ID   MYODA_XENLA             Reviewed;         289 AA.
AC   P13904; A0A1L8GE03; Q3KQ98;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Myoblast determination protein 1 homolog A;
DE   AltName: Full=Myogenic factor 1;
GN   Name=myod1-a; Synonyms=mf1, myod;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2555164; DOI=10.1002/j.1460-2075.1989.tb08505.x;
RA   Hopwood N.D., Pluck A., Gurdon J.B.;
RT   "MyoD expression in the forming somites is an early response to mesoderm
RT   induction in Xenopus embryos.";
RL   EMBO J. 8:3409-3417(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1690844; DOI=10.1128/mcb.10.4.1516-1524.1990;
RA   Scales J.B., Olson E.N., Perry M.;
RT   "Two distinct Xenopus genes with homology to MyoD1 are expressed before
RT   somite formation in early embryogenesis.";
RL   Mol. Cell. Biol. 10:1516-1524(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2167198; DOI=10.1242/dev.108.4.669;
RA   Harvey R.P.;
RT   "The Xenopus MyoD gene: an unlocalised maternal mRNA predates lineage-
RT   restricted expression in the early embryo.";
RL   Development 108:669-680(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J;
RX   PubMed=27762356; DOI=10.1038/nature19840;
RA   Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA   Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I.,
RA   Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA   Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA   Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA   Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA   Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA   Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA   Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA   Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA   Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA   Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J.,
RA   Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT   "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL   Nature 538:336-343(2016).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May act as a transcriptional activator that promotes
CC       transcription of muscle-specific target genes and plays a role in
CC       muscle differentiation. {ECO:0000250}.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DEVELOPMENTAL STAGE: Expression is specific to the mesoderm of the
CC       gastrula.
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DR   EMBL; X16106; CAA34232.1; -; mRNA.
DR   EMBL; M31116; AAA49900.1; -; mRNA.
DR   EMBL; CM004473; OCT82147.1; -; Genomic_DNA.
DR   EMBL; BC106319; AAI06320.1; -; mRNA.
DR   PIR; A34783; A34783.
DR   AlphaFoldDB; P13904; -.
DR   SMR; P13904; -.
DR   STRING; 8355.P13904; -.
DR   OMA; GPMEMTE; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0071392; P:cellular response to estradiol stimulus; ISS:UniProtKB.
DR   GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IGI:BHF-UCL.
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; IEA:UniProtKB-KW.
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   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..289
FT                   /note="Myoblast determination protein 1 homolog A"
FT                   /id="PRO_0000127370"
FT   DOMAIN          95..146
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          165..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..212
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        255..256
FT                   /note="LQ -> A (in Ref. 2; AAA49900)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   289 AA;  32307 MW;  D0A985DC66136284 CRC64;
     MELLPPPLRD MEVTEGSLCA FPTPDDFYDD PCFNTSDMSF FEDLDPRLVH VTLLKPEEPH
     HNEDEHVRAP SGHHQAGRCL LWACKACKRK TTNADRRKAA TMRERRRLSK VNEAFETLKR
     YTSTNPNQRL PKVEILRNAI RYIESLQALL HDQDEAFYPV LEHYSGDSDA SSPRSNCSDG
     MMDYNSPPCG SRRRNSYDSS FYSDSPNDSR LGKSSVISSL DCLSSIVERI STQSPSCPVP
     TAVDSGSEGS PCSPLQGETL SERVITIPSP SNTCTQLSQD PSSTIYHVL