MYCD_PIG
ID MYCD_PIG Reviewed; 933 AA.
AC Q7YR76;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Myocardin;
GN Name=MYOCD;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Large white; TISSUE=Heart;
RX PubMed=12920479; DOI=10.1007/s00109-003-0470-7;
RA Torrado M., Lopez E., Centeno A., Medrano C., Castro-Beiras A.,
RA Mikhailov A.T.;
RT "Myocardin mRNA is augmented in the failing myocardium: expression
RT profiling in the porcine model and human dilated cardiomyopathy.";
RL J. Mol. Med. 81:566-577(2003).
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) (By similarity).
CC {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) (By similarity). Interacts with
CC HDAC4 and HDAC5 (By similarity). Interacts with MEF2C (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the heart and in smooth muscle cells-
CC containing tissues (aorta, pulmonary vein, lung), but is not detectable
CC in skeletal muscle, liver, kidney and spleen.
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 the intrinsic myocardin
CC transcriptional activity. {ECO:0000250}.
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DR EMBL; AY292293; AAQ19023.1; -; mRNA.
DR RefSeq; NP_998910.1; NM_213745.1.
DR AlphaFoldDB; Q7YR76; -.
DR SMR; Q7YR76; -.
DR PRIDE; Q7YR76; -.
DR Ensembl; ENSSSCT00035056954; ENSSSCP00035022907; ENSSSCG00035042838.
DR Ensembl; ENSSSCT00055043628; ENSSSCP00055034732; ENSSSCG00055021922.
DR Ensembl; ENSSSCT00065042841; ENSSSCP00065018194; ENSSSCG00065031624.
DR GeneID; 396571; -.
DR KEGG; ssc:396571; -.
DR CTD; 93649; -.
DR InParanoid; Q7YR76; -.
DR OrthoDB; 190145at2759; -.
DR ChiTaRS; MYOCD; pig.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; IBA:GO_Central.
DR GO; GO:2000727; P:positive regulation of cardiac muscle cell differentiation; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035065; P:regulation of histone acetylation; ISS:UniProtKB.
DR GO; GO:0051145; P:smooth muscle cell differentiation; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Activator; Coiled coil; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation.
FT CHAIN 1..933
FT /note="Myocardin"
FT /id="PRO_0000412529"
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 368..402
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT REGION 153..205
FT /note="HDAC5-binding"
FT /evidence="ECO:0000250"
FT REGION 154..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 515..550
FT /evidence="ECO:0000255"
FT MOTIF 12..27
FT /note="MEF2C-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 159..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 445
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 449
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 453
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 457
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 621
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 625
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 629
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 633
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 810
FT /note="Phosphoserine; by MAPK1 AND MAPK3"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 857
FT /note="Phosphoserine; by MAPK1 AND MAPK3"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 864
FT /note="Phosphoserine; by MAPK1 AND MAPK3"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 891
FT /note="Phosphothreonine; by MAPK1 AND MAPK3"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
SQ SEQUENCE 933 AA; 100652 MW; 516999CFC1F7EDFF CRC64;
MTLLGSEHSL LIRSKFRSVL QLRLQQRRTQ EQLANEGIIP PLRSPPAFHE QRRRLESDKA
ADTLKHKVRN RSDRGNVVKM HILQASSAER PVPAAQMKLK RARLADDLNE KIALRPGPLE
LVEKNILPVD CAVKEAIKGN QVSLSKSADA FAFEEDSSSD GLSPDQTRSE DLPGSAGSPL
DTKAAETPLA GPRGTVQDLT LGSENERNDS APQSGNQSDL GKQGLGPLGS PLPVHAAVKS
KSLSDGKNRH KKPKDPKPKV KKLKYHQYIP PDQKAEKSPP PMDSAYARLL QQQQLFLQLQ
ILSQQQQHRF SYPGIHQAQL KEPNEQMARN PNSSSAPLSS TPLSPAKNSF SGQTGVSSLK
PGPLPSNLDD LKVSELRQQL RIRGLPVSGT KTALMDRLRP FQDCSGNPVP NFGDITTVTF
PVTPSNALPS YQSSPSTSAF YHFGSTSSSP PISPASSDLS VAGSLPDTFN DASPSFGLHP
SPVHACAEES LMSSLNGGSL PPELDGLDSE KDKMLVEKQK VINELTWKLQ QEQRQVEELR
MQLQKQKRGT CPEKKPLPFL AAPIKQEDAG SSCPFAPLPR AVKRQSNSSE EQPAAGDAAR
LRPLGNTHCA ESSGQTNVLS STFLSPQCSP QHSPFGAVKS PQHISLPPSP NNPYFLPASS
GAPGEEHRVS SPVSSQVCTA QMVGLHSSDK AGPKFSNPSP TFSKSASAVS EITQPPSYED
AVKQQMTRSQ QMDELLDVLI ESGEMPADAR EDHSCLQKVP KIPGSSRSPT AALPKPSATF
DQASSGGQLA FDHYSNDSDE HLEVLLNSQS PLGKVSEVAL LKIGSEEPAF DGMADGFSGK
AAEELFNAHE ILPGPLSPMH TQFSPSSVDS SGLPLGFTES PWESMEWLDL TPPSSTQGFS
SLSTGGPSIF NIDFLDVTDL NLNSPMDLHL QQW
