ID SMD3_HUMAN Reviewed; 126 AA. AC P62318; B4DJP7; B5BU13; P43331; DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 04-NOV-2026, entry version 200. DE RecName: Full=Small nuclear ribonucleoprotein Sm D3; DE Short=Sm-D3; DE AltName: Full=snRNP core protein D3; GN Name=SNRPD3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE. RX PubMed=7527560; DOI=10.1073/pnas.91.25.12317; RA Lehmeier T., Raker V., Hermann H., Luehrmann R.; RT "cDNA cloning of the Sm proteins D2 and D3 from human small nuclear RT ribonucleoproteins: evidence for a direct D1-D2 interaction."; RL Proc. Natl. Acad. Sci. U.S.A. 91:12317-12321(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Thalamus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=19054851; DOI=10.1038/nmeth.1273; RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., RA Nomura N.; RT "Human protein factory for converting the transcriptome into an in vitro- RT expressed proteome."; RL Nat. Methods 5:1011-1017(2008). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; 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 [8] RP INTERACTION WITH SMN1. RX PubMed=10500148; DOI=10.1073/pnas.96.20.11167; RA Pellizzoni L., Charroux B., Dreyfuss G.; RT "SMN mutants of spinal muscular atrophy patients are defective in binding RT to snRNP proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 96:11167-11172(1999). RN [9] RP METHYLATION. RX PubMed=11747828; DOI=10.1016/s0960-9822(01)00592-9; RA Meister G., Eggert C., Buehler D., Brahms H., Kambach C., Fischer U.; RT "Methylation of Sm proteins by a complex containing PRMT5 and the putative RT U snRNP assembly factor pICln."; RL Curr. Biol. 11:1990-1994(2001). RN [10] RP INTERACTION WITH SMN1. RX PubMed=11135666; DOI=10.1038/83014; RA Selenko P., Sprangers R., Stier G., Buhler D., Fischer U., Sattler M.; RT "SMN tudor domain structure and its interaction with the Sm proteins."; RL Nat. Struct. Biol. 8:27-31(2001). RN [11] RP IDENTIFICATION IN THE U7 SNRNP COMPLEX, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=11574479; DOI=10.1093/emboj/20.19.5470; RA Pillai R.S., Will C.L., Luehrmann R., Schuemperli D., Mueller B.; RT "Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new RT 14 kDa Sm D1-like protein."; RL EMBO J. 20:5470-5479(2001). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C RP COMPLEX, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=11991638; DOI=10.1017/s1355838202021088; RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.; RT "Purification and characterization of native spliceosomes suitable for RT three-dimensional structural analysis."; RL RNA 8:426-439(2002). RN [13] RP INTERACTION WITH SMN1. RX PubMed=12628254; DOI=10.1016/s0022-2836(03)00148-7; RA Sprangers R., Groves M.R., Sinning I., Sattler M.; RT "High-resolution X-ray and NMR structures of the SMN Tudor domain: RT conformational variation in the binding site for symmetrically dimethylated RT arginine residues."; RL J. Mol. Biol. 327:507-520(2003). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [15] RP IDENTIFICATION IN A COMPLEX WITH THE MINOR SPLICEOSOME, IDENTIFICATION BY RP MASS SPECTROMETRY, AND SUBUNIT. RX PubMed=15146077; DOI=10.1261/rna.7320604; RA Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S., RA Tuschl T., Luehrmann R.; RT "The human 18S U11/U12 snRNP contains a set of novel proteins not found in RT the U2-dependent spliceosome."; RL RNA 10:929-941(2004). RN [16] RP IDENTIFICATION IN THE SMN-SM COMPLEX. RX PubMed=16314521; DOI=10.1128/mcb.25.24.10989-11004.2005; RA Golembe T.J., Yong J., Dreyfuss G.; RT "Specific sequence features, recognized by the SMN complex, identify snRNAs RT and determine their fate as snRNPs."; RL Mol. Cell. Biol. 25:10989-11004(2005). RN [17] RP METHYLATION, AND INTERACTION WITH PRMT5 AND PRMT7. RX PubMed=17709427; DOI=10.1083/jcb.200702147; RA Gonsalvez G.B., Tian L., Ospina J.K., Boisvert F.