MYOD1_COTJA
ID MYOD1_COTJA Reviewed; 297 AA.
AC P21572;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Myoblast determination protein 1 homolog;
DE AltName: Full=Myogenic factor 1;
GN Name=MYOD1; Synonyms=MF1;
OS Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2361591; DOI=10.1101/gad.4.4.567;
RA de la Brousse C.F., Emerson C.P. Jr.;
RT "Localized expression of a myogenic regulatory gene, qmf1, in the somite
RT dermatome of avian embryos.";
RL Genes Dev. 4:567-581(1990).
CC -!- FUNCTION: Acts as a transcriptional activator that promotes
CC transcription of muscle-specific target genes and plays a role in
CC muscle differentiation. Induces fibroblasts to differentiate into
CC myoblasts. Interacts with and is inhibited by the twist protein. This
CC interaction probably involves the basic domains of both proteins (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Seems to form active heterodimers with ITF-2.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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DR EMBL; L16686; AAA49495.1; -; mRNA.
DR PIR; A35874; A35874.
DR RefSeq; XP_015719628.1; XM_015864142.1.
DR AlphaFoldDB; P21572; -.
DR SMR; P21572; -.
DR Ensembl; ENSCJPT00005018298; ENSCJPP00005012666; ENSCJPG00005010754.
DR GeneID; 107314669; -.
DR KEGG; cjo:107314669; -.
DR CTD; 4654; -.
DR GeneTree; ENSGT00950000182959; -.
DR OrthoDB; 1471470at2759; -.
DR Proteomes; UP000694412; Chromosome 5.
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:0005667; C:transcription regulator complex; IEA:Ensembl.
DR GO; GO:0043425; F:bHLH transcription factor binding; IEA:Ensembl.
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: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:0007518; P:myoblast fate determination; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:1901741; P:positive regulation of myoblast fusion; IEA:Ensembl.
DR GO; GO:0043415; P:positive regulation of skeletal muscle tissue regeneration; IEA:Ensembl.
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; IEA:Ensembl.
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:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
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 Activator; Developmental protein; Differentiation; DNA-binding; Myogenesis;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..297
FT /note="Myoblast determination protein 1 homolog"
FT /id="PRO_0000127366"
FT DOMAIN 101..152
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 52..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 297 AA; 32951 MW; 547F3691083CE4B2 CRC64;
MDLLGPMEMT EGSLCSFAAA DDFYDDPCFN TSDMHFFEDL DPRLVHVGGL LKPEEHPHHH
GHHHGHPHEE EHVRAPSGHH QAGRCLLWAC KACKRKTTNA DRRKAATMRE RRRLSKVNEA
FETLKRCTST NPNQRLPKVE ILRNAIRYIE SLQALLREQE DAYYPVLEHY SGESDASSPR
SNCSDGMMEY SGPPCSSRRR NSYDSSYYTE SPNDPKHGKS SVVSSLDCLS SIVERISTDN
STCPILPPAE AVAEGSPCSP QEGASLNDSG AQIPSPTNCT PLPQDSSSSS NPIYQVL
