SMD3_DROME
ID SMD3_DROME Reviewed; 151 AA.
AC O44437;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Small nuclear ribonucleoprotein Sm D3;
DE Short=Sm-D3;
DE AltName: Full=snRNP core protein D3;
GN Name=SmD3; Synonyms=guf2; ORFNames=CG8427;
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 TISSUE=Embryo;
RX PubMed=9488472; DOI=10.1128/mcb.18.3.1553;
RA Ivanov I.P., Simin K., Letsou A., Atkins J.F., Gesteland R.F.;
RT "The Drosophila gene for antizyme requires ribosomal frameshifting for
RT expression and contains an intronic gene for snRNP Sm D3 on the opposite
RT strand.";
RL Mol. Cell. Biol. 18:1553-1561(1998).
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 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 [6]
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).
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 {ECO:0000250|UniProtKB:P62318}.
CC -!- SUBUNIT: Interacts with the SMN complex. {ECO:0000269|PubMed:18621711}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P62318}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62318}.
CC -!- PTM: Methylated on arginine residues by Art5 and Art7; methylation is
CC not required for assembly and biogenesis of snRNPs.
CC {ECO:0000269|PubMed:18369183}.
CC -!- SIMILARITY: Belongs to the snRNP core protein family. {ECO:0000305}.
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DR EMBL; AF038598; AAB92621.1; -; mRNA.
DR EMBL; AE013599; AAF58566.1; -; Genomic_DNA.
DR EMBL; AY113465; AAM29470.1; -; mRNA.
DR RefSeq; NP_725106.1; NM_165866.3.
DR AlphaFoldDB; O44437; -.
DR SMR; O44437; -.
DR BioGRID; 62087; 11.
DR DIP; DIP-19470N; -.
DR IntAct; O44437; 26.
DR STRING; 7227.FBpp0087094; -.
DR PaxDb; O44437; -.
DR PRIDE; O44437; -.
DR EnsemblMetazoa; FBtr0087986; FBpp0087094; FBgn0023167.
DR GeneID; 36306; -.
DR KEGG; dme:Dmel_CG8427; -.
DR CTD; 36306; -.
DR FlyBase; FBgn0023167; SmD3.
DR VEuPathDB; VectorBase:FBgn0023167; -.
DR eggNOG; KOG3172; Eukaryota.
DR GeneTree; ENSGT00610000086153; -.
DR HOGENOM; CLU_099537_1_0_1; -.
DR InParanoid; O44437; -.
DR OMA; MNCQLRD; -.
DR OrthoDB; 1534014at2759; -.
DR PhylomeDB; O44437; -.
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 SignaLink; O44437; -.
DR BioGRID-ORCS; 36306; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 36306; -.
DR PRO; PR:O44437; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0023167; Expressed in egg cell and 24 other tissues.
DR ExpressionAtlas; O44437; baseline and differential.
DR Genevisible; O44437; DM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR GO; GO:0000243; C:commitment complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:FlyBase.
DR GO; GO:0034715; C:pICln-Sm protein complex; IBA:GO_Central.
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; TAS:FlyBase.
DR GO; GO:0034719; C:SMN-Sm protein complex; IBA:GO_Central.
DR GO; GO:0097526; C:spliceosomal tri-snRNP complex; IBA:GO_Central.
DR GO; GO:0005685; C:U1 snRNP; IBA:GO_Central.
DR GO; GO:0005689; C:U12-type spliceosomal complex; IBA:GO_Central.
DR GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR GO; GO:0005687; C:U4 snRNP; 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:0007417; P:central nervous system development; IMP:FlyBase.
DR GO; GO:0048542; P:lymph gland development; IMP:FlyBase.
DR GO; GO:0000278; P:mitotic cell cycle; HMP:FlyBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:FlyBase.
DR GO; GO:0007517; P:muscle organ development; IMP:FlyBase.
DR GO; GO:0030182; P:neuron differentiation; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0007422; P:peripheral nervous system development; IMP:FlyBase.
DR GO; GO:0045451; P:pole plasm oskar mRNA localization; IMP:FlyBase.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IBA:GO_Central.
DR CDD; cd01721; Sm_D3; 1.
DR InterPro; IPR027141; LSm4/Sm_D1/D3.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR034099; SmD3.
DR PANTHER; PTHR23338; PTHR23338; 1.
DR Pfam; PF01423; LSM; 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; Spliceosome.
FT CHAIN 1..151
FT /note="Small nuclear ribonucleoprotein Sm D3"
FT /id="PRO_0000122218"
FT REPEAT 108..109
FT /note="1"
FT REPEAT 110..111
FT /note="2"
FT REPEAT 112..113
FT /note="3"
FT REGION 108..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..113
FT /note="3 X 2 AA tandem repeats of R-G"
SQ SEQUENCE 151 AA; 15582 MW; 65F0B899EACA1C77 CRC64;
MSIGVPIKVL HEAEGHIITC ETITGEVYRG KLIEAEDNMN CQMTQITVTY RDGRTANLEN
VYIRGSKIRF LILPDMLKNA PMFKKQTGKG LGGTAGRGKA AILRAQARGR GRGGPPGGGR
GTGGPPGAPG GSGGRGAWQG GPTGGRGRGG L
