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MYOD1_CHICK
ID   MYOD1_CHICK             Reviewed;         298 AA.
AC   P16075; Q90916;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Myoblast determination protein 1 homolog;
DE            Short=MYOD1 homolog;
GN   Name=MYOD1; Synonyms=CMD1, MYOD;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2777078; DOI=10.1101/gad.3.7.986;
RA   Lin Z.Y., Dechesne C.A., Eldridge J., Paterson B.M.;
RT   "An avian muscle factor related to MyoD1 activates muscle-specific
RT   promoters in nonmuscle cells of different germ-layer origin and in BrdU-
RT   treated myoblasts.";
RL   Genes Dev. 3:986-996(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SPAFAS; TISSUE=Skeletal muscle;
RX   PubMed=8035824; DOI=10.1128/mcb.14.8.5474-5486.1994;
RA   Dechesne C.A., Wei Q., Eldridge J., Gannoun-Zaki L., Millasseau P.,
RA   Bougueleret L., Caterina D., Paterson B.M.;
RT   "E-box- and MEF-2-independent muscle-specific expression, positive
RT   autoregulation, and cross-activation of the chicken MyoD (CMD1) promoter
RT   reveal an indirect regulatory pathway.";
RL   Mol. Cell. Biol. 14:5474-5486(1994).
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; X16189; CAA34315.1; -; mRNA.
DR   EMBL; L34006; AAA74374.1; -; Genomic_DNA.
DR   PIR; A32872; A32872.
DR   RefSeq; NP_989545.2; NM_204214.2.
DR   AlphaFoldDB; P16075; -.
DR   SMR; P16075; -.
DR   STRING; 9031.ENSGALP00000038684; -.
DR   GeneID; 374048; -.
DR   KEGG; gga:374048; -.
DR   CTD; 4654; -.
DR   VEuPathDB; HostDB:geneid_374048; -.
DR   eggNOG; KOG3960; Eukaryota.
DR   InParanoid; P16075; -.
DR   OrthoDB; 1471470at2759; -.
DR   PhylomeDB; P16075; -.
DR   PRO; PR:P16075; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005667; C:transcription regulator complex; IDA:BHF-UCL.
DR   GO; GO:0043425; F:bHLH transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0070888; F:E-box binding; IDA:BHF-UCL.
DR   GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0071392; P:cellular response to estradiol stimulus; ISS:UniProtKB.
DR   GO; GO:0043966; P:histone H3 acetylation; ISS:UniProtKB.
DR   GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR   GO; GO:0042693; P:muscle cell fate commitment; IDA:BHF-UCL.
DR   GO; GO:0007517; P:muscle organ development; NAS:AgBase.
DR   GO; GO:0045663; P:positive regulation of myoblast differentiation; IBA:GO_Central.
DR   GO; GO:0048743; P:positive regulation of skeletal muscle fiber development; IBA:GO_Central.
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; IDA:BHF-UCL.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0035914; P:skeletal muscle cell differentiation; IBA:GO_Central.
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..298
FT                   /note="Myoblast determination protein 1 homolog"
FT                   /id="PRO_0000127365"
FT   DOMAIN          100..151
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          53..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          170..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..298
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        53
FT                   /note="P -> A (in Ref. 1; CAA34315)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   298 AA;  32991 MW;  1C001869E4657B7A CRC64;
     MDLLGPMEMT EGSLCSFTAA DDFYDDPCFN TSDMHFFEDL DPRLVHVGGL LKPEEHPHTR
     APPREPTEEE HVRAPSGHHQ AGRCLLWACK ACKRKTTNAD RRKAATMRER RRLSKVNEAF
     ETLKRCTSTN PNQRLPKVEI LRNAIRYIES LQALLREQED AYYPVLEHYS GESDASSPRS
     NCSDGMMEYS GPPCSSRRRN SYDSSYYTES PNDPKHGKSS VVSSLDCLSS IVERISTDNS
     TCPILPPAEA VAEGSPCSPQ EGGNLSDSGA QIPSPTNCTP LPQESSSSSS SNPIYQVL
 
 
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