SMBT1_RAT
ID SMBT1_RAT Reviewed; 863 AA.
AC Q9JMD2; Q66HN3;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Scm-like with four MBT domains protein 1;
GN Name=Sfmbt1;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; 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].
RC TISSUE=Testis;
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].
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: 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 (By similarity). {ECO:0000250}.
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
CC RCOR1/CoREST. Interacts with MYOD1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the testis, low expression was
CC detected in brain, kidney, heart and lung.
CC {ECO:0000269|PubMed:10806358}.
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}.
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DR EMBL; AB032164; BAA96304.1; -; mRNA.
DR EMBL; BC081770; AAH81770.1; -; mRNA.
DR RefSeq; NP_113835.2; NM_031647.2.
DR RefSeq; XP_006252718.1; XM_006252656.3.
DR RefSeq; XP_006252719.1; XM_006252657.3.
DR RefSeq; XP_006252720.1; XM_006252658.2.
DR RefSeq; XP_008769225.1; XM_008771003.2.
DR RefSeq; XP_008769226.1; XM_008771004.2.
DR RefSeq; XP_008769227.1; XM_008771005.2.
DR RefSeq; XP_008769228.1; XM_008771006.2.
DR RefSeq; XP_017455728.1; XM_017600239.1.
DR AlphaFoldDB; Q9JMD2; -.
DR SMR; Q9JMD2; -.
DR STRING; 10116.ENSRNOP00000022865; -.
DR iPTMnet; Q9JMD2; -.
DR PhosphoSitePlus; Q9JMD2; -.
DR PaxDb; Q9JMD2; -.
DR Ensembl; ENSRNOT00000022865; ENSRNOP00000022865; ENSRNOG00000016645.
DR GeneID; 58967; -.
DR KEGG; rno:58967; -.
DR UCSC; RGD:61999; rat.
DR CTD; 51460; -.
DR RGD; 61999; Sfmbt1.
DR eggNOG; KOG3766; Eukaryota.
DR GeneTree; ENSGT00940000157363; -.
DR HOGENOM; CLU_005352_0_0_1; -.
DR InParanoid; Q9JMD2; -.
DR OMA; HQVGWAS; -.
DR OrthoDB; 237430at2759; -.
DR PhylomeDB; Q9JMD2; -.
DR TreeFam; TF316498; -.
DR PRO; PR:Q9JMD2; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000016645; Expressed in testis and 18 other tissues.
DR Genevisible; Q9JMD2; RN.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; IEA:UniProtKB-KW.
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_0000071968"
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..714
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 764
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 772
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 195
FT /note="Q -> H (in Ref. 1; BAA96304)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 863 AA; 97506 MW; 4045B1505385123B CRC64;
MNGEQQLDAD LGSGVEVEEF SWEDYLEETG ATTAPYASFK HVDICLQSGF APGMKLEVAL
RKDPETYWVA TVITACEQLL LLRYEGYGED RKADFWCDIR RAGLYPIGWC QQNKKTLEAP
EGIRDKVSDW SAFLQRTLTG ACGPPVALLE GLRNGRNPLD LIAPGSRLEC QDFRDSVSTW
IVTVVENIGG RLKLQYEGLE RHDGFEHWLY YLDPFLHHIG WAAQQGYELQ PPLAIRHLKN
EADWQEILAR VKEEEPLPSY LFKDKQVIRT HEFSINMKLE AVDPWSPFGI SPATIAKVFD
DKYFLVEIDD LRPEDHARRS FVCHANSPGI FPVQWSLKNG LHINPPPGFR SQDFDWADYL
KQCGAEAAPQ KCFPQSVSEH QFKENMKLEA VNPLFPEEVS IATVTAVRGS YLWLQLEGSK
KPVPEFIVSV ESMNIFPLGW CETNGHPLST PRRARGHKLR KIAVVQPEKQ ILSSRTVHEG
LKNQLNSPHS VMINGKYCCP KIYFNHRCFS GPYLNKGRIA ELPQCVGPGN CVLVLREVLT
LLINAAYKPS RVLRELQLDK DSVWHGCGEV LKAKYKGKSY RATVEIVRTA DRVTEFCRQT
CIKLECCPNL FGPRMVLDTC SENCSVLTKT KYTHYYGKKK NKRIGRPPGG HSNLSCALKK
TSKRRKRRKN IFVHKKKRSS ASVDNTPVGS PQGSGGEDED DADDGDDDSL TEGSTSEQQD
ELHEESEVSE KKSCSPSPTQ SEMSTPLPPD TQTDKREAQT SSLSDGENKP PSPKEIRIEV
DERLHLDSNP LKWSVADVVR FIRSTDCAPL ARIFLDQEID GQALLLLTLP TVQECMDLKL
GPAIKLCHHI ERIKFAFYEQ FAN
