ID   MYOG_COTJA              Reviewed;         226 AA.
AC   P34060;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Myogenin;
DE   AltName: Full=Myogenic factor 2;
GN   Name=MYOG; Synonyms=MF2;
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].
RC   TISSUE=Muscle;
RX   PubMed=1315698; DOI=10.1016/0012-1606(92)90214-2;
RA   Pownall M.E., Emerson C.P. Jr.;
RT   "Sequential activation of three myogenic regulatory genes during somite
RT   morphogenesis in quail embryos.";
RL   Dev. Biol. 151:67-79(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. Induces somite cells to differentiate into
CC       myoblasts. Probable sequence specific DNA-binding protein (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer and heterodimer. Efficient DNA binding requires
CC       dimerization with another bHLH protein (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
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DR   EMBL; L15473; AAA49496.1; -; mRNA.
DR   PIR; A43912; A43912.
DR   AlphaFoldDB; P34060; -.
DR   SMR; P34060; -.
DR   Proteomes; UP000694412; Unplaced.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0032993; C:protein-DNA complex; ISS:UniProtKB.
DR   GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0071392; P:cellular response to estradiol stimulus; ISS:UniProtKB.
DR   GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0014737; P:positive regulation of muscle atrophy; ISS:UniProtKB.
DR   GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:UniProtKB.
DR   GO; GO:0010831; P:positive regulation of myotube differentiation; ISS:UniProtKB.
DR   GO; GO:0048743; P:positive regulation of skeletal muscle fiber development; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR   GO; GO:1901739; P:regulation of myoblast fusion; ISS:UniProtKB.
DR   GO; GO:0014842; P:regulation of skeletal muscle satellite cell proliferation; ISS:UniProtKB.
DR   GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; ISS:UniProtKB.
DR   GO; GO:0014878; P:response to electrical stimulus involved in regulation of muscle adaptation; ISS:UniProtKB.
DR   GO; GO:0014873; P:response to muscle activity involved in regulation of muscle adaptation; ISS:UniProtKB.
DR   GO; GO:0014891; P:striated muscle atrophy; ISS:UniProtKB.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
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   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..226
FT                   /note="Myogenin"
FT                   /id="PRO_0000127380"
FT   DOMAIN          82..133
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          143..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   226 AA;  25688 MW;  49B9677108AE404D CRC64;
     MSDFILKKSF FPEQRFYDGE NFLGSRLQGY EAATFPERPE VSLCPESRGA LEEKDSTLPD
     HCPGQCLPWA CKICKRKTVS IDRRRAATLR EKRRLKKVNE AFEALKRSTL LNPNQRLPKV
     EILRSSIQYT ERLQSLLSLN QQERDERELR YRPTAPQPAA PSECGSGSSS CSPEWSTQLE
     FGTNPTDHLL SDDAAEDRNL HSLSSIVESI AVEDVAVTFP EERVQN