MYOD1_CAEEL
ID MYOD1_CAEEL Reviewed; 324 AA.
AC P22980;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Myoblast determination protein 1 homolog;
DE Short=MyoD protein 1;
DE AltName: Full=Helix-loop-helix protein 1;
GN Name=hlh-1 {ECO:0000312|WormBase:B0304.1b};
GN ORFNames=B0304.1 {ECO:0000312|WormBase:B0304.1b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=2175254; DOI=10.1016/0092-8674(90)90494-y;
RA Krause M., Fire A., Harrison S.W., Priess J., Weintraub H.;
RT "CeMyoD accumulation defines the body wall muscle cell fate during C.
RT elegans embryogenesis.";
RL Cell 63:907-919(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 222-GLN--LEU-324.
RX PubMed=15892873; DOI=10.1186/gb-2005-6-5-r45;
RA Baugh L.R., Wen J.C., Hill A.A., Slonim D.K., Brown E.L., Hunter C.P.;
RT "Synthetic lethal analysis of Caenorhabditis elegans posterior embryonic
RT patterning genes identifies conserved genetic interactions.";
RL Genome Biol. 6:RESEARCH0045.1-RESEARCH0045.8(2005).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=17142668; DOI=10.1101/gad.1481706;
RA Fukushige T., Brodigan T.M., Schriefer L.A., Waterston R.H., Krause M.;
RT "Defining the transcriptional redundancy of early bodywall muscle
RT development in C. elegans: evidence for a unified theory of animal muscle
RT development.";
RL Genes Dev. 20:3395-3406(2006).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21307099; DOI=10.1242/dev.062240;
RA Tian C., Shi H., Colledge C., Stern M., Waterston R., Liu J.;
RT "The C. elegans SoxC protein SEM-2 opposes differentiation factors to
RT promote a proliferative blast cell fate in the postembryonic mesoderm.";
RL Development 138:1033-1043(2011).
CC -!- FUNCTION: Involved in myogenesis, in cooperation with transcription
CC factors unc-120 and hnd-1 (PubMed:2175254, PubMed:15892873,
CC PubMed:17142668). Acts redundantly with fozi-1 to promote body wall
CC muscle cell and coelomocyte specification in postembryonic mesoderm
CC progenitors, probably through suppression of sem-2 (PubMed:21307099).
CC {ECO:0000269|PubMed:15892873, ECO:0000269|PubMed:17142668,
CC ECO:0000269|PubMed:21307099, ECO:0000269|PubMed:2175254}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:2175254}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b {ECO:0000312|WormBase:B0304.1b};
CC IsoId=P22980-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:B0304.1a};
CC IsoId=P22980-2; Sequence=VSP_002142;
CC Name=c {ECO:0000312|WormBase:B0304.1c};
CC IsoId=P22980-3; Sequence=VSP_002143;
CC -!- TISSUE SPECIFICITY: Body wall muscle cells; in clonal muscle
CC precursors, in a set of early embryonic blastomeres (the ms-
CC granddaughters), and in six glial-like cells called GLRS.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in a low
CC frequency of embryonic lethality, with embryos arresting paralyzed at
CC the two-fold stage; increases in frequency significantly on an hnd-1 or
CC unc-120 mutant background (PubMed:15892873). Many embryos that survive
CC to hatch become uncoordinated, dumpy larvae (PubMed:15892873). Double
CC RNAi-mediated knockdown with sem-2 results in no sex myoblast
CC production (PubMed:21307099). {ECO:0000269|PubMed:15892873,
CC ECO:0000269|PubMed:21307099}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M59940; AAA16289.1; -; Unassigned_DNA.
DR EMBL; M59940; AAA16290.1; -; Unassigned_DNA.
DR EMBL; FO080166; CCD61731.1; -; Genomic_DNA.
DR EMBL; FO080166; CCD61732.1; -; Genomic_DNA.
DR EMBL; FO080166; CCD61733.1; -; Genomic_DNA.
DR PIR; A36289; A36289.
DR PIR; B36289; B36289.
DR RefSeq; NP_001021892.1; NM_001026721.1. [P22980-1]
DR RefSeq; NP_001021893.1; NM_001026722.2. [P22980-3]
DR RefSeq; NP_494798.4; NM_062397.4.
