MYOD1_PIG
ID MYOD1_PIG Reviewed; 319 AA.
AC P49811;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Myoblast determination protein 1;
GN Name=MYOD1; Synonyms=MYOD;
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 [GENOMIC DNA].
RC STRAIN=Large white X Landrace;
RX PubMed=7559997; DOI=10.1007/bf00121133;
RA Chang K.C., Fernandes K., Chantler P.D.;
RT "Cloning and in vivo expression of the pig MyoD gene.";
RL J. Muscle Res. Cell Motil. 16:243-247(1995).
CC -!- FUNCTION: Acts as a transcriptional activator that promotes
CC transcription of muscle-specific target genes and plays a role in
CC muscle differentiation. Together with MYF5 and MYOG, co-occupies
CC muscle-specific gene promoter core region during myogenesis. Induces
CC fibroblasts to differentiate into myoblasts. Interacts with and is
CC inhibited by the twist protein. This interaction probably involves the
CC basic domains of both proteins (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Seems to form active heterodimers with ITF-2. Interacts with
CC SUV39H1. Interacts with DDX5. Interacts with CHD2. Interacts with
CC TSC22D3 (By similarity). Interacts with SETD3 (By similarity).
CC Interacts with P-TEFB complex; promotes the transcriptional activity of
CC MYOD1 through its CDK9-mediated phosphorylation (By similarity).
CC Interacts with CSRP3 (By similarity). Interacts with NUPR1 (By
CC similarity). {ECO:0000250|UniProtKB:P10085,
CC ECO:0000250|UniProtKB:Q02346}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Phosphorylated by CDK9. This phosphorylation promotes its function
CC in muscle differentiation (By similarity). {ECO:0000250}.
CC -!- PTM: Acetylated by a complex containing EP300 and PCAF. The acetylation
CC is essential to activate target genes. Conversely, its deacetylation by
CC SIRT1 inhibits its function (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated on the N-terminus; which is required for proteasomal
CC degradation. {ECO:0000250}.
CC -!- PTM: Methylation at Lys-104 by EHMT2/G9a inhibits myogenic activity.
CC {ECO:0000250}.
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DR EMBL; U12574; AAA87061.1; -; Genomic_DNA.
DR RefSeq; NP_001002824.1; NM_001002824.1.
DR AlphaFoldDB; P49811; -.
DR SMR; P49811; -.
DR STRING; 9823.ENSSSCP00000014214; -.
DR PaxDb; P49811; -.
DR GeneID; 407604; -.
DR KEGG; ssc:407604; -.
DR CTD; 4654; -.
DR eggNOG; KOG3960; Eukaryota.
DR InParanoid; P49811; -.
DR OrthoDB; 1471470at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; ISS:AgBase.
DR GO; GO:0043425; F:bHLH transcription factor binding; ISS:AgBase.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:AgBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
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:0071392; P:cellular response to estradiol stimulus; ISS:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; ISS:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; ISS:AgBase.
DR GO; GO:0045445; P:myoblast differentiation; ISS:UniProtKB.
DR GO; GO:0007518; P:myoblast fate determination; ISS:UniProtKB.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IBA:GO_Central.
DR GO; GO:0048743; P:positive regulation of skeletal muscle fiber development; IBA:GO_Central.
DR GO; GO:0043415; P:positive regulation of skeletal muscle tissue regeneration; ISS:UniProtKB.
DR GO; GO:1905382; P:positive regulation of snRNA transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IBA:GO_Central.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISS:UniProtKB.
DR GO; GO:0051146; P:striated muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; ISS:AgBase.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR022032; Myf5.
DR InterPro; IPR002546; MyoD_N.
DR InterPro; IPR039704; Myogenic_factor.
DR PANTHER; PTHR11534; PTHR11534; 1.
DR Pfam; PF01586; Basic; 1.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF12232; Myf5; 1.
DR SMART; SM00520; BASIC; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 3: Inferred from homology;
KW Acetylation; Activator; Developmental protein; Differentiation;
KW DNA-binding; Methylation; Myogenesis; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..319
FT /note="Myoblast determination protein 1"
FT /id="PRO_0000127362"
FT DOMAIN 109..160
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 174..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 104
FT /note="N6-methyllysine; by EHMT2"
FT /evidence="ECO:0000250|UniProtKB:P15172"
FT CROSSLNK 1
FT /note="Peptide (Met-Gly) (interchain with G-Cter in
FT ubiquitin)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 319 AA; 34243 MW; B84E5A5C8CF9B288 CRC64;
MELLSPPLRD VDLTGPDGSL CNFATADDFY DDPCFDSPDL RFFEDLDPRL VHVGALLKPE
EHSHFPAAAH PAPGAREDEH VRAPSGHHQA GRCLLWACKA CKRKTTNADR RKAATMRERR
RLSKVNEAFE TLKRCTSSNP NQRLPKVEIL RNAIRYIEGL QALLRDQDAA PPGAAAAFYA
PGPLPPGRGG EHYSGDSDAS SPRSNCSDGM MDYSGPPSGA RRRNCYDGTY YSEAPSEPRP
GKNAAVSSLD CLSSIVESIS TESPAAPALL LADTPRESSP GPQEAAAGSE VERGTPTPSP
DAAPQCPASA NPNPIYQVL
