ID SMCE1_RAT Reviewed; 376 AA.
AC Q56A18; C0IMX4; C0IMX5; C0IMX6; Q5BJV2;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;
DE AltName: Full=BRG1-associated factor 57;
DE Short=BAF57;
GN Name=Smarce1; Synonyms=Baf57;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-142 (ISOFORMS 1; 3 AND 4).
RC TISSUE=Brain;
RX PubMed=19245665; DOI=10.1111/j.1471-4159.2009.06005.x;
RA Kazantseva A., Sepp M., Kazantseva J., Sadam H., Pruunsild P., Timmusk T.,
RA Neuman T., Palm K.;
RT "N-terminally truncated BAF57 isoforms contribute to the diversity of
RT SWI/SNF complexes in neurons.";
RL J. Neurochem. 109:807-818(2009).
RN [3]
RP INTERACTION WITH BRDT.
RX PubMed=22215678; DOI=10.1074/jbc.m111.288167;
RA Dhar S., Thota A., Rao M.R.;
RT "Insights into role of bromodomain, testis-specific (Brdt) in acetylated
RT histone H4-dependent chromatin remodeling in mammalian spermiogenesis.";
RL J. Biol. Chem. 287:6387-6405(2012).
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. Belongs to the neural progenitors-specific chromatin remodeling
CC complex (npBAF complex) and the neuron-specific chromatin remodeling
CC complex (nBAF complex). During neural development a switch from a
CC stem/progenitor to a postmitotic chromatin remodeling mechanism occurs
CC as neurons exit the cell cycle and become committed to their adult
CC state. The transition from proliferating neural stem/progenitor cells
CC to postmitotic neurons requires a switch in subunit composition of the
CC npBAF and nBAF complexes. As neural progenitors exit mitosis and
CC differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A
CC and PHF10/BAF45A, are exchanged for homologous alternative
CC ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-
CC specific complexes (nBAF). The npBAF complex is essential for the self-
CC renewal/proliferative capacity of the multipotent neural stem cells.
CC The nBAF complex along with CREST plays a role regulating the activity
CC of genes essential for dendrite growth (By similarity). Required for
CC the coactivation of estrogen responsive promoters by SWI/SNF complexes
CC and the SRC/p160 family of histone acetyltransferases (HATs). Also
CC specifically interacts with the CoREST corepressor resulting in
CC repression of neuronal specific gene promoters in non-neuronal cells
CC (By similarity). {ECO:0000250|UniProtKB:O54941,
CC ECO:0000250|UniProtKB:Q969G3}.
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/BAF190B,
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. In muscle cells, the
CC BAF complex also contains DPF3. Component of neural progenitors-
CC specific chromatin remodeling complex (npBAF complex) composed of at
CC 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. May be a 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) (By similarity). Interacts with BRDT (PubMed:22215678). Also
CC binds to the SRC/p160 family of histone acetyltransferases (HATs)
CC composed of NCOA1, NCOA2, and NCOA3. Interacts with RCOR1/CoREST, NR3C1
CC and ZMIM2/ZIMP7 (By similarity). {ECO:0000250|UniProtKB:O54941,
CC ECO:0000250|UniProtKB:Q969G3, ECO:0000269|PubMed:22215678}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q56A18-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q56A18-2; Sequence=VSP_044513, VSP_044516;
CC Name=3;
CC IsoId=Q56A18-3; Sequence=VSP_044514;
CC Name=4;
CC IsoId=Q56A18-4; Sequence=VSP_044515;
CC -!- DOMAIN: The HMG domain is essential for CD4 silencing and CD8
CC activation; mutation of this domain blocks thymus development.
CC {ECO:0000250|UniProtKB:O54941}.
CC -!- PTM: Ubiquitinated by TRIP12, leading to its degradation by the
CC proteasome. Ubiquitination is prevented upon interaction between TRIP12
CC and SMARCC1 (By similarity). {ECO:0000250|UniProtKB:Q969G3}.
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DR EMBL; BC091314; AAH91314.1; -; mRNA.
DR EMBL; BC092210; AAH92210.1; -; mRNA.
DR EMBL; EU327027; ACA81401.1; -; mRNA.
DR EMBL; EU327028; ACA81402.1; -; mRNA.
DR EMBL; EU327029; ACA81403.1; -; mRNA.
DR EMBL; EU327030; ACA81404.1; -; mRNA.
DR EMBL; EU327031; ACA81405.1; -; mRNA.
DR RefSeq; NP_001020164.1; NM_001024993.1. [Q56A18-1]
DR AlphaFoldDB; Q56A18; -.
