MTG16_MOUSE
ID MTG16_MOUSE Reviewed; 620 AA.
AC O54972; Q7TND6; Q8BZS0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Protein CBFA2T3;
DE AltName: Full=Eight twenty one protein 2;
DE AltName: Full=MTG8-related protein 2;
DE AltName: Full=Protein ETO-2;
GN Name=Cbfa2t3; Synonyms=Cbfa2t3h, Mtgr2;
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] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Spleen;
RX PubMed=10022820; DOI=10.1038/sj.onc.1202412;
RA Davis J.N., Williams B.J., Herron J.T., Galiano F.J., Meyers S.;
RT "ETO-2, a new member of the ETO-family of nuclear proteins.";
RL Oncogene 18:1375-1383(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cecum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 401-620 (ISOFORMS 1/2).
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND INTERACTION WITH HDAC1; HDAC2; HDAC3; HDAC6; HDAC8; NCOR1 AND
RP NCOR2.
RX PubMed=11533236; DOI=10.1128/mcb.21.19.6470-6483.2001;
RA Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N.,
RA Downing J.R., Meyers S., Hiebert S.W.;
RT "ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with
RT multiple histone deacetylases and binds mSin3A through its oligomerization
RT domain.";
RL Mol. Cell. Biol. 21:6470-6483(2001).
RN [5]
RP FUNCTION, INTERACTION WITH NCOR1, AND TISSUE SPECIFICITY.
RX PubMed=15231665; DOI=10.1158/0008-5472.can-03-3689;
RA Ibanez V., Sharma A., Buonamici S., Verma A., Kalakonda S., Wang J.,
RA Kadkol S., Saunthararajah Y.;
RT "AML1-ETO decreases ETO-2 (MTG16) interactions with nuclear receptor
RT corepressor, an effect that impairs granulocyte differentiation.";
RL Cancer Res. 64:4547-4554(2004).
RN [6]
RP FUNCTION, AND IDENTIFICATION IN TAL-1 COMPLEX.
RX PubMed=16407974; DOI=10.1038/sj.emboj.7600934;
RA Goardon N., Lambert J.A., Rodriguez P., Nissaire P., Herblot S.,
RA Thibault P., Dumenil D., Strouboulis J., Romeo P.-H., Hoang T.;
RT "ETO2 coordinates cellular proliferation and differentiation during
RT erythropoiesis.";
RL EMBO J. 25:357-366(2006).
RN [7]
RP INDUCTION.
RX PubMed=17533052; DOI=10.1016/j.exphem.2007.03.002;
RA Okumura A.J., Peterson L.F., Lo M.-C., Zhang D.-E.;
RT "Expression of AML/Runx and ETO/MTG family members during hematopoietic
RT differentiation of embryonic stem cells.";
RL Exp. Hematol. 35:978-988(2007).
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.
CC Reduces the protein levels and stability of the transcriptinal
CC regulator HIF1A; interacts with EGLN1 and promotes the HIF1A prolyl
CC hydroxylation-dependent ubiquitination and proteasomal degradation
CC pathway. Contributes to inhibition of glycolysis and stimulation of
CC mitochondrial respiration by down-regulating the expression of
CC glycolytic genes including PFKFB3, PFKFB4, PDK1, PFKP, LDHA and HK1
CC which are direct targets of HIF1A (By similarity). Regulates the
CC proliferation and the differentiation of erythroid progenitors by
CC repressing the expression of TAL1 target genes (PubMed:16407974). Plays
CC a role in granulocyte differentiation (PubMed:15231665).
CC {ECO:0000250|UniProtKB:O75081, ECO:0000269|PubMed:11533236,
CC ECO:0000269|PubMed:15231665, ECO:0000269|PubMed:16407974}.
CC -!- SUBUNIT: Heterodimer with RUNX1T1 and CBFA2T2. Interacts with ZNF652
CC and ERBB4. May interact with PRKAR2A, PDE7A and probably PDE4A.
