DA_DROME
ID DA_DROME Reviewed; 710 AA.
AC P11420; Q9VKX3;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Protein daughterless;
GN Name=da; ORFNames=CG5102;
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].
RX PubMed=3203380; DOI=10.1016/0092-8674(88)90250-4;
RA Caudy M., Vaessin H., Brand M., Tuma R., Jan L.Y., Jan Y.N.;
RT "Daughterless, a Drosophila gene essential for both neurogenesis and sex
RT determination, has sequence similarities to myc and the achaete-scute
RT complex.";
RL Cell 55:1061-1067(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2850968; DOI=10.1101/gad.2.12a.1666;
RA Cronmiller C., Schedl P., Cline T.W.;
RT "Molecular characterization of daughterless, a Drosophila sex determination
RT gene with multiple roles in development.";
RL Genes Dev. 2:1666-1676(1988).
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).
RN [5]
RP HOMODIMERIZATION, AND INTERACTION WITH SISA; SC AND DA.
RX PubMed=7651341; DOI=10.1007/bf02190799;
RA Liu Y., Belote J.M.;
RT "Protein-protein interactions among components of the Drosophila primary
RT sex determination signal.";
RL Mol. Gen. Genet. 248:182-189(1995).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-535 AND SER-536, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Daughterless/Achaete-scute complex heterodimers act as
CC transcriptional activators of neural cell fates and are involved in sex
CC determination.
CC -!- SUBUNIT: Homodimer. Efficient DNA binding requires dimerization with
CC another bHLH protein. Interacts with Amos. Interacts (via bHLH motif)
CC with sisA and sc. Interacts with dpn (via bHLH motif).
CC {ECO:0000269|PubMed:7651341}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
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DR EMBL; J03148; AAA28442.1; -; mRNA.
DR EMBL; Y00221; CAA68368.1; -; mRNA.
DR EMBL; AE014134; AAF52934.2; -; Genomic_DNA.
DR PIR; S06891; A31641.
DR RefSeq; NP_001260340.1; NM_001273411.1.
DR RefSeq; NP_001260341.1; NM_001273412.1.
DR RefSeq; NP_477189.1; NM_057841.4.
DR AlphaFoldDB; P11420; -.
DR SMR; P11420; -.
DR BioGRID; 60497; 56.
DR DIP; DIP-50N; -.
DR IntAct; P11420; 25.
DR STRING; 7227.FBpp0304504; -.
DR iPTMnet; P11420; -.
DR PaxDb; P11420; -.
DR EnsemblMetazoa; FBtr0080008; FBpp0079598; FBgn0267821.
DR EnsemblMetazoa; FBtr0332195; FBpp0304504; FBgn0267821.
DR EnsemblMetazoa; FBtr0332196; FBpp0304505; FBgn0267821.
DR GeneID; 34413; -.
DR KEGG; dme:Dmel_CG5102; -.
DR UCSC; CG5102-RA; d. melanogaster.
DR CTD; 13130; -.
DR FlyBase; FBgn0267821; da.
DR VEuPathDB; VectorBase:FBgn0267821; -.
DR eggNOG; KOG3910; Eukaryota.
DR GeneTree; ENSGT00940000168822; -.
DR HOGENOM; CLU_387465_0_0_1; -.
DR InParanoid; P11420; -.
DR OMA; VFQGVRM; -.
DR OrthoDB; 571132at2759; -.
DR PhylomeDB; P11420; -.
DR Reactome; R-DME-525793; Myogenesis.
DR Reactome; R-DME-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR SignaLink; P11420; -.
DR BioGRID-ORCS; 34413; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 34413; -.
DR PRO; PR:P11420; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0267821; Expressed in cleaving embryo and 26 other tissues.
DR ExpressionAtlas; P11420; baseline and differential.
DR Genevisible; P11420; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005667; C:transcription regulator complex; IPI:FlyBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:FlyBase.
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:0008134; F:transcription factor binding; IGI:FlyBase.
DR GO; GO:0008407; P:chaeta morphogenesis; IMP:FlyBase.
DR GO; GO:0030237; P:female sex determination; IMP:FlyBase.
DR GO; GO:0061525; P:hindgut development; IMP:FlyBase.
DR GO; GO:0061382; P:Malpighian tubule tip cell differentiation; IMP:FlyBase.
DR GO; GO:0007400; P:neuroblast fate determination; IMP:FlyBase.
DR GO; GO:0061101; P:neuroendocrine cell differentiation; IMP:FlyBase.
DR GO; GO:0048663; P:neuron fate commitment; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:FlyBase.
DR GO; GO:0050821; P:protein stabilization; IDA:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007423; P:sensory organ development; IMP:FlyBase.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP: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 Activator; Developmental protein; Differentiation; DNA-binding;
KW Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..710
FT /note="Protein daughterless"
FT /id="PRO_0000127166"
FT REPEAT 198..226
FT /note="His-rich"
FT REPEAT 227..256
FT /note="His-rich"
FT DOMAIN 554..607
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 167..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..632
FT /note="Class A specific domain"
FT REGION 645..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 710 AA; 73864 MW; C69163BD3F46FEA5 CRC64;
MATSDDEPMH LYEVFQNCFN KIANKQPTGT VGADRGGGGG YHSPYGSLGV ENGMYPSDFN
SMHDTVNGGN NRYANASTVD QYFDSAAAGS GGAWCQPQMS SANSYMGQSA YQNSGPLSGH
SIDQQQQQVH QADGLGMGGG GGGGVGADGM HCPVTTGLPP ISSFRPTSGG IGGPGAGQQA
PVNVNVNPPA VFNSPQAHNH NHTVQAQHSA LSTAGPLGHH SLNHTPHAHS HTLPLPHALP
HGHTLPHPHH SQQNSPAVQS SDAFSGAGAS VKVAGAGNSS AAALRQQMYM PADQSISSFG
SNPSTPVNSP PPLTQSVVGG GGEPSVSGGS GWGHSVLNGG PSSSYASEMV PVSSLHTMAS
VFQGVRMEER LDDALNVLRN HCEPEMLAGV NQSLASIDNI DALTSFVPNS PSHLGSGGNS
GSVSNTSNAA LVHEVLALGA AAAAGTSGQS VGGAGSLASL KLDRSASTSL PKQTKKRKEH
TAISNSVPAG VSTTSSLTSL DISDTKPTSS IESSNSGLQQ HSQGKGTKRP RRYCSSADED
DDAEPAVKAI REKERRQANN ARERIRIRDI NEALKELGRM CMTHLKSDKP QTKLGILNMA
VEVIMTLEQQ VRERNLNPKA ACLKRREEEK AEDGPKLSAQ HHMIPQPQQV GGTPGSSYHS
QPAQLVPPSS QTISTMTISL PVNQANNGLP PHLQQQQQQQ SQLGHAQLPQ
