ID   BRMS1_RAT               Reviewed;         246 AA.
AC   Q5M7T3;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Breast cancer metastasis-suppressor 1 homolog;
GN   Name=Brms1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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).
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: Homohexamer (Potential). Interacts with SNX6, HDAC1 and RELA.
CC       Interacts with ARID4A. Identified in mSin3A corepressor complexes
CC       together with SIN3A, SIN3B, RBBP4, RBBP7, SAP30, SUDS3, ARID4A, HDAC1
CC       and HDAC2. Interacts with SPOP; this recruits the protein to a
CC       ubiquitin ligase complex containing SPOP and CUL3 (By similarity).
CC       {ECO:0000250, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Note=Predominantly nuclear. {ECO:0000250}.
CC   -!- DOMAIN: Contains an N-terminal anti-parallel coiled coil formed by two
CC       BRMS1 chains; this region can form homohexamers. {ECO:0000250}.
CC   -!- PTM: Ubiquitinated by a cullin-RING-based BCR (BTB-CUL3-RBX1) E3
CC       ubiquitin-protein ligase complex containing SPOP, leading to
CC       proteasomal degradation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the BRMS1 family. {ECO:0000305}.
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DR   EMBL; BC088469; AAH88469.1; -; mRNA.
DR   RefSeq; NP_001009605.1; NM_001009605.1.
DR   RefSeq; XP_017445773.1; XM_017590284.1.
DR   AlphaFoldDB; Q5M7T3; -.
DR   SMR; Q5M7T3; -.
DR   STRING; 10116.ENSRNOP00000027258; -.
DR   jPOST; Q5M7T3; -.
DR   PaxDb; Q5M7T3; -.
DR   GeneID; 293668; -.
DR   KEGG; rno:293668; -.
DR   UCSC; RGD:1311057; rat.
DR   CTD; 25855; -.
DR   RGD; 1311057; Brms1.
DR   VEuPathDB; HostDB:ENSRNOG00000020117; -.
DR   eggNOG; KOG4466; Eukaryota.
DR   HOGENOM; CLU_050862_1_0_1; -.
DR   InParanoid; Q5M7T3; -.
DR   OMA; SEKHMAV; -.
DR   OrthoDB; 1456563at2759; -.
DR   PhylomeDB; Q5M7T3; -.
DR   TreeFam; TF323740; -.
DR   Reactome; R-RNO-3214815; HDACs deacetylate histones.
DR   PRO; PR:Q5M7T3; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000020117; Expressed in testis and 19 other tissues.
DR   Genevisible; Q5M7T3; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
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; ISO:RGD.
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; Coiled coil; Cytoplasm; Isopeptide bond; Nucleus;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Tumor suppressor; Ubl conjugation.
FT   CHAIN           1..246
FT                   /note="Breast cancer metastasis-suppressor 1 homolog"
FT                   /id="PRO_0000305307"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          51..98
FT                   /evidence="ECO:0000250"
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;  28306 MW;  2C9E5AFEC959A902 CRC64;
     MPIQPSGKET EEMEAEGDSA AEMNGEADES EEERSGSQTE SEEESSEMDD EDYERRRSEC
     VSEMLDLEKQ FSELKEKLFR ERLSQLRLRL EEVGAERAPE YTEPLGGLQQ SLKIRIQVAG
     IYKGFCLDVI RNKYECELQG AKQHLESEKL LLYDTLLGEL QERIQRLEED RQSLDISSEW
     WDDKLHSRGS SKTWDSVPPS KRKKAPLVSG PYIVYMLQEI DILEDWTAIK KARAAVSPQK
     RKADGP