CC Interacts with PLXNA1, PLXNA3 and PRKAR1A (By similarity). Interacts
CC with HDAC1, HDAC2, HDAC3, HDAC6, HDAC8, NCOR1 and NCOR2. Component of a
CC TAL-1 complex composed at least of CBFA2T3, LDB1, TAL1 and TCF3.
CC Interacts with ZBTB4, ZBTB38 and ZBTB33. Interacts with HIF1A and EGLN1
CC (By similarity). {ECO:0000250|UniProtKB:O75081,
CC ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:15231665,
CC ECO:0000269|PubMed:16407974}.
CC -!- INTERACTION:
CC O54972; P70662: Ldb1; NbExp=2; IntAct=EBI-8006703, EBI-6272082;
CC O54972; P22091: Tal1; NbExp=11; IntAct=EBI-8006703, EBI-8006437;
CC O54972; Q60722: Tcf4; NbExp=2; IntAct=EBI-8006703, EBI-310070;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10022820}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:10022820}. Golgi apparatus
CC membrane {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O54972-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O54972-2; Sequence=VSP_028626, VSP_028627;
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in heart,
CC brain, lung and spleen. Expressed in hematopoietic cells (at protein
CC level). {ECO:0000269|PubMed:10022820, ECO:0000269|PubMed:15231665}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis from 7 to 17 dpc.
CC {ECO:0000269|PubMed:10022820}.
CC -!- INDUCTION: Up-regulated during hematopoietic differentiation.
CC {ECO:0000269|PubMed:17533052}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC28426.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF038029; AAB92651.1; -; mRNA.
DR EMBL; AK033680; BAC28426.1; ALT_FRAME; mRNA.
DR EMBL; BC055951; AAH55951.1; -; mRNA.
DR CCDS; CCDS22744.1; -. [O54972-1]
DR CCDS; CCDS52696.1; -. [O54972-2]
DR RefSeq; NP_001103343.1; NM_001109873.1.
DR RefSeq; NP_033954.2; NM_009824.2.
DR RefSeq; NP_796263.1; NM_177289.1. [O54972-2]
DR AlphaFoldDB; O54972; -.
DR BMRB; O54972; -.
DR SMR; O54972; -.
DR BioGRID; 198523; 2.
DR IntAct; O54972; 5.
DR MINT; O54972; -.
DR STRING; 10090.ENSMUSP00000118997; -.
DR iPTMnet; O54972; -.
DR PhosphoSitePlus; O54972; -.
DR MaxQB; O54972; -.
DR PaxDb; O54972; -.
DR PRIDE; O54972; -.
DR ProteomicsDB; 290109; -. [O54972-1]
DR ProteomicsDB; 290110; -. [O54972-2]
DR Antibodypedia; 30813; 136 antibodies from 27 providers.
DR DNASU; 12398; -.
DR Ensembl; ENSMUST00000006525; ENSMUSP00000006525; ENSMUSG00000006362. [O54972-2]
DR GeneID; 12398; -.
DR KEGG; mmu:12398; -.
DR UCSC; uc009ntl.2; mouse. [O54972-1]
DR UCSC; uc009ntm.2; mouse. [O54972-2]
DR CTD; 863; -.
DR MGI; MGI:1338013; Cbfa2t3.
DR VEuPathDB; HostDB:ENSMUSG00000006362; -.
DR eggNOG; ENOG502QTD6; Eukaryota.
DR GeneTree; ENSGT00950000183176; -.
DR HOGENOM; CLU_022077_2_0_1; -.
DR InParanoid; O54972; -.
DR OrthoDB; 334242at2759; -.
DR BioGRID-ORCS; 12398; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Cbfa2t3; mouse.
DR PRO; PR:O54972; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; O54972; protein.
DR Bgee; ENSMUSG00000006362; Expressed in internal carotid artery and 189 other tissues.
