the ubiquitination mark required for TP53BP1
CC localization at DNA breaks, thereby promoting homologous recombination
CC (HR). {ECO:0000250|UniProtKB:Q05BQ5}.
CC -!- SUBUNIT: Monomer. Component of the NuA4 histone acetyltransferase
CC complex. {ECO:0000250|UniProtKB:Q05BQ5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q05BQ5}.
CC Chromosome {ECO:0000250|UniProtKB:Q05BQ5}.
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DR EMBL; CR760838; CAJ83167.1; -; mRNA.
DR EMBL; BC075504; AAH75504.1; -; mRNA.
DR RefSeq; NP_001006742.1; NM_001006741.1.
DR AlphaFoldDB; Q6DIN3; -.
DR SMR; Q6DIN3; -.
DR STRING; 8364.ENSXETP00000002764; -.
DR PaxDb; Q6DIN3; -.
DR DNASU; 448411; -.
DR Ensembl; ENSXETT00000002764; ENSXETP00000002764; ENSXETG00000001291.
DR GeneID; 448411; -.
DR KEGG; xtr:448411; -.
DR CTD; 54799; -.
DR Xenbase; XB-GENE-949653; mbtd1.
DR eggNOG; KOG3766; Eukaryota.
DR HOGENOM; CLU_005352_2_1_1; -.
DR InParanoid; Q6DIN3; -.
DR OMA; LHPIHKS; -.
DR OrthoDB; 1334498at2759; -.
DR PhylomeDB; Q6DIN3; -.
DR TreeFam; TF316498; -.
DR Proteomes; UP000008143; Chromosome 10.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000001291; Expressed in gastrula and 19 other tissues.
DR ExpressionAtlas; Q6DIN3; baseline.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.30.60.160; -; 1.
DR InterPro; IPR004092; Mbt.
DR InterPro; IPR012313; Znf_FCS.
DR InterPro; IPR038603; Znf_FCS_sf.
DR Pfam; PF02820; MBT; 4.
DR SMART; SM00561; MBT; 4.
DR PROSITE; PS51079; MBT; 4.
DR PROSITE; PS51024; ZF_FCS; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Chromosome; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..651
FT /note="MBT domain-containing protein 1"
FT /id="PRO_0000313720"
FT REPEAT 164..268
FT /note="MBT 1"
FT REPEAT 276..373
FT /note="MBT 2"
FT REPEAT 374..479
FT /note="MBT 3"
FT REPEAT 487..583
FT /note="MBT 4"
FT ZN_FING 68..103
FT /note="FCS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT REGION 21..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
SQ SEQUENCE 651 AA; 72910 MW; CA8055148D95D614 CRC64;
MEKTKDLADL SSLSERKRRD SFGMFDGYDS CSEDTSSSSS SDESEEEVAP LPSSLPIIKN
NGQVYTYPDG KSGMATCEMC GMVGVRDAFY SKTKRFCSVS CSRSYSSNSK KASILARLQG
KPPTKKAKVL QKKPLVAKLA AYAQYKATLK NQSVNKAPVT VEGFSWGNYI TSNNTAAAPV
TCFRHAPMGN CWGDIAEGVR VEVPNTDSNL PTKVFWISGI VKLAGFNALL RYEGFENDSS
LDFWCNICGP DVHPVGWCAT SGKPLVPPQT IQHKYTNWKA FLVKRLTGAK TLPPDFSQKV
SESMQYPFKP SMRVEVVDKT HLCRTRVAVV DSVIGGRLRL VYEESEDKTD DFWCHMYSPL
IHPIGWSRSI GHRFKRTDIL KKQESNYDAP SHLFTKVKDI EQGSEWFKEG MKLEAIDPLN
LSAICVATIR KVLADGYLMI GIDGSEAADG SDWFCYHASS PSIFPVGFCE INKIELTPPR
GYTKLPFKWF DYLRETGSIA APVKLFNKEV PNHGFRVGMK LEAVDLMEPR LVCVATVTRI
IHRLLRIHFD GWEDEYDQWV DCESSDLYPV GWCQLTGYQL QPPAPQSNKD SQSNISKQKK
KSKSQPYKGH KKITALQLKD EMLDGDDYTF LQGASDQESN GSGSYYIKQE P
