DEL_DROME
ID DEL_DROME Reviewed; 981 AA.
AC Q9VIF5; Q86P81;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Protein deadlock;
GN Name=del; ORFNames=CG9252;
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 [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]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16616913; DOI=10.1016/j.ydbio.2006.03.002;
RA Wehr K., Swan A., Schupbach T.;
RT "Deadlock, a novel protein of Drosophila, is required for germline
RT maintenance, fusome morphogenesis and axial patterning in oogenesis and
RT associates with centrosomes in the early embryo.";
RL Dev. Biol. 294:406-417(2006).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28847004; DOI=10.1038/nature23482;
RA Andersen P.R., Tirian L., Vunjak M., Brennecke J.;
RT "A heterochromatin-dependent transcription machinery drives piRNA
RT expression.";
RL Nature 549:54-59(2017).
CC -!- FUNCTION: Developmental protein involved in oogenesis
CC (PubMed:16616913). Required for germline maintenance, stability of
CC mitotic spindles, localization of patterning determinants, oocyte
CC growth and fusome biogenesis in males and females (PubMed:16616913).
CC Also required for dorso-ventral and antero-posterior patterning of
CC oocyte and eggshell (PubMed:16616913). May be involved in microtubule
CC function during oogenesis (PubMed:16616913). Part of a rhi-dependent
CC transcription machinery that enables the generation of piRNA precursors
CC from heterochromatin while maintaining the suppression of transposon-
CC encoded promoters and enhancers (PubMed:28847004). Component of the RDC
CC complex (rhi, del and cuff) which binds to repressive H3K9me3 marks in
CC the piRNA clusters (PubMed:28847004). RDC promotes the bidirectional
CC transcription of piRNA clusters at these sites by interacting with
CC Moonshiner which forms a complex with the transcription initiation
CC factors TfIIA-S and Trf2 (PubMed:28847004). This mechanism allows
CC transcription to occur in piRNA clusters despite the lack of proper
CC promoter elements and in the presence of the repressive H3K9me3 mark
CC (PubMed:28847004). {ECO:0000269|PubMed:16616913,
CC ECO:0000269|PubMed:28847004}.
CC -!- INTERACTION:
CC Q9VIF5; Q9V629: cuff; NbExp=4; IntAct=EBI-151790, EBI-185996;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16616913,
CC ECO:0000269|PubMed:28847004}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:16616913}.
CC Note=Colocalizes with the oocyte nucleus at midstages of oogenesis and
CC with the centrosomes of early embryos (PubMed:16616913). Expressed in
CC nuclear foci (PubMed:28847004). {ECO:0000269|PubMed:16616913,
CC ECO:0000269|PubMed:28847004}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO39437.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014134; AAF53964.2; -; Genomic_DNA.
DR EMBL; BT003434; AAO39437.1; ALT_INIT; mRNA.
DR RefSeq; NP_001260666.1; NM_001273737.1.
DR RefSeq; NP_610091.2; NM_136247.3.
DR PDB; 5XYV; X-ray; 2.10 A; C/D=1-60.
DR PDBsum; 5XYV; -.
DR AlphaFoldDB; Q9VIF5; -.
DR SMR; Q9VIF5; -.
DR BioGRID; 61335; 8.
DR ComplexPortal; CPX-3213; Rhino-Deadlock-Cutoff Complex.
DR IntAct; Q9VIF5; 6.
DR STRING; 7227.FBpp0305298; -.
DR PaxDb; Q9VIF5; -.
DR DNASU; 35380; -.
DR EnsemblMetazoa; FBtr0081502; FBpp0081030; FBgn0086251.
DR EnsemblMetazoa; FBtr0333085; FBpp0305298; FBgn0086251.
DR GeneID; 35380; -.
DR KEGG; dme:Dmel_CG9252; -.
DR UCSC; CG9252-RA; d. melanogaster.
DR CTD; 35380; -.
DR FlyBase; FBgn0086251; del.
DR VEuPathDB; VectorBase:FBgn0086251; -.
