ID   SMD2_MOUSE              Reviewed;         118 AA.
AC   P62317; P43330;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   28-JAN-2026, entry version 163.
DE   RecName: Full=Small nuclear ribonucleoprotein Sm D2;
DE            Short=Sm-D2;
DE   AltName: Full=snRNP core protein D2;
GN   Name=Snrpd2;
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=Corpora quadrigemina, Pancreas, and Thymus;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, and 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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-12, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Pancreas, Spleen,
RC   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. As a component of the minor spliceosome, involved in the
CC       splicing of U12-type introns in pre-mRNAs.
CC       {ECO:0000250|UniProtKB:P62316}.
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 minor spliceosome,
CC       which splices U12-type introns. 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 with SMN1; the interaction is direct. Interacts with
CC       GEMIN2; the interaction is direct. Interacts with SNRPD1; the
CC       interaction is direct. Interacts with SNRPF; the interaction is direct.
CC       {ECO:0000250|UniProtKB:P62316}.
CC   -!- INTERACTION:
CC       P62317; P57678: GEMIN4; Xeno; NbExp=2; IntAct=EBI-6665916, EBI-356700;
CC       P62317; Q16637: SMN2; Xeno; NbExp=3; IntAct=EBI-6665916, EBI-395421;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P62316}. Nucleus {ECO:0000250|UniProtKB:P62316}.
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:P62316}.
CC   -!- SIMILARITY: Belongs to the snRNP core protein family. {ECO:0000305}.
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DR   EMBL; AK007389; BAB25006.1; -; mRNA.
DR   EMBL; AK045968; BAC32551.1; -; mRNA.
DR   EMBL; AK088105; BAC40147.1; -; mRNA.
DR   EMBL; BC043014; AAH43014.1; -; mRNA.
DR   EMBL; BC051208; AAH51208.1; -; mRNA.
DR   CCDS; CCDS20892.1; -.
DR   RefSeq; NP_081219.1; NM_026943.2.
DR   RefSeq; XP_030097829.1; XM_030241969.1.
DR   AlphaFoldDB; P62317; -.
DR   SMR; P62317; -.
DR   BioGRID; 223486; 77.
DR   FunCoup; P62317; 3351.
DR   IntAct; P62317; 5.
DR   MINT; P62317; -.
DR   STRING; 10090.ENSMUSP00000037597; -.
DR   GlyGen; P62317; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P62317; -.
DR   PhosphoSitePlus; P62317; -.
DR   SwissPalm; P62317; -.
DR   jPOST; P62317; -.
DR   PaxDb; 10090-ENSMUSP00000037597; -.
DR   PeptideAtlas; P62317; -.
DR   ProteomicsDB; 257520; -.
DR   Pumba; P62317; -.
DR   Antibodypedia; 31375; 204 antibodies from 28 providers.
DR   DNASU; 107686; -.
DR   Ensembl; ENSMUST00000049294.4; ENSMUSP00000037597.3; ENSMUSG00000040824.4.
DR   GeneID; 107686; -.
DR   KEGG; mmu:107686; -.
DR   UCSC; uc009fkv.1; mouse.
DR   AGR; MGI:98345; -.
DR   CTD; 6633; -.
DR   MGI; MGI:98345; Snrpd2.
DR   VEuPathDB; HostDB:ENSMUSG00000040824; -.
DR   eggNOG; KOG3459; Eukaryota.
DR   GeneTree; ENSGT00390000017608; -.
DR   HOGENOM; CLU_076902_2_1_1; -.
DR   InParanoid; P62317; -.
DR   OMA; DVKEMWT; -.
DR   OrthoDB; 437526at2759; -.
DR   PhylomeDB; P62317; -.
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; 107686; 28 hits in 76 CRISPR screens.
DR   EvolutionaryTrace; P62317; -.
DR   PRO; PR:P62317; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P62317; protein.
DR   Bgee; ENSMUSG00000040824; Expressed in yolk sac and 69 other cell types or tissues.
DR   ExpressionAtlas; P62317; baseline and differential.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0034709; C:methylosome; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:GO_Central.
DR   GO; GO:0005685; C:U1 snRNP; ISS:UniProtKB.
DR   GO; GO:0005689; C:U12-type spliceosomal complex; ISO:GO_Central.
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:0005684; C:U2-type spliceosomal complex; 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; IEA:InterPro.
DR   GO; GO:1990446; F:U1 snRNP binding; ISO:GO_Central.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
DR   CDD; cd01720; Sm_D2; 1.
DR   FunFam; 2.30.30.100:FF:000069; Small nuclear ribonucleoprotein Sm D2; 1.
DR   Gene3D; 2.30.30.100; -; 1.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR047575; Sm.
DR   InterPro; IPR027248; Sm_D2.
DR   InterPro; IPR001163; Sm_dom_euk/arc.
DR   PANTHER; PTHR12777; SMALL NUCLEAR RIBONUCLEOPROTEIN SM D2; 1.
DR   Pfam; PF01423; LSM; 1.
DR   SMART; SM00651; Sm; 1.
DR   SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR   PROSITE; PS52002; SM; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Isopeptide bond; mRNA processing; mRNA splicing;
KW   Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW   Spliceosome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P62316"
FT   CHAIN           2..118
FT                   /note="Small nuclear ribonucleoprotein Sm D2"
FT                   /id="PRO_0000122208"
FT   DOMAIN          29..115
FT                   /note="Sm"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01346"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62316"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62316"
FT   MOD_RES         12
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CROSSLNK        6
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62316"
FT   CROSSLNK        8
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62316"
FT   CONFLICT        31
FT                   /note="V -> M (in Ref. 1; BAC32551)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   118 AA;  13527 MW;  D986059D82B7E045 CRC64;
     MSLLNKPKSE MTPEELQKRE EEEFNTGPLS VLTQSVKNNT QVLINCRNNK KLLGRVKAFD
     RHCNMVLENV KEMWTEVPKS GKGKKKSKPV NKDRYISKMF LRGDSVIVVL RNPLIAGK
//