DEI_DROME
ID DEI_DROME Reviewed; 384 AA.
AC P41894; Q961H7; Q9VBF2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Helix-loop-helix protein delilah;
DE AltName: Full=Protein taxi;
GN Name=tx; Synonyms=dei; ORFNames=CG5441;
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], FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Epidermis;
RX PubMed=8196652; DOI=10.1128/mcb.14.6.4145-4154.1994;
RA Armand P., Knapp A.C., Hirsch A.J., Wieschaus E.F., Cole M.D.;
RT "A novel basic helix-loop-helix protein is expressed in muscle attachment
RT sites of the Drosophila epidermis.";
RL Mol. Cell. Biol. 14:4145-4154(1994).
RN [2]
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 [3]
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably plays an important role in the differentiation of
CC epidermal cells into the tendon cells that form the attachment sites
CC for all muscles. {ECO:0000269|PubMed:8196652}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein, possibly with da. {ECO:0000269|PubMed:8196652}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed almost exclusively in the attachments
CC sites of the somatic muscles to tendon cells in the epidermis.
CC {ECO:0000269|PubMed:8196652}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA28449.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L33401; AAA28449.1; ALT_FRAME; mRNA.
DR EMBL; AE014297; AAF56590.1; -; Genomic_DNA.
DR EMBL; AY051581; AAK93005.1; -; mRNA.
DR EMBL; BT003640; AAO39644.1; -; mRNA.
DR PIR; A56066; A56066.
DR RefSeq; NP_001287543.1; NM_001300614.1.
DR RefSeq; NP_524516.2; NM_079792.3.
DR AlphaFoldDB; P41894; -.
DR SMR; P41894; -.
DR BioGRID; 68086; 25.
DR IntAct; P41894; 6.
DR STRING; 7227.FBpp0084381; -.
DR PaxDb; P41894; -.
DR DNASU; 43190; -.
DR EnsemblMetazoa; FBtr0085009; FBpp0084381; FBgn0263118.
DR EnsemblMetazoa; FBtr0339598; FBpp0308670; FBgn0263118.
DR GeneID; 43190; -.
DR KEGG; dme:Dmel_CG5441; -.
DR UCSC; CG5441-RA; d. melanogaster.
DR CTD; 43190; -.
DR FlyBase; FBgn0263118; tx.
DR VEuPathDB; VectorBase:FBgn0263118; -.
DR eggNOG; KOG4395; Eukaryota.
DR HOGENOM; CLU_720163_0_0_1; -.
DR InParanoid; P41894; -.
DR OMA; QPSACIS; -.
DR OrthoDB; 990874at2759; -.
DR PhylomeDB; P41894; -.
DR BioGRID-ORCS; 43190; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43190; -.
DR PRO; PR:P41894; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0263118; Expressed in capitellum (Drosophila) and 25 other tissues.
DR ExpressionAtlas; P41894; baseline and differential.
DR Genevisible; P41894; DM.
DR GO; GO:0005634; C:nucleus; HDA:FlyBase.
DR GO; GO:0043425; F:bHLH transcription factor binding; IDA:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:FlyBase.
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:0033627; P:cell adhesion mediated by integrin; IMP:FlyBase.
DR GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
DR GO; GO:0007498; P:mesoderm development; IEP:FlyBase.
DR GO; GO:0016203; P:muscle attachment; TAS:FlyBase.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:FlyBase.
DR GO; GO:0007525; P:somatic muscle development; TAS:FlyBase.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
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 Developmental protein; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..384
FT /note="Helix-loop-helix protein delilah"
FT /id="PRO_0000127167"
FT DOMAIN 94..153
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 244..250
FT /note="IGSPASS -> DWIACLL (in Ref. 1; AAA28449)"
FT /evidence="ECO:0000305"
FT CONFLICT 355..356
FT /note="QP -> HR (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 384 AA; 41549 MW; E79F820623F491B1 CRC64;
MKSNTYELHN YADLNDMARA TDSKDSRKRK TASARGEKYS LRQKRQKRGS NEDGESANLA
DFQLELDPIA EPASKSRKNA PTKSKTKAPP LSKYRRKTAN ARERTRMREI NTAFETLRHC
VPEAIKGEDA ANTNEKLTKI TTLRLAMKYI TMLTDSIRDP SYESEFIGEC LEESANREAR
VDLEANEEAE VELPVPVAKK PAKTKGSGKK SSAASKRQSQ KQAKIVPQIP PISSGESCYA
TSSIGSPASS AYASLSSSSN SHSSSSSPGL ELDSLVGLNG ISALDSLLLD TSDGDSLSCL
SPGYGSLLTG SGESLLPGCR GDLPMSGLEK SDVELSLRLL DQSSKDSFDF ASDQQPSACI
SSFSALDGYP FDLLHSDFPD MFLT
