MYCD_MOUSE
ID MYCD_MOUSE Reviewed; 935 AA.
AC Q8VIM5; Q5SS65; Q6W8X1; Q8C3W6; Q8VIL4;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Myocardin;
DE AltName: Full=Basic SAP coiled-coil transcription activator 2;
DE AltName: Full=SRF cofactor protein;
GN Name=Myocd; Synonyms=Bsac2, Mycd, Srfcp;
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 1), FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, INTERACTION WITH SRF, AND
RP MUTAGENESIS OF 387-GLU--ARG-389 AND 408-ASP--LEU-410.
RC TISSUE=Heart;
RX PubMed=11439182; DOI=10.1016/s0092-8674(01)00404-4;
RA Wang D.-Z., Chang P.S., Wang Z., Sutherland L., Richardson J.A., Small E.,
RA Krieg P.A., Olson E.N.;
RT "Activation of cardiac gene expression by myocardin, a transcriptional
RT cofactor for serum response factor.";
RL Cell 105:851-862(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SEQUENCE REVISION TO 1-128.
RX PubMed=12397177; DOI=10.1073/pnas.222561499;
RA Wang D.-Z., Li S., Hockemeyer D., Sutherland L., Wang Z., Schratt G.,
RA Richardson J.A., Nordheim A., Olson E.N.;
RT "Potentiation of serum response factor activity by a family of myocardin-
RT related transcription factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14855-14860(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RC STRAIN=NIH Swiss;
RX PubMed=14645532; DOI=10.1128/mcb.23.24.9222-9232.2003;
RA Ueyama T., Kasahara H., Ishiwata T., Nie Q., Izumo S.;
RT "Myocardin expression is regulated by Nkx2.5, and its function is required
RT for cardiomyogenesis.";
RL Mol. Cell. Biol. 23:9222-9232(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Heart;
RA Sawada T., Okazaki T., Nakano H.;
RT "An alternative splicing form of myocardin (BSAC2), myocardin A (BSAC2A).";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12640126; DOI=10.1128/mcb.23.7.2425-2437.2003;
RA Du K.L., Ip H.S., Li J., Chen M., Dandre F., Yu W., Lu M.M., Owens G.K.,
RA Parmacek M.S.;
RT "Myocardin is a critical serum response factor cofactor in the
RT transcriptional program regulating smooth muscle cell differentiation.";
RL Mol. Cell. Biol. 23:2425-2437(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryonic heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH SRF.
RX PubMed=12663482; DOI=10.1161/01.res.0000068405.49081.09;
RA Yoshida T., Sinha S., Dandre F., Wamhoff B.R., Hoofnagle M.H., Kremer B.E.,
RA Wang D.-Z., Olson E.N., Owens G.K.;
RT "Myocardin is a key regulator of CArG-dependent transcription of multiple
RT smooth muscle marker genes.";
RL Circ. Res. 92:856-864(2003).
RN [9]
RP PHOSPHORYLATION AT SER-454; SER-458; SER-462; SER-466; SER-624; SER-628;
RP SER-632 AND SER-636.
RX PubMed=16141410; DOI=10.1161/01.res.0000184684.88750.fe;
RA Badorff C., Seeger F.H., Zeiher A.M., Dimmeler S.;
RT "Glycogen synthase kinase 3beta inhibits myocardin-dependent transcription
RT and hypertrophy induction through site-specific phosphorylation.";
RL Circ. Res. 97:645-654(2005).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH EP300; HDAC4 AND HDAC5.
RX PubMed=15601857; DOI=10.1128/mcb.25.1.364-376.2005;
RA Cao D., Wang Z., Zhang C.L., Oh J., Xing W., Li S., Richardson J.A.,
RA Wang D.Z., Olson E.N.;
RT "Modulation of smooth muscle gene expression by association of histone
RT acetyltransferases and deacetylases with myocardin.";
RL Mol. Cell. Biol. 25:364-376(2005).
RN [11]
RP ALTERNATIVE SPLICING (ISOFORMS 2 AND 4), INTERACTION WITH MEF2C, AND
RP FUNCTION.