DR SMR; Q56A18; -.
DR BioGRID; 257563; 2.
DR STRING; 10116.ENSRNOP00000014230; -.
DR iPTMnet; Q56A18; -.
DR PhosphoSitePlus; Q56A18; -.
DR jPOST; Q56A18; -.
DR PaxDb; 10116-ENSRNOP00000014230; -.
DR PeptideAtlas; Q56A18; -.
DR Ensembl; ENSRNOT00000014230.8; ENSRNOP00000014230.7; ENSRNOG00000010676.8. [Q56A18-1]
DR Ensembl; ENSRNOT00055057573; ENSRNOP00055047465; ENSRNOG00055033308. [Q56A18-1]
DR Ensembl; ENSRNOT00060038207; ENSRNOP00060031493; ENSRNOG00060021983. [Q56A18-1]
DR Ensembl; ENSRNOT00065045922; ENSRNOP00065037686; ENSRNOG00065026498. [Q56A18-1]
DR GeneID; 303518; -.
DR KEGG; rno:303518; -.
DR UCSC; RGD:1304726; rat.
DR AGR; RGD:1304726; -.
DR CTD; 6605; -.
DR RGD; 1304726; Smarce1.
DR eggNOG; KOG4715; Eukaryota.
DR GeneTree; ENSGT00390000003628; -.
DR InParanoid; Q56A18; -.
DR OrthoDB; 3062313at2759; -.
DR Reactome; R-RNO-3214858; RMTs methylate histone arginines.
DR Reactome; R-RNO-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR PRO; PR:Q56A18; -.
DR Proteomes; UP000002494; Chromosome 10.
DR GO; GO:0071565; C:nBAF complex; ISO:RGD.
DR GO; GO:0071564; C:npBAF complex; ISO:RGD.
DR GO; GO:0016514; C:SWI/SNF complex; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008080; F:N-acetyltransferase activity; ISO:RGD.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0006338; P:chromatin remodeling; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IMP:RGD.
DR GO; GO:0022008; P:neurogenesis; ISO:RGD.
DR GO; GO:0006337; P:nucleosome disassembly; ISO:RGD.
DR GO; GO:0007286; P:spermatid development; IEP:RGD.
DR CDD; cd21983; HMG-box_SMARCE1; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR PANTHER; PTHR46232; SMARCE1 REGULATOR OF CHROMATIN; 1.
DR PANTHER; PTHR46232:SF1; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY E MEMBER 1; 1.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; HMG-box; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Coiled coil; DNA-binding;
KW Isopeptide bond; Methylation; Neurogenesis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..376
FT /note="SWI/SNF-related matrix-associated actin-dependent
FT regulator of chromatin subfamily E member 1"
FT /id="PRO_0000420477"
FT DNA_BIND 31..99
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 187..283
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q969G3"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969G3"
FT CROSSLNK 3
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q969G3"
FT CROSSLNK 57
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q969G3"
FT CROSSLNK 57
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q969G3"
FT CROSSLNK 96
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q969G3"
FT CROSSLNK 111
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q969G3"
FT CROSSLNK 131
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q969G3"
FT CROSSLNK 242
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q969G3"
FT VAR_SEQ 1..67
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044513"
FT VAR_SEQ 1..35
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19245665"
FT /id="VSP_044514"
FT VAR_SEQ 1..16
FT /note="MSKRPSYAPPPTPAPA -> MPSTPGFVGYNPYSHLAYNNYRLGGNPGTNSR
FT V (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:19245665"
FT /id="VSP_044515"
FT VAR_SEQ 234..235
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044516"
SQ SEQUENCE 376 AA; 42831 MW; A66CBB2492711C1E CRC64;
MSKRPSYAPP PTPAPATASS GITIPKPPKP PDKPLMPYMR YSRKVWDQVK ASNPDLKLWE
IGKIIGGMWR DLTDEEKQEY LNEYEAEKIE YNESMKAYHN SPAYLAYINA KSRAEAALEE
ESRQRQSRME KGEPYMSIQP AEDPDDYDDG FSMKHTATAR FQRNHRLISE ILSESVVPDV
RSVVTTARMQ VLKRQVQSLM VHQRKLEAEL LQIEERHQEK KRKFLESTDS FNNELKRLCG
LKVEVDMEKI AAEIAQAEEQ ARKRQEEREK EAAEQAERSQ GSIAPEEEQV ANKAEEKKDE
ENIPMETEET HLEDTAENQQ NGEEGTSTPE DKESGQEGVD SMEVEGTSDS NTGSESNSAT
VEEPPTDPVP EDEKKE
//
