SMBT1_MOUSE
ID SMBT1_MOUSE Reviewed; 863 AA.
AC Q9JMD1; Q6NZD3; Q8CFS1;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Scm-like with four MBT domains protein 1;
GN Name=Sfmbt1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=10806358; DOI=10.1016/s0378-1119(00)00131-1;
RA Usui H., Ichikawa T., Kobayashi K., Kumanishi T.;
RT "Cloning of a novel murine gene Sfmbt, Scm-related gene containing four mbt
RT domains, structurally belonging to the Polycomb group of genes.";
RL Gene 248:127-135(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-644.
RC TISSUE=Eye;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-764 AND SER-772, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP IDENTIFICATION IN THE SLC COMPLEX, AND TISSUE SPECIFICITY.
RX PubMed=23592795; DOI=10.1101/gad.210963.112;
RA Zhang J., Bonasio R., Strino F., Kluger Y., Holloway J.K.,
RA Modzelewski A.J., Cohen P.E., Reinberg D.;
RT "SFMBT1 functions with LSD1 to regulate expression of canonical histone
RT genes and chromatin-related factors.";
RL Genes Dev. 27:749-766(2013).
RN [5]
RP FUNCTION, INTERACTION WITH MYOD1, AND DEVELOPMENTAL STAGE.
RX PubMed=23349461; DOI=10.1074/jbc.m112.429605;
RA Lin S., Shen H., Li J.L., Tang S., Gu Y., Chen Z., Hu C., Rice J.C., Lu J.,
RA Wu L.;
RT "Proteomic and functional analyses reveal the role of chromatin reader
RT SFMBT1 in regulating epigenetic silencing and the myogenic gene program.";
RL J. Biol. Chem. 288:6238-6247(2013).
CC -!- FUNCTION: Histone-binding protein, which is part of various corepressor
CC complexes. Mediates the recruitment of corepressor complexes to target
CC genes, followed by chromatin compaction and repression of
CC transcription. Plays a role during myogenesis: required for the
CC maintenance of undifferentiated states of myogenic progenitor cells via
CC interaction with MYOD1. Interaction with MYOD1 leads to the recruitment
CC of associated corepressors and silencing of MYOD1 target genes. Part of
CC the SLC complex in germ cells, where it may play a role during
CC spermatogenesis. {ECO:0000269|PubMed:23349461}.
CC -!- SUBUNIT: Interacts with MYOD1 (By similarity). Component of the SLC
CC (SFMBT1-LSD1-CoREST) corepressor complex, which also contains
CC KDM1A/LSD1 and RCOR1/CoREST. Interacts with KDM1A/LSD1 and RCOR1/CoREST
CC (By similarity). Interacts with MYOD1. {ECO:0000250,
CC ECO:0000269|PubMed:23349461, ECO:0000269|PubMed:23592795}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the testis, low expression is
CC detected in brain, kidney, heart and lung. Highly expressed in germ
CC cells, where it associates with the synaptic regions of meiotic
CC chromosomes in pachytene stage spermatocytes.
CC {ECO:0000269|PubMed:10806358, ECO:0000269|PubMed:23592795}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in undifferentiated myoblasts and
CC expression is reduced during the course of differentiation.
CC {ECO:0000269|PubMed:23349461}.
CC -!- DOMAIN: The MBT repeats mediate binding to histones tails; however, in
CC contrast to other MBT repeats, does not bind specific histone lysine
CC modifications. The MBT repeats lack the conserved Asp and aromatic cage
CC at conserved positions (By similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH36972.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH66188.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB032165; BAA96305.1; -; mRNA.
DR EMBL; BC036972; AAH36972.1; ALT_SEQ; mRNA.
DR EMBL; BC066188; AAH66188.1; ALT_SEQ; mRNA.
DR CCDS; CCDS26897.1; -.
DR RefSeq; NP_001160003.1; NM_001166531.1.
DR RefSeq; NP_001160004.1; NM_001166532.1.
DR RefSeq; NP_062333.1; NM_019460.2.
DR RefSeq; XP_006519350.1; XM_006519287.3.
DR RefSeq; XP_006519351.1; XM_006519288.3.
DR RefSeq; XP_006519352.1; XM_006519289.3.
DR RefSeq; XP_011243422.1; XM_011245120.2.
DR RefSeq; XP_011243423.1; XM_011245121.2.
DR AlphaFoldDB; Q9JMD1; -.
DR SMR; Q9JMD1; -.
DR BioGRID; 207710; 2.
DR STRING; 10090.ENSMUSP00000056744; -.
DR iPTMnet; Q9JMD1; -.
DR PhosphoSitePlus; Q9JMD1; -.
DR MaxQB; Q9JMD1; -.
DR PaxDb; Q9JMD1; -.
DR PRIDE; Q9JMD1; -.
DR ProteomicsDB; 261519; -.
DR Antibodypedia; 31362; 144 antibodies from 21 providers.
