ID MEF2_DROME Reviewed; 540 AA.
AC P40791; A1Z821; Q24394; Q8MT88; Q95R70; Q95RW1; Q9U5I8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 3.
DT 27-MAR-2024, entry version 192.
DE RecName: Full=Myocyte-specific enhancer factor 2;
DE Short=D-mef2;
DE AltName: Full=MADS domain transcription factor;
GN Name=Mef2; ORFNames=CG1429;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS C AND D), FUNCTION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=8202544; DOI=10.1073/pnas.91.12.5662;
RA Lilly B., Galewsky S., Firulli A.B., Schulz R.A., Olson E.N.;
RT "D-MEF2: a MADS box transcription factor expressed in differentiating
RT mesoderm and muscle cell lineages during Drosophila embryogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:5662-5666(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=8052612; DOI=10.1073/pnas.91.16.7520;
RA Nguyen H.T., Bodmer R., Abmayr S.M., McDermott J.C., Spoerel N.A.;
RT "D-mef2: a Drosophila mesoderm-specific MADS box-containing gene with a
RT biphasic expression profile during embryogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:7520-7524(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; C AND D), AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=7605749; DOI=10.1016/0925-4773(94)00323-f;
RA Taylor M.V., Beatty K.E., Hunter H.K., Baylies M.K.;
RT "Drosophila MEF2 is regulated by twist and is expressed in both the
RT primordia and differentiated cells of the embryonic somatic, visceral and
RT heart musculature.";
RL Mech. Dev. 50:29-41(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=7839146; DOI=10.1126/science.7839146;
RA Lilly B., Zhao B., Ranganayakulu G., Paterson B.M., Schulz R.A.,
RA Olson E.N.;
RT "Requirement of MADS domain transcription factor D-MEF2 for muscle
RT formation in Drosophila.";
RL Science 267:688-693(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [6]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C AND F), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-192 (ISOFORMS C/D).
RC STRAIN=Berkeley; TISSUE=Embryo, and Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 AND SER-98, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25797154; DOI=10.1016/j.ydbio.2015.02.026;
RA Brunetti T.M., Fremin B.J., Cripps R.M.;
RT "Identification of singles bar as a direct transcriptional target of
RT Drosophila Myocyte enhancer factor-2 and a regulator of adult myoblast
RT fusion.";
RL Dev. Biol. 401:299-309(2015).
CC -!- FUNCTION: Transcription factor that could be a key player in early
CC mesoderm differentiation and may be required for subsequent cell fate
CC specifications within the somatic and visceral/heart mesodermal layers
CC (PubMed:7839146, PubMed:8052612, PubMed:8202544). Essential for
CC myoblast fusion and consequently muscle formation in adults
CC (PubMed:25797154). During embryonic and pupal development, binds to the
CC enhancer of the myoblast fusion gene sing and activates its
CC transcription (PubMed:25797154). {ECO:0000269|PubMed:25797154,
CC ECO:0000269|PubMed:7839146, ECO:0000269|PubMed:8052612,
CC ECO:0000269|PubMed:8202544}.
CC -!- INTERACTION:
CC P40791; P20227: Tbp; NbExp=2; IntAct=EBI-235994, EBI-169179;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=D; Synonyms=1;
CC IsoId=P40791-1; Sequence=Displayed;
CC Name=A; Synonyms=3;
CC IsoId=P40791-2; Sequence=VSP_006237, VSP_006238;
CC Name=B;
CC IsoId=P40791-3; Sequence=VSP_006237, VSP_006239;
CC Name=C; Synonyms=2;
CC IsoId=P40791-4; Sequence=VSP_006239;
CC Name=F;
CC IsoId=P40791-6; Sequence=VSP_041851;
CC -!- TISSUE SPECIFICITY: Expressed in all presumptive mesoderm prior to the
CC splitting process that generates the somatic and visceral/ heart
CC mesoderm. After the subdivision, it is found in both the somatic and
CC the visceral/heart mesoderm. {ECO:0000269|PubMed:7605749,
CC ECO:0000269|PubMed:8052612, ECO:0000269|PubMed:8202544}.
