MYOD1_SHEEP
ID MYOD1_SHEEP Reviewed; 319 AA.
AC P29331;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Myoblast determination protein 1;
GN Name=MYOD1; Synonyms=MYOD;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Coopworth; TISSUE=Thigh muscle;
RX PubMed=1741269; DOI=10.1093/nar/20.2.374;
RA Huynen L., Bass J., Gardner R.C., Bellamy A.R.;
RT "Nucleotide sequence of the sheep MyoD1 gene.";
RL Nucleic Acids Res. 20:374-374(1992).
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; X62102; CAA44012.1; -; mRNA.
DR PIR; S20086; S20086.
DR RefSeq; NP_001009390.1; NM_001009390.1.
DR AlphaFoldDB; P29331; -.
DR SMR; P29331; -.
DR Ensembl; ENSOART00020004894; ENSOARP00020004022; ENSOARG00020003202.
DR GeneID; 443405; -.
DR KEGG; oas:443405; -.
DR CTD; 4654; -.
DR OrthoDB; 1471470at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0000791; C:euchromatin; IEA:Ensembl.
DR GO; GO:0030016; C:myofibril; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:AgBase.
DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR GO; GO:0016922; F:nuclear receptor binding; IEA:Ensembl.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; ISS:UniProtKB.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEA:Ensembl.
DR GO; GO:0071453; P:cellular response to oxygen levels; IEA:Ensembl.
DR GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
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:0007520; P:myoblast fusion; IEA:Ensembl.
DR GO; GO:0014908; P:myotube differentiation involved in skeletal muscle regeneration; IEA:Ensembl.
DR GO; GO:0035562; P:negative regulation of chromatin binding; IEA:Ensembl.
DR GO; GO:2000818; P:negative regulation of myoblast proliferation; IEA:Ensembl.
DR GO; GO:0051099; P:positive regulation of binding; IEA:Ensembl.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:1901741; P:positive regulation of myoblast fusion; IEA:Ensembl.
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:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0043503; P:skeletal muscle fiber adaptation; IEA:Ensembl.
DR GO; GO:0048741; P:skeletal muscle fiber development; IEA:Ensembl.
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:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
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 2: Evidence at transcript level;
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_0000127364"
FT DOMAIN 109..160
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 174..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..208
FT /note="Polar residues"
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; 34209 MW; 92ECB27BAD568E0D CRC64;
MELLSPPLRD VDLTGPDGSL CNFATADDFY DDPCFDSPDL RFFEDLDPRL VHVGALLKPE
EHSHFPAAAH PAPGAREDEH VRAPSGHHQA GRCLLWACKA CKRKTTNADR RKAATMRERR
RLSKVNEAFE TLKRCTSSNP NQRLPKVEIL RNAIRYIEGL QALLRDQDAA PPGAAAAFYA
PGPLPPGRSG EHYSGDSDAS SPRSNCSDGM MDYSGPPSGA RRRNCYDRAY YSEAPNEPRP
GKSAAVSSLD CLSSIVERIS TESPAAPALL LADAPPESSP GPQEAAAGSE VECGTPAPSP
DTAPQGLAGA NPNPIYQVL