RX PubMed=16818234; DOI=10.1016/j.molcel.2006.05.026;
RA Creemers E.E., Sutherland L.B., Oh J., Barbosa A.C., Olson E.N.;
RT "Coactivation of MEF2 by the SAP domain proteins myocardin and MASTR.";
RL Mol. Cell 23:83-96(2006).
RN [12]
RP PHOSPHORYLATION AT SER-812; SER-859; SER-866 AND THR-893, AND MUTAGENESIS
RP OF SER-812; SER-859; SER-866 AND THR-893.
RX PubMed=19776005; DOI=10.1074/jbc.m109.048983;
RA Taurin S., Sandbo N., Yau D.M., Sethakorn N., Kach J., Dulin N.O.;
RT "Phosphorylation of myocardin by extracellular signal-regulated kinase.";
RL J. Biol. Chem. 284:33789-33794(2009).
RN [13]
RP ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4 AND 5), TISSUE SPECIFICITY OF
RP ISOFORMS, AND FUNCTION.
RX PubMed=20385216; DOI=10.1016/j.gene.2010.03.012;
RA Imamura M., Long X., Nanda V., Miano J.M.;
RT "Expression and functional activity of four myocardin isoforms.";
RL Gene 464:1-10(2010).
RN [14]
RP FUNCTION.
RX PubMed=31513549; DOI=10.1172/jci128545;
RA Houweling A.C., Beaman G.M., Postma A.V., Gainous T.B., Lichtenbelt K.D.,
RA Brancati F., Lopes F.M., van der Made I., Polstra A.M., Robinson M.L.,
RA Wright K.D., Ellingford J.M., Jackson A.R., Overwater E., Genesio R.,
RA Romano S., Camerota L., D'Angelo E., Meijers-Heijboer E.J.,
RA Christoffels V.M., McHugh K.M., Black B.L., Newman W.G., Woolf A.S.,
RA Creemers E.E.;
RT "Loss-of-function variants in myocardin cause congenital megabladder in
RT humans and mice.";
RL J. Clin. Invest. 129:5374-5380(2019).
CC -!- FUNCTION: Smooth muscle cells (SM) and cardiac muscle cells-specific
CC transcriptional factor which uses the canonical single or multiple CArG
CC boxes DNA sequence. Acts as a cofactor of serum response factor (SRF)
CC with the potential to modulate SRF-target genes. Plays a crucial role
CC in cardiogenesis, urinary bladder development, and differentiation of
CC the smooth muscle cell lineage (myogenesis). Isoform 1 mediates the
CC cardiac transcription factor MEF2C-dependent transcription. Isoform 1
CC and isoform 3 are more active than isoform 2 and isoform 4 in
CC stimulating cardiac muscle promoters. {ECO:0000269|PubMed:11439182,
CC ECO:0000269|PubMed:12640126, ECO:0000269|PubMed:12663482,
CC ECO:0000269|PubMed:16818234, ECO:0000269|PubMed:20385216,
CC ECO:0000269|PubMed:31513549}.
CC -!- SUBUNIT: Homodimer. Interacts with MLLT7/FOXO4 (By similarity).
CC Interacts with SRF, its association does not depend on specific DNA
CC sequences for ternary complex formation. Interacts (via C-terminal)
CC with EP300 (via CREB-binding domain). Interacts with HDAC4 and HDAC5.
CC Interacts with MEF2C. {ECO:0000250, ECO:0000269|PubMed:11439182,
CC ECO:0000269|PubMed:12663482, ECO:0000269|PubMed:15601857,
CC ECO:0000269|PubMed:16818234}.