DR eggNOG; ENOG502T86W; Eukaryota.
DR InParanoid; Q9VIF5; -.
DR OrthoDB; 482084at2759; -.
DR PhylomeDB; Q9VIF5; -.
DR SignaLink; Q9VIF5; -.
DR BioGRID-ORCS; 35380; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35380; -.
DR PRO; PR:Q9VIF5; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0086251; Expressed in oocyte and 16 other tissues.
DR ExpressionAtlas; Q9VIF5; baseline and differential.
DR Genevisible; Q9VIF5; DM.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000792; C:heterochromatin; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0045478; P:fusome organization; IMP:UniProtKB.
DR GO; GO:0007293; P:germarium-derived egg chamber formation; IMP:FlyBase.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:UniProtKB.
DR GO; GO:0048599; P:oocyte development; IMP:UniProtKB.
DR GO; GO:0030717; P:oocyte karyosome formation; IMP:FlyBase.
DR GO; GO:0030720; P:oocyte localization involved in germarium-derived egg chamber formation; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; IMP:FlyBase.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; Nucleus; Oogenesis; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..981
FT /note="Protein deadlock"
FT /id="PRO_0000235296"
FT REGION 72..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:5XYV"
FT HELIX 9..23
FT /evidence="ECO:0007829|PDB:5XYV"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:5XYV"
FT HELIX 30..45
FT /evidence="ECO:0007829|PDB:5XYV"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:5XYV"
SQ SEQUENCE 981 AA; 110817 MW; 9A825881240BDC1B CRC64;
MEKLDKIRMS QKLSCWQHIL TTLGTSSKTE QEWNTFFKGF LESWRKPYCI QTSCDPSIPL
RKELLVRPRK ALQENPHGPG STLPESPVFL EPINSTAPRE HPSPSKSHST GSTGCDPGNG
ERSPSVSNKN SKYKNPGNSK YAKIWKRSNN HTTSIFSKAQ ISKRRDKLSS TKKRPDTCAP
TDDSRKNREP RACAPNKNIF KTRETNAPNL TKNSCALPNV LILSPNSASK ITQRGHSVGQ
TQDYKASPGK IIKRVPRYSL QCLKKKTEKV HNKIMDKPKN KQQPQTPPPF LLNNEYTESS
DDSDDQLPLS ELSQKMKSNK LNTLFLSRNE DCSPAPEKVK LKGERPAQNK KEQLTWEPSI
LTNLTDLGKQ VAEPLRKSVK KSAKQQKPRV RAPPQGKKTL PQLQTGLKTQ DKQSTHEMIS
EQAKTISEAS GQQTSQVQSS LSPNNIRNNS VKLISAKTLM PAQRSQDYSP NKMQVGQPLG
FAIELPSPVD GKEASVEIDT QLVHTSKFLE NMTRPSTVEV HKFDLMDIFM GENEKLDYEY
DDDDVLSVAA SWNGLDDENV PEDEPRKEAK TAEQLPKPEP STETLKPIEK ENAQKMQSIK
SFQIPKLNAK NLKTQPSVMR SIYENEELEK NKVLAKPAPP SLVHQPLAES NRNQRDEATA
ARRAKETFPV FAPLYRVAPE SAATLVSANS QQVIPQVYFS TSNQDGVNWI KDVFGIRCMQ
SVDNKCISIN CDHTMNSLGE VQKRLMRMDE DTLLSLYRQT IRSFFLFQTY YTSFVDIFKF
RNLWQYLLIM LVDCRLYKSI SAPLLAHVYE ALSKCGMQKE AVKRIMEHVW LPCKAHKYRD
LMLTTLNILS NANWEDYCDK LTQLDKDYNF EIPHKNLITI LKSSVDCSDK FANALKLITL
HPNSIRTNET IMSILSNASK SYSYMHNESA SASQGPPGAA SFLAPPAAIQ PPHTTVPNFG
YLPNPSFHYS NEYAINIHNF D