DR DNASU; 54650; -.
DR Ensembl; ENSMUST00000054230; ENSMUSP00000056744; ENSMUSG00000006527.
DR Ensembl; ENSMUST00000112184; ENSMUSP00000107802; ENSMUSG00000006527.
DR Ensembl; ENSMUST00000228006; ENSMUSP00000153861; ENSMUSG00000006527.
DR GeneID; 54650; -.
DR KEGG; mmu:54650; -.
DR UCSC; uc007svp.2; mouse.
DR CTD; 51460; -.
DR MGI; MGI:1859609; Sfmbt1.
DR VEuPathDB; HostDB:ENSMUSG00000006527; -.
DR eggNOG; KOG3766; Eukaryota.
DR GeneTree; ENSGT00940000157363; -.
DR HOGENOM; CLU_005352_0_0_1; -.
DR InParanoid; Q9JMD1; -.
DR OMA; HQVGWAS; -.
DR OrthoDB; 237430at2759; -.
DR PhylomeDB; Q9JMD1; -.
DR TreeFam; TF316498; -.
DR BioGRID-ORCS; 54650; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Sfmbt1; mouse.
DR PRO; PR:Q9JMD1; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9JMD1; protein.
DR Bgee; ENSMUSG00000006527; Expressed in animal zygote and 227 other tissues.
DR ExpressionAtlas; Q9JMD1; baseline and differential.
DR Genevisible; Q9JMD1; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0048635; P:negative regulation of muscle organ development; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; TAS:UniProtKB.
DR CDD; cd09581; SAM_Scm-like-4MBT1_2; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 3.90.1150.190; -; 1.
DR InterPro; IPR004092; Mbt.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR037604; Scm-like-4MBT1/2_SAM.
DR InterPro; IPR021987; SLED.
DR InterPro; IPR038348; SLED_sf.
DR Pfam; PF02820; MBT; 4.
DR Pfam; PF00536; SAM_1; 1.
DR Pfam; PF12140; SLED; 1.
DR SMART; SM00561; MBT; 4.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS51079; MBT; 4.
PE 1: Evidence at protein level;
KW Chromatin regulator; Differentiation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Spermatogenesis; Transcription;
KW Transcription regulation.
FT CHAIN 1..863
FT /note="Scm-like with four MBT domains protein 1"
FT /id="PRO_0000071967"
FT REPEAT 20..120
FT /note="MBT 1"
FT REPEAT 128..232
FT /note="MBT 2"
FT REPEAT 242..346
FT /note="MBT 3"
FT REPEAT 354..451
FT /note="MBT 4"
FT DOMAIN 793..861
FT /note="SAM"
FT REGION 638..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..676
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..724
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 764
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 772
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 863 AA; 97338 MW; DB1CADA81B42566D CRC64;
MSGEQQLDAD LGSGVEVEEF SWEDYLEETG STTVPYASFK HVDIRLQNGF APGMKLEVAL
KNDPETYWVA TIITACEQLL LLRYEGYGED RKADFWCDIR KAGLYPIGWC QQNKKTLEAP
EGIRDKVSDW NAFLQQTLIG ACGPPVSLLE GLRNGRNPLD LIAPGSKLEC QDFRDSLSTW
LVTVVENIGG RLKLRYEGLE SRDGFEHWLY YLDPFLHHIG WAAQQGCDLQ PPLAIKHLKS
EADWQEILAK VKEEEPLPSY LFKDKQVIGT HEFSINMKLE AVDPWSPFGI SPATIAKVFD
DKYFLVEMDD LRPEDHTRRS FVCHANSPGI FPVQWSLKNG LHINPPPGFR SQDFDWADYL
KQCGAEAAPQ KCFPQSISEH QFKENMKLEA VNPLFPEEVC IATVTAVRGS YLWLQLEGSK
KPVPEFIVSA ESMNIFPLGW CETNGHPLST PRRARGHKLR KIAVVQPEKQ ILSSRTVHEG
LKNQLNSTHS VMINGKYCCP KIYFNHRCFS GPYLNKGRIA ELPQCVGPGN CVLVLREVLT
LLINAAYKPS RVLRELQLDK DSVWHGCGEV LKAKYKGKSY RATVEIVRTA DRVTEFCRQT
CIKLECCPNL FGPRMVLDTC SENCSVLTKT KYTHYYGKKK NKRIGRPPGG HSNLSCALKK
SSKRRKRRKN IFVHKKKRSS ASVDNTPVGS PQGSGGEDEE DADDGDEDSL TEGSTSEQQE
ELQEESEVSE KKSSSSSPTQ SETPTPLPPD TQTNKRDAQT SSVSDDENKP PSPKEIRIEV
DERLHLDSNP LKWSVADVVR FIRSTDCAPL ARIFLDQEID GQALLLLTLP TVQECMDLKL
GPAIKLCHHI ERIKFAFYEQ FAN
