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Myocardin (Basic SAP coiled-coil transcription activator 2) (SRF cofactor protein)

 MYCD_MOUSE              Reviewed;         935 AA.
Q8VIM5; Q5SS65; Q6W8X1; Q8C3W6; Q8VIL4;
27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
05-DEC-2018, entry version 150.
RecName: Full=Myocardin;
AltName: Full=Basic SAP coiled-coil transcription activator 2;
AltName: Full=SRF cofactor protein;
Name=Myocd; Synonyms=Bsac2, Mycd, Srfcp;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, INTERACTION WITH SRF, AND
MUTAGENESIS OF 387-GLU--ARG-389 AND 408-ASP--LEU-410.
TISSUE=Heart;
PubMed=11439182; DOI=10.1016/S0092-8674(01)00404-4;
Wang D.-Z., Chang P.S., Wang Z., Sutherland L., Richardson J.A.,
Small E., Krieg P.A., Olson E.N.;
"Activation of cardiac gene expression by myocardin, a transcriptional
cofactor for serum response factor.";
Cell 105:851-862(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SEQUENCE REVISION TO
1-128.
PubMed=12397177; DOI=10.1073/pnas.222561499;
Wang D.-Z., Li S., Hockemeyer D., Sutherland L., Wang Z., Schratt G.,
Richardson J.A., Nordheim A., Olson E.N.;
"Potentiation of serum response factor activity by a family of
myocardin-related transcription factors.";
Proc. Natl. Acad. Sci. U.S.A. 99:14855-14860(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
STRAIN=NIH Swiss;
PubMed=14645532; DOI=10.1128/MCB.23.24.9222-9232.2003;
Ueyama T., Kasahara H., Ishiwata T., Nie Q., Izumo S.;
"Myocardin expression is regulated by Nkx2.5, and its function is
required for cardiomyogenesis.";
Mol. Cell. Biol. 23:9222-9232(2003).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Heart;
Sawada T., Okazaki T., Nakano H.;
"An alternative splicing form of myocardin (BSAC2), myocardin A
(BSAC2A).";
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
AND DEVELOPMENTAL STAGE.
PubMed=12640126; DOI=10.1128/MCB.23.7.2425-2437.2003;
Du K.L., Ip H.S., Li J., Chen M., Dandre F., Yu W., Lu M.M.,
Owens G.K., Parmacek M.S.;
"Myocardin is a critical serum response factor cofactor in the
transcriptional program regulating smooth muscle cell
differentiation.";
Mol. Cell. Biol. 23:2425-2437(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Embryonic heart;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[8]
FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH SRF.
PubMed=12663482; DOI=10.1161/01.RES.0000068405.49081.09;
Yoshida T., Sinha S., Dandre F., Wamhoff B.R., Hoofnagle M.H.,
Kremer B.E., Wang D.-Z., Olson E.N., Owens G.K.;
"Myocardin is a key regulator of CArG-dependent transcription of
multiple smooth muscle marker genes.";
Circ. Res. 92:856-864(2003).
[9]
PHOSPHORYLATION AT SER-454; SER-458; SER-462; SER-466; SER-624;
SER-628; SER-632 AND SER-636.
PubMed=16141410; DOI=10.1161/01.RES.0000184684.88750.FE;
Badorff C., Seeger F.H., Zeiher A.M., Dimmeler S.;
"Glycogen synthase kinase 3beta inhibits myocardin-dependent
transcription and hypertrophy induction through site-specific
phosphorylation.";
Circ. Res. 97:645-654(2005).
[10]
SUBCELLULAR LOCATION, AND INTERACTION WITH EP300; HDAC4 AND HDAC5.
PubMed=15601857; DOI=10.1128/MCB.25.1.364-376.2005;
Cao D., Wang Z., Zhang C.L., Oh J., Xing W., Li S., Richardson J.A.,
Wang D.Z., Olson E.N.;
"Modulation of smooth muscle gene expression by association of histone
acetyltransferases and deacetylases with myocardin.";
Mol. Cell. Biol. 25:364-376(2005).
[11]
ALTERNATIVE SPLICING (ISOFORMS 2 AND 4), INTERACTION WITH MEF2C, AND
FUNCTION.
PubMed=16818234; DOI=10.1016/j.molcel.2006.05.026;
Creemers E.E., Sutherland L.B., Oh J., Barbosa A.C., Olson E.N.;
"Coactivation of MEF2 by the SAP domain proteins myocardin and
MASTR.";
Mol. Cell 23:83-96(2006).
