MODU_DROME
ID MODU_DROME Reviewed; 542 AA.
AC P13469; Q9V9S2;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=DNA-binding protein modulo;
GN Name=mod; ORFNames=CG2050;
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].
RC STRAIN=Oregon-R;
RX PubMed=2510126; DOI=10.1093/nar/17.20.8101;
RA Krejci E., Garzino V., Mary C., Bennani N., Pradel J.;
RT "Modulo, a new maternally expressed Drosophila gene encodes a DNA-binding
RT protein with distinct acidic and basic regions.";
RL Nucleic Acids Res. 17:8101-8116(1989).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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]
RP POSSIBLE FUNCTION.
RX PubMed=7813788; DOI=10.1006/dbio.1994.1349;
RA Graba Y., Laurenti P., Perrin L., Aragnol D., Pradel J.;
RT "The modifier of variegation modulo gene acts downstream of dorsoventral
RT and HOM-C genes and is required for morphogenesis in Drosophila.";
RL Dev. Biol. 166:704-715(1994).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-44; SER-129 AND
RP SER-304, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-44; SER-120; SER-129;
RP SER-142 AND SER-443, 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).
CC -!- FUNCTION: Its capacity to bind DNA and protein(s), and its differential
CC expression during development suggest a role in the regulation of gene
CC expression during Drosophila development. It could, in interaction with
CC other factors, be required for the translation of instructions provided
CC by pattern forming genes and controls, via chromatin changes, the
CC activity of genes critical for the process of morphogenesis of several
CC embryonic territories.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: The N-terminus is blocked.
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DR EMBL; X15702; CAA33732.1; -; mRNA.
DR EMBL; AE014297; AAF57213.1; -; Genomic_DNA.
DR EMBL; AY058519; AAL13748.1; -; mRNA.
DR PIR; S06602; S06602.
DR RefSeq; NP_001247401.1; NM_001260472.2.
DR RefSeq; NP_524614.2; NM_079875.3.
DR AlphaFoldDB; P13469; -.
DR SMR; P13469; -.
DR BioGRID; 68602; 17.
DR DIP; DIP-19479N; -.
DR IntAct; P13469; 23.
DR MINT; P13469; -.
DR STRING; 7227.FBpp0085233; -.
DR iPTMnet; P13469; -.
DR PaxDb; P13469; -.
DR PRIDE; P13469; -.
DR DNASU; 43764; -.
DR EnsemblMetazoa; FBtr0085874; FBpp0085233; FBgn0002780.
DR EnsemblMetazoa; FBtr0310268; FBpp0301951; FBgn0002780.
DR GeneID; 43764; -.
DR KEGG; dme:Dmel_CG2050; -.
DR CTD; 43764; -.
DR FlyBase; FBgn0002780; mod.
DR VEuPathDB; VectorBase:FBgn0002780; -.
DR eggNOG; ENOG502T98N; Eukaryota.
DR GeneTree; ENSGT00940000175980; -.
DR HOGENOM; CLU_502757_0_0_1; -.
DR InParanoid; P13469; -.
DR OMA; KPFNKRP; -.
DR OrthoDB; 969613at2759; -.
DR PhylomeDB; P13469; -.
DR Reactome; R-DME-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-DME-72187; mRNA 3'-end processing.
DR Reactome; R-DME-73856; RNA Polymerase II Transcription Termination.
DR SignaLink; P13469; -.
DR BioGRID-ORCS; 43764; 0 hits in 1 CRISPR screen.
DR ChiTaRS; mod; fly.
DR GenomeRNAi; 43764; -.
DR PRO; PR:P13469; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0002780; Expressed in cleaving embryo and 33 other tissues.
DR ExpressionAtlas; P13469; baseline and differential.
DR Genevisible; P13469; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0032991; C:protein-containing complex; IPI:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 4.
DR SMART; SM00360; RRM; 4.
DR SUPFAM; SSF54928; SSF54928; 3.
DR PROSITE; PS50102; RRM; 4.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding.
FT CHAIN 1..542
FT /note="DNA-binding protein modulo"
FT /id="PRO_0000081635"
FT DOMAIN 175..251
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 258..331
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 340..429
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 420..489
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..115
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 330
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 74
FT /note="P -> A (in Ref. 1; CAA33732)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="I -> V (in Ref. 1; CAA33732)"
FT /evidence="ECO:0000305"
FT CONFLICT 505..542
FT /note="RAPRKFQKDTKPNFGKKPFNKRPAQENGGKSFVKRARF -> APRGSSKRTL
FT SQTLVKNHLTSARHKRMVVNRLLKGQDFRT (in Ref. 1; CAA33732)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 542 AA; 60310 MW; E5E383B2A0595E2E CRC64;
MAQKKAVTVK GKKATNGEEK PLAKRVTKST KVQEEETVVP QSPSKKSRKQ PVKEVPQFSE
EDESDVEEQN DEQPGDDSDF ETEEAAGLID DEAEEDEEYN SDDEEDDDDD ELEPGEVSKS
EGADEVDESD DDEEAPVEKP VSKKSEKANS EKSEENRGIP KVKVGKIPLG TPKNQIVFVT
NLPNEYLHKD LVALFAKFGR LSALQRFTNL NGNKSVLIAF DTSTGAEAVL QAKPKALTLG
DNVLSVSQPR NKEENNERTV VVGLIGPNIT KDDLKTFFEK VAPVEAVTIS SNRLMPRAFV
RLASVDDIPK ALKLHSTELF SRFITVRRIS QESISRTSEL TLVVENVGKH ESYSSDALEK
IFKKFGDVEE IDVVCSKAVL AFVTFKQSDA ATKALAQLDG KTVNKFEWKL HRFERSTSGR
AILVTNLTSD ATEADLRKVF NDSGEIESII MLGQKAVVKF KDDEGFCKSF LANESIVNNA
PIFIEPNSLL KHRLLKKRLA IGQTRAPRKF QKDTKPNFGK KPFNKRPAQE NGGKSFVKRA
RF
