SMD1_MOUSE
ID SMD1_MOUSE Reviewed; 119 AA.
AC P62315; P13641; Q3UYM0;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Small nuclear ribonucleoprotein Sm D1;
DE Short=Sm-D1;
DE AltName: Full=Sm-D autoantigen;
DE AltName: Full=snRNP core protein D1;
GN Name=Snrpd1;
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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Lymphoma;
RX PubMed=1388635; DOI=10.1016/0896-8411(92)90143-e;
RA Mitsuda T., Eisenberg R.A., Cohen P.L.;
RT "The murine Sm-D autoantigen: multiple genes, genetic polymorphism,
RT evolutionary conservation and lack of intervening sequences in the coding
RT region.";
RL J. Autoimmun. 5:277-287(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Egg, Medulla oblongata, Pancreas, and Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Pancreas, Spleen, and
RC 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. May act as
CC a charged protein scaffold to promote snRNP assembly or strengthen
CC snRNP-snRNP interactions through non-specific electrostatic contacts
CC with RNA. {ECO:0000250|UniProtKB:P62314}.
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. Component of the U11/U12 snRNPs that
CC are part of the U12-type spliceosome. Part of the SMN-Sm complex that
CC contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6,
CC GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2,
CC SNRPD3, SNRPE, SNRPF and SNRPG; catalyzes core snRNPs assembly. Forms a
CC 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE,
CC SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics
CC additional Sm proteins and which is unable to assemble into the core
CC snRNP. Interacts (via C-terminus) with SMN1 (via Tudor domain); the
CC interaction is direct. Interacts with GEMIN2; the interaction is
CC direct. Interacts with SNRPD2; the interaction is direct.
CC {ECO:0000250|UniProtKB:P62314}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P62314}. Nucleus {ECO:0000250|UniProtKB:P62314}.
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:P62314}.
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:P62314}.
CC -!- SIMILARITY: Belongs to the snRNP core protein family. {ECO:0000305}.
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DR EMBL; M58558; AAA96493.1; -; mRNA.
DR EMBL; AK005517; BAB24092.1; -; mRNA.
DR EMBL; AK007674; BAB25178.1; -; mRNA.
DR EMBL; AK011455; BAB27628.1; -; mRNA.
DR EMBL; AK013075; BAB28635.1; -; mRNA.
DR EMBL; AK134582; BAE22192.1; -; mRNA.
DR EMBL; AK135979; BAE22759.1; -; mRNA.
DR EMBL; BC024875; AAH24875.1; -; mRNA.
DR CCDS; CCDS29056.1; -.
DR RefSeq; NP_033252.1; NM_009226.4.
DR AlphaFoldDB; P62315; -.
DR SMR; P62315; -.
DR BioGRID; 203379; 70.
DR IntAct; P62315; 5.
DR MINT; P62315; -.
DR STRING; 10090.ENSMUSP00000002551; -.
DR iPTMnet; P62315; -.
DR PhosphoSitePlus; P62315; -.
DR EPD; P62315; -.
DR jPOST; P62315; -.
DR MaxQB; P62315; -.
DR PaxDb; P62315; -.
DR PeptideAtlas; P62315; -.
DR PRIDE; P62315; -.
DR ProteomicsDB; 257269; -.
DR Antibodypedia; 7243; 181 antibodies from 27 providers.
DR DNASU; 20641; -.
DR Ensembl; ENSMUST00000002551; ENSMUSP00000002551; ENSMUSG00000002477.
DR GeneID; 20641; -.
DR KEGG; mmu:20641; -.
DR UCSC; uc008eaz.1; mouse.
DR CTD; 6632; -.
DR MGI; MGI:98344; Snrpd1.
DR VEuPathDB; HostDB:ENSMUSG00000002477; -.
DR eggNOG; KOG3428; Eukaryota.
DR GeneTree; ENSGT00510000047245; -.
DR HOGENOM; CLU_123956_3_0_1; -.
DR InParanoid; P62315; -.
DR OMA; SVTPQMN; -.
DR OrthoDB; 1579192at2759; -.
DR PhylomeDB; P62315; -.
DR TreeFam; TF314224; -.
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 BioGRID-ORCS; 20641; 27 hits in 75 CRISPR screens.
DR ChiTaRS; Snrpd1; mouse.
DR PRO; PR:P62315; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P62315; protein.
DR Bgee; ENSMUSG00000002477; Expressed in somite and 245 other tissues.
DR ExpressionAtlas; P62315; baseline and differential.
DR Genevisible; P62315; 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: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: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:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:1990446; F:U1 snRNP binding; ISO:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
DR CDD; cd01724; Sm_D1; 1.
DR InterPro; IPR027141; LSm4/Sm_D1/D3.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR034102; Sm_D1.
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; Isopeptide bond; Methylation; mRNA processing; mRNA splicing;
KW Nucleus; Reference proteome; Repeat; Ribonucleoprotein; Spliceosome;
KW Ubl conjugation.
FT CHAIN 1..119
FT /note="Small nuclear ribonucleoprotein Sm D1"
FT /id="PRO_0000122202"
FT REGION 1..80
FT /note="Sufficient for interaction with CLNS1A"
FT /evidence="ECO:0000250"
FT REGION 69..119
FT /note="Required for interaction with SMN1"
FT /evidence="ECO:0000250|UniProtKB:P62314"
FT REGION 88..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..119
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 86
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62314"
SQ SEQUENCE 119 AA; 13282 MW; 0C81C94BF98E0810 CRC64;
MKLVRFLMKL SHETVTIELK NGTQVHGTIT GVDVSMNTHL KAVKMTLKNR EPVQLETLSI
RGNNIRYFIL PDSLPLDTLL VDVEPKVKSK KREAVAGRGR GRGRGRGRGR GRGRGGPRR
