RSMB_DROME
ID RSMB_DROME Reviewed; 199 AA.
AC Q05856; M9MRL9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Small nuclear ribonucleoprotein-associated protein B;
DE Short=snRNP-B;
DE AltName: Full=Sm protein B;
DE Short=Sm-B;
DE Short=SmB;
GN Name=SmB; ORFNames=CG5352;
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=Canton-S; TISSUE=Ovary;
RX PubMed=7680326; DOI=10.1016/0378-1119(93)90404-q;
RA Brunet C., Quan T., Craft J.E.;
RT "Comparison of the Drosophila melanogaster, human and murine Sm B cDNAs:
RT evolutionary conservation.";
RL Gene 124:269-273(1993).
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 INTERACTION WITH SMN.
RX PubMed=16753561; DOI=10.1016/j.cub.2006.04.037;
RA Gonsalvez G.B., Rajendra T.K., Tian L., Matera A.G.;
RT "The Sm-protein methyltransferase, dart5, is essential for germ-cell
RT specification and maintenance.";
RL Curr. Biol. 16:1077-1089(2006).
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 METHYLATION.
RX PubMed=18369183; DOI=10.1261/rna.940708;
RA Gonsalvez G.B., Praveen K., Hicks A.J., Tian L., Matera A.G.;
RT "Sm protein methylation is dispensable for snRNP assembly in Drosophila
RT melanogaster.";
RL RNA 14:878-887(2008).
RN [8]
RP FUNCTION, INTERACTION WITH STAU AND YPS, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20570937; DOI=10.1242/dev.042721;
RA Gonsalvez G.B., Rajendra T.K., Wen Y., Praveen K., Matera A.G.;
RT "Sm proteins specify germ cell fate by facilitating oskar mRNA
RT localization.";
RL Development 137:2341-2351(2010).
RN [9]
RP INTERACTION WITH CSUL; VSL AND TUD, TISSUE SPECIFICITY, AND METHYLATION.
RX PubMed=17164419; DOI=10.1242/dev.02687;
RA Anne J., Ollo R., Ephrussi A., Mechler B.M.;
RT "Arginine methyltransferase Capsuleen is essential for methylation of
RT spliceosomal Sm proteins and germ cell formation in Drosophila.";
RL Development 134:137-146(2007).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, METHYLATION, AND
RP MUTAGENESIS OF ARG-112; ARG-130; ARG-145; ARG-174; ARG-181; ARG-189 AND
RP ARG-196.
RX PubMed=20659974; DOI=10.1242/dev.052944;
RA Anne J.;
RT "Arginine methylation of SmB is required for Drosophila germ cell
RT development.";
RL Development 137:2819-2828(2010).
RN [11]
RP INTERACTION WITH MSK AND SNUP.
RX PubMed=23885126; DOI=10.1091/mbc.e13-03-0118;
RA Natalizio A.H., Matera A.G.;
RT "Identification and characterization of Drosophila Snurportin reveals a
RT role for the import receptor Moleskin/Importin7 in snRNP biogenesis.";
RL Mol. Biol. Cell 24:2932-2942(2013).
CC -!- FUNCTION: Plays a role in pre-mRNA splicing as a core component of the
CC spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins
CC (snRNPs), the building blocks of the spliceosome (By similarity).
CC Involved in germline establishment and development (PubMed:20570937,
CC PubMed:20659974). {ECO:0000250|UniProtKB:P14678,
CC ECO:0000269|PubMed:20570937, ECO:0000269|PubMed:20659974}.
CC -!- SUBUNIT: Component of the osk mRNP (PubMed:20570937). Interacts with
CC stau and yps (PubMed:20570937). Interacts with csul (via the N-terminal
CC region) (PubMed:17164419). Interacts with vls (PubMed:17164419).
CC Interacts (methylated) with tud (PubMed:17164419). Interacts with Smn;
CC this interaction may be favored by SmB methylation (PubMed:16753561).
CC Interacts with the SMN complex (PubMed:18621711). Interacts with msk
CC and Snup; these interactions are RNA-dependent (PubMed:23885126).
CC {ECO:0000269|PubMed:16753561, ECO:0000269|PubMed:17164419,
CC ECO:0000269|PubMed:18621711, ECO:0000269|PubMed:20570937,
CC ECO:0000269|PubMed:23885126}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P14678}. Nucleus,
CC Cajal body {ECO:0000305}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P14678}.
CC -!- TISSUE SPECIFICITY: Expressed in the posterior part of the oocyte and
CC embryo. Expressed in the pole plasm (at protein level), colocalizing
CC with SmD3. {ECO:0000269|PubMed:17164419, ECO:0000269|PubMed:20570937}.
CC -!- DEVELOPMENTAL STAGE: Maternally and zygotically expressed. In early
CC stages of egg chamber development, predominantly accumulated in the
CC nuclei of nurse cells and oocyte. Enriched at the posterior of stage 10
CC oocytes which persists after fertilization, at the posterior of pre-
CC blastoderm stage embryos. {ECO:0000269|PubMed:20570937,
CC ECO:0000269|PubMed:20659974}.
CC -!- PTM: Symmetrically dimethylated on arginine residues present in the RG
CC repeats by csul (or csul-vls complex) and Art7; methylation is not
CC required for assembly and biogenesis of snRNPs, but required for pole
CC plasm localization. There seems to be a specific role of two subsets of
CC arginine residues in the C-terminal region: the subset containing Arg-
CC 112, Arg-130 and Arg-145 is required during embryogenesis for gonad
CC formation, whereas the subset containing Arg-174, Arg-181, Arg-189 and
CC Arg-196 is involved in pole cell formation by controlling polar granule
CC maintenance at the posterior pole of the oocyte.
