ESM3_DROME
ID ESM3_DROME Reviewed; 224 AA.
AC Q01068; Q5S455; Q5S479; Q5S4J9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Enhancer of split m3 protein;
DE Short=E(spl)m3;
DE AltName: Full=HLH-m3;
GN Name=E(spl)m3-HLH {ECO:0000312|FlyBase:FBgn0002609}; Synonyms=HLHm3;
GN ORFNames=CG8346 {ECO:0000312|FlyBase:FBgn0002609};
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].
RC STRAIN=Canton-S; TISSUE=Embryo;
RX PubMed=1528887; DOI=10.1073/pnas.89.18.8731;
RA Delidakis C., Artavanis-Tsakonas S.;
RT "The Enhancer of split [E(spl)] locus of Drosophila encodes seven
RT independent helix-loop-helix proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8731-8735(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-143 DEL.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=1427040; DOI=10.1093/genetics/132.2.505;
RA Knust E., Schrons H., Grawe F., Campos-Ortega J.A.;
RT "Seven genes of the Enhancer of split complex of Drosophila melanogaster
RT encode helix-loop-helix proteins.";
RL Genetics 132:505-518(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PHE-83; GLN-143 DEL AND
RP GLN-151.
RC STRAIN=NVIII-1, NVIII-18, NVIII-2, NVIII-22, NVIII-24, NVIII-28, NVIII-41,
RC NVIII-42, NVIII-46, NVIII-5, NVIII-9, NVIII-m11, NVIII-m12, NVIII-m13,
RC NVIII-m15, and NVIII-m19;
RX PubMed=15537803; DOI=10.1093/molbev/msi046;
RA Macdonald S.J., Long A.D.;
RT "Identifying signatures of selection at the enhancer of split neurogenic
RT gene complex in Drosophila.";
RL Mol. Biol. Evol. 22:607-619(2005).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [7]
RP DOMAIN WRPW MOTIF.
RX PubMed=8001118; DOI=10.1016/0092-8674(94)90070-1;
RA Paroush Z., Finley R.L. Jr., Kidd T., Wainwright S.M., Ingham P.W.,
RA Brent R., Ish-Horowicz D.;
RT "Groucho is required for Drosophila neurogenesis, segmentation, and sex
RT determination and interacts directly with hairy-related bHLH proteins.";
RL Cell 79:805-815(1994).
CC -!- FUNCTION: Transcriptional repressor of genes that require a bHLH
CC protein for their transcription. May serve as a transcriptional
CC regulator of the Achaete-scute complex (AS-C) genes. Belongs to notch
CC signaling pathway and depends on Su(H) for transcriptional activation.
CC -!- SUBUNIT: Transcription repression requires formation of a complex with
CC a corepressor protein (Groucho).
CC -!- INTERACTION:
CC Q01068; P16371: gro; NbExp=4; IntAct=EBI-121622, EBI-153866;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: The RNA is supplied maternally, and later on,
CC expression is ubiquitous during all stages of embryonic development.
CC -!- DOMAIN: Has a particular type of basic domain (presence of a helix-
CC interrupting proline) that binds to the N-box (CACNAG), rather than the
CC canonical E-box (CANNTG). {ECO:0000269|PubMed:8001118}.
CC -!- DOMAIN: The C-terminal WRPW motif is a transcriptional repression
CC domain necessary for the interaction with Groucho, a transcriptional
CC corepressor recruited to specific target DNA by Hairy-related proteins.
CC {ECO:0000269|PubMed:8001118}.
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DR EMBL; M96165; AAA28908.1; -; mRNA.
DR EMBL; X67046; CAA47431.1; -; mRNA.
DR EMBL; AY779906; AAV59048.1; -; Genomic_DNA.
DR EMBL; AY779907; AAV59060.1; -; Genomic_DNA.
DR EMBL; AY779908; AAV59072.1; -; Genomic_DNA.
DR EMBL; AY779909; AAV59084.1; -; Genomic_DNA.
DR EMBL; AY779910; AAV59096.1; -; Genomic_DNA.
DR EMBL; AY779911; AAV59108.1; -; Genomic_DNA.
DR EMBL; AY779912; AAV59120.1; -; Genomic_DNA.
