MYCD_RAT
ID MYCD_RAT Reviewed; 938 AA.
AC Q8R5I7; Q7M6Y4; Q8R5I8;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Myocardin;
GN Name=Myocd; Synonyms=Mycd;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Aorta;
RX PubMed=12392995; DOI=10.1006/jmcc.2002.2086;
RA Chen J., Kitchen C.M., Streb J.W., Miano J.M.;
RT "Myocardin: a component of a molecular switch for smooth muscle
RT differentiation.";
RL J. Mol. Cell. Cardiol. 34:1345-1356(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 251-399.
RC TISSUE=Aorta;
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 [3]
RP SUBUNIT, AND MUTAGENESIS OF ILE-534; LEU-537 AND LEU-541.
RX PubMed=12756293; DOI=10.1073/pnas.1232341100;
RA Wang Z., Wang D.-Z., Pipes G.C., Olson E.N.;
RT "Myocardin is a master regulator of smooth muscle gene expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7129-7134(2003).
RN [4]
RP TISSUE SPECIFICITY OF ISOFORMS.
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).
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 (By similarity). Plays
CC a crucial role in cardiogenesis, urinary bladder development, and
CC differentiation of the smooth muscle cell lineage (myogenesis) (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with MLLT7/FOXO4. Interacts with SRF, its
CC association does not depend on specific DNA sequences for ternary
CC complex formation (By similarity). Interacts (via C-terminal) with
CC EP300 (via the CREB-binding domain). Interacts with HDAC4 and HDAC5 (By
CC similarity). Interacts with MEF2C (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: High expression in heart, aorta media and bladder.
CC {ECO:0000269|PubMed:20385216}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation regulates negatively transcriptional activity.
CC {ECO:0000250}.
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DR EMBL; AF464909; AAL75447.1; -; mRNA.
DR EMBL; AF464910; AAL75446.1; -; mRNA.
DR EMBL; AB091378; BAC65150.1; -; mRNA.
DR EMBL; BK001422; DAA01467.1; -; mRNA.
DR RefSeq; NP_872608.1; NM_182667.2.
DR AlphaFoldDB; Q8R5I7; -.
DR SMR; Q8R5I7; -.
DR CORUM; Q8R5I7; -.
DR STRING; 10116.ENSRNOP00000054372; -.
DR PaxDb; Q8R5I7; -.
DR Ensembl; ENSRNOT00000057562; ENSRNOP00000054372; ENSRNOG00000003669.
DR GeneID; 246297; -.
DR KEGG; rno:246297; -.
DR UCSC; RGD:631347; rat.
DR CTD; 93649; -.
DR RGD; 631347; Myocd.
DR eggNOG; ENOG502QTAN; Eukaryota.
DR GeneTree; ENSGT00950000182979; -.
DR HOGENOM; CLU_007042_2_0_1; -.
DR InParanoid; Q8R5I7; -.
DR PhylomeDB; Q8R5I7; -.
DR TreeFam; TF326024; -.
DR PRO; PR:Q8R5I7; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003669; Expressed in heart and 10 other tissues.
DR ExpressionAtlas; Q8R5I7; baseline and differential.
DR Genevisible; Q8R5I7; RN.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0035035; F:histone acetyltransferase binding; ISO:RGD.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
DR GO; GO:0070412; F:R-SMAD binding; ISO:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; ISO:RGD.
DR GO; GO:0060947; P:cardiac vascular smooth muscle cell differentiation; IDA:BHF-UCL.
DR GO; GO:0003231; P:cardiac ventricle development; ISO:RGD.
DR GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; IMP:RGD.
DR GO; GO:0043954; P:cellular component maintenance; ISO:RGD.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0048565; P:digestive tract development; ISO:RGD.
DR GO; GO:0097070; P:ductus arteriosus closure; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0035733; P:hepatic stellate cell activation; IMP:RGD.
DR GO; GO:0048286; P:lung alveolus development; ISO:RGD.
DR GO; GO:0042692; P:muscle cell differentiation; ISO:RGD.
DR GO; GO:1900222; P:negative regulation of amyloid-beta clearance; ISO:RGD.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; ISO:RGD.
DR GO; GO:0060354; P:negative regulation of cell adhesion molecule production; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0010832; P:negative regulation of myotube differentiation; ISO:RGD.
DR GO; GO:2000587; P:negative regulation of platelet-derived growth factor receptor-beta signaling pathway; ISO:RGD.
DR GO; GO:2001015; P:negative regulation of skeletal muscle cell differentiation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; ISO:RGD.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:2000727; P:positive regulation of cardiac muscle cell differentiation; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISO:RGD.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:1903800; P:positive regulation of miRNA maturation; ISO:RGD.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:RGD.
