MYOD1_TAKRU
ID MYOD1_TAKRU Reviewed; 307 AA.
AC Q6Q2A8; Q2HWR0; Q6SYV8; Q6SYW0;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Myoblast determination protein 1 homolog;
DE AltName: Full=Myogenic factor 1;
DE AltName: Full=TmyoD1;
GN Name=myod;
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3), AND TISSUE
RP SPECIFICITY.
RX PubMed=17292566; DOI=10.1016/j.gene.2006.12.015;
RA Fernandes J.M., Kinghorn J.R., Johnston I.A.;
RT "Differential regulation of multiple alternatively spliced transcripts of
RT MyoD.";
RL Gene 391:178-185(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Ikeda D., Ono Y., Snell P., Edwards Y.J., Elgar G., Watabe S.;
RT "Evolutionary lineage of the fish myosin heavy chain gene family different
RT from the tetrapod counterpart: evidence by comparative analysis based on
RT torafugu Takifugu rubripes genome database.";
RL Submitted (SEP-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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=TmyoD1-beta;
CC IsoId=Q6Q2A8-1; Sequence=Displayed;
CC Name=2; Synonyms=TmyoD1-alpha;
CC IsoId=Q6Q2A8-2; Sequence=VSP_024457;
CC Name=3; Synonyms=TmyoD1-gamma;
CC IsoId=Q6Q2A8-3; Sequence=VSP_024455, VSP_024456;
CC -!- TISSUE SPECIFICITY: Expressed in fast and myotomal muscle. Very weak
CC expression in brain, skin and gonads. {ECO:0000269|PubMed:17292566}.
CC -!- MISCELLANEOUS: [Isoform 2]: Most abundant isoform. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
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DR EMBL; AY566281; AAS76647.1; -; Genomic_DNA.
DR EMBL; AY445315; AAR39413.1; -; mRNA.
DR EMBL; AY445316; AAR39414.1; -; mRNA.
DR EMBL; AY445317; AAR39415.1; -; mRNA.
DR EMBL; AB235116; BAE79389.1; -; mRNA.
DR RefSeq; NP_001027941.1; NM_001032769.1. [Q6Q2A8-3]
DR AlphaFoldDB; Q6Q2A8; -.
DR SMR; Q6Q2A8; -.
DR STRING; 31033.ENSTRUP00000042483; -.
DR Ensembl; ENSTRUT00000042627; ENSTRUP00000042483; ENSTRUG00000016609. [Q6Q2A8-2]
DR GeneID; 446036; -.
DR KEGG; tru:446036; -.
DR CTD; 4654; -.
DR eggNOG; KOG3960; Eukaryota.
DR GeneTree; ENSGT00950000182959; -.
DR InParanoid; Q6Q2A8; -.
DR OMA; GPMEMTE; -.
DR OrthoDB; 1471470at2759; -.
DR TreeFam; TF316344; -.
DR Proteomes; UP000005226; Chromosome 9.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0002074; P:extraocular skeletal muscle development; IEA:Ensembl.
DR GO; GO:0043282; P:pharyngeal muscle development; IEA:Ensembl.
DR GO; GO:1905382; P:positive regulation of snRNA transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0048741; P:skeletal muscle fiber development; IEA:Ensembl.
DR GO; GO:0055002; P:striated muscle cell development; 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; 2.
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; Alternative splicing; Developmental protein; Differentiation;
KW DNA-binding; Myogenesis; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..307
FT /note="Myoblast determination protein 1 homolog"
FT /id="PRO_0000284129"
FT DOMAIN 109..160
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 271..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 197..207
FT /note="TDFNGPTCQSN -> VGPGPGGINVH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17292566"
FT /id="VSP_024455"
FT VAR_SEQ 208..307
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17292566"
FT /id="VSP_024456"
FT VAR_SEQ 223..248
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17292566, ECO:0000303|Ref.2"
FT /id="VSP_024457"
FT CONFLICT 136
FT /note="T -> K (in Ref. 2; BAE79389)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="V -> G (in Ref. 2; BAE79389)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 307 AA; 33630 MW; 0AA399E22E246A13 CRC64;
MELSEISFSI PAADDFYDDP CFSTSDMHFF EDMDPRLVHA GLLKPDDCCS SSSLSPSSSS
ASPSSLLHIH HHTEAEDDEH IRAPSGHHHA GRCLLWACKA CKRKTTNVDR RKAATLRERR
RLSKVNEAFE TLKRCTNTNP NQRLPKVEIL RNAISYIESL QALLRGGQDE AFYTVLEHYS
GDSDASSPRS NCSDGMTDFN GPTCQSNRRG SYYSSYFSQT PKAFAPPGSA IFVPPGSVNN
CSAWFCFAGS LKAERNSSLD CLSSIVERIS TATSSGPPPV DGRGSPGPLQ ASSPRSSREP
NLIYQVL