DR ExpressionAtlas; O54972; baseline and differential.
DR Genevisible; O54972; MM.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0030851; P:granulocyte differentiation; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0045820; P:negative regulation of glycolytic process; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:1903715; P:regulation of aerobic respiration; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.20.120.1110; -; 1.
DR InterPro; IPR013289; CBFA2T1/2/3.
DR InterPro; IPR013292; CBFA2T3.
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 Pfam; PF08788; NHR2; 1.
DR Pfam; PF07531; TAFH; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR PRINTS; PR01875; ETOFAMILY.
DR PRINTS; PR01878; MTG16PROTEIN.
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 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Differentiation; Golgi apparatus;
KW Membrane; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..620
FT /note="Protein CBFA2T3"
FT /id="PRO_0000307174"
FT DOMAIN 146..241
FT /note="TAFH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00440"
FT ZN_FING 533..569
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 1..412
FT /note="Mediates localization to the nucleus"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..217
FT /note="Interaction with ZBTB33"
FT /evidence="ECO:0000250|UniProtKB:O75081"
FT REGION 151..243
FT /note="Interaction with HIF1A"
FT /evidence="ECO:0000250|UniProtKB:O75081"
FT REGION 256..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..389
FT /note="Nervy homology region 2 (NHR2); essential for down-
FT regulation of PFKFB3, PFKFB4 and PDK1 expression"
FT /evidence="ECO:0000250|UniProtKB:O75081"
FT REGION 419..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..510
FT /note="Nervy homology region 3 (NHR3); essential for down-
FT regulation of PFKFB3, PFKFB4 and PDK1 expression"
FT /evidence="ECO:0000250|UniProtKB:O75081"
FT REGION 462..483
FT /note="Mediates interaction with PRKAR2A"
FT /evidence="ECO:0000250"
FT REGION 577..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 465..520
FT /evidence="ECO:0000255"
FT COMPBIAS 49..64
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..620
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 533
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 536
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 544
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 547
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 553
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 557
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 565
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75081"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75081"
FT VAR_SEQ 1..35
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028626"
FT VAR_SEQ 76..101
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028627"
FT CONFLICT 150
FT /note="S -> N (in Ref. 1; AAB92651)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="S -> N (in Ref. 1; AAB92651)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 620 AA; 68032 MW; 78DC1995BE365E43 CRC64;
MSQASTTTLE SGALLSGPRG LQYGSPAHRK EKAAAMPDSP AEVKTQPRST PPSMPPPPPT
SSQGATRPPS FTPHTHGEDG PATSLPHGRF HGCLKWSMVC LLMNGSSHSP TAIHGAPSTP
NGFSNGPATS STASLSTQHL PPACGARQLS KLKRFLTTLQ QFGSDISPEI GERVRTLVLG
LVNSTLTIEE FHAKLQEATN FPLRPFVIPF LKANLPLLQR ELLHCARLAK QTPAQYLAQH
EQLLLDASAT SPVDSSELLL EVNENGKRRT PDRTKENGSD RDPLHPDHLS KRSCTLSPAQ
RCSPSNGLPH PTPPPPPHYR LEDMAMAHHF RDSYRHPDPR ELRERHRPLA IPGSRQEEVI
DHRLTEREWA EEWKHLNSLL NCIMDMVEKT RRSLTVLRRC QEADREELNH WIRCYSDSEE
GKKGPTPISA RSLNSCSGPE GSQLDVHRDF TPRTLSGYMP EEIWRKAEEA VNEVKRQAMS
ELQKAVSDAE RKAHELITTE RAKMERALAE AKRQASEDAL TVINQQEDSS ESCWNCGRKA
SETCSGCNAA RYCGSFCQHK DWEKHHHVCG QSLQGPAAAV ADPLPGQPDA TASPSEAGSA
GPSRPCSPGP PGPLDAAVPR
