DRI_DROME
ID DRI_DROME Reviewed; 911 AA.
AC Q24573; Q8MSB0; Q9W1M0;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Protein dead ringer;
DE AltName: Full=Protein retained;
GN Name=retn; Synonyms=dri; ORFNames=CG5403;
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 {ECO:0000312|EMBL:AAF47037.3};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo {ECO:0000269|PubMed:8622680};
RX PubMed=8622680; DOI=10.1128/mcb.16.3.792;
RA Gregory S.L., Kortschak R.D., Kalionis B., Saint R.;
RT "Characterization of the dead ringer gene identifies a novel, highly
RT conserved family of sequence-specific DNA-binding proteins.";
RL Mol. Cell. Biol. 16:792-799(1996).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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] {ECO:0000305}
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12620977; DOI=10.1242/dev.00377;
RA Shandala T., Takizawa K., Saint R.;
RT "The dead ringer/retained transcriptional regulatory gene is required for
RT positioning of the longitudinal glia in the Drosophila embryonic CNS.";
RL Development 130:1505-1513(2003).
RN [6]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=15576402; DOI=10.1242/dev.01568;
RA Ditch L.M., Shirangi T., Pitman J.L., Latham K.L., Finley K.D., Edeen P.T.,
RA Taylor B.J., McKeown M.;
RT "Drosophila retained/dead ringer is necessary for neuronal pathfinding,
RT female receptivity and repression of fruitless independent male courtship
RT behaviors.";
RL Development 132:155-164(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; THR-35; SER-44; SER-592;
RP SER-594 AND SER-720, AND 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).
RN [8] {ECO:0000305}
RP STRUCTURE BY NMR OF 274-410, AND DNA-BINDING.
RX PubMed=11867548; DOI=10.1093/emboj/21.5.1197;
RA Iwahara J., Iwahara M., Daughdrill G.W., Ford J., Clubb R.T.;
RT "The structure of the Dead ringer-DNA complex reveals how AT-rich
RT interaction domains (ARIDs) recognize DNA.";
RL EMBO J. 21:1197-1209(2002).
CC -!- FUNCTION: Transcription factor which is a downstream target of gcm and
CC repo. Directly or indirectly activates the transcription of locos and
CC pros, which are essential for the development of some glial cells.
CC Plays an essential role in defining the cell shape and migration
CC characteristics of longitudinal glia that enable them to establish a
CC normal axon scaffold. {ECO:0000269|PubMed:12620977,
CC ECO:0000269|PubMed:15576402}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355,
CC ECO:0000269|PubMed:8622680}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B {ECO:0000303|PubMed:10731132};
CC IsoId=Q24573-1; Sequence=Displayed;
CC Name=A {ECO:0000303|PubMed:10731132};
CC IsoId=Q24573-2; Sequence=VSP_050694;
CC -!- TISSUE SPECIFICITY: Present in the pharyngeal muscles, hindgut
CC epithelium, amnioserosa, ring gland, midgut-hindgut junction, posterior
CC region of each brain lobe, longitudinal glial cells of the CNS and the
CC salivary gland duct of germ-band retracted embryos.
CC {ECO:0000269|PubMed:12620977, ECO:0000269|PubMed:8622680}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally throughout the embryo at the
CC syncytial cleavage divisions and zygotically at the termini and in a
CC broad central band during cellularization. At germ band extension, the
CC protein is found in the mesoderm. Expressed in a subset of neurons from
CC larva and pupa. {ECO:0000269|PubMed:15576402,
CC ECO:0000269|PubMed:8622680}.
CC -!- DISRUPTION PHENOTYPE: Flies show axon guidance abnormalities in
CC mushroom bodies and pathfinding errors by photoreceptor and
CC subesophageal neurons. Female flies with retn defects are strikingly
CC resistant to male courtship and show male-like courtship of females and
CC males, especially as they age. {ECO:0000269|PubMed:15576402}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB05771.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U62542; AAB05771.1; ALT_INIT; mRNA.
DR EMBL; AE013599; AAO41347.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF47037.3; -; Genomic_DNA.
DR EMBL; AY118955; AAM50815.1; -; mRNA.
DR PIR; JC6093; JC6093.
DR RefSeq; NP_476864.2; NM_057516.4. [Q24573-2]
DR RefSeq; NP_788434.1; NM_176254.2. [Q24573-1]
DR PDB; 1C20; NMR; -; A=274-401.
DR PDB; 1KQQ; NMR; -; A=274-410.
DR PDBsum; 1C20; -.
DR PDBsum; 1KQQ; -.
DR AlphaFoldDB; Q24573; -.
DR BMRB; Q24573; -.
DR SMR; Q24573; -.
DR BioGRID; 70031; 15.
DR IntAct; Q24573; 15.
DR STRING; 7227.FBpp0071982; -.
DR iPTMnet; Q24573; -.
DR PaxDb; Q24573; -.
DR PRIDE; Q24573; -.
DR DNASU; 45976; -.
DR EnsemblMetazoa; FBtr0072072; FBpp0071981; FBgn0004795. [Q24573-2]
DR EnsemblMetazoa; FBtr0072073; FBpp0071982; FBgn0004795. [Q24573-1]
DR GeneID; 45976; -.
DR KEGG; dme:Dmel_CG5403; -.
DR CTD; 56729; -.
DR FlyBase; FBgn0004795; retn.
DR VEuPathDB; VectorBase:FBgn0004795; -.
DR eggNOG; KOG2744; Eukaryota.
