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 18-SEP-2019, entry version 82. 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; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; 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., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA 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., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA 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., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., 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., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic 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 RT 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 RT in 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 RT ecdysial 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 RT single 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 RT expression 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 RT activates 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., RA Sweedler J., 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) CC cell function and neuroendocrine cell fate. Acts as a master CC regulator of common NS functions such as Phm expression and CC neuropeptide production. Plays a role as a regulator of peptide- CC containing large dense-core vesicle (LDCV) production and CC peptidergic cell differentiation. Controls transcription of CC FMRFamide in Tv neuronal cells and Fur1 in Ap-let cells (Tvb and CC dorsal apterous cells). Also required for up-regulation of Phm in CC Tv and Ap-let cells, and expression of three neuropeptide genes, CC Ms, FMRFamide and Lk. Influences both regulated and constitutive CC secretory activity in neuroendocrine cells at embryonic and CC postembryonic level. Loss of function studies show reduced CC cellular levels of various neuropeptides and neuropeptide CC biosynthetic enzymes. {ECO:0000269|PubMed:12642483, CC ECO:0000269|PubMed:15081360, ECO:0000269|PubMed:15748845, CC ECO:0000269|PubMed:16651547, ECO:0000269|PubMed:16870731, CC ECO:0000269|PubMed:17967878, ECO:0000269|PubMed:20045330}. CC -!- SUBUNIT: Forms homodimers via the bHLH domain. These dimers bind CC the core E-box sequence. {ECO:0000269|PubMed:15748845, CC ECO:0000269|PubMed:17967878}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16870731}. CC -!- TISSUE SPECIFICITY: Detected in the developing nervous system in CC the bilateral domains in the cephalic region that later on forms CC part of the ring gland. Concomitantly expressed in the larval CC central nervous system (CNS), including the dorsal chain neurons CC as well as several bilateral clusters of neurons: large, midline CC protocerebral brain cells (MC), lateral protocerebral brain cells CC (LC), ventral subesophageal neurons (SE) and lateral abdominal CC neurons, and the transverse nerves. Outside the CNS, detected in CC at least three classes of endocrine cells: intrinsic cells of the CC corpora cardiaca, midgut cells, the Inka cells, lateral Bipolar CC neurons associated with the segmental transverse nerve, and CC 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 CC early stage 11, but this expression is transient. Zygotic CC expression is first detected in stage 12 embryos and cytoplasmic CC expression is detected in many cells around stage 14. Embryonic CC cells maintain expression throughout their lifetime and expression CC continues into hatchling larvae less than 24 hours old. CC {ECO:0000269|PubMed:10973473, ECO:0000269|PubMed:12642483, CC ECO:0000269|PubMed:15748845, ECO:0000269|PubMed:16870731}. CC -!- DOMAIN: The basic domain binds to the canonical E-box (5'-CANNTG- CC 3'), with a particular preference for TA relative to AT or CG in CC the variable central nucleotide positions. CC {ECO:0000269|PubMed:17967878}. CC -!- SEQUENCE CAUTION: CC Sequence=ABI34200.4; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC Sequence=ABI34232.3; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; B6VQA1; -. DR BioGrid; 61353; 34. DR IntAct; B6VQA1; 28. DR STRING; 7227.FBpp0305546; -. DR PaxDb; B6VQA1; -. DR PRIDE; B6VQA1; -. 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 eggNOG; ENOG410IQ4H; Eukaryota. DR eggNOG; ENOG4111ZMK; LUCA. DR InParanoid; B6VQA1; -. DR OMA; DFMQLQH; -. DR OrthoDB; 1287614at2759; -. DR PhylomeDB; B6VQA1; -. DR GenomeRNAi; 35404; -. DR PRO; PR:B6VQA1; -. DR Proteomes; UP000000803; Chromosome 2L. DR Bgee; FBgn0023091; Expressed in 18 organ(s), highest expression level in embryonic/larval corpus cardiacum (Drosophila). DR ExpressionAtlas; B6VQA1; 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:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0061101; P:neuroendocrine cell differentiation; IMP:FlyBase. 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:0006355; P:regulation of transcription, DNA-templated; ISS:FlyBase. DR GO; GO:0007419; P:ventral cord development; HMP:FlyBase. DR CDD; cd00083; HLH; 1. 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 Complete proteome; Cytoplasm; Developmental protein; Differentiation; KW DNA-binding; Glycoprotein; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 390 Protein dimmed. FT /FTId=PRO_0000412993. FT DOMAIN 156 208 bHLH. {ECO:0000255|PROSITE- FT ProRule:PRU00981}. FT COMPBIAS 296 341 Gln-rich. {ECO:0000255}. FT CARBOHYD 61 61 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 128 128 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 133 133 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 140 140 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 207 207 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 237 237 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 347 347 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT MUTAGEN 164 166 RER->GGG: Reduced DNA-binding activity. FT {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 //