CC -!- INTERACTION:
CC Q8VIM5-1; P10085: Myod1; NbExp=2; IntAct=EBI-15626132, EBI-4405734;
CC Q8VIM5-1; Q9Y6Q9: NCOA3; Xeno; NbExp=5; IntAct=EBI-15626132, EBI-81196;
CC Q8VIM5-1; Q04206: RELA; Xeno; NbExp=2; IntAct=EBI-15626132, EBI-73886;
CC Q8VIM5-1; Q04206-1: RELA; Xeno; NbExp=2; IntAct=EBI-15626132, EBI-10826776;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:11439182,
CC ECO:0000269|PubMed:15601857}. Note=Nuclear, with a punctate
CC intranuclear pattern with exclusion from nuclei.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=MYOCD-v2;
CC IsoId=Q8VIM5-1; Sequence=Displayed;
CC Name=2; Synonyms=BSAC2A, Myocardin A, MYOCD-v5;
CC IsoId=Q8VIM5-2; Sequence=VSP_007662, VSP_007663;
CC Name=3; Synonyms==Myocardin A, MYOCD-v1;
CC IsoId=Q8VIM5-3; Sequence=VSP_007663;
CC Name=4; Synonyms=MYOCD-v3;
CC IsoId=Q8VIM5-4; Sequence=VSP_041684, VSP_007663;
CC Name=5; Synonyms=MYOCD-v4;
CC IsoId=Q8VIM5-5; Sequence=VSP_041684;
CC -!- TISSUE SPECIFICITY: Expressed in heart, aorta, and in smooth muscle
CC cell-containing tissues: stomach, bladder and uterus. Isoform 1 and
CC isoform 3 are predominantly expressed in cardiac muscle whereas isoform
CC 4 and isoform 5 are predominantly expressed in SMC-rich tissues.
CC Isoform 3 is the most abundant isoform in the heart from embryo to
CC adult. {ECO:0000269|PubMed:11439182, ECO:0000269|PubMed:12640126,
CC ECO:0000269|PubMed:12663482, ECO:0000269|PubMed:14645532,
CC ECO:0000269|PubMed:20385216}.
CC -!- DEVELOPMENTAL STAGE: Detected in the cardiac crescent at 7.75 dpc and
CC in the linear heart tube at 8.0 dpc and the developing atrial and
CC aortic ventricular chambers until birth. Also detected in a subset of
CC vascular and visceral smooth muscle cells: aortic arch arteries at 9.5
CC dpc; walls of the esophagus, dorsal aorta, pulmonary outflow tract,
CC lung, gut, stomach, small intestine, bladder, and the head mesenchyme
CC at 13.5 dpc until birth. Not detected in skeletal muscle cells.
CC {ECO:0000269|PubMed:11439182, ECO:0000269|PubMed:12640126}.
CC -!- DOMAIN: The C-terminal region contains a general transcription
CC activation domain. The N-terminal region, comprising a basic and a Gln-
CC rich domain, confers transcriptional potency and specificity by
CC mediating association with the MADS box of SRF. The basic domain may be
CC required for nuclear localization. The SAP domain is important for
CC transactivation and ternary complex formation.
CC -!- PTM: Phosphorylation regulates negatively transcriptional activity.
CC {ECO:0000269|PubMed:16141410, ECO:0000269|PubMed:19776005}.
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DR EMBL; AF384055; AAK71683.2; -; mRNA.
DR EMBL; AY303755; AAQ63841.1; -; mRNA.
DR EMBL; AF437877; AAL30892.1; -; mRNA.
DR EMBL; AK084700; BAC39258.1; -; mRNA.
DR EMBL; AK142216; BAE24980.1; -; mRNA.
DR EMBL; AL669846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS24843.1; -. [Q8VIM5-1]
DR CCDS; CCDS48819.1; -. [Q8VIM5-3]
DR RefSeq; NP_660118.3; NM_145136.4. [Q8VIM5-3]
DR RefSeq; NP_666498.2; NM_146386.3. [Q8VIM5-1]
DR RefSeq; XP_011247197.1; XM_011248895.1. [Q8VIM5-4]
DR AlphaFoldDB; Q8VIM5; -.
DR SMR; Q8VIM5; -.
DR BioGRID; 229522; 16.
DR CORUM; Q8VIM5; -.
DR DIP; DIP-29754N; -.
DR ELM; Q8VIM5; -.
DR IntAct; Q8VIM5; 9.
DR STRING; 10090.ENSMUSP00000099695; -.
DR iPTMnet; Q8VIM5; -.
DR PhosphoSitePlus; Q8VIM5; -.
DR MaxQB; Q8VIM5; -.
DR PaxDb; Q8VIM5; -.
DR PRIDE; Q8VIM5; -.
DR ProteomicsDB; 287562; -. [Q8VIM5-1]
DR ProteomicsDB; 287563; -. [Q8VIM5-2]
DR ProteomicsDB; 287564; -. [Q8VIM5-3]
DR ProteomicsDB; 287565; -. [Q8VIM5-4]
DR ProteomicsDB; 287566; -. [Q8VIM5-5]
DR Antibodypedia; 25055; 125 antibodies from 24 providers.