DR EMBL; AY779913; AAV59132.1; -; Genomic_DNA.
DR EMBL; AY779914; AAV59144.1; -; Genomic_DNA.
DR EMBL; AY779915; AAV59156.1; -; Genomic_DNA.
DR EMBL; AY779916; AAV59168.1; -; Genomic_DNA.
DR EMBL; AY779917; AAV59180.1; -; Genomic_DNA.
DR EMBL; AY779918; AAV59192.1; -; Genomic_DNA.
DR EMBL; AY779919; AAV59204.1; -; Genomic_DNA.
DR EMBL; AY779920; AAV59216.1; -; Genomic_DNA.
DR EMBL; AY779921; AAV59228.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF56550.1; -; Genomic_DNA.
DR EMBL; AY094858; AAM11211.1; -; mRNA.
DR PIR; D46177; D46177.
DR RefSeq; NP_524509.2; NM_079785.4.
DR AlphaFoldDB; Q01068; -.
DR SMR; Q01068; -.
DR BioGRID; 68056; 20.
DR DIP; DIP-356N; -.
DR ELM; Q01068; -.
DR IntAct; Q01068; 13.
DR STRING; 7227.FBpp0084332; -.
DR PaxDb; Q01068; -.
DR EnsemblMetazoa; FBtr0084958; FBpp0084332; FBgn0002609.
DR GeneID; 43156; -.
DR KEGG; dme:Dmel_CG8346; -.
DR CTD; 43156; -.
DR FlyBase; FBgn0002609; E(spl)m3-HLH.
DR VEuPathDB; VectorBase:FBgn0002609; -.
DR eggNOG; KOG4304; Eukaryota.
DR HOGENOM; CLU_068550_2_2_1; -.
DR InParanoid; Q01068; -.
DR OMA; TIMVMEM; -.
DR OrthoDB; 1483774at2759; -.
DR PhylomeDB; Q01068; -.
DR SignaLink; Q01068; -.
DR BioGRID-ORCS; 43156; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 43156; -.
DR PRO; PR:Q01068; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0002609; Expressed in wing disc and 52 other tissues.
DR ExpressionAtlas; Q01068; baseline and differential.
DR Genevisible; Q01068; DM.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:UniProtKB.
DR GO; GO:0050767; P:regulation of neurogenesis; 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; IPR003650; Orange_dom.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00511; ORANGE; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS51054; ORANGE; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Developmental protein; Differentiation; DNA-binding;
KW Neurogenesis; Notch signaling pathway; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..224
FT /note="Enhancer of split m3 protein"
FT /id="PRO_0000127171"
FT DOMAIN 11..68
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 98..130
FT /note="Orange"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00380"
FT REGION 205..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 221..224
FT /note="WRPW motif"
FT VARIANT 83
FT /note="V -> F (in strain: NVIII-m11)"
FT /evidence="ECO:0000269|PubMed:15537803"
FT VARIANT 143
FT /note="Missing (in strain: NVIII-1, NVIII-18, NVIII-2,
FT NVIII-22, NVIII-24, NVIII-41, NVIII-42, NVIII-46, NVIII-5,
FT NVIII-9, NVIII-m12, NVIII-m15, NVIII-m19 and Oregon-R)"
FT /evidence="ECO:0000269|PubMed:1427040,
FT ECO:0000269|PubMed:15537803"
FT VARIANT 151
FT /note="H -> Q (in strain: NVIII-m11)"
FT /evidence="ECO:0000269|PubMed:15537803"
FT CONFLICT 174..177
FT /note="AAAA -> SRR (in Ref. 2; CAA47431)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 224 AA; 24983 MW; E16D13530FD283C9 CRC64;
MVMEMSKTYQ YRKVMKPLLE RKRRARINKC LDDLKDLMVE CLQQEGEHVT RLEKADILEL
TVDHMRKLKQ RGGLSLQGVV AGVGSPPTST STAHVESFRS GYVHAADQIT QVLLQTQQTD
EIGRKIMKFL STRLIELQTQ LLQQQQQQQQ HQQQQIPQSS GRLAFPLLGG YGPAAAAAAI
SYSSFLTSKD ELIDVTSVDG NALSETASVS SQESGASEPV WRPW
