ID   SMRD2_BOVIN             Reviewed;         531 AA.
AC   E1BJD1;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2;
DE   AltName: Full=60 kDa BRG-1/Brm-associated factor subunit B;
DE   AltName: Full=BRG1-associated factor 60B;
DE            Short=BAF60B;
GN   Name=SMARCD2;
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 GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19390049; DOI=10.1126/science.1169588;
RG   The bovine genome sequencing and analysis consortium;
RT   "The genome sequence of taurine cattle: a window to ruminant biology and
RT   evolution.";
RL   Science 324:522-528(2009).
CC   -!- FUNCTION: Involved in transcriptional activation and repression of
CC       select genes by chromatin remodeling (alteration of DNA-nucleosome
CC       topology). Component of SWI/SNF chromatin remodeling complexes that
CC       carry out key enzymatic activities, changing chromatin structure by
CC       altering DNA-histone contacts within a nucleosome in an ATP-dependent
CC       manner. Critical regulator of myeloid differentiation, controlling
CC       granulocytopoiesis and the expression of genes involved in neutrophil
CC       granule formation. {ECO:0000250|UniProtKB:Q92925}.
CC   -!- SUBUNIT: Component of the multiprotein chromatin-remodeling complexes
CC       SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The
CC       canonical complex contains a catalytic subunit (either
CC       SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B), and at least SMARCE1,
CC       ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47.
CC       Other subunits specific to each of the complexes may also be present
CC       permitting several possible combinations developmentally and tissue
CC       specific. Component of the BAF complex, which includes at least actin
CC       (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM, SMARCA4/BRG1,
CC       ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155,
CC       SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A,
CC       SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex
CC       also contains DPF3. Component of the SWI/SNF-B (PBAF) chromatin
CC       remodeling complex, at least composed of SMARCA4/BRG1,
CC       SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57,
CC       SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155,
CC       SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin (ACTB). Interacts
CC       with UNKL. Interacts with CEBPE. {ECO:0000250|UniProtKB:Q92925}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92925}.
CC   -!- PTM: Ubiquitinated through a signaling process involving RAC1 and the
CC       RING finger protein UNKL. {ECO:0000250|UniProtKB:Q92925}.
CC   -!- SIMILARITY: Belongs to the SMARCD family. {ECO:0000305}.
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DR   EMBL; AAFC03085035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001192391.1; NM_001205462.2.
DR   AlphaFoldDB; E1BJD1; -.
DR   SMR; E1BJD1; -.
DR   STRING; 9913.ENSBTAP00000028049; -.
DR   PaxDb; E1BJD1; -.
DR   PRIDE; E1BJD1; -.
DR   Ensembl; ENSBTAT00000028049; ENSBTAP00000028049; ENSBTAG00000021062.
DR   GeneID; 789613; -.
DR   KEGG; bta:789613; -.
DR   CTD; 6603; -.
DR   VEuPathDB; HostDB:ENSBTAG00000021062; -.
DR   VGNC; VGNC:34994; SMARCD2.
DR   eggNOG; KOG2570; Eukaryota.
DR   GeneTree; ENSGT00940000158654; -.
DR   HOGENOM; CLU_023529_0_2_1; -.
DR   InParanoid; E1BJD1; -.
DR   OMA; LMGIWEY; -.
DR   OrthoDB; 1027566at2759; -.
DR   TreeFam; TF106486; -.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000021062; Expressed in parenchyma of mammary gland and 107 other tissues.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016514; C:SWI/SNF complex; IBA:GO_Central.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0006337; P:nucleosome disassembly; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.245.10; -; 1.
DR   InterPro; IPR030090; BAF60B.
DR   InterPro; IPR019835; SWIB_domain.
DR   InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR   InterPro; IPR003121; SWIB_MDM2_domain.
DR   PANTHER; PTHR13844:SF2; PTHR13844:SF2; 1.
DR   Pfam; PF02201; SWIB; 1.
DR   SMART; SM00151; SWIB; 1.
DR   SUPFAM; SSF47592; SSF47592; 1.
DR   PROSITE; PS51925; SWIB_MDM2; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..531
FT                   /note="SWI/SNF-related matrix-associated actin-dependent
FT                   regulator of chromatin subfamily D member 2"
FT                   /id="PRO_0000404203"
FT   DOMAIN          306..383
FT                   /note="SWIB/MDM2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01273"
FT   REGION          205..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         81
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92925"
FT   MOD_RES         104
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92925"
FT   MOD_RES         203
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92925"
FT   MOD_RES         217
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92925"
FT   CROSSLNK        226
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q92925"
SQ   SEQUENCE   531 AA;  58968 MW;  D7A23E3A43CDB59C CRC64;
     MSGRGAGGFP LPPLSPGGGA VAAALGAPPP PAGPGMLPGP ALRGPGPAGG VGGPGAAAFR
     PMGPAGPAAQ YQRPGMSPGS RMPMAGLQVG PPAGSPFGTA APLRPGMPPT MMDPFRKRLL
     VPQAQPPMPA QRRGLKRRKM ADKVLPQRIR ELVPESQAYM DLLAFERKLD QTIARKRMEI
     QEAIKKPLTQ KRKLRIYISN TFSPSKAEGD TAGTTGTPGG TPAGDKVASW ELRVEGKLLD
     DPSKQKRKFS SFFKSLVIEL DKELYGPDNH LVEWHRMPTT QETDGFQVKR PGDLNVKCTL
     LLMLDHQPPQ YKLDPRLARL LGVHTQTRAA IMQALWLYIK HNQLQDGHER EYINCNRYFR
     QIFSCGRLRF SEIPMKLAGL LQHPDPIVIN HVISVDPNDQ KKTACYDIDV EVDDPLKAQM
     SNFLASTTNQ QEIASLDVKI HETIESINQL KTQRDFMLSF STDPQDFIQE WLRSQRRDLK
     IITDVIGNPE EERRAAFYHQ PWAQEAVGRH IFAKVQQRRQ ELEQVLGIRL T