CC -!- DEVELOPMENTAL STAGE: First detectable in the presumptive mesoderm at
CC late cellular blastoderm stage. {ECO:0000269|PubMed:8052612,
CC ECO:0000269|PubMed:8202544}.
CC -!- INDUCTION: TWI activity is required for MEF2 expression. SNA activity
CC is needed for maintaining MEF2 expression.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in pupae results in
CC smaller muscle founder templates that display a reduced number of
CC nuclei. No effect on the initiation of myoblast fusion.
CC {ECO:0000269|PubMed:25797154}.
CC -!- SIMILARITY: Belongs to the MEF2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28644.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM48340.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U03292; AAA19957.1; -; mRNA.
DR EMBL; U07422; AAA20463.1; -; mRNA.
DR EMBL; X83527; CAA58508.1; -; mRNA.
DR EMBL; U19493; AAF06817.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58872.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM71042.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM71043.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM71044.1; -; Genomic_DNA.
DR EMBL; AE013599; AAS64881.1; -; Genomic_DNA.
DR EMBL; AY061096; AAL28644.1; ALT_INIT; mRNA.
DR EMBL; AY061589; AAL29137.1; -; mRNA.
DR EMBL; AY118311; AAM48340.1; ALT_INIT; mRNA.
DR RefSeq; NP_477018.1; NM_057670.5. [P40791-4]
DR RefSeq; NP_477019.1; NM_057671.5. [P40791-3]
DR RefSeq; NP_477020.1; NM_057672.5. [P40791-1]
DR RefSeq; NP_477021.1; NM_057673.5. [P40791-2]
DR RefSeq; NP_995789.1; NM_206067.4. [P40791-6]
DR AlphaFoldDB; P40791; -.
DR SMR; P40791; -.
DR BioGRID; 61860; 29.
DR IntAct; P40791; 4.
DR STRING; 7227.FBpp0303551; -.
DR iPTMnet; P40791; -.
DR PaxDb; 7227-FBpp0087529; -.
DR EnsemblMetazoa; FBtr0088443; FBpp0087529; FBgn0011656. [P40791-1]
DR EnsemblMetazoa; FBtr0088444; FBpp0087530; FBgn0011656. [P40791-2]
DR EnsemblMetazoa; FBtr0088445; FBpp0087531; FBgn0011656. [P40791-4]
DR EnsemblMetazoa; FBtr0088446; FBpp0087532; FBgn0011656. [P40791-3]
DR EnsemblMetazoa; FBtr0088447; FBpp0089303; FBgn0011656. [P40791-6]
DR GeneID; 36032; -.
DR KEGG; dme:Dmel_CG1429; -.
DR UCSC; CG1429-RF; d. melanogaster.
DR AGR; FB:FBgn0011656; -.
DR CTD; 36032; -.
DR FlyBase; FBgn0011656; Mef2.
DR VEuPathDB; VectorBase:FBgn0011656; -.
DR eggNOG; KOG0014; Eukaryota.
DR GeneTree; ENSGT00940000169350; -.
DR InParanoid; P40791; -.
DR OMA; MATNSYS; -.
DR PhylomeDB; P40791; -.
DR Reactome; R-DME-525793; Myogenesis.
DR SignaLink; P40791; -.
DR BioGRID-ORCS; 36032; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36032; -.
DR PRO; PR:P40791; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0011656; Expressed in spermathecum and 54 other cell types or tissues.
DR ExpressionAtlas; P40791; baseline and differential.
DR Genevisible; P40791; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:FlyBase.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0007496; P:anterior midgut development; IMP:FlyBase.
DR GO; GO:0019730; P:antimicrobial humoral response; IMP:FlyBase.
DR GO; GO:0052576; P:carbohydrate storage; IMP:FlyBase.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0007507; P:heart development; TAS:FlyBase.
DR GO; GO:0007526; P:larval somatic muscle development; IMP:FlyBase.
DR GO; GO:0019915; P:lipid storage; IMP:FlyBase.
DR GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
DR GO; GO:0007498; P:mesoderm development; IMP:FlyBase.
DR GO; GO:0055001; P:muscle cell development; IMP:FlyBase.
DR GO; GO:0007517; P:muscle organ development; IMP:FlyBase.