-M., Lamond A.I., RA Matera A.G.; RT "Two distinct arginine methyltransferases are required for biogenesis of RT Sm-class ribonucleoproteins."; RL J. Cell Biol. 178:733-740(2007). RN [18] RP FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN 6S PICLN-SM COMPLEX, RP IDENTIFICATION IN SMN-SM COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=18984161; DOI=10.1016/j.cell.2008.09.020; RA Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., RA Englbrecht C., Sickmann A., Stark H., Fischer U.; RT "An assembly chaperone collaborates with the SMN complex to generate RT spliceosomal SnRNPs."; RL Cell 135:497-509(2008). RN [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [22] RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH SNRPB. RX PubMed=10025403; DOI=10.1016/s0092-8674(00)80550-4; RA Kambach C., Walke S., Young R., Avis J.M., de la Fortelle E., Raker V.A., RA Luehrmann R., Li J., Nagai K.; RT "Crystal structures of two Sm protein complexes and their implications for RT the assembly of the spliceosomal snRNPs."; RL Cell 96:375-387(1999). RN [23] RP X-RAY CRYSTALLOGRAPHY IN SPLICEOSOMAL U1 SNRNP, FUNCTION, AND SUBUNIT. RX PubMed=19325628; DOI=10.1038/nature07851; RA Pomeranz Krummel D.A., Oubridge C., Leung A.K., Li J., Nagai K.; RT "Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution."; RL Nature 458:475-480(2009). RN [24] RP X-RAY CRYSTALLOGRAPHY IN SPLICEOSOMAL CORE U4 SNRNP, AND SUBUNIT. RX PubMed=21516107; DOI=10.1038/nature09956; RA Leung A.K., Nagai K., Li J.; RT "Structure of the spliceosomal U4 snRNP core domain and its implication for RT snRNP biogenesis."; RL Nature 473:536-539(2011). RN [25] {ECO:0007744|PDB:4PJO} RP X-RAY CRYSTALLOGRAPHY, AND SUBUNIT. RX PubMed=25555158; DOI=10.7554/elife.04986; RA Kondo Y., Oubridge C., van Roon A.M., Nagai K.; RT "Crystal structure of human U1 snRNP, a small nuclear ribonucleoprotein RT particle, reveals the mechanism of 5' splice site recognition."; RL Elife 4:0-0(2015). RN [26] {ECO:0007744|PDB:3JCR} RP STRUCTURE BY ELECTRON MICROSCOPY, SUBCELLULAR LOCATION, SUBUNIT, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=26912367; DOI=10.1126/science.aad2085; RA Agafonov D.E., Kastner B., Dybkov O., Hofele R.V., Liu W.T., Urlaub H., RA Luhrmann R., Stark H.; RT "Molecular architecture of the human U4/U6.U5 tri-snRNP."; RL Science 351:1416-1420(2016). RN [27] {ECO:0007744|PDB:5XJC} RP STRUCTURE BY ELECTRON MICROSCOPY, FUNCTION, SUBCELLULAR LOCATION, AND RP SUBUNIT. RX PubMed=28502770; DOI=10.1016/j.cell.2017.04.033; RA Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.; RT "An Atomic Structure of the Human Spliceosome."; RL Cell 169:918-929(2017). RN [28] {ECO:0007744|PDB:5O9Z} RP STRUCTURE BY ELECTRON MICROSCOPY, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, RP AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=28781166; DOI=10.1016/j.cell.2017.07.011; RA Bertram K., Agafonov D.E., Dybkov O., Haselbach D., Leelaram M.N., RA Will C.L., Urlaub H., Kastner B., Luhrmann R., Stark H.; RT "Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for RT Activation."; RL Cell 170:701-713(2017). RN [29] {ECO:0007744|PDB:5MQF} RP STRUCTURE BY ELECTRON MICROSCOPY, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, RP AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=28076346; DOI=10.1038/nature21079; RA Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., Hartmuth K., RA Urlaub H., Kastner B., Stark H., Luhrmann R.; RT "Cryo-EM structure of a human spliceosome activated for step 2 of RT splicing."; RL Nature 542:318-323(2017). RN [30] {ECO:0007744|PDB:6Y5Q} RP STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH THE 17S U2 SNRNP COMPLEX, RP FUNCTION, AND IDENTIFICATION IN THE 17S U2 SNRNP COMPLEX. RX PubMed=32494006; DOI=10.1038/s41586-020-2344-3; RA Zhang Z., Will C.L., Bertram K., Dybkov O., Hartmuth K., Agafonov D.E., RA Hofele