[12]
PHOSPHORYLATION AT SER-812; SER-859; SER-866 AND THR-893, AND
MUTAGENESIS OF SER-812; SER-859; SER-866 AND THR-893.
PubMed=19776005; DOI=10.1074/jbc.M109.048983;
Taurin S., Sandbo N., Yau D.M., Sethakorn N., Kach J., Dulin N.O.;
"Phosphorylation of myocardin by extracellular signal-regulated
kinase.";
J. Biol. Chem. 284:33789-33794(2009).
[13]
ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4 AND 5), TISSUE SPECIFICITY
OF ISOFORMS, AND FUNCTION.
PubMed=20385216; DOI=10.1016/j.gene.2010.03.012;
Imamura M., Long X., Nanda V., Miano J.M.;
"Expression and functional activity of four myocardin isoforms.";
Gene 464:1-10(2010).
-!- FUNCTION: Smooth muscle cells (SM) and cardiac muscle cells-
specific transcriptional factor which uses the canonical single or
multiple CArG boxes DNA sequence. Acts as a cofactor of serum
response factor (SRF) with the potential to modulate SRF-target
genes. Plays a crucial role in cardiogenesis and differentiation
of the smooth muscle cell lineage (myogenesis). Isoform 1 mediates
the cardiac transcription factor MEF2C-dependent transcription.
Isoform 1 and isoform 3 are more active than isoform 2 and isoform
4 in stimulating cardiac muscle promoters.
{ECO:0000269|PubMed:11439182, ECO:0000269|PubMed:12640126,
ECO:0000269|PubMed:12663482, ECO:0000269|PubMed:16818234,
ECO:0000269|PubMed:20385216}.
-!- SUBUNIT: Homodimer. Interacts with MLLT7/FOXO4 (By similarity).
Interacts with SRF, its association does not depend on specific
DNA sequences for ternary complex formation. Interacts (via C-
terminal) with EP300 (via CREB-binding domain). Interacts with
HDAC4 and HDAC5. Interacts with MEF2C. {ECO:0000250,
ECO:0000269|PubMed:11439182, ECO:0000269|PubMed:12663482,
ECO:0000269|PubMed:15601857, ECO:0000269|PubMed:16818234}.
-!- INTERACTION:
P10085:Myod1; NbExp=2; IntAct=EBI-15626132, EBI-4405734;
Q9Y6Q9:NCOA3 (xeno); NbExp=5; IntAct=EBI-15626132, EBI-81196;
Q04206:RELA (xeno); NbExp=2; IntAct=EBI-15626132, EBI-73886;
Q04206-1:RELA (xeno); NbExp=2; IntAct=EBI-15626132, EBI-10826776;
-!- SUBCELLULAR LOCATION: Nucleus speckle
{ECO:0000269|PubMed:11439182, ECO:0000269|PubMed:15601857}.
Note=Nuclear, with a punctate intranuclear pattern with exclusion
from nuclei.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=MYOCD-v2;
IsoId=Q8VIM5-1; Sequence=Displayed;
Name=2; Synonyms=BSAC2A, Myocardin A, MYOCD-v5;
IsoId=Q8VIM5-2; Sequence=VSP_007662, VSP_007663;
Note=No experimental confirmation available.;
Name=3; Synonyms==Myocardin A, MYOCD-v1;
IsoId=Q8VIM5-3; Sequence=VSP_007663;
Name=4; Synonyms=MYOCD-v3;
IsoId=Q8VIM5-4; Sequence=VSP_041684, VSP_007663;
Name=5; Synonyms=MYOCD-v4;
IsoId=Q8VIM5-5; Sequence=VSP_041684;
-!- TISSUE SPECIFICITY: Expressed in heart, aorta, and in smooth
muscle cell-containing tissues: stomach, bladder and uterus.
Isoform 1 and isoform 3 are predominantly expressed in cardiac
muscle whereas isoform 4 and isoform 5 are predominantly expressed
in SMC-rich tissues. Isoform 3 is the most abundant isoform in the
heart from embryo to adult. {ECO:0000269|PubMed:11439182,
ECO:0000269|PubMed:12640126, ECO:0000269|PubMed:12663482,
ECO:0000269|PubMed:14645532, ECO:0000269|PubMed:20385216}.
