ID   BRMS1_BOVIN             Reviewed;         246 AA.
AC   Q1LZE0;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Breast cancer metastasis-suppressor 1 homolog;
GN   Name=BRMS1;
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=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcriptional repressor. Down-regulates transcription
CC       activation by NF-kappa-B by promoting the deacetylation of RELA at
CC       'Lys-310'. Promotes HDAC1 binding to promoter regions. Down-regulates
CC       expression of anti-apoptotic genes that are controlled by NF-kappa-B.
CC       Promotes apoptosis in cells that have inadequate adherence to a
CC       substrate, a process called anoikis, and may thereby inhibit metastasis
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with SNX6, HDAC1 and RELA. Interacts with ARID4A.
CC       Identified in mSin3A corepressor complexes together with SIN3A, SIN3B,
CC       RBBP4, RBBP7, SAP30, SUDS3, ARID4A, HDAC1 and HDAC2 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Note=Predominantly nuclear. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the BRMS1 family. {ECO:0000305}.
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DR   EMBL; BC116061; AAI16062.1; -; mRNA.
DR   RefSeq; NP_001069872.1; NM_001076404.1.
DR   AlphaFoldDB; Q1LZE0; -.
DR   SMR; Q1LZE0; -.
DR   STRING; 9913.ENSBTAP00000023526; -.
DR   PaxDb; Q1LZE0; -.
DR   PRIDE; Q1LZE0; -.
DR   Ensembl; ENSBTAT00000023526; ENSBTAP00000023526; ENSBTAG00000017689.
DR   GeneID; 615952; -.
DR   KEGG; bta:615952; -.
DR   CTD; 25855; -.
DR   VEuPathDB; HostDB:ENSBTAG00000017689; -.
DR   VGNC; VGNC:54781; BRMS1.
DR   eggNOG; KOG4466; Eukaryota.
DR   GeneTree; ENSGT00940000161779; -.
DR   HOGENOM; CLU_050862_1_0_1; -.
DR   InParanoid; Q1LZE0; -.
DR   OMA; SEKHMAV; -.
DR   OrthoDB; 1456563at2759; -.
DR   TreeFam; TF323740; -.
DR   Reactome; R-BTA-3214815; HDACs deacetylate histones.
DR   Proteomes; UP000009136; Chromosome 29.
DR   Bgee; ENSBTAG00000017689; Expressed in ruminant reticulum and 107 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0070822; C:Sin3-type complex; IBA:GO_Central.
DR   GO; GO:0042826; F:histone deacetylase binding; IBA:GO_Central.
DR   GO; GO:0051059; F:NF-kappaB binding; IEA:Ensembl.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR   GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:2000210; P:positive regulation of anoikis; ISS:UniProtKB.
DR   GO; GO:0090312; P:positive regulation of protein deacetylation; ISS:UniProtKB.
DR   GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR   InterPro; IPR013907; Sds3.
DR   PANTHER; PTHR21964; PTHR21964; 1.
DR   Pfam; PF08598; Sds3; 1.
DR   SMART; SM01401; Sds3; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Cytoplasm; Isopeptide bond; Nucleus; Reference proteome;
KW   Repressor; Transcription; Transcription regulation; Tumor suppressor;
KW   Ubl conjugation.
FT   CHAIN           1..246
FT                   /note="Breast cancer metastasis-suppressor 1 homolog"
FT                   /id="PRO_0000305306"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..49
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        184
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HCU9"
FT   CROSSLNK        242
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q5PSV4"
SQ   SEQUENCE   246 AA;  28460 MW;  EEA8F4A2C859AD17 CRC64;
     MPVQPPSKDT EEMEAEGDSA AEMNGEEEES EEERSGSQTE SEEESSEMDE EDCERRRSEC
     VSEMMDLEKQ FSELKEKLFR ERLSQLRVRL EEVGAERAPE YTEPLGGLQR SLKIRIQVAG
     IYKGFCLDVI RNKYECELQG AKQHLESEKL LLYDTLQGEL QERIQRLEED RQSLDISSEW
     WDDKLHARGS SRTWDSLPPN KRKKAPLVSG PYIVYMLQEI DILEDWTAIK KARAAVSPQK
     RKSDGP