DR GO; GO:0007520; P:myoblast fusion; IMP:FlyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0010468; P:regulation of gene expression; IMP:FlyBase.
DR CDD; cd00265; MADS_MEF2_like; 1.
DR Gene3D; 3.40.1810.10; Transcription factor, MADS-box; 1.
DR InterPro; IPR022102; HJURP_C.
DR InterPro; IPR033896; MADS_MEF2-like.
DR InterPro; IPR002100; TF_MADSbox.
DR InterPro; IPR036879; TF_MADSbox_sf.
DR PANTHER; PTHR48019:SF109; MYOCYTE-SPECIFIC ENHANCER FACTOR 2A; 1.
DR PANTHER; PTHR48019; SERUM RESPONSE FACTOR HOMOLOG; 1.
DR Pfam; PF12347; HJURP_C; 1.
DR Pfam; PF00319; SRF-TF; 1.
DR PRINTS; PR00404; MADSDOMAIN.
DR SMART; SM00432; MADS; 1.
DR SUPFAM; SSF55455; SRF-like; 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; Developmental protein; Differentiation;
KW DNA-binding; Myogenesis; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..540
FT /note="Myocyte-specific enhancer factor 2"
FT /id="PRO_0000199427"
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 162..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 187..225
FT /note="Missing (in isoform F)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_041851"
FT VAR_SEQ 187..193
FT /note="GGMSLII -> V (in isoform A and isoform B)"
FT /evidence="ECO:0000303|PubMed:7605749"
FT /id="VSP_006237"
FT VAR_SEQ 468..491
FT /note="GHDKYEGYPYRALMGHNPRWNLNF -> DFIILN (in isoform A)"
FT /evidence="ECO:0000303|PubMed:7605749"
FT /id="VSP_006238"
FT VAR_SEQ 469..493
FT /note="Missing (in isoform B and isoform C)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:7605749, ECO:0000303|PubMed:8052612,
FT ECO:0000303|PubMed:8202544"
FT /id="VSP_006239"
FT CONFLICT 1..3
FT /note="MGR -> WAA (in Ref. 7; AAL28644/AAM48340)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="D -> E (in Ref. 4; AAF06817)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="A -> G (in Ref. 4; AAF06817)"
FT /evidence="ECO:0000305"
FT CONFLICT 112..114
FT /note="EAK -> GGM (in Ref. 4; AAF06817)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="S -> R (in Ref. 2; AAA20463)"
FT /evidence="ECO:0000305"
FT CONFLICT 364..377
FT /note="ASGHQQNSNGSTGS -> PAVISRIAMVPRAG (in Ref. 1;
FT AAA19957 and 4; AAF06817)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="S -> T (in Ref. 4; AAF06817)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 540 AA; 57172 MW; 0B82D0C61EE1899E CRC64;
MGRKKIQISR ITDERNRQVT FNKRKFGVMK KAYELSVLCD CEIALIIFSS SNKLYQYAST
DMDRVLLKYT EYNEPHESLT NKNIIEKENK NGVMSPDSPE AETDYTLTPR TEAKYNKIDE
EFQNMMQRNQ MAIGGAGAPR QLPNSSYTLP VSVPVPGSYG DNLLQASPQM SHTNISPRPS
SSETDSGGMS LIIYPSGSML EMSNGYPHSH SPLVGSPSPG PSPGIAHHLS IKQQSPGSQN
GRASNLRVVI PPTIAPIPPN MSAPDDVGYA DQRQSQTSLN TPVVTLQTPI PALTSYSFGA
QDFSSSGVMN SADIMSLNTW HQGLVPHSSL SHLAVSNSTP PPATSPVSIK VKAEPQSPPR
DLSASGHQQN SNGSTGSGGS SSSTSSNASG GAGGGGAVSA ANVITHLNNV SVLAGGPSGQ
GGGGGGGGSN GNVEQATNLS VLSHAQQHHL GMPNSRPSST GHITPTPGHD KYEGYPYRAL
MGHNPRWNLN FAGAPSSDQD VRLAAVAVQQ QQQQPHQQQQ LGDYDAPNHK RPRISGGWGT
//