-!- DEVELOPMENTAL STAGE: Detected in the cardiac crescent at 7.75 dpc
and in the linear heart tube at 8.0 dpc and the developing atrial
and aortic ventricular chambers until birth. Also detected in a
subset of vascular and visceral smooth muscle cells: aortic arch
arteries at 9.5 dpc; walls of the esophagus, dorsal aorta,
pulmonary outflow tract, lung, gut, stomach, small intestine,
bladder, and the head mesenchyme at 13.5 dpc until birth. Not
detected in skeletal muscle cells. {ECO:0000269|PubMed:11439182,
ECO:0000269|PubMed:12640126}.
-!- DOMAIN: The C-terminal region contains a general transcription
activation domain. The N-terminal region, comprising a basic and a
Gln-rich domain, confers transcriptional potency and specificity
by mediating association with the MADS box of SRF. The basic
domain may be required for nuclear localization. The SAP domain is
important for transactivation and ternary complex formation.
-!- PTM: Phosphorylation regulates negatively transcriptional
activity. {ECO:0000269|PubMed:16141410,
ECO:0000269|PubMed:19776005}.
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EMBL; AF384055; AAK71683.2; -; mRNA.
EMBL; AY303755; AAQ63841.1; -; mRNA.
EMBL; AF437877; AAL30892.1; -; mRNA.
EMBL; AK084700; BAC39258.1; -; mRNA.
EMBL; AK142216; BAE24980.1; -; mRNA.
EMBL; AL669846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS24843.1; -. [Q8VIM5-1]
CCDS; CCDS48819.1; -. [Q8VIM5-3]
RefSeq; NP_660118.3; NM_145136.4. [Q8VIM5-3]
RefSeq; NP_666498.2; NM_146386.3. [Q8VIM5-1]
RefSeq; XP_011247197.1; XM_011248895.1. [Q8VIM5-4]
UniGene; Mm.32257; -.
ProteinModelPortal; Q8VIM5; -.
SMR; Q8VIM5; -.
BioGrid; 229522; 16.
CORUM; Q8VIM5; -.
DIP; DIP-29754N; -.
ELM; Q8VIM5; -.
IntAct; Q8VIM5; 4.
STRING; 10090.ENSMUSP00000104335; -.
iPTMnet; Q8VIM5; -.
PhosphoSitePlus; Q8VIM5; -.
PaxDb; Q8VIM5; -.
PRIDE; Q8VIM5; -.
DNASU; 214384; -.
Ensembl; ENSMUST00000101042; ENSMUSP00000098603; ENSMUSG00000020542. [Q8VIM5-2]
Ensembl; ENSMUST00000102635; ENSMUSP00000099695; ENSMUSG00000020542. [Q8VIM5-1]
Ensembl; ENSMUST00000108695; ENSMUSP00000104335; ENSMUSG00000020542. [Q8VIM5-3]
GeneID; 214384; -.
KEGG; mmu:214384; -.
UCSC; uc007jky.2; mouse. [Q8VIM5-3]
UCSC; uc007jkz.2; mouse. [Q8VIM5-1]
CTD; 93649; -.
MGI; MGI:2137495; Myocd.
eggNOG; ENOG410IE2C; Eukaryota.
eggNOG; ENOG410XNR1; LUCA.
GeneTree; ENSGT00940000155346; -.
HOGENOM; HOG000038001; -.
HOVERGEN; HBG036493; -.
InParanoid; Q8VIM5; -.
KO; K22526; -.
OMA; CPKSPGV; -.
OrthoDB; EOG091G02RT; -.
TreeFam; TF326024; -.
PRO; PR:Q8VIM5; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020542; Expressed in 116 organ(s), highest expression level in urinary bladder.
CleanEx; MM_MYOCD; -.
ExpressionAtlas; Q8VIM5; baseline and differential.
Genevisible; Q8VIM5; MM.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0070514; C:SRF-myogenin-E12 complex; IC:BHF-UCL.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:BHF-UCL.
GO; GO:0035035; F:histone acetyltransferase binding; IPI:MGI.
GO; GO:0042826; F:histone deacetylase binding; IPI:MGI.
GO; GO:0001077; F:proximal promoter DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
GO; GO:0070412; F:R-SMAD binding; IPI:BHF-UCL.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0061629; F:RNA polymerase II sequence-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:BHF-UCL.
GO; GO:0003231; P:cardiac ventricle development; IMP:MGI.
GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; ISO:MGI.
GO; GO:0043954; P:cellular component maintenance; IMP:MGI.
GO; GO:0048565; P:digestive tract development; IMP:MGI.
GO; GO:0097070; P:ductus arteriosus closure; IMP:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0035733; P:hepatic stellate cell activation; ISO:MGI.
GO; GO:0048286; P:lung alveolus development; IMP:MGI.
GO; GO:0042692; P:muscle cell differentiation; IMP:MGI.
GO; GO:1900222; P:negative regulation of amyloid-beta clearance; ISO:MGI.
GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IMP:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; ISO:MGI.
GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0010832; P:negative regulation of myotube differentiation; IMP:MGI.
GO; GO:2000587; P:negative regulation of platelet-derived growth factor receptor-beta signaling pathway; IDA:BHF-UCL.
GO; GO:2001015; P:negative regulation of skeletal muscle cell differentiation; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; IDA:BHF-UCL.
GO; GO:1904706; P:negative regulation of vascular smooth muscle cell proliferation; IDA:BHF-UCL.
GO; GO:2000727; P:positive regulation of cardiac muscle cell differentiation; ISO:MGI.
GO; GO:2000724; P:positive regulation of cardiac vascular smooth muscle cell differentiation; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
GO; GO:0043388; P:positive regulation of DNA binding; IGI:MGI.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:MGI.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
GO; GO:0051152; P:positive regulation of smooth muscle cell differentiation; ISO:MGI.
GO; GO:0045987; P:positive regulation of smooth muscle contraction; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:1901228; P:positive regulation of transcription from RNA polymerase II promoter involved in heart development; IDA:BHF-UCL.
GO; GO:0003257; P:positive regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation; ISO:MGI.
GO; GO:2000721; P:positive regulation of transcription from RNA polymerase II promoter involved in smooth muscle cell differentiation; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0001560; P:regulation of cell growth by extracellular stimulus; IDA:MGI.
GO; GO:0035065; P:regulation of histone acetylation; IDA:UniProtKB.
GO; GO:0045661; P:regulation of myoblast differentiation; IMP:MGI.
GO; GO:1900239; P:regulation of phenotypic switching; IGI:BHF-UCL.
GO; GO:0051150; P:regulation of smooth muscle cell differentiation; ISO:MGI.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0051145; P:smooth muscle cell differentiation; IMP:MGI.
GO; GO:0060157; P:urinary bladder development; IMP:MGI.
GO; GO:0060065; P:uterus development; IMP:MGI.
GO; GO:0035886; P:vascular smooth muscle cell differentiation; IGI:BHF-UCL.
GO; GO:0001570; P:vasculogenesis; IMP:MGI.
GO; GO:0055012; P:ventricular cardiac muscle cell differentiation; IMP:MGI.
Gene3D; 1.10.720.30; -; 1.
InterPro; IPR028721; MYOCD.
InterPro; IPR004018; RPEL_repeat.
InterPro; IPR003034; SAP_dom.
InterPro; IPR036361; SAP_dom_sf.
PANTHER; PTHR22793:SF11; PTHR22793:SF11; 1.
Pfam; PF02755; RPEL; 1.
Pfam; PF02037; SAP; 1.
SMART; SM00707; RPEL; 3.
SMART; SM00513; SAP; 1.
SUPFAM; SSF68906; SSF68906; 1.
PROSITE; PS51073; RPEL; 3.
PROSITE; PS50800; SAP; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Coiled coil; Complete proteome;
Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
Transcription regulation.
CHAIN 1 935 Myocardin.
/FTId=PRO_0000126632.
REPEAT 18 43 RPEL 1.
REPEAT 62 87 RPEL 2.
REPEAT 106 131 RPEL 3.
DOMAIN 380 414 SAP. {ECO:0000255|PROSITE-
ProRule:PRU00186}.
REGION 153 201 HDAC5-binding.
COILED 287 322 {ECO:0000255}.
COILED 519 563 {ECO:0000255}.
MOTIF 12 27 MEF2C-binding.
COMPBIAS 287 320 Gln-rich.
COMPBIAS 300 320 Poly-Gln.
MOD_RES 454 454 Phosphoserine; by GSK3-beta.
{ECO:0000269|PubMed:16141410}.
MOD_RES 458 458 Phosphoserine; by GSK3-beta.
{ECO:0000269|PubMed:16141410}.
