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MYOD_DROME
ID   MYOD_DROME              Reviewed;         332 AA.
AC   P22816; Q9VCJ1;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 3.
DT   03-AUG-2022, entry version 173.
DE   RecName: Full=Myogenic-determination protein;
DE   AltName: Full=Protein nautilus;
DE   AltName: Full=dMyd;
GN   Name=nau; Synonyms=MYD; ORFNames=CG10250;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=1902570; DOI=10.1073/pnas.88.9.3782;
RA   Paterson B.M., Walldorf U., Eldridge J., Duebendorfer A., Frasch M.,
RA   Gehring W.J.;
RT   "The Drosophila homologue of vertebrate myogenic-determination genes
RT   encodes a transiently expressed nuclear protein marking primary myogenic
RT   cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:3782-3786(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=2176634; DOI=10.1101/gad.4.12a.2086;
RA   Michelson A.M., Abmayr S.M., Bate M., Arias A.M., Maniatis T.;
RT   "Expression of a MyoD family member prefigures muscle pattern in Drosophila
RT   embryos.";
RL   Genes Dev. 4:2086-2097(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
CC   -!- FUNCTION: May play an important role in the early development of
CC       muscle. {ECO:0000269|PubMed:2176634}.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC       ECO:0000269|PubMed:1902570}.
CC   -!- DEVELOPMENTAL STAGE: Initially localized to segmentally repeated
CC       clusters of mesodermal cells, and subsequently in at least a subset of
CC       growing muscle precursors and mature muscle fibers that exhibit
CC       distinct segmental differences. {ECO:0000269|PubMed:1902570,
CC       ECO:0000269|PubMed:2176634}.
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DR   EMBL; M68897; AAA28477.1; -; mRNA.
DR   EMBL; X56161; CAA39629.1; -; mRNA.
DR   EMBL; AE014297; AAF56168.1; -; Genomic_DNA.
DR   PIR; A36663; A36663.
DR   RefSeq; NP_476650.1; NM_057302.3.
DR   AlphaFoldDB; P22816; -.
DR   SMR; P22816; -.
DR   BioGRID; 67737; 18.
DR   IntAct; P22816; 5.
DR   STRING; 7227.FBpp0083863; -.
DR   PaxDb; P22816; -.
DR   DNASU; 42799; -.
DR   EnsemblMetazoa; FBtr0084472; FBpp0083863; FBgn0002922.
DR   GeneID; 42799; -.
DR   KEGG; dme:Dmel_CG10250; -.
DR   CTD; 42799; -.
DR   FlyBase; FBgn0002922; nau.
DR   VEuPathDB; VectorBase:FBgn0002922; -.
DR   eggNOG; KOG3960; Eukaryota.
DR   GeneTree; ENSGT00950000182959; -.
DR   HOGENOM; CLU_804791_0_0_1; -.
DR   InParanoid; P22816; -.
DR   PhylomeDB; P22816; -.
DR   Reactome; R-DME-525793; Myogenesis.
DR   SignaLink; P22816; -.
DR   BioGRID-ORCS; 42799; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 42799; -.
DR   PRO; PR:P22816; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0002922; Expressed in embryonic/larval somatic muscle (Drosophila) and 5 other tissues.
DR   ExpressionAtlas; P22816; baseline and differential.
DR   Genevisible; P22816; DM.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0016204; P:determination of muscle attachment site; IMP:FlyBase.
DR   GO; GO:0007526; P:larval somatic muscle development; IMP:FlyBase.
DR   GO; GO:0007517; P:muscle organ development; IMP:FlyBase.
DR   GO; GO:0045663; P:positive regulation of myoblast differentiation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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   Developmental protein; Differentiation; DNA-binding; Myogenesis; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..332
FT                   /note="Myogenic-determination protein"
FT                   /id="PRO_0000127374"
FT   DOMAIN          161..212
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          22..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        28..29
FT                   /note="PT -> QA (in Ref. 2; CAA39629)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        95..97
FT                   /note="HPA -> NPV (in Ref. 3; AAF56168)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        131
FT                   /note="L -> H (in Ref. 1; AAA28477)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   332 AA;  36185 MW;  5DD23D24CAA8BEFC CRC64;
     MTKYNSGSSE MPAAQTIKQE YHNGYGQPTH PGYGFSAYSQ QNPIAHPGQN PHQTLQNFFS
     RFNAVGDASA GNGGAASISA NGSGSSCNYS HANHHPAELD KPLGMNMTPS PIYTTDYDDE
     NSSLSSEEHV LAPLVCSSAQ SSRPCLTWAC KACKKKSVTV DRRKAATMRE RRRLRKVNEA
     FEILKRRTSS NPNQRLPKVE ILRNAIEYIE SLEDLLQESS TTRDGDNLAP SLSGKSCQSD
     YLSSYAGAYL EDKLSFYNKH MEKYGQFTDF DGNANGSSLD CLNLIVQSIN KSTTSPIQNK
     ATPSASDTQS PPSSGATAPT SLHVNFKRKC ST
 
 
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