SMD3_MOUSE
ID SMD3_MOUSE Reviewed; 126 AA.
AC P62320; P43331; Q3TV81;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Small nuclear ribonucleoprotein Sm D3;
DE Short=Sm-D3;
DE AltName: Full=snRNP core protein D3;
GN Name=Snrpd3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, Lung, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP FUNCTION, RNA-BINDING, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=19470752; DOI=10.1128/mcb.00296-09;
RA Yang X.-C., Torres M.P., Marzluff W.F., Dominski Z.;
RT "Three proteins of the U7-specific Sm ring function as the molecular ruler
RT to determine the site of 3'-end processing in mammalian histone pre-mRNA.";
RL Mol. Cell. Biol. 29:4045-4056(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. Component of both the
CC pre-catalytic spliceosome B complex and activated spliceosome C
CC complexes. Is also a component of the minor U12 spliceosome (By
CC similarity). As part of the U7 snRNP it is involved in histone pre-mRNA
CC 3'-end processing (PubMed:19470752). {ECO:0000250|UniProtKB:P62318,
CC ECO:0000269|PubMed:19470752}.
CC -!- SUBUNIT: Core component of the spliceosomal U1, U2, U4 and U5 small
CC nuclear ribonucleoproteins (snRNPs), the building blocks of the
CC spliceosome. Most spliceosomal snRNPs contain a common set of Sm
CC proteins, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that
CC assemble in a heptameric protein ring on the Sm site of the small
CC nuclear RNA to form the core snRNP. Component of the U1 snRNP. The U1
CC snRNP is composed of the U1 snRNA and the 7 core Sm proteins SNRPB,
CC SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG, and at least three U1
CC snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C.
CC Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and
CC U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200,
CC TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG,
CC DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3,
CC LSM4, LSM5, LSM6, LSM7 and LSM8 (By similarity). Component of the U7
CC snRNP complex, or U7 Sm protein core complex, that is composed of the
CC U7 snRNA and at least LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF and
CC SNRPG; the complex does not contain SNRPD1 and SNRPD2
CC (PubMed:19470752). Component of the U11/U12 snRNPs that are part of the
CC U12-type spliceosome. Part of the SMN-Sm complex that contains SMN1,
CC GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8,
CC STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE,
CC SNRPF and SNRPG; catalyzes core snRNPs assembly. Forms a 6S pICln-Sm
CC complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and
CC SNRPG; ring-like structure where CLNS1A/pICln mimics additional Sm
CC proteins and which is unable to assemble into the core snRNP. Interacts
CC (via C-terminus) with SMN1 (via Tudor domain); the interaction is
CC direct (By similarity). {ECO:0000250|UniProtKB:P62318,
CC ECO:0000269|PubMed:19470752}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P62318}. Nucleus {ECO:0000269|PubMed:19470752}.
CC Note=SMN-mediated assembly into core snRNPs occurs in the cytosol
CC before SMN-mediated transport to the nucleus to be included in
CC spliceosomes. {ECO:0000250|UniProtKB:P62318}.
CC -!- PTM: Methylated on arginine residues by PRMT5 and PRMT7; probable
CC asymmetric dimethylation which is required for assembly and biogenesis
CC of snRNPs. {ECO:0000250|UniProtKB:P62318}.
CC -!- SIMILARITY: Belongs to the snRNP core protein family. {ECO:0000305}.
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DR EMBL; AK005341; BAB23963.1; -; mRNA.
DR EMBL; AK006692; BAB24705.1; -; mRNA.
DR EMBL; AK019453; BAB31729.1; -; mRNA.
DR EMBL; AK160321; BAE35738.1; -; mRNA.
DR CCDS; CCDS23926.1; -.
DR RefSeq; NP_080371.1; NM_026095.4.
DR AlphaFoldDB; P62320; -.
DR SMR; P62320; -.
DR BioGRID; 212112; 76.
DR IntAct; P62320; 6.
DR MINT; P62320; -.
DR STRING; 10090.ENSMUSP00000020397; -.
DR iPTMnet; P62320; -.
DR PhosphoSitePlus; P62320; -.
