ID   MTA3_BOVIN              Reviewed;         590 AA.
AC   A6QL72;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Metastasis-associated protein MTA3;
GN   Name=MTA3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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 (By
CC       similarity). {ECO:0000250|UniProtKB:Q924K8,
CC       ECO:0000250|UniProtKB:Q9BTC8}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512,
CC       ECO:0000255|PROSITE-ProRule:PRU00624}. Cytoplasm {ECO:0000250}.
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DR   EMBL; BC147861; AAI47862.1; -; mRNA.
DR   RefSeq; NP_001095434.1; NM_001101964.1.
DR   AlphaFoldDB; A6QL72; -.
DR   SMR; A6QL72; -.
DR   STRING; 9913.ENSBTAP00000033014; -.
DR   PaxDb; A6QL72; -.
DR   GeneID; 512854; -.
DR   KEGG; bta:512854; -.
DR   CTD; 57504; -.
DR   eggNOG; KOG3554; Eukaryota.
DR   InParanoid; A6QL72; -.
DR   OrthoDB; 802091at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0016581; C:NuRD complex; IBA:GO_Central.
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: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:0016575; P:histone deacetylation; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; IPR017930; Myb_dom.
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   Pfam; PF00249; Myb_DNA-binding; 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   2: Evidence at transcript level;
KW   Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..590
FT                   /note="Metastasis-associated protein MTA3"
FT                   /id="PRO_0000347221"
FT   DOMAIN          4..147
FT                   /note="BAH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT   DOMAIN          148..259
FT                   /note="ELM2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT   DOMAIN          266..318
FT                   /note="SANT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT   ZN_FING         378..402
FT                   /note="GATA-type; atypical"
FT   MOD_RES         429
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q924K8"
FT   MOD_RES         454
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTC8"
FT   MOD_RES         518
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTC8"
SQ   SEQUENCE   590 AA;  67207 MW;  7B8C660CB0F1F20C CRC64;
     MAANMYRVGD YVYFENSSSN PYLIRRIEEL NKTATGNVEA KVLCFYRRRD ISNTLIMLAD
     KHAKEIEEES ETTVEADLTD KQKHQLKHRE LFLSRQYESL PATHIRGKCS VALLNETESV
     LSYLDKEDTF FYSLVYDPSV KTLLADKGEI RVGPRYQADI PEMLLEGESD EREQSKLEVK
     VWDPNSPLTD RQIDQFLVVA RAVGTFARAL DCSSSVRQPS LHMSAAAASR DITLFHSMDT
     LYRHGYDLSS AISVLVPLGG PVLCRDEMEE WSASEASLFE EALEKYGKDF NDIRQDFLPW
     KSLTSIIEYY YMWKTTDRYV QQKRLKAAEA ESKLKQVYIP TYKPNPNQIS TSNGKPGAVN
     GAVGTTFQPQ NPLLGRACES CYATQSHQWY SWGPPNMQCR LCATCWLYWK KYGGLKMPTQ
     SEEEKLPPSP ATEDPRVRSH MSRQAMQGMP VRNTGSPKSA VNTRQAFFLH TTYFTKFARQ
     VCKNTLRLRQ AARRPFVPIN YAAIRAEYAD RHADLSGSPL KSKSTRKPLA CIIGYLEIHP
     SKKPNVIRST PSLQTPTTKR MLATPNHTSL SILGKRNYSH HNGLDERLMK