MTA3_MOUSE
ID MTA3_MOUSE Reviewed; 591 AA.
AC Q924K8; Q8VC18;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Metastasis-associated protein MTA3;
GN Name=Mta3;
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), AND SUBCELLULAR LOCATION.
RC STRAIN=129/Sv;
RX PubMed=11483358; DOI=10.1016/s0378-1119(01)00563-7;
RA Simpson A., Uitto J., Rodeck U., Mahoney M.G.;
RT "Differential expression and subcellular distribution of the mouse
RT metastasis-associated proteins Mta1 and Mta3.";
RL Gene 273:29-39(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425 AND SER-427, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP INTERACTION WITH PWWP2B.
RX PubMed=34180153; DOI=10.1002/advs.202102060;
RA Yan L., Jin W., Zhao Q., Cui X., Shi T., Xu Y., Li F., Jin W., Zhang Z.,
RA Zhang Z., Tang Q.Q., Pan D.;
RT "PWWP2B Fine-Tunes Adipose Thermogenesis by Stabilizing HDACs in a NuRD
RT Subcomplex.";
RL Adv. Sci. 8:e2102060-e2102060(2021).
RN [5]
RP STRUCTURE BY NMR OF 267-323.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the myb-like DNA-binding domain of mouse MTA3
RT protein.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Plays a role in maintenance of the normal epithelial
CC architecture through the repression of SNAI1 transcription in a histone
CC deacetylase-dependent manner, and thus the regulation of E-cadherin
CC levels. Contributes to transcriptional repression by BCL6 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the nucleosome-remodeling and histone-deacetylase
CC multiprotein complex (NuRD). Interacts with BCL6 (By similarity).
CC Interacts with NACC2 (By similarity). Interacts with PWWP2B
CC (PubMed:34180153). {ECO:0000250|UniProtKB:Q9BTC8,
CC ECO:0000269|PubMed:34180153}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512,
CC ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:11483358}.
CC Cytoplasm {ECO:0000269|PubMed:11483358}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q924K8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q924K8-2; Sequence=VSP_001605, VSP_001606;
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung, liver and
CC kidney.
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DR EMBL; AF288138; AAK83045.1; -; mRNA.
DR EMBL; BC022124; AAH22124.1; -; mRNA.
DR CCDS; CCDS28997.1; -. [Q924K8-1]
DR RefSeq; NP_001164525.1; NM_001171054.1.
DR RefSeq; NP_473423.1; NM_054082.2. [Q924K8-1]
DR PDB; 2CRG; NMR; -; A=267-323.
DR PDBsum; 2CRG; -.
DR AlphaFoldDB; Q924K8; -.
DR SMR; Q924K8; -.
DR BioGRID; 228046; 15.
DR ComplexPortal; CPX-953; MBD2/NuRD nucleosome remodeling and deacetylase complex.
DR ComplexPortal; CPX-954; MBD3/NuRD nucleosome remodeling and deacetylase complex.
DR CORUM; Q924K8; -.
DR DIP; DIP-61664N; -.
DR IntAct; Q924K8; 4.
DR STRING; 10090.ENSMUSP00000068931; -.
DR iPTMnet; Q924K8; -.
DR PhosphoSitePlus; Q924K8; -.
DR EPD; Q924K8; -.
DR jPOST; Q924K8; -.
DR MaxQB; Q924K8; -.
DR PaxDb; Q924K8; -.
DR PeptideAtlas; Q924K8; -.
DR PRIDE; Q924K8; -.
DR ProteomicsDB; 290067; -. [Q924K8-1]
DR ProteomicsDB; 290068; -. [Q924K8-2]
DR Antibodypedia; 29760; 274 antibodies from 28 providers.
DR DNASU; 116871; -.
DR Ensembl; ENSMUST00000067826; ENSMUSP00000068931; ENSMUSG00000055817. [Q924K8-1]
DR GeneID; 116871; -.
DR KEGG; mmu:116871; -.
DR UCSC; uc012axw.1; mouse. [Q924K8-1]
DR CTD; 57504; -.
DR MGI; MGI:2151172; Mta3.
DR VEuPathDB; HostDB:ENSMUSG00000055817; -.
DR eggNOG; KOG3554; Eukaryota.