DR GO; GO:0051152; P:positive regulation of smooth muscle cell differentiation; ISO:RGD.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; ISO:RGD.
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:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR GO; GO:0001560; P:regulation of cell growth by extracellular stimulus; ISO:RGD.
DR GO; GO:0035065; P:regulation of histone acetylation; ISS:UniProtKB.
DR GO; GO:0045661; P:regulation of myoblast differentiation; ISO:RGD.
DR GO; GO:1900239; P:regulation of phenotypic switching; ISO:RGD.
DR GO; GO:0051150; P:regulation of smooth muscle cell differentiation; IMP:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0001666; P:response to hypoxia; ISO:RGD.
DR GO; GO:0051145; P:smooth muscle cell differentiation; IMP:RGD.
DR GO; GO:0060157; P:urinary bladder development; ISO:RGD.
DR GO; GO:0060065; P:uterus development; ISO:RGD.
DR GO; GO:0035886; P:vascular associated smooth muscle cell differentiation; ISO:RGD.
DR GO; GO:0001570; P:vasculogenesis; ISO:RGD.
DR GO; GO:0055012; P:ventricular cardiac muscle cell differentiation; ISO:RGD.
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; Coiled coil; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation.
FT CHAIN 1..938
FT /note="Myocardin"
FT /id="PRO_0000126633"
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 383..417
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT REGION 37..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..205
FT /note="HDAC5-binding"
FT /evidence="ECO:0000250"
FT REGION 155..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 522..566
FT /evidence="ECO:0000255"
FT MOTIF 12..27
FT /note="MEF2C-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 46..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 457
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 461
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 465
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 469
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 627
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 631
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 635
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 639
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 815
FT /note="Phosphoserine; by MAPK1 AND MAPK3"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 862
FT /note="Phosphoserine; by MAPK1 AND MAPK3"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 869
FT /note="Phosphoserine; by MAPK1 AND MAPK3"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 896
FT /note="Phosphothreonine; by MAPK1 AND MAPK3"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MUTAGEN 534
FT /note="I->T: Abolishes homodimerization."
FT /evidence="ECO:0000269|PubMed:12756293"
FT MUTAGEN 537
FT /note="L->T: Abolishes homodimerization."
FT /evidence="ECO:0000269|PubMed:12756293"
FT MUTAGEN 541
FT /note="L->T: Abolishes homodimerization."
FT /evidence="ECO:0000269|PubMed:12756293"
SQ SEQUENCE 938 AA; 101872 MW; C64F10796AD53618 CRC64;
MTLLGSEHSL LIRRKFRSVL QLRLQQRRTQ EQLANQGLIP PLKSPTEFHD PRKKLDSAKT
EDSLRRKVRN RSDRASLVNM HILQASTAER SIPTAQMKLK RARLADDLNE KIALRPGPLE
LVEKNILPMD SSVKEAIKGT EVSLSKAADA FAFEDDSSRD GLSPDQARSE DPQGSGGSTP
DIKSTEAPLA GPLDTIQDLT PGSESDKNDT ASQLSNQSDS GKQVLGPLST PIPVHTAVKS
KSLGDSKNRH KKPKDPKPKV KKLKYHQYIP PDQKAEKSPP PMDSAYARLL QQQQLFLQLQ
ILSQQQQQQQ QQQQQQQQQQ QQQRFSYPGM HQAHLKEPNE QMTRNPNSSS TPLNNTPLSP
VKNSLSGQTG VSSLKPGPLP PNLDDLKVSE LRQQLRIRGL PVSGTKTALV DRLRPFQDCA
GNPVPNFGDI TTVTFPVTPN TLPSYQSSPS GFYHFGSTSS SPPISPASSD LSAAGSLPDT
FTDASPGFGL HASPVPACTD ESLLSSLNGG SGPSEPDGLD SEKDKMLVEK QKVINQLTWK
LRQEQRQVEE LRMQLQKQKS GCNDQKPLPF LATTIKQEDV SSCPFAAQQA SGKGQGHSSD
SPPPACETAQ LLPHCVESSG QTHVLSSTFL SPQCSPQHSP LGTLKSPQHI SLPPSPNNHY
FLASSSGAQR ENHGVSSPNS SQGCAQMTGL QSSDKVGPTF SIPSPTFPKS SPTVPEITQP
PSYEDAVKQQ MTRSQQMDEL LDVLIESGEM PADAREDHSC LQKIPKIPGS SCSPTTILPK
SSASFEQASS GGQISFDHYA TDSEEHLEVL LNSHSPIGKV SDVTLLKIGS EEPPFDGIMD
GFPGKAAEDL FSAHELLPGP LSPMHTQLSP PSVDSSGLQL SFTESPWETM EWLDLTPPSS
TPGFSNLTSS GPSIFNIDFL DVTDLNLNSP MDLHLQQW
