MTG8_MOUSE
ID MTG8_MOUSE Reviewed; 577 AA.
AC Q61909;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Protein CBFA2T1;
DE AltName: Full=Protein MTG8;
GN Name=Runx1t1; Synonyms=Cbfa2t1, Cbfa2t1h, Mtg8;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=8575770; DOI=10.1006/geno.1995.9941;
RA Niwa-Kawakita M., Miyoshi H., Gotoh O., Matsushima Y., Nishimura M.,
RA Shisa H., Ohki M.;
RT "Cloning and gene mapping of the mouse homologue of the CBFA2T1 gene
RT associated with human acute myeloid leukemia.";
RL Genomics 29:755-759(1995).
RN [2]
RP FUNCTION.
RX PubMed=23527555; DOI=10.1111/febs.12256;
RA Wang S.S., Huang H.Y., Chen S.Z., Li X., Zhang W.T., Tang Q.Q.;
RT "Gdf6 induces commitment of pluripotent mesenchymal C3H10T1/2 cells to the
RT adipocyte lineage.";
RL FEBS J. 280:2644-2651(2013).
CC -!- FUNCTION: Transcriptional corepressor which facilitates transcriptional
CC repression via its association with DNA-binding transcription factors
CC and recruitment of other corepressors and histone-modifying enzymes.
CC Can repress the expression of MMP7 in a ZBTB33-dependent manner. Can
CC repress transactivation mediated by TCF12 (By similarity). Acts as a
CC negative regulator of adipogenesis (PubMed:23527555).
CC {ECO:0000250|UniProtKB:Q06455, ECO:0000269|PubMed:23527555}.
CC -!- SUBUNIT: Homotetramer (By similarity). Heterotetramer with CBFA2T2 and
CC CBFA2T3 (By similarity). Interacts with TCF12, SIN3A, HDAC1, HDAC2,
CC HDAC3, NCOR1 and NCOR2. Interacts with ATN1 (via its N-terminus); the
CC interaction enhances the transcriptional repression (By similarity).
CC {ECO:0000250|UniProtKB:Q06455}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00440}.
CC Note=Colocalizes with ATN1 in discrete nuclear dots. {ECO:0000250}.
CC -!- DOMAIN: The TAFH domain mediates interaction with transcription
CC regulators. {ECO:0000250|UniProtKB:Q06455}.
CC -!- DOMAIN: Nervy homology region 2 (NHR2) mediates homo- and possibly
CC heterotypic oligomerization by forming a four-helix bundle tetrameric
CC structure. {ECO:0000250|UniProtKB:Q06455}.
CC -!- SIMILARITY: Belongs to the CBFA2T family. {ECO:0000305}.
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DR EMBL; D32007; BAA06774.1; -; mRNA.
DR CCDS; CCDS17978.1; -.
DR RefSeq; NP_033952.1; NM_009822.3.
DR AlphaFoldDB; Q61909; -.
DR BMRB; Q61909; -.
DR SMR; Q61909; -.
DR BioGRID; 198520; 7.
DR IntAct; Q61909; 9.
DR MINT; Q61909; -.
DR STRING; 10090.ENSMUSP00000006761; -.
DR iPTMnet; Q61909; -.
DR PhosphoSitePlus; Q61909; -.
DR MaxQB; Q61909; -.
DR PaxDb; Q61909; -.
DR PRIDE; Q61909; -.
DR ProteomicsDB; 286073; -.
DR Antibodypedia; 25672; 283 antibodies from 34 providers.
DR DNASU; 12395; -.
DR Ensembl; ENSMUST00000098256; ENSMUSP00000095856; ENSMUSG00000006586.
DR GeneID; 12395; -.
DR KEGG; mmu:12395; -.
DR UCSC; uc008sax.3; mouse.
DR CTD; 862; -.
DR MGI; MGI:104793; Runx1t1.
DR VEuPathDB; HostDB:ENSMUSG00000006586; -.
