MEF2B_MOUSE
ID MEF2B_MOUSE Reviewed; 349 AA.
AC O55087; O55088; O55089; O55090; O55231; Q61843;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Myocyte-specific enhancer factor 2B;
GN Name=Mef2b;
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] (ISOFORM B-1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=7646512; DOI=10.1006/bbrc.1995.2167;
RA Hidaka K., Morisaki T., Byun S.-H., Hashido K., Toyama K., Mukai T.;
RT "The MEF2B homologue differentially expressed in mouse embryonal carcinoma
RT cells.";
RL Biochem. Biophys. Res. Commun. 213:555-560(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM B-1), FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv; TISSUE=Heart;
RX PubMed=8668199; DOI=10.1128/mcb.16.7.3814;
RA Molkentin J.D., Firulli A.B., Black B.L., Martin J.F., Hustad C.M.,
RA Copeland N.G., Jenkins N.A., Lyons G., Olson E.N.;
RT "MEF2B is a potent transactivator expressed in early myogenic lineages.";
RL Mol. Cell. Biol. 16:3814-3824(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS B-1; B-2; B-3 AND B-4),
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=129/Sv; TISSUE=Teratocarcinoma;
RX PubMed=9443808; DOI=10.1093/oxfordjournals.jbchem.a021855;
RA Morisaki T., Sermsuvitayawong K., Byun S.-H., Matsuda Y., Hidaka K.,
RA Morisaki H., Mukai T.;
RT "Mouse Mef2b gene: unique member of MEF2 gene family.";
RL J. Biochem. 122:939-946(1997).
RN [4]
RP INTERACTION WITH HDAC7.
RX PubMed=11585834; DOI=10.1074/jbc.m107631200;
RA Kao H.-Y., Verdel A., Tsai C.-C., Simon C., Juguilon H., Khochbin S.;
RT "Mechanism for nucleocytoplasmic shuttling of histone deacetylase 7.";
RL J. Biol. Chem. 276:47496-47507(2001).
CC -!- FUNCTION: Transcriptional activator which binds specifically to the
CC MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific
CC genes. Activates transcription via this element. May be involved in
CC muscle-specific and/or growth factor-related transcription.
CC {ECO:0000269|PubMed:8668199, ECO:0000269|PubMed:9443808}.
CC -!- SUBUNIT: Heterodimer. Interacts with HDAC9 (By similarity). Interacts
CC with HDAC7. {ECO:0000250, ECO:0000269|PubMed:11585834}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=B-1;
CC IsoId=O55087-1; Sequence=Displayed;
CC Name=B-2;
CC IsoId=O55087-2; Sequence=VSP_006243;
CC Name=B-3;
CC IsoId=O55087-3; Sequence=VSP_006245, VSP_006247;
CC Name=B-4;
CC IsoId=O55087-4; Sequence=VSP_006244, VSP_006246;
CC -!- TISSUE SPECIFICITY: Highest expression found in embryonic heart and
CC skeletal muscle. Low levels found in adult spleen, lung and testis
CC while no expression is found in adult heart, brain or skeletal muscle.
CC {ECO:0000269|PubMed:7646512, ECO:0000269|PubMed:8668199,
CC ECO:0000269|PubMed:9443808}.
CC -!- DEVELOPMENTAL STAGE: Higher expression in early embryo than in adult.
CC {ECO:0000269|PubMed:9443808}.
CC -!- SIMILARITY: Belongs to the MEF2 family. {ECO:0000305}.
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DR EMBL; D50311; BAA08850.1; -; mRNA.
DR EMBL; D87831; BAA24539.1; -; Genomic_DNA.
DR EMBL; D87831; BAA24540.1; -; Genomic_DNA.
DR EMBL; D87831; BAA24541.1; -; Genomic_DNA.
DR EMBL; D87835; BAA24544.1; -; mRNA.
DR EMBL; D87836; BAA24545.1; -; mRNA.
DR EMBL; D87834; BAA24543.1; -; mRNA.
DR EMBL; D87833; BAA24542.1; -; mRNA.
DR CCDS; CCDS22361.1; -. [O55087-1]
DR CCDS; CCDS40368.1; -. [O55087-2]
DR PIR; JC5881; JC5881.
