SMRD2_RAT
ID SMRD2_RAT Reviewed; 531 AA.
AC O54772; O54771;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 3.
DT 03-AUG-2022, entry version 139.
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; Synonyms=Baf60b;
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 [GENOMIC DNA / MRNA].
RC STRAIN=Wistar; TISSUE=Brain, and Liver;
RX PubMed=9427560; DOI=10.1016/s0378-1119(97)00469-1;
RA Nomoto K., Nakazato S., Kazahari K., Ono M.;
RT "Gene structure of rat BAF60b, a component of mammalian SWI/SNF complexes,
RT and its physical linkage to the growth hormone gene and transcription
RT factor SUG/proteasome p45 gene.";
RL Gene 202:157-165(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 63-531.
RC TISSUE=Prostate;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(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. 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA24105.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB003504; BAA24105.1; ALT_INIT; mRNA.
DR EMBL; AB003505; BAA24106.1; -; Genomic_DNA.
DR EMBL; BC062063; AAH62063.1; -; mRNA.
DR PIR; JC6508; JC6508.
DR RefSeq; NP_114189.1; NM_031983.2.
DR AlphaFoldDB; O54772; -.
DR SMR; O54772; -.
DR BioGRID; 249859; 1.
DR STRING; 10116.ENSRNOP00000014508; -.
DR iPTMnet; O54772; -.
DR PhosphoSitePlus; O54772; -.
DR jPOST; O54772; -.
DR PaxDb; O54772; -.
DR PRIDE; O54772; -.
DR GeneID; 83833; -.
DR KEGG; rno:83833; -.
DR CTD; 6603; -.
DR RGD; 69289; Smarcd2.
DR VEuPathDB; HostDB:ENSRNOG00000010557; -.
DR eggNOG; KOG2570; Eukaryota.
DR HOGENOM; CLU_023529_0_2_1; -.
DR InParanoid; O54772; -.
DR OMA; LMGIWEY; -.
DR OrthoDB; 1027566at2759; -.
DR PhylomeDB; O54772; -.
DR TreeFam; TF106486; -.
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:O54772; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000010557; Expressed in thymus and 20 other tissues.
DR Genevisible; O54772; RN.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016514; C:SWI/SNF complex; ISO:RGD.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; ISO:RGD.
DR GO; GO:0006337; P:nucleosome disassembly; ISO:RGD.
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 1: Evidence at protein level;
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_0000071987"
FT DOMAIN 306..383
FT /note="SWIB/MDM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01273"
FT REGION 20..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..218
FT /note="Polar residues"
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"
FT CONFLICT 66
FT /note="G -> A (in Ref. 1; BAA24105)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 531 AA; 59128 MW; D8E11A36B0201B73 CRC64;
MSGRGAGGFP LPPLSPGGGA VAAALGAPPP PAGPGMLPNP ALRGPGPSGG MGVPGAAAFR
PMGPAGPAAQ YQRPGMSPGS RMPMAGLQVG PPAGSPFGTA APLRPGMPPT MMDPFRKRLL
VPQAQPPMPA QRRGLKRRKM ADKVLPQRIR ELVPESQAYM DLLAFERKLD QTIARKRMEI
QEAIKKPLTQ KRKLRIYISN TFSPSKADGD NSGTAGTPGG TPAADKVASW ELRVEGKLLD
DPSKQKRKFS SFFKSLVIEL DKELYGPDNH LVEWHRMPTT QETDGFQVKR PGDLNVKCTL
LLMLDHQPPQ YKLDPRLARL LGVHTQTRAA IMQALWLYIK HNQLQDGHER EYINCNRYFR
QIFSCGRLRF SEIPMKLAGL LQHPDPIVIN HVISVDPNDQ KKTACYDIDV EVDDPLKAQM
SNFLASTTNQ QEIASLDVKI HETIESINQL KTQRDFMLSF STEPQDFIQE WLRSQRRDLK
IITDVIGNPE EERRAAFYHQ PWAQEAVGRH IFAKVQQRRQ ELEQVLGIRL T