DR SwissPalm; P62320; -.
DR CPTAC; non-CPTAC-4012; -.
DR EPD; P62320; -.
DR jPOST; P62320; -.
DR MaxQB; P62320; -.
DR PaxDb; P62320; -.
DR PeptideAtlas; P62320; -.
DR PRIDE; P62320; -.
DR ProteomicsDB; 261090; -.
DR DNASU; 67332; -.
DR Ensembl; ENSMUST00000020397; ENSMUSP00000020397; ENSMUSG00000020180.
DR GeneID; 67332; -.
DR KEGG; mmu:67332; -.
DR UCSC; uc007fqm.1; mouse.
DR CTD; 6634; -.
DR MGI; MGI:1914582; Snrpd3.
DR VEuPathDB; HostDB:ENSMUSG00000020180; -.
DR eggNOG; KOG3172; Eukaryota.
DR GeneTree; ENSGT00610000086153; -.
DR HOGENOM; CLU_099537_1_0_1; -.
DR InParanoid; P62320; -.
DR OMA; MNCQLRD; -.
DR OrthoDB; 1584810at2759; -.
DR PhylomeDB; P62320; -.
DR TreeFam; TF354302; -.
DR Reactome; R-MMU-111367; SLBP independent Processing of Histone Pre-mRNAs.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-MMU-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
DR BioGRID-ORCS; 67332; 28 hits in 72 CRISPR screens.
DR ChiTaRS; Snrpd3; mouse.
DR PRO; PR:P62320; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P62320; protein.
DR Bgee; ENSMUSG00000020180; Expressed in floor plate of midbrain and 259 other tissues.
DR ExpressionAtlas; P62320; baseline and differential.
DR Genevisible; P62320; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0000243; C:commitment complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0034709; C:methylosome; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0034715; C:pICln-Sm protein complex; ISS:UniProtKB.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR GO; GO:0034719; C:SMN-Sm protein complex; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; ISO:MGI.
DR GO; GO:0097526; C:spliceosomal tri-snRNP complex; IBA:GO_Central.
DR GO; GO:0005697; C:telomerase holoenzyme complex; ISO:MGI.
DR GO; GO:0005685; C:U1 snRNP; ISS:UniProtKB.
DR GO; GO:0005689; C:U12-type spliceosomal complex; ISO:MGI.
DR GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; ISS:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0005687; C:U4 snRNP; ISS:UniProtKB.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISS:UniProtKB.
DR GO; GO:0005682; C:U5 snRNP; IBA:GO_Central.
DR GO; GO:0005683; C:U7 snRNP; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0071208; F:histone pre-mRNA DCP binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0070034; F:telomerase RNA binding; ISO:MGI.
DR GO; GO:1990446; F:U1 snRNP binding; ISO:MGI.
DR GO; GO:0071209; F:U7 snRNA binding; ISO:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0006479; P:protein methylation; ISO:MGI.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
DR CDD; cd01721; Sm_D3; 1.
DR DisProt; DP01706; -.
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 Acetylation; Cytoplasm; Methylation; mRNA processing; mRNA splicing;
KW Nucleus; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Spliceosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62318"
FT CHAIN 2..126
FT /note="Small nuclear ribonucleoprotein Sm D3"
FT /id="PRO_0000122215"
FT REPEAT 110..111
FT /note="1"
FT REPEAT 112..113
FT /note="2"
FT REPEAT 114..115
FT /note="3"
FT REPEAT 116..117
FT /note="4"
FT REPEAT 118..119
FT /note="5"
FT REGION 110..119
FT /note="5 X 2 AA tandem repeats of [RM]-G"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P62318"
SQ SEQUENCE 126 AA; 13916 MW; 59A6E78E860AA3E0 CRC64;
MSIGVPIKVL HEAEGHIVTC ETNTGEVYRG KLIEAEDNMN CQMSNITVTY RDGRVAQLEQ
VYIRGSKIRF LILPDMLKNA PMLKSMKNKN QGSGAGRGKA AILKAQVAAR GRGRGMGRGN
IFQKRR