CC {ECO:0000269|PubMed:17164419, ECO:0000269|PubMed:18369183,
CC ECO:0000269|PubMed:20659974}.
CC -!- SIMILARITY: Belongs to the snRNP SmB/SmN family. {ECO:0000305}.
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DR EMBL; L02919; AAA28858.1; -; mRNA.
DR EMBL; AE014134; ADV37030.1; -; Genomic_DNA.
DR EMBL; AY061171; AAL28719.1; -; mRNA.
DR PIR; JN0574; JN0574.
DR RefSeq; NP_001188780.1; NM_001201851.2.
DR AlphaFoldDB; Q05856; -.
DR SMR; Q05856; -.
DR BioGRID; 60507; 71.
DR DIP; DIP-18712N; -.
DR IntAct; Q05856; 14.
DR STRING; 7227.FBpp0293061; -.
DR PaxDb; Q05856; -.
DR PRIDE; Q05856; -.
DR DNASU; 34426; -.
DR EnsemblMetazoa; FBtr0304118; FBpp0293061; FBgn0262601.
DR GeneID; 34426; -.
DR KEGG; dme:Dmel_CG5352; -.
DR CTD; 34426; -.
DR FlyBase; FBgn0262601; SmB.
DR VEuPathDB; VectorBase:FBgn0262601; -.
DR eggNOG; KOG3168; Eukaryota.
DR GeneTree; ENSGT00940000155052; -.
DR HOGENOM; CLU_076902_1_0_1; -.
DR InParanoid; Q05856; -.
DR OMA; KMINYRM; -.
DR OrthoDB; 1488395at2759; -.
DR PhylomeDB; Q05856; -.
DR Reactome; R-DME-111367; SLBP independent Processing of Histone Pre-mRNAs.
DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-DME-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-DME-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-DME-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
DR BioGRID-ORCS; 34426; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 34426; -.
DR PRO; PR:Q05856; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0262601; Expressed in adult abdomen and 25 other tissues.
DR Genevisible; Q05856; DM.
DR GO; GO:0015030; C:Cajal body; IDA:FlyBase.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0045495; C:pole plasm; IDA:FlyBase.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; ISS:FlyBase.
DR GO; GO:0005681; C:spliceosomal complex; ISS:FlyBase.
DR GO; GO:0005685; C:U1 snRNP; IBA:GO_Central.
DR GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
DR GO; GO:0005687; C:U4 snRNP; IBA:GO_Central.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IBA:GO_Central.
DR GO; GO:0005682; C:U5 snRNP; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISS:FlyBase.
DR GO; GO:0007281; P:germ cell development; IMP:FlyBase.
DR GO; GO:0008406; P:gonad development; IMP:FlyBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR017131; snRNP-assoc_SmB/SmN.
DR Pfam; PF01423; LSM; 1.
DR PIRSF; PIRSF037187; snRNP_SmB/SmN; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1..199
FT /note="Small nuclear ribonucleoprotein-associated protein
FT B"
FT /id="PRO_0000125526"
FT REPEAT 111..113
FT /note="1"
FT REPEAT 144..146
FT /note="2"
FT REPEAT 173..175
FT /note="3"
FT REPEAT 195..197
FT /note="4"
FT REGION 111..197
FT /note="4 X 3 AA repeats of G-R-G"
FT REGION 170..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..191
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 112
FT /note="R->L: Unable to localize to the pole plasm; when
FT associated with G-130; L-145; L-174; L-181; L-189 and G-
FT 196."
FT /evidence="ECO:0000269|PubMed:20659974"
FT MUTAGEN 130
FT /note="R->G: Unable to localize to the pole plasm; when
FT associated with L-112; L-145; L-174; L-181; L-189 and G-
FT 196."
FT /evidence="ECO:0000269|PubMed:20659974"
FT MUTAGEN 145
FT /note="R->L: Unable to localize to the pole plasm; when
FT associated with L-112; G-130; L-174; L-181; L-189 and G-
FT 196."
FT /evidence="ECO:0000269|PubMed:20659974"
FT MUTAGEN 174
FT /note="R->L: Unable to localize to the pole plasm; when
FT associated with L-112; G-130; L-145; L-181; L-189 and G-
FT 196."
FT /evidence="ECO:0000269|PubMed:20659974"
FT MUTAGEN 181
FT /note="R->L: Unable to localize to the pole plasm; when
FT associated with L-112; G-130; L-145; L-174; L-189 and G-
FT 196."
FT /evidence="ECO:0000269|PubMed:20659974"
FT MUTAGEN 189
FT /note="R->L: Unable to localize to the pole plasm; when
FT associated with L-112; G-130; L-145; L-174; L-181 and G-
FT 196."
FT /evidence="ECO:0000269|PubMed:20659974"
FT MUTAGEN 196
FT /note="R->G: Unable to localize to the pole plasm; when
FT associated with L-112; G-130; L-145; L-174; L-181 and L-
FT 189."
FT /evidence="ECO:0000269|PubMed:20659974"
SQ SEQUENCE 199 AA; 21021 MW; EEEDBE1202E51848 CRC64;
MTIGKNNKMI QHLNYRVRIV LQDSRTFIGT FKAFDKHMNL ILGDCEEFRK IRSKNSKVPE
REEKRVLGFV LLRGENIVSL TVEGPPPPEE GLPRVPIPGA APGPGIGRVA GRGMPINLSA
VPAGLQGPVR GVGGPAQQHM APMGRGVPRA PMMGAPPPGM IPGGMPSMPG NMGRGAPPPM
RGPPPSMIRG APPPGRGGY