MOD_RES 462 462 Phosphoserine; by GSK3-beta.
{ECO:0000269|PubMed:16141410}.
MOD_RES 466 466 Phosphoserine; by GSK3-beta.
{ECO:0000269|PubMed:16141410}.
MOD_RES 624 624 Phosphoserine; by GSK3-beta.
{ECO:0000269|PubMed:16141410}.
MOD_RES 628 628 Phosphoserine; by GSK3-beta.
{ECO:0000269|PubMed:16141410}.
MOD_RES 632 632 Phosphoserine; by GSK3-beta.
{ECO:0000269|PubMed:16141410}.
MOD_RES 636 636 Phosphoserine; by GSK3-beta.
{ECO:0000269|PubMed:16141410}.
MOD_RES 812 812 Phosphoserine; by MAPK1 AND MAPK3.
{ECO:0000269|PubMed:19776005}.
MOD_RES 859 859 Phosphoserine; by MAPK1 and MAPK3.
{ECO:0000269|PubMed:19776005}.
MOD_RES 866 866 Phosphoserine; by MAPK1 and MAPK3.
{ECO:0000269|PubMed:19776005}.
MOD_RES 893 893 Phosphothreonine; by MAPK1 and MAPK3.
{ECO:0000269|PubMed:19776005}.
VAR_SEQ 1 128 Missing (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_007662.
VAR_SEQ 1 79 Missing (in isoform 4 and isoform 5).
{ECO:0000305}.
/FTId=VSP_041684.
VAR_SEQ 683 683 Q -> QNSGAHEGHSSSFSSPASSLHQPFSGTQADSSHSAG
LNPCPKSPSIHPK (in isoform 2, isoform 3
and isoform 4).
{ECO:0000303|PubMed:14645532,
ECO:0000303|Ref.4}.
/FTId=VSP_007663.
MUTAGEN 387 389 ELR->PSF: Activation of ANF promoter
abolished, no effect on SM22 promoter.
{ECO:0000269|PubMed:11439182}.
MUTAGEN 408 410 DRL->PGH: Activation of ANF promoter
abolished, no effect on SM22 promoter.
{ECO:0000269|PubMed:11439182}.
MUTAGEN 812 812 S->A: No effect on SRF activation. No
effect on SRF activation, on interaction
with EP300 and on SM-promoter activation;
when associated with A-859; A-866 and A-
893. {ECO:0000269|PubMed:19776005}.
MUTAGEN 812 812 S->D: No effect on SRF activation.
Impairs SRF activation, reduces
interaction with EP300 and SM-promoter
activation; when associated with D-859;
D-866 and D-893.
{ECO:0000269|PubMed:19776005}.
MUTAGEN 859 859 S->A: No effect on SRF activation; No
effect on SRF activation. No effect on
SRF activation, on interaction with EP300
and on SM-promoter activation; when
associated with A-812, A-866 and A-893.
{ECO:0000269|PubMed:19776005}.
MUTAGEN 859 859 S->D: No effect on SRF activation.
Impairs SRF activation, reduces
interaction with EP300 and SM-promoter
activation; when associated with D-812;
D-866 and D-893.
{ECO:0000269|PubMed:19776005}.
MUTAGEN 866 866 S->A: No effect on SRF activation; No
effect on SRF activation, on interaction
with EP300 and on SM-promoter activation;
when associated with A-812; A-859 and A-
893. {ECO:0000269|PubMed:19776005}.
MUTAGEN 866 866 S->D: No effect on SRF activation.
Impairs SRF activation, reduces
interaction with EP300 and SM-promoter
activation; when associated with D-812;
D-859 and D-893.
{ECO:0000269|PubMed:19776005}.
MUTAGEN 893 893 T->A: No effect on SRF activation; No
effect on SRF activation, on interaction
with EP300 and on SM-specific genes
transcription; when associated with A-
812; A-859 and A-866.
{ECO:0000269|PubMed:19776005}.
MUTAGEN 893 893 T->D: No effect on SRF activation.
Impairs SRF activation, reduces
interaction with EP300 and SM-promoter
activation; when associated with D-812;
D-859 and D-866.
{ECO:0000269|PubMed:19776005}.
CONFLICT 116 116 P -> Q (in Ref. 1; AAK71683).
{ECO:0000305}.
CONFLICT 794 794 D -> G (in Ref. 1; AAK71683).
{ECO:0000305}.
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


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