DR GeneTree; ENSGT01030000234573; -.
DR InParanoid; Q924K8; -.
DR OMA; GPAHMQC; -.
DR OrthoDB; 802091at2759; -.
DR PhylomeDB; Q924K8; -.
DR TreeFam; TF106444; -.
DR Reactome; R-MMU-3214815; HDACs deacetylate histones.
DR Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
DR BioGRID-ORCS; 116871; 4 hits in 78 CRISPR screens.
DR ChiTaRS; Mta3; mouse.
DR EvolutionaryTrace; Q924K8; -.
DR PRO; PR:Q924K8; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q924K8; protein.
DR Bgee; ENSMUSG00000055817; Expressed in placenta labyrinth and 251 other tissues.
DR ExpressionAtlas; Q924K8; baseline and differential.
DR Genevisible; Q924K8; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016581; C:NuRD complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0042826; F:histone deacetylase binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0120325; F:NuRD complex binding; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:1990739; P:granulosa cell proliferation; IMP:MGI.
DR GO; GO:0016575; P:histone deacetylation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:1904197; P:positive regulation of granulosa cell proliferation; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0042659; P:regulation of cell fate specification; IC:ComplexPortal.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IC:ComplexPortal.
DR CDD; cd00202; ZnF_GATA; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR000949; ELM2_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR040138; MIER/MTA.
DR InterPro; IPR035170; MTA1_R1.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR000679; Znf_GATA.
DR PANTHER; PTHR10865; PTHR10865; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF01448; ELM2; 1.
DR Pfam; PF00320; GATA; 1.
DR Pfam; PF17226; MTA_R1; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM01189; ELM2; 1.
DR SMART; SM00717; SANT; 1.
DR SMART; SM00401; ZnF_GATA; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS51293; SANT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; DNA-binding; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..591
FT /note="Metastasis-associated protein MTA3"
FT /id="PRO_0000083499"
FT DOMAIN 1..147
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT DOMAIN 148..258
FT /note="ELM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT DOMAIN 265..317
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT ZN_FING 377..404
FT /note="GATA-type; atypical"
FT REGION 417..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 452
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTC8"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTC8"
FT VAR_SEQ 506..512
FT /note="YADRHAE -> CKTLFNS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_001605"
FT VAR_SEQ 513..591
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_001606"
FT CONFLICT 166
FT /note="E -> EG (in Ref. 2; AAH22124)"
FT /evidence="ECO:0000305"
FT HELIX 272..284
FT /evidence="ECO:0007829|PDB:2CRG"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:2CRG"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:2CRG"
FT HELIX 302..313
FT /evidence="ECO:0007829|PDB:2CRG"
SQ SEQUENCE 591 AA; 67077 MW; ABA5CB9E86FCE7E2 CRC64;
MAANMYRVGD YVYFENSSSN PYLIRRIEEL NKTASGNVEA KVVCFYRRRD ISNTLIMLAD
KHAKETEEES ETPVEADLTE KQKHQLKHRE LFLSRQYESL PATHIRGKCS VALLNETESV
LSYLDKEDTF FYSLVYDPSV KTLLADKGEI RVGPKYQADI PDMLPEDSDE REQSKLEVKV
WDPNSPLTDR QIDQFLVVAR AVGTFARALD CSSSVRQPSL HMSAAAASRD ITLFHAMDTL
YRHGYDLSSA ISVLVPLGGP VLCRDEMEEW SASEACLFEE ALEKYGKDFN DIRQDFLPWK
SLTSIIEYYY MWKTTDRYVQ QKRLKAAEAE SKLKQVYIPT YKPNPNQISS SNGKAGTVNG
AVGTQFQPQS ALLGRACESC YATQSHQWYS WGPPNMQCRL CATCWLYWKK YGGLKMPTQS
DEEKSPSPTA EDPRARSHMS RQALQGMPVR NTGSPKSAVK TRQAFFLRTT YFTKIARQVC
KSTLRLRQAA RRPFVAINYA AIRAEYADRH AELSGSPLKS RSTRKPLSCI IGYLEIHPAK
KPNVIRSPPS LQTPATKRML AAPNHTSLSI LGKRNYSHHN GLDGPERWLS R