DR DNASU; 214384; -.
DR Ensembl; ENSMUST00000101042; ENSMUSP00000098603; ENSMUSG00000020542. [Q8VIM5-2]
DR Ensembl; ENSMUST00000102635; ENSMUSP00000099695; ENSMUSG00000020542. [Q8VIM5-1]
DR Ensembl; ENSMUST00000108695; ENSMUSP00000104335; ENSMUSG00000020542. [Q8VIM5-3]
DR GeneID; 214384; -.
DR KEGG; mmu:214384; -.
DR UCSC; uc007jky.2; mouse. [Q8VIM5-3]
DR UCSC; uc007jkz.2; mouse. [Q8VIM5-1]
DR CTD; 93649; -.
DR MGI; MGI:2137495; Myocd.
DR VEuPathDB; HostDB:ENSMUSG00000020542; -.
DR eggNOG; ENOG502QTAN; Eukaryota.
DR GeneTree; ENSGT00950000182979; -.
DR HOGENOM; CLU_007042_2_0_1; -.
DR InParanoid; Q8VIM5; -.
DR OMA; HFEGMME; -.
DR OrthoDB; 190145at2759; -.
DR TreeFam; TF326024; -.
DR BioGRID-ORCS; 214384; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Myocd; mouse.
DR PRO; PR:Q8VIM5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8VIM5; protein.
DR Bgee; ENSMUSG00000020542; Expressed in ascending aorta and 105 other tissues.
DR ExpressionAtlas; Q8VIM5; baseline and differential.
DR Genevisible; Q8VIM5; MM.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070514; C:SRF-myogenin-E12 complex; IC:BHF-UCL.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0035035; F:histone acetyltransferase binding; IPI:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:MGI.
DR GO; GO:0070412; F:R-SMAD binding; IPI:BHF-UCL.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:BHF-UCL.
DR GO; GO:0010659; P:cardiac muscle cell apoptotic process; IMP:MGI.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:BHF-UCL.
DR GO; GO:0060379; P:cardiac muscle cell myoblast differentiation; ISO:MGI.
DR GO; GO:0003231; P:cardiac ventricle development; IMP:MGI.
DR GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; ISO:MGI.
DR GO; GO:0043954; P:cellular component maintenance; IMP:MGI.
DR GO; GO:0048565; P:digestive tract development; IMP:MGI.
DR GO; GO:0097070; P:ductus arteriosus closure; IMP:MGI.
DR GO; GO:0007507; P:heart development; IDA:BHF-UCL.
DR GO; GO:0035733; P:hepatic stellate cell activation; ISO:MGI.
DR GO; GO:0048286; P:lung alveolus development; IMP:MGI.
DR GO; GO:1900222; P:negative regulation of amyloid-beta clearance; ISO:MGI.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IMP:MGI.
DR GO; GO:0060354; P:negative regulation of cell adhesion molecule production; IDA:ARUK-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0010832; P:negative regulation of myotube differentiation; IMP:MGI.
DR GO; GO:2000587; P:negative regulation of platelet-derived growth factor receptor-beta signaling pathway; IDA:BHF-UCL.
DR GO; GO:2001015; P:negative regulation of skeletal muscle cell differentiation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; IDA:BHF-UCL.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IDA:BHF-UCL.
DR GO; GO:2000727; P:positive regulation of cardiac muscle cell differentiation; ISO:MGI.
DR GO; GO:2000724; P:positive regulation of cardiac vascular smooth muscle cell differentiation; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0043388; P:positive regulation of DNA binding; IGI:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IDA:BHF-UCL.
DR GO; GO:0051152; P:positive regulation of smooth muscle cell differentiation; ISO:MGI.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:2000721; P:positive regulation of transcription from RNA polymerase II promoter involved in smooth muscle cell differentiation; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0001560; P:regulation of cell growth by extracellular stimulus; IDA:MGI.
DR GO; GO:0035065; P:regulation of histone acetylation; IDA:UniProtKB.
DR GO; GO:0045661; P:regulation of myoblast differentiation; IMP:MGI.
