SMRD1_BOVIN
ID SMRD1_BOVIN Reviewed; 515 AA.
AC Q2TBN1;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1;
DE AltName: Full=60 kDa BRG-1/Brm-associated factor subunit A;
DE AltName: Full=BRG1-associated factor 60A;
DE Short=BAF60A;
DE AltName: Full=SWI/SNF complex 60 kDa subunit;
GN Name=SMARCD1; Synonyms=BAF60A;
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=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Belongs to the neural progenitors-specific
CC chromatin remodeling complex (npBAF complex) and the neuron-specific
CC chromatin remodeling complex (nBAF complex). During neural development
CC a switch from a stem/progenitor to a postmitotic chromatin remodeling
CC mechanism occurs as neurons exit the cell cycle and become committed to
CC their adult state. The transition from proliferating neural
CC stem/progenitor cells to postmitotic neurons requires a switch in
CC subunit composition of the npBAF and nBAF complexes. As neural
CC progenitors exit mitosis and differentiate into neurons, npBAF
CC complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged
CC for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C
CC subunits in neuron-specific complexes (nBAF). The npBAF complex is
CC essential for the self-renewal/proliferative capacity of the
CC multipotent neural stem cells. The nBAF complex along with CREST plays
CC a role regulating the activity of genes essential for dendrite growth
CC (By similarity). Has a strong influence on vitamin D-mediated
CC transcriptional activity from an enhancer vitamin D receptor element
CC (VDRE). May be a link between mammalian SWI-SNF-like chromatin
CC remodeling complexes and the vitamin D receptor (VDR) heterodimer.
CC Mediates critical interactions between nuclear receptors and the
CC BRG1/SMARCA4 chromatin-remodeling complex for transactivation (By
CC similarity). Interacts with AKIRIN2 (By similarity).
CC {ECO:0000250|UniProtKB:Q61466, ECO:0000250|UniProtKB:Q96GM5}.
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,
CC SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57,
CC SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more
CC SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C (By similarity). In
CC muscle cells, the BAF complex also contains DPF3. Component of neural
CC progenitors-specific chromatin remodeling complex (npBAF complex)
CC composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A,
CC SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A,
CC SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170,
CC PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific
CC chromatin remodeling complex (nBAF complex) composed of at least,
CC ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
CC SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
CC SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B,
CC DPF3/BAF45C, ACTL6B/BAF53B and actin (By similarity). Component of the
CC SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of
CC SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B,
CC SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C,
CC SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin
CC (ACTB). Component of SWI/SNF (GBAF) subcomplex, which includes at least
CC BICRA or BICRAL (mutually exclusive), BRD9, SS18, SMARCA2/BRM,
CC SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, SMARCC1/BAF155, and SMARCD1/BAF60A.
CC Specifically interacts with the VDR heterodimer complex. Interacts with
CC ESR1, NR3C1, NR1H4, PGR, SMARCA4, SMARCC1 and SMARCC2 (By similarity).
CC Interacts with DPF2. Interacts with FOS, FOSB, FOSL1 and FOSL2 (By
CC similarity). {ECO:0000250|UniProtKB:Q61466,
CC ECO:0000250|UniProtKB:Q96GM5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SMARCD family. {ECO:0000305}.
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DR EMBL; BC109890; AAI09891.1; -; mRNA.
DR RefSeq; NP_001033648.1; NM_001038559.2.
DR AlphaFoldDB; Q2TBN1; -.
DR SMR; Q2TBN1; -.
DR STRING; 9913.ENSBTAP00000001284; -.
DR PaxDb; Q2TBN1; -.
DR PRIDE; Q2TBN1; -.
DR GeneID; 533232; -.
DR KEGG; bta:533232; -.
DR CTD; 6602; -.
DR eggNOG; KOG2570; Eukaryota.
DR InParanoid; Q2TBN1; -.
DR OrthoDB; 1027566at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0071565; C:nBAF complex; ISS:UniProtKB.
DR GO; GO:0071564; C:npBAF complex; ISS:UniProtKB.
DR GO; GO:0016514; C:SWI/SNF complex; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR Gene3D; 1.10.245.10; -; 1.
DR InterPro; IPR038041; SMARCD1.
DR InterPro; IPR019835; SWIB_domain.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR PANTHER; PTHR13844:SF1; PTHR13844:SF1; 1.
DR Pfam; PF02201; SWIB; 1.
DR SMART; SM00151; SWIB; 1.
DR SUPFAM; SSF47592; SSF47592; 1.
DR PROSITE; PS51925; SWIB_MDM2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chromatin regulator; Coiled coil; Isopeptide bond;
KW Methylation; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..515
FT /note="SWI/SNF-related matrix-associated actin-dependent
FT regulator of chromatin subfamily D member 1"
FT /id="PRO_0000375224"
FT DOMAIN 290..367
FT /note="SWIB/MDM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01273"
FT REGION 1..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..167
FT /note="Interaction with ESR1, NR1H4, NR3C1, PGR and
FT SMARCA4"
FT /evidence="ECO:0000250"
FT REGION 168..474
FT /note="Interaction with SMARCC1 and SMARCC2"
FT /evidence="ECO:0000250"
FT REGION 180..515
FT /note="Necessary for GR/NR3C1-mediated remodeling and
FT transcription from chromatin; required for GR/NR3C1
FT interaction with the BRG1/SMARCA4 complex in vivo"
FT /evidence="ECO:0000250"
FT COILED 412..440
FT /evidence="ECO:0000255"
FT COMPBIAS 99..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 68
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q92925"
FT MOD_RES 88
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61466"
FT MOD_RES 203
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92925"
FT MOD_RES 223
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61466"
FT CROSSLNK 101
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96GM5"
SQ SEQUENCE 515 AA; 58252 MW; FB1D081C18C5D729 CRC64;
MAARAGFQSV APSGGAGASG GAGAAAALGP GGTPGPPVRM GPAPGQGLYR SPMPGAAYPR
PGMLPGSRMT PQGPSMGPPG YGGNPSVRPG LAQSGMDQSL KRPAPQQIKQ VQQQAVQNRN
HNAKKKKMAD KILPQRIREL VPESQDYMDL LAFERKLDQT IMRKRLDIQE ALKRPIKQKR
KLRIFISNTF NPAKSDAEDG EGTVASWELR VEGRLLEDSA LSKYDATKQK RKFSSFFKSL
VIELDKDLYG PDNHLVEWHR TATTQETDGF QVKRPGDVNV RCTVLLMLDY QPPQFKLDPR
LARLLGIHTQ TRPVIIQALW QYIKTHKLQD PHEREFVICD KYLQQIFESQ RMKFSEIPQR
LHALLMPPEP IIINHVISVD PNDQKKTACY DIDEEVDDTL KTQMNSFLLS TASQQEIATL
DNKIHETIET INQLKTQREF MLSFARDPQG FINDWLQSQC RDLKVMTDVV GNSEEERRAE
FYFQPWAQEA VCRYFYSKVQ QRRQELEQAL GIRNT
