DIMM_DROME
ID DIMM_DROME Reviewed; 390 AA.
AC B6VQA1; Q0IGR9; Q9VID2;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Protein dimmed {ECO:0000312|EMBL:AAF53991.1};
GN Name=dimm; ORFNames=CG8667;
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] {ECO:0000312|EMBL:AAF53991.1}
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 [2] {ECO:0000305, ECO:0000312|EMBL:AAF53991.1}
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 [3] {ECO:0000312|EMBL:ABI34200.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.E.;
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10973473; DOI=10.1073/pnas.170301897;
RA Moore A.W., Barbel S., Jan L.Y., Jan Y.N.;
RT "A genomewide survey of basic helix-loop-helix factors in Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10436-10441(2000).
RN [5] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Head {ECO:0000269|PubMed:15748845};
RX PubMed=12642483; DOI=10.1242/dev.00404;
RA Hewes R.S., Park D., Gauthier S.A., Schaefer A.M., Taghert P.H.;
RT "The bHLH protein Dimmed controls neuroendocrine cell differentiation in
RT Drosophila.";
RL Development 130:1771-1781(2003).
RN [6] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15081360; DOI=10.1016/j.ydbio.2004.01.015;
RA Park D., Han M., Kim Y.C., Han K.A., Taghert P.H.;
RT "Ap-let neurons--a peptidergic circuit potentially controlling ecdysial
RT behavior in Drosophila.";
RL Dev. Biol. 269:95-108(2004).
RN [7] {ECO:0000305}
RP FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15748845; DOI=10.1016/j.neuron.2005.01.026;
RA Allan D.W., Park D., St Pierre S.E., Taghert P.H., Thor S.;
RT "Regulators acting in combinatorial codes also act independently in single
RT differentiating neurons.";
RL Neuron 45:689-700(2005).
RN [8] {ECO:0000305}
RP FUNCTION.
RX PubMed=16651547; DOI=10.1242/jeb.02202;
RA Gauthier S.A., Hewes R.S.;
RT "Transcriptional regulation of neuropeptide and peptide hormone expression
RT by the Drosophila dimmed and cryptocephal genes.";
RL J. Exp. Biol. 209:1803-1815(2006).
RN [9] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Head {ECO:0000269|PubMed:15081360};
RX PubMed=16870731; DOI=10.1523/jneurosci.1759-06.2006;
RA Hewes R.S., Gu T., Brewster J.A., Qu C., Zhao T.;
RT "Regulation of secretory protein expression in mature cells by DIMM, a
RT basic helix-loop-helix neuroendocrine differentiation factor.";
RL J. Neurosci. 26:7860-7869(2006).
RN [10] {ECO:0000305}
RP FUNCTION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF 164-ARG--ARG-166.
RX PubMed=17967878; DOI=10.1128/mcb.01104-07;
RA Park D., Shafer O.T., Shepherd S.P., Suh H., Trigg J.S., Taghert P.H.;
RT "The Drosophila basic helix-loop-helix protein DIMMED directly activates
RT PHM, a gene encoding a neuropeptide-amidating enzyme.";
RL Mol. Cell. Biol. 28:410-421(2008).
RN [11] {ECO:0000305}
RP FUNCTION.
RX PubMed=20045330; DOI=10.1016/j.cub.2009.11.065;
RA Hamanaka Y., Park D., Yin P., Annangudi S.P., Edwards T.N., Sweedler J.,
RA Meinertzhagen I.A., Taghert P.H.;
RT "Transcriptional orchestration of the regulated secretory pathway in
RT neurons by the bHLH protein DIMM.";
RL Curr. Biol. 20:9-18(2010).
CC -!- FUNCTION: Transcription factor that regulates neurosecretory (NS) cell
CC function and neuroendocrine cell fate. Acts as a master regulator of
CC common NS functions such as Phm expression and neuropeptide production.
CC Plays a role as a regulator of peptide-containing large dense-core
CC vesicle (LDCV) production and peptidergic cell differentiation.
CC Controls transcription of FMRFamide in Tv neuronal cells and Fur1 in
CC Ap-let cells (Tvb and dorsal apterous cells). Also required for up-
CC regulation of Phm in Tv and Ap-let cells, and expression of three
CC neuropeptide genes, Ms, FMRFamide and Lk. Influences both regulated and
CC constitutive secretory activity in neuroendocrine cells at embryonic
CC and postembryonic level. Loss of function studies show reduced cellular
CC levels of various neuropeptides and neuropeptide biosynthetic enzymes.
CC {ECO:0000269|PubMed:12642483, ECO:0000269|PubMed:15081360,
CC ECO:0000269|PubMed:15748845, ECO:0000269|PubMed:16651547,
CC ECO:0000269|PubMed:16870731, ECO:0000269|PubMed:17967878,
CC ECO:0000269|PubMed:20045330}.
CC -!- SUBUNIT: Forms homodimers via the bHLH domain. These dimers bind the
CC core E-box sequence. {ECO:0000269|PubMed:15748845,
CC ECO:0000269|PubMed:17967878}.
CC -!- INTERACTION:
CC B6VQA1; P23792: disco; NbExp=3; IntAct=EBI-166061, EBI-152064;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16870731}.
