RU17_DROME
ID RU17_DROME Reviewed; 448 AA.
AC P17133; Q564D5; Q9VM56;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=U1 small nuclear ribonucleoprotein 70 kDa;
DE Short=U1 snRNP 70 kDa;
DE Short=U1-70K;
DE Short=snRNP70;
GN Name=snRNP-U1-70K; Synonyms=snRNP27D, snRNP70K; ORFNames=CG8749;
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 [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RX PubMed=1692955; DOI=10.1128/mcb.10.6.2492-2502.1990;
RA Mancebo R., Lo P.C.H., Mount S.M.;
RT "Structure and expression of the Drosophila melanogaster gene for the U1
RT small nuclear ribonucleoprotein particle 70K protein.";
RL Mol. Cell. Biol. 10:2492-2502(1990).
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 FUNCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=15611175; DOI=10.1534/genetics.104.032532;
RA Salz H.K., Mancebo R.S.Y., Nagengast A.A., Speck O., Psotka M., Mount S.M.;
RT "The Drosophila U1-70K protein is required for viability, but its arginine-
RT rich domain is dispensable.";
RL Genetics 168:2059-2065(2004).
RN [6]
RP INTERACTION WITH THE SMN COMPLEX.
RX PubMed=18621711; DOI=10.1073/pnas.0802287105;
RA Kroiss M., Schultz J., Wiesner J., Chari A., Sickmann A., Fischer U.;
RT "Evolution of an RNP assembly system: a minimal SMN complex facilitates
RT formation of UsnRNPs in Drosophila melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10045-10050(2008).
RN [7]
RP STRUCTURE BY NMR OF 405-425 IN COMPLEX WITH PSI.
RX PubMed=15990112; DOI=10.1016/j.jmb.2005.04.077;
RA Ignjatovic T., Yang J.-C., Butler J., Neuhaus D., Nagai K.;
RT "Structural basis of the interaction between P-element somatic inhibitor
RT and U1-70k essential for the alternative splicing of P-element
RT transposase.";
RL J. Mol. Biol. 351:52-65(2005).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24244416; DOI=10.1371/journal.pone.0079048;
RA Klusza S., Novak A., Figueroa S., Palmer W., Deng W.M.;
RT "Prp22 and spliceosome components regulate chromatin dynamics in germ-line
RT polyploid cells.";
RL PLoS ONE 8:E79048-E79048(2013).
CC -!- FUNCTION: Mediates the splicing of pre-mRNA by binding to the stem loop
CC I region of U1-snRNA (PubMed:15611175). Required during oogenesis for
CC nurse cell chromatin dispersal (PubMed:24244416).
CC {ECO:0000269|PubMed:15611175, ECO:0000269|PubMed:24244416}.
CC -!- SUBUNIT: Component of the U1 snRNP (By similarity). Interacts with Psi;
CC essential for alternative splicing of P-element transposase. Interacts
CC with the SMN complex. {ECO:0000250|UniProtKB:P08621,
CC ECO:0000269|PubMed:15990112, ECO:0000269|PubMed:18621711}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q62376}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q62376}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC throughout all development. {ECO:0000269|PubMed:1692955}.
CC -!- DOMAIN: Protein interactions mediated by the Arg-rich domain are not
CC essential for viability, but do contribute to an essential U1 snRNP
CC function. {ECO:0000269|PubMed:15611175}.
CC -!- DOMAIN: The RRM domain mediates interaction with U1 RNA.
CC {ECO:0000250|UniProtKB:P08621}.
CC -!- DISRUPTION PHENOTYPE: Lethal during embryogenesis (PubMed:15611175).
CC RNAi-mediated knockdown in the germline results in defective nurse cell
CC nuclei decondensation and dispersal ultimately affecting oogenesis
CC (PubMed:24244416). {ECO:0000269|PubMed:15611175,
CC ECO:0000269|PubMed:24244416}.
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; M31162; AAA28859.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF52471.1; -; Genomic_DNA.
DR EMBL; AY061501; AAL29049.1; -; mRNA.
DR EMBL; AY089622; AAL90360.1; -; mRNA.
DR PIR; A36311; A36311.