DR GO; GO:1900239; P:regulation of phenotypic switching; IGI:BHF-UCL.
DR GO; GO:0051150; P:regulation of smooth muscle cell differentiation; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0051145; P:smooth muscle cell differentiation; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0060157; P:urinary bladder development; IMP:MGI.
DR GO; GO:0060065; P:uterus development; IMP:MGI.
DR GO; GO:0035886; P:vascular associated smooth muscle cell differentiation; IGI:BHF-UCL.
DR GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR GO; GO:0055012; P:ventricular cardiac muscle cell differentiation; IMP:MGI.
DR Gene3D; 1.10.720.30; -; 1.
DR InterPro; IPR043451; Myocardin-like.
DR InterPro; IPR028721; MYOCD.
DR InterPro; IPR004018; RPEL_repeat.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR PANTHER; PTHR22793; PTHR22793; 1.
DR PANTHER; PTHR22793:SF11; PTHR22793:SF11; 1.
DR Pfam; PF02755; RPEL; 1.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00707; RPEL; 3.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS51073; RPEL; 3.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Coiled coil; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..935
FT /note="Myocardin"
FT /id="PRO_0000126632"
FT REPEAT 18..43
FT /note="RPEL 1"
FT REPEAT 62..87
FT /note="RPEL 2"
FT REPEAT 106..131
FT /note="RPEL 3"
FT DOMAIN 380..414
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT REGION 37..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..201
FT /note="HDAC5-binding"
FT REGION 155..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 287..322
FT /evidence="ECO:0000255"
FT COILED 519..563
FT /evidence="ECO:0000255"
FT MOTIF 12..27
FT /note="MEF2C-binding"
FT COMPBIAS 46..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 454
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000269|PubMed:16141410"
FT MOD_RES 458
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000269|PubMed:16141410"
FT MOD_RES 462
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000269|PubMed:16141410"
FT MOD_RES 466
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000269|PubMed:16141410"
FT MOD_RES 624
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000269|PubMed:16141410"
FT MOD_RES 628
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000269|PubMed:16141410"
FT MOD_RES 632
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000269|PubMed:16141410"
FT MOD_RES 636
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000269|PubMed:16141410"
FT MOD_RES 812
FT /note="Phosphoserine; by MAPK1 AND MAPK3"
FT /evidence="ECO:0000269|PubMed:19776005"
FT MOD_RES 859
FT /note="Phosphoserine; by MAPK1 and MAPK3"
FT /evidence="ECO:0000269|PubMed:19776005"
FT MOD_RES 866
FT /note="Phosphoserine; by MAPK1 and MAPK3"
FT /evidence="ECO:0000269|PubMed:19776005"
FT MOD_RES 893
FT /note="Phosphothreonine; by MAPK1 and MAPK3"
FT /evidence="ECO:0000269|PubMed:19776005"
FT VAR_SEQ 1..128
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_007662"
FT VAR_SEQ 1..79
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_041684"
FT VAR_SEQ 683
FT /note="Q -> QNSGAHEGHSSSFSSPASSLHQPFSGTQADSSHSAGLNPCPKSPSIH
FT PK (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14645532, ECO:0000303|Ref.4"
FT /id="VSP_007663"
FT MUTAGEN 387..389
FT /note="ELR->PSF: Activation of ANF promoter abolished, no
FT effect on SM22 promoter."
FT /evidence="ECO:0000269|PubMed:11439182"
FT MUTAGEN 408..410
FT /note="DRL->PGH: Activation of ANF promoter abolished, no
FT effect on SM22 promoter."
FT /evidence="ECO:0000269|PubMed:11439182"
FT MUTAGEN 812
FT /note="S->A: No effect on SRF activation. No effect on SRF
FT activation, on interaction with EP300 and on SM-promoter
FT activation; when associated with A-859; A-866 and A-893."
FT /evidence="ECO:0000269|PubMed:19776005"
FT MUTAGEN 812
FT /note="S->D: No effect on SRF activation. Impairs SRF
FT activation, reduces interaction with EP300 and SM-promoter
FT activation; when associated with D-859; D-866 and D-893."
FT /evidence="ECO:0000269|PubMed:19776005"
FT MUTAGEN 859
FT /note="S->A: No effect on SRF activation; No effect on SRF
FT activation. No effect on SRF activation, on interaction
FT with EP300 and on SM-promoter activation; when associated
FT with A-812, A-866 and A-893."
