ID   SNF5_XENLA              Reviewed;         378 AA.
AC   Q6GQ82;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;
GN   Name=smarcb1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in chromatin-remodeling. Core component of the BAF
CC       (SWI/SNF) complex. This ATP-dependent chromatin-remodeling complex
CC       plays important roles in cell proliferation and differentiation, in
CC       cellular antiviral activities and inhibition of tumor formation.
CC       Belongs to the neural progenitors-specific chromatin remodeling complex
CC       (npBAF complex) and the neuron-specific chromatin remodeling complex
CC       (nBAF complex) and may play a role in neural development (By
CC       similarity). {ECO:0000250|UniProtKB:Q12824}.
CC   -!- SUBUNIT: Component of the multiprotein chromatin-remodeling complexes
CC       SWI/SNF. Component of neural progenitors-specific chromatin remodeling
CC       complex (npBAF complex) and the neuron-specific chromatin remodeling
CC       complex (nBAF complex) (By similarity). Component of the BAF (SWI/SNF)
CC       chromatin remodeling complex. Component of the SWI/SNF-B (PBAF)
CC       chromatin remodeling complex. Binds to double-stranded DNA (By
CC       similarity). {ECO:0000250|UniProtKB:Q12824,
CC       ECO:0000250|UniProtKB:Q9Z0H3}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The N-terminal DNA-binding region is structurally similar to
CC       winged helix domains. {ECO:0000250|UniProtKB:Q12824}.
CC   -!- SIMILARITY: Belongs to the SNF5 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC072865; AAH72865.1; -; mRNA.
DR   RefSeq; NP_001085508.1; NM_001092039.1.
DR   AlphaFoldDB; Q6GQ82; -.
DR   SMR; Q6GQ82; -.
DR   BioGRID; 102097; 1.
DR   DNASU; 443934; -.
DR   GeneID; 443934; -.
DR   KEGG; xla:443934; -.
DR   CTD; 443934; -.
DR   Xenbase; XB-GENE-866272; smarcb1.S.
DR   OrthoDB; 790205at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 443934; Expressed in neurula embryo and 19 other tissues.
DR   GO; GO:0000228; C:nuclear chromosome; IEA:InterPro.
DR   GO; GO:0070603; C:SWI/SNF superfamily-type complex; IEA:UniProt.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   InterPro; IPR017393; Sfh1/SNF5.
DR   InterPro; IPR006939; SNF5.
DR   Pfam; PF04855; SNF5; 1.
DR   PIRSF; PIRSF038126; SWI_SNF; 1.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Neurogenesis; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..378
FT                   /note="SWI/SNF-related matrix-associated actin-dependent
FT                   regulator of chromatin subfamily B member 1"
FT                   /id="PRO_0000205951"
FT   REGION          1..106
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q12824"
SQ   SEQUENCE   378 AA;  43298 MW;  DFD6E643076AF8A8 CRC64;
     MIMALSKTFG QKPVKFQLEE DGDYYMIGSE VGNYLRMFRG SLYKRYPSLW RRLATVEERK
     KIVASSHGKK YHGHTTLATS VTLLKASEVE EILDGNDEKY KAVSISTEPP TYLREQKAKR
     NSQWVPTLPN SSHHLDAVPC STTINRNRMG RDKKRTFPLC FDDHDPAVIH ENAAQPEVLV
     PIRLDMEIDG QKLRDAFTWN MNEKLMTPEM FAEILCDDLD LNPLAFVPAI ASAIRQQIES
     YPTDSILEDQ SDQRVIIKLN IHVGNISLVD QFEWDMSEKE NSPEKFALKL CSELGLGGEF
     VTTIAYSIRG QLSWHQKTYA FSENPLPTVE IAIRNTGDAD QWCPLLETLT DAEMEKKIRD
     QDRNTRRMRR LANTAPAW