DR eggNOG; ENOG502QTD6; Eukaryota.
DR GeneTree; ENSGT00950000183176; -.
DR HOGENOM; CLU_022077_2_0_1; -.
DR InParanoid; Q61909; -.
DR OMA; SFQNRRH; -.
DR OrthoDB; 334242at2759; -.
DR BioGRID-ORCS; 12395; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Runx1t1; mouse.
DR PRO; PR:Q61909; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q61909; protein.
DR Bgee; ENSMUSG00000006586; Expressed in rostral migratory stream and 239 other tissues.
DR ExpressionAtlas; Q61909; baseline and differential.
DR Genevisible; Q61909; MM.
DR GO; GO:0016363; C:nuclear matrix; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0017053; C:transcription repressor complex; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0045444; P:fat cell differentiation; IDA:MGI.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0051101; P:regulation of DNA binding; IDA:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.20.120.1110; -; 1.
DR InterPro; IPR013290; CBFA2T1.
DR InterPro; IPR013289; CBFA2T1/2/3.
DR InterPro; IPR014896; NHR2.
DR InterPro; IPR037249; TAFH/NHR1_dom_sf.
DR InterPro; IPR003894; TAFH_NHR1.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR10379; PTHR10379; 1.
DR PANTHER; PTHR10379:SF5; PTHR10379:SF5; 1.
DR Pfam; PF08788; NHR2; 1.
DR Pfam; PF07531; TAFH; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR PRINTS; PR01875; ETOFAMILY.
DR PRINTS; PR01876; MTG8PROTEIN.
DR SMART; SM00549; TAFH; 1.
DR SUPFAM; SSF158553; SSF158553; 1.
DR PROSITE; PS51119; TAFH; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..577
FT /note="Protein CBFA2T1"
FT /id="PRO_0000218300"
FT DOMAIN 93..188
FT /note="TAFH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00440"
FT ZN_FING 488..524
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..356
FT /note="Important for oligomerization"
FT /evidence="ECO:0000250"
FT REGION 310..356
FT /note="Nervy homology region 2 (NHR2)"
FT /evidence="ECO:0000250|UniProtKB:Q06455"
FT REGION 374..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..465
FT /note="Nervy homology region 3 (NHR3)"
FT /evidence="ECO:0000250|UniProtKB:Q06455"
FT REGION 529..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 488
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 491
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 499
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 502
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 508
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 512
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 520
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 524
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06455"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06455"
SQ SEQUENCE 577 AA; 64338 MW; 2656F185318C4B11 CRC64;
MPDRTEKHST MPDSPVDVKT QSRLTPPAMP PPPTTQGAPR TSSFTPTTLT NGTSHSPTAL
NGAPSPPNGF SNGPSSSSSS SLANQQLPPA CGARQLSKLK RFLTTLQQFG NDISPEIGER
VRTLVLGLVN STLTIEEFHS KLQEATNFPL RPFVIPFLKA NLPLLQRELL HCARLAKQNP
AQYLAQHEQL LLDASTTSPV DSSELLLDVN ENGKRRTPDR TKENGFDREP LHSEHPSKRP
CTISPGQRYS PNNGLSYQPN GLPHPTPPPP QHYRLDDMAI AHHYRDSYRH PSHRDLRDRN
RPMGLHGTRQ EEMIDHRLTD REWAEEWKHL DHLLNCIMDM VEKTRRSLTV LRRCQEADRE
ELNYWIRRYS DAEDLKKGGS SSSSHSRQQS PVNPDPVALD AHREFLHRPA SGYVPEEIWK
KAEEAVNEVK RQAMTELQKA VSEAERKAHD MITTERAKME RTVAEAKRQA AEDALAVINQ
QEDSSESCWN CGRKASETCS GCNTARYCGS FCQHKDWEKH HHICGQTLQA PQQGDTPAVS
SSVTPSSGAG SPMDTPPAAT PRSTTPGTPS TIETTPR