DR PIR; JC5882; JC5882.
DR PIR; JC5883; JC5883.
DR AlphaFoldDB; O55087; -.
DR SMR; O55087; -.
DR STRING; 10090.ENSMUSP00000105773; -.
DR iPTMnet; O55087; -.
DR PhosphoSitePlus; O55087; -.
DR PaxDb; O55087; -.
DR PRIDE; O55087; -.
DR ProteomicsDB; 293455; -. [O55087-1]
DR ProteomicsDB; 293456; -. [O55087-2]
DR MGI; MGI:104526; Mef2b.
DR eggNOG; KOG0014; Eukaryota.
DR InParanoid; O55087; -.
DR PhylomeDB; O55087; -.
DR Reactome; R-MMU-525793; Myogenesis.
DR PRO; PR:O55087; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O55087; protein.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IC:MGI.
DR GO; GO:0005667; C:transcription regulator complex; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042826; F:histone deacetylase binding; IDA:MGI.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR CDD; cd00265; MADS_MEF2_like; 1.
DR Gene3D; 3.40.1810.10; -; 1.
DR InterPro; IPR033896; MADS_MEF2-like.
DR InterPro; IPR002100; TF_MADSbox.
DR InterPro; IPR036879; TF_MADSbox_sf.
DR Pfam; PF00319; SRF-TF; 1.
DR PRINTS; PR00404; MADSDOMAIN.
DR SMART; SM00432; MADS; 1.
DR SUPFAM; SSF55455; SSF55455; 1.
DR PROSITE; PS00350; MADS_BOX_1; 1.
DR PROSITE; PS50066; MADS_BOX_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..349
FT /note="Myocyte-specific enhancer factor 2B"
FT /id="PRO_0000199432"
FT DOMAIN 3..57
FT /note="MADS-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00251"
FT DNA_BIND 58..86
FT /note="Mef2-type"
FT /evidence="ECO:0000255"
FT REGION 237..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 210..232
FT /note="VGARGGLGTSRSLYSGLQSPGAP -> IAARETQLRDPCNPHPGHQRGTL
FT (in isoform B-4)"
FT /evidence="ECO:0000303|PubMed:9443808"
FT /id="VSP_006244"
FT VAR_SEQ 210..219
FT /note="Missing (in isoform B-2)"
FT /evidence="ECO:0000303|PubMed:9443808"
FT /id="VSP_006243"
FT VAR_SEQ 220..242
FT /note="RSLYSGLQSPGAPGPALGSFAFL -> IAARETQLRDPCNPHPGHQRGTL
FT (in isoform B-3)"
FT /evidence="ECO:0000303|PubMed:9443808"
FT /id="VSP_006245"
FT VAR_SEQ 233..349
FT /note="Missing (in isoform B-4)"
FT /evidence="ECO:0000303|PubMed:9443808"
FT /id="VSP_006246"
FT VAR_SEQ 243..349
FT /note="Missing (in isoform B-3)"
FT /evidence="ECO:0000303|PubMed:9443808"
FT /id="VSP_006247"
FT CONFLICT 291
FT /note="A -> G (in Ref. 3; BAA24542/BAA24544)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 37435 MW; 4C49E2A2A8D493D8 CRC64;
MGRKKIQISR ILDQRNRQVT FTKRKFGLMK KAYELSVLCD CDIALIIFNS AQRLFQYASS
DMDRVLLKYT EYSEPHESRT NADILQTLKR RGVGLDGPEL DMEEGPEGPG EKLLRTLGGD
RGSASPRPRI YPVAPAMSVS ELSYRVPPAT PGCDPGGLGE VPSVHSRPAY FRPPGLGHPI
FSPSHLASKT PPPLYLATDG RRPDLPPGLV GARGGLGTSR SLYSGLQSPG APGPALGSFA
FLPSGSTDCS PGDAAQGPLQ PSPWPPTRDA VDPARPVARS LCKEGPPSRG ASPPTPPVSI
KSERLSPVTG TSGDFPRSFP YPLLLARPLA EPLRPSASLH RLTPDSWPR