DR AlphaFoldDB; P22980; -.
DR SMR; P22980; -.
DR BioGRID; 39144; 6.
DR IntAct; P22980; 2.
DR STRING; 6239.B0304.1b; -.
DR EPD; P22980; -.
DR PaxDb; P22980; -.
DR PeptideAtlas; P22980; -.
DR PRIDE; P22980; -.
DR EnsemblMetazoa; B0304.1a.1; B0304.1a.1; WBGene00001948. [P22980-2]
DR EnsemblMetazoa; B0304.1a.2; B0304.1a.2; WBGene00001948. [P22980-2]
DR EnsemblMetazoa; B0304.1b.1; B0304.1b.1; WBGene00001948. [P22980-1]
DR EnsemblMetazoa; B0304.1c.1; B0304.1c.1; WBGene00001948. [P22980-3]
DR GeneID; 173788; -.
DR KEGG; cel:CELE_B0304.1; -.
DR UCSC; B0304.1a; c. elegans. [P22980-1]
DR CTD; 173788; -.
DR WormBase; B0304.1a; CE31766; WBGene00001948; hlh-1. [P22980-2]
DR WormBase; B0304.1b; CE02423; WBGene00001948; hlh-1. [P22980-1]
DR WormBase; B0304.1c; CE30067; WBGene00001948; hlh-1. [P22980-3]
DR eggNOG; KOG3960; Eukaryota.
DR GeneTree; ENSGT00950000182959; -.
DR InParanoid; P22980; -.
DR OMA; IMEQNQH; -.
DR OrthoDB; 1433570at2759; -.
DR Reactome; R-CEL-525793; Myogenesis.
DR PRO; PR:P22980; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001948; Expressed in embryonic cell and 98 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:WormBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:WormBase.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:WormBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:WormBase.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0048337; P:positive regulation of mesodermal cell fate specification; IGI:UniProtKB.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; IGI:UniProtKB.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:WormBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:WormBase.
DR GO; GO:0051146; P:striated muscle cell differentiation; IMP:WormBase.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR039704; Myogenic_factor.
DR PANTHER; PTHR11534; PTHR11534; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Differentiation; DNA-binding;
KW Myogenesis; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..324
FT /note="Myoblast determination protein 1 homolog"
FT /id="PRO_0000127373"
FT DOMAIN 155..206
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 125..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 150..154
FT /note="FVLSV -> L (in isoform a)"
FT /evidence="ECO:0000303|PubMed:2175254"
FT /id="VSP_002142"
FT VAR_SEQ 277..324
FT /note="AVDLRRRNSLDRLSRIVASIPNEEAMTDEQLLQPANDVIDGEKKLEML ->
FT GELLLKTNGRSASAKLFGQIVADRCEHSQRGSNDRRTTPPTSK (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_002143"
FT MUTAGEN 222..324
FT /note="Missing: In cc561; low frequency of embryonic
FT lethality, with embryos arresting paralyzed at the two-fold
FT stage (Pat); increases in frequency significantly on an
FT hnd-1 or unc-120 mutant background. Many embryos that
FT survive to hatch become uncoordinated, dumpy larvae."
FT /evidence="ECO:0000269|PubMed:15892873"
SQ SEQUENCE 324 AA; 36449 MW; 3899BA6C7C6AC83F CRC64;
MNTETSTQSA PSDTYDTSIY YNSSPRVTAN DITTLTSFAA PAPQVLDYAN TQYDIYRNQP
AYYLPSYAPT APTTFYSDFA NFNVTRSQDF ASVPAVANSS DVKPIIIKQE KSTPNATELI
IQSRVDSQHE DTTTSTAGGA GVGGPRRTKF VLSVDRRKAA TMRERRRLRK VNEAFEVVKQ
RTCPNPNQRL PKVEILRSAI DYINNLERML QQAGKMTKIM EQNQHLQMTQ QINGAPPHDY
VTSSHFASSS YNPENMFDDD DLTDSDDDRD HHKLGNAVDL RRRNSLDRLS RIVASIPNEE
AMTDEQLLQP ANDVIDGEKK LEML