FT /evidence="ECO:0000269|PubMed:19776005"
FT MUTAGEN 859
FT /note="S->D: No effect on SRF activation. Impairs SRF
FT activation, reduces interaction with EP300 and SM-promoter
FT activation; when associated with D-812; D-866 and D-893."
FT /evidence="ECO:0000269|PubMed:19776005"
FT MUTAGEN 866
FT /note="S->A: No effect on SRF activation; No effect on SRF
FT activation, on interaction with EP300 and on SM-promoter
FT activation; when associated with A-812; A-859 and A-893."
FT /evidence="ECO:0000269|PubMed:19776005"
FT MUTAGEN 866
FT /note="S->D: No effect on SRF activation. Impairs SRF
FT activation, reduces interaction with EP300 and SM-promoter
FT activation; when associated with D-812; D-859 and D-893."
FT /evidence="ECO:0000269|PubMed:19776005"
FT MUTAGEN 893
FT /note="T->A: No effect on SRF activation; No effect on SRF
FT activation, on interaction with EP300 and on SM-specific
FT genes transcription; when associated with A-812; A-859 and
FT A-866."
FT /evidence="ECO:0000269|PubMed:19776005"
FT MUTAGEN 893
FT /note="T->D: No effect on SRF activation. Impairs SRF
FT activation, reduces interaction with EP300 and SM-promoter
FT activation; when associated with D-812; D-859 and D-866."
FT /evidence="ECO:0000269|PubMed:19776005"
FT CONFLICT 116
FT /note="P -> Q (in Ref. 1; AAK71683)"
FT /evidence="ECO:0000305"
FT CONFLICT 794
FT /note="D -> G (in Ref. 1; AAK71683)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 935 AA; 101400 MW; A8FCFC68A923A5CB CRC64;
MTLLGSEHSL LIRRKFRSVL QLRLQQRRTQ EQLANQGLIP PLKGPTEFHD PRKQLDSAKT
EDSLRRKGRN RSDRASLVTM HILQASTAER SIPTAQMKLK RARLADDLNE KIALRPGPLE
LVEKNILPMD SSVKEAIKGT EVSLSKAADA FAFEDDSSRD GLSPDQARSE DPQGSTGSTP
DIKSTEAPLD TIQDLTPGSE SDKNDAASQP GNQSDPGKQV LGPLSTPIPV HTAVKSKSLG
DSKNRHKKPK DPKPKVKKLK YHQYIPPDQK AEKSPPPMDS AYARLLQQQQ LFLQLQILSQ
QQQQQQQQQQ QQQQQQQQQQ RFSYPGMHQT HLKEPNEQMA RNPNPSSTPL SNTPLSPVKN
SISGQTGVSS LKPGPLPPNL DDLKVSELRQ QLRIRGLPVS GTKTALVDRL RPFQDCAGNP
VPNFGDITTV TFPVTPNTLP SYQSSPTGFY HFGSTSSSPP ISPASSDLSA AGSLPDTFTD
ASPGFGLHAS PVPACTDESL LSSLNGGSGP SEPDGLDSEK DKMLVEKQKV INQLTWKLRQ
EQRQVEELRM QLQKQKSSCS DQKPLPFLAT TIKQEDVSSC PFAPQQASGK GQGHSSDSPP
PACETAQLLP HCVESSGQTH VLSSTFLSPQ CSPQHSPLGG LKSPQHISLP PSPNNHYFLA
SSSGAQRENH GVSSPSSSQG CAQMTGLQSS DKVGPTFSIP SPTFSKSSSA VSDITQPPSY
EDAVKQQMTR SQQMDELLDV LIESGEMPAD AREDHSCLQK IPKIPGSSCS PTAIPPKPSA
SFEQASSGGQ MAFDHYANDS DEHLEVLLNS HSPIGKVSDV TLLKIGSEEP PFDSIMDGFP
GKAAEDLFSA HELLPGPLSP MHAQLSPPSV DSSGLQLSFT ESPWETMEWL DLTPPSSTPG
FSNLTSSGPS IFNIDFLDVT DLNLNSPMDL HLQQW