DR GeneTree; ENSGT00940000169348; -.
DR InParanoid; Q24573; -.
DR OMA; ADQDMEG; -.
DR PhylomeDB; Q24573; -.
DR SignaLink; Q24573; -.
DR BioGRID-ORCS; 45976; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; Q24573; -.
DR GenomeRNAi; 45976; -.
DR PRO; PR:Q24573; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0004795; Expressed in cleaving embryo and 50 other tissues.
DR ExpressionAtlas; Q24573; baseline and differential.
DR Genevisible; Q24573; DM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:FlyBase.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:FlyBase.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:FlyBase.
DR GO; GO:0042063; P:gliogenesis; IMP:UniProtKB.
DR GO; GO:0008049; P:male courtship behavior; IMP:FlyBase.
DR GO; GO:0007517; P:muscle organ development; IMP:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; HMP:FlyBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0045924; P:regulation of female receptivity; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007431; P:salivary gland development; NAS:FlyBase.
DR Gene3D; 1.10.150.60; -; 1.
DR InterPro; IPR045147; ARI3A/B/C.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR023334; REKLES_domain.
DR PANTHER; PTHR15348; PTHR15348; 1.
DR Pfam; PF01388; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SUPFAM; SSF46774; SSF46774; 1.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51486; REKLES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Developmental protein;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..911
FT /note="Protein dead ringer"
FT /id="PRO_0000200583"
FT DOMAIN 293..385
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT DOMAIN 731..825
FT /note="REKLES"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00819"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..873
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 35
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 248..252
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:8622680"
FT /id="VSP_050694"
FT CONFLICT 176
FT /note="S -> A (in Ref. 1; AAB05771)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="G -> GA (in Ref. 1; AAB05771)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="Missing (in Ref. 1; AAB05771)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="Missing (in Ref. 1; AAB05771)"
FT /evidence="ECO:0000305"
FT CONFLICT 761
FT /note="V -> L (in Ref. 1; AAB05771)"
FT /evidence="ECO:0000305"
FT CONFLICT 853
FT /note="E -> EEE (in Ref. 1; AAB05771)"
FT /evidence="ECO:0000305"
FT CONFLICT 873
FT /note="V -> A (in Ref. 1; AAB05771)"
FT /evidence="ECO:0000305"
FT CONFLICT 902
FT /note="V -> VGV (in Ref. 1; AAB05771)"
FT /evidence="ECO:0000305"
FT HELIX 277..289
FT /evidence="ECO:0007829|PDB:1C20"
FT HELIX 294..307
FT /evidence="ECO:0007829|PDB:1C20"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:1C20"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:1KQQ"
FT HELIX 327..336
FT /evidence="ECO:0007829|PDB:1C20"
FT HELIX 340..346
FT /evidence="ECO:0007829|PDB:1C20"
FT HELIX 349..355
FT /evidence="ECO:0007829|PDB:1C20"
FT HELIX 365..376
FT /evidence="ECO:0007829|PDB:1C20"
FT HELIX 378..385
FT /evidence="ECO:0007829|PDB:1C20"
FT HELIX 390..400
FT /evidence="ECO:0007829|PDB:1C20"
SQ SEQUENCE 911 AA; 97365 MW; 4A2F0BFAB468906A CRC64;
MQLRVHPTMD CSGRSTSNIE RDSDLGDDLS HGDRTDDEMR DCDSVDGEHH QLSAKAAIAA
RLSHTVSGGG GSFASPEPQT ELPLSHHHQL PPNHPLNALG SFMGIGGLHS IPNLQHSDVL
EKLKMQVRDM KVGLMEQDYA AAAHAAAFGA NMLPTTISSG FPLPHNSVAF GHVTSSPSGG
NGSSYNGGTT PTNSSNSNAT TNGGGTAGPG GTGGSGGGGG GGGGGGGGVG GHQFSFASPT
AAPSGKEARH FAANSASNSS TSSEASNSSQ QNNGWSFEEQ FKQVRQLYEI NDDPKRKEFL
DDLFSFMQKR GTPINRLPIM AKSVLDLYEL YNLVIARGGL VDVINKKLWQ EIIKGLHLPS
SITSAAFTLR TQYMKYLYPY ECEKKNLSTP AELQAAIDGN RREGRRSSYG QYEAMHNQMP
MTPISRPSLP GGMQQMSPLA LVTHAAVANN QQAQAAAAAA AAHHRLMGAP AFGQMPNLVK
QEIESRMMEY LQLIQAKKEQ GMPPVLGGNH PHQQQHSQQQ QQQQHHHQQQ QQQQSQQQHH
LQQQRQRSQS PDLSKHEALS AQVALWHMYH NNNSPPGSAH TSPQQREALN LSDSPPNLTN
IKREREREPT PEPVDQDDKF VDQPPPAKRV GSGLLPPGFP ANFYLNPHNM AAVAAAAGFH
HPSMGHQQDA ASEGEPEDDY AHGEHNTTGN SSSMHDDSEP QQMNGHHHHQ THHLDKSDDS
AIENSPTTST TTGGSVGHRH SSPVSTKKKG GAKPQSGGKD VPTEDKDASS SGKLNPLETL
SLLSGMQFQV ARNGTGDNGE PQLIVNLELN GVKYSGVLVA NVPLSQSETR TSSPCHAEAP
TVEEEKDEEE EEEPKAAEEE SHRSPVKQEN EDVDQDMEGS EVLLNGGASA VGGAGAGVGV
GVPLLKDAVV S