CC -!- TISSUE SPECIFICITY: Detected in the developing nervous system in the
CC bilateral domains in the cephalic region that later on forms part of
CC the ring gland. Concomitantly expressed in the larval central nervous
CC system (CNS), including the dorsal chain neurons as well as several
CC bilateral clusters of neurons: large, midline protocerebral brain cells
CC (MC), lateral protocerebral brain cells (LC), ventral subesophageal
CC neurons (SE) and lateral abdominal neurons, and the transverse nerves.
CC Outside the CNS, detected in at least three classes of endocrine cells:
CC intrinsic cells of the corpora cardiaca, midgut cells, the Inka cells,
CC lateral Bipolar neurons associated with the segmental transverse nerve,
CC and several peptidergic cells of the enteric nervous system. Expressed
CC only in central and peripheral neuroendocrine secretory cells and
CC neurosecretory neurons but not in sensory or motor neurons.
CC {ECO:0000269|PubMed:10973473, ECO:0000269|PubMed:12642483,
CC ECO:0000269|PubMed:15081360, ECO:0000269|PubMed:15748845,
CC ECO:0000269|PubMed:16870731}.
CC -!- DEVELOPMENTAL STAGE: First detected in the embryonic ectoderm at early
CC stage 11, but this expression is transient. Zygotic expression is first
CC detected in stage 12 embryos and cytoplasmic expression is detected in
CC many cells around stage 14. Embryonic cells maintain expression
CC throughout their lifetime and expression continues into hatchling
CC larvae less than 24 hours old. {ECO:0000269|PubMed:10973473,
CC ECO:0000269|PubMed:12642483, ECO:0000269|PubMed:15748845,
CC ECO:0000269|PubMed:16870731}.
CC -!- DOMAIN: The basic domain binds to the canonical E-box (5'-CANNTG-3'),
CC with a particular preference for TA relative to AT or CG in the
CC variable central nucleotide positions. {ECO:0000269|PubMed:17967878}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABI34200.4; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABI34232.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014134; AAF53991.1; -; Genomic_DNA.
DR EMBL; BT028819; ABI34200.4; ALT_INIT; mRNA.
DR EMBL; BT028851; ABI34232.3; ALT_INIT; mRNA.
DR RefSeq; NP_001260674.1; NM_001273745.1.
DR RefSeq; NP_523611.1; NM_078887.3.
DR AlphaFoldDB; B6VQA1; -.
DR SMR; B6VQA1; -.
DR BioGRID; 61353; 41.
DR IntAct; B6VQA1; 32.
DR STRING; 7227.FBpp0305546; -.
DR GlyGen; B6VQA1; 7 sites.
DR PaxDb; B6VQA1; -.
DR DNASU; 35404; -.
DR EnsemblMetazoa; FBtr0081514; FBpp0081042; FBgn0023091.
DR EnsemblMetazoa; FBtr0333354; FBpp0305546; FBgn0023091.
DR GeneID; 35404; -.
DR KEGG; dme:Dmel_CG8667; -.
DR UCSC; CG8667-RA; d. melanogaster.
DR CTD; 35404; -.
DR FlyBase; FBgn0023091; dimm.
DR VEuPathDB; VectorBase:FBgn0023091; -.
DR eggNOG; KOG3898; Eukaryota.
DR HOGENOM; CLU_704527_0_0_1; -.
DR InParanoid; B6VQA1; -.
DR OMA; GSHDFMQ; -.
DR OrthoDB; 1287614at2759; -.
DR PhylomeDB; B6VQA1; -.
DR SignaLink; B6VQA1; -.
DR BioGRID-ORCS; 35404; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35404; -.
DR PRO; PR:B6VQA1; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0023091; Expressed in embryonic/larval neuron (Drosophila) and 17 other tissues.
DR ExpressionAtlas; B6VQA1; baseline and differential.
DR Genevisible; B6VQA1; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0061101; P:neuroendocrine cell differentiation; IMP:FlyBase.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0046887; P:positive regulation of hormone secretion; IMP:FlyBase.
DR GO; GO:0002793; P:positive regulation of peptide secretion; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
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:0007419; P:ventral cord development; HMP: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 Cytoplasm; Developmental protein; Differentiation; DNA-binding;
KW Glycoprotein; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..390
FT /note="Protein dimmed"
FT /id="PRO_0000412993"
FT DOMAIN 156..208
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 24..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 164..166
FT /note="RER->GGG: Reduced DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:17967878"
SQ SEQUENCE 390 AA; 40980 MW; C877F99770EDDCF8 CRC64;
MDATQLTELM GSHDFMQLQH QLHHNNNNYN TDGHNGLSSE SAEGSSRPVR RATRRTSQLS
NNTYDLEMTD SSSQSDDTSG GGGSSNGGGS TTNTGHPSGC SLGGQGPSGR GRVQQASSGA
CPSTIAPNST SSNSSNANGN ASRRRKGALN AKERNMRRLE SNERERMRMH SLNDAFQSLR
EVIPHVEMER RLSKIETLTL AKNYIINLTH IILSKRNEEA AALELNSGAV GGVLLSNLSS
ESGGPVASGI PANSNAATIC FEDTLASGGA FDCAILAATD GSLLNAATVT TSPAMQSIQS
QAIHLQTPME QQQQQASHLP HHQQAMHGHG HLGASIQSQQ QPSLVLNGTT SVGLGIGIGV
GVGVGVGVCN NAPSFADIND NFDEPFREFL