DR RefSeq; NP_001260173.1; NM_001273244.1.
DR RefSeq; NP_477205.1; NM_057857.5.
DR PDB; 2BN5; NMR; -; B=405-425.
DR PDBsum; 2BN5; -.
DR AlphaFoldDB; P17133; -.
DR BMRB; P17133; -.
DR SMR; P17133; -.
DR BioGRID; 60131; 25.
DR DIP; DIP-19840N; -.
DR IntAct; P17133; 2.
DR STRING; 7227.FBpp0303792; -.
DR PaxDb; P17133; -.
DR PRIDE; P17133; -.
DR DNASU; 33982; -.
DR EnsemblMetazoa; FBtr0079355; FBpp0078983; FBgn0016978.
DR EnsemblMetazoa; FBtr0331375; FBpp0303793; FBgn0016978.
DR GeneID; 33982; -.
DR KEGG; dme:Dmel_CG8749; -.
DR CTD; 33982; -.
DR FlyBase; FBgn0016978; snRNP-U1-70K.
DR VEuPathDB; VectorBase:FBgn0016978; -.
DR eggNOG; KOG0113; Eukaryota.
DR GeneTree; ENSGT00940000160292; -.
DR HOGENOM; CLU_045151_2_1_1; -.
DR InParanoid; P17133; -.
DR OMA; GVAKFMA; -.
DR OrthoDB; 1455080at2759; -.
DR PhylomeDB; P17133; -.
DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 33982; 1 hit in 1 CRISPR screen.
DR EvolutionaryTrace; P17133; -.
DR GenomeRNAi; 33982; -.
DR PRO; PR:P17133; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0016978; Expressed in secondary oocyte and 37 other tissues.
DR ExpressionAtlas; P17133; baseline and differential.
DR Genevisible; P17133; DM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IC:FlyBase.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:0005681; C:spliceosomal complex; ISS:UniProtKB.
DR GO; GO:0005685; C:U1 snRNP; ISS:UniProtKB.
DR GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0017069; F:snRNA binding; IBA:GO_Central.
DR GO; GO:0030619; F:U1 snRNA binding; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IPI:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; HMP:FlyBase.
DR GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR CDD; cd12236; RRM_snRNP70; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR IDEAL; IID50033; -.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034143; snRNP70_RRM.
DR InterPro; IPR022023; U1snRNP70_N.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF12220; U1snRNP70_N; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; Nucleus; Reference proteome;
KW Ribonucleoprotein; RNA-binding.
FT CHAIN 1..448
FT /note="U1 small nuclear ribonucleoprotein 70 kDa"
FT /id="PRO_0000081884"
FT DOMAIN 102..180
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 91..201
FT /note="Required for interaction with U1 RNA"
FT /evidence="ECO:0000250|UniProtKB:P08621"
FT REGION 188..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..425
FT /note="Mediates binding to Psi"
FT COMPBIAS 205..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 278
FT /note="N -> S (in Ref. 1; AAA28859)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 448 AA; 52901 MW; 0DDFB5A39CA72AEB CRC64;
MTQYLPPNLL ALFAAREPIP FMPPVDKLPH EKKSRGYLGV AKFMADFEDP KDTPLPKTVE
TRQERLERRR REKAEQVAYK LEREIALWDP TEIKNATEDP FRTLFIARIN YDTSESKLRR
EFEFYGPIKK IVLIHDQESG KPKGYAFIEY EHERDMHAAY KHADGKKIDS KRVLVDVERA
RTVKGWLPRR LGGGLGGTRR GGNDVNIKHS GREDNERERE RYRLERERED REGPGRGGGS
NGLDARPGRG FGAERRRSRS RERRDRERDR GRGAVASNGR SRSRSRERRK RRAGSRERYD
EFDRRDRRDR ERERDRDRER EKKKKRSKSR ERESSRERRE RKRERRDRER GTGSGGDVKE
RKPDFRDMDV IKIKEEPVDD GYPTFDYQNA TIKREIDDED EEKYRPPPAH HNMFSVPPPP
ILGRGNASTN PNPDNGQQSS GDPSWWRQ