R., Urlaub H., Kastner B., Luehrmann R., Stark H.; RT "Molecular architecture of the human 17S U2 snRNP."; RL Nature 583:310-313(2020). RN [31] {ECO:0007744|PDB:7DVQ} RP STRUCTURE BY ELECTRON MICROSCOPY, FUNCTION, AND SUBUNIT. RX PubMed=33509932; DOI=10.1126/science.abg0879; RA Bai R., Wan R., Wang L., Xu K., Zhang Q., Lei J., Shi Y.; RT "Structure of the activated human minor spliceosome."; RL Science 371:0-0(2021). RN [32] {ECO:0007744|PDB:8HK1} RP STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH THE 17S U2 SNRNP COMPLEX, RP AND IDENTIFICATION IN THE 17S U2 SNRNP COMPLEX. RX PubMed=36797247; DOI=10.1038/s41467-023-36489-x; RA Yang F., Bian T., Zhan X., Chen Z., Xing Z., Larsen N.A., Zhang X., Shi Y.; RT "Mechanisms of the RNA helicases DDX42 and DDX46 in human U2 snRNP RT assembly."; RL Nat. Commun. 14:897-897(2023). 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 (PubMed:11991638, CC PubMed:18984161, PubMed:19325628, PubMed:25555158, PubMed:26912367, CC PubMed:28076346, PubMed:28502770, PubMed:28781166, PubMed:32494006). CC Component of both the pre-catalytic spliceosome B complex and activated CC spliceosome C complexes (PubMed:11991638, PubMed:28076346, CC PubMed:28502770, PubMed:28781166). As a component of the minor CC spliceosome, involved in the splicing of U12-type introns in pre-mRNAs CC (PubMed:15146077, PubMed:33509932). As part of the U7 snRNP it is CC involved in histone pre-mRNA 3'-end processing (By similarity). CC {ECO:0000250|UniProtKB:P62320, ECO:0000269|PubMed:11991638, CC ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:18984161, CC ECO:0000269|PubMed:19325628, ECO:0000269|PubMed:25555158, CC ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28076346, CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166, CC ECO:0000269|PubMed:32494006, ECO:0000269|PubMed:33509932}. CC -!- SUBUNIT: Core component of the spliceosomal U1, U2, U4 and U5 small CC nuclear ribonucleoproteins (snRNPs), the building blocks of the CC spliceosome (PubMed:10025403, PubMed:11991638, PubMed:19325628, CC PubMed:21516107, PubMed:25555158, PubMed:26912367, PubMed:28076346, CC PubMed:28502770, PubMed:28781166, PubMed:32494006, PubMed:36797247). CC Most spliceosomal snRNPs contain a common set of Sm proteins, SNRPB, CC SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a CC heptameric protein ring on the Sm site of the small nuclear RNA to form CC the core snRNP (PubMed:10025403, PubMed:19325628, PubMed:21516107, CC PubMed:25555158, PubMed:26912367, PubMed:28076346, PubMed:28502770, CC PubMed:28781166). Component of the U1 snRNP (PubMed:19325628, CC PubMed:25555158). The U1 snRNP is composed of the U1 snRNA and the 7 CC core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG, CC and at least three U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1- CC A and SNRPC/U1-C (PubMed:19325628, PubMed:25555158). Component of the CC U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at CC least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, CC SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, CC PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, CC LSM6, LSM7 and LSM8 (PubMed:26912367). Component of the U7 snRNP CC complex, or U7 Sm protein core complex, that is composed of the U7 CC snRNA and at least LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF and SNRPG; CC the complex does not contain SNRPD1 and SNRPD2 (PubMed:11574479). CC Component of the minor spliceosome, which splices U12-type introns CC (PubMed:15146077, PubMed:33509932). 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 CC (PubMed:16314521). Forms a 6S pICln-Sm complex composed of CC CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like CC structure where CLNS1A/pICln mimics additional Sm proteins and which is CC unable to assemble into the core snRNP. Interacts (via C-terminus) with CC SMN1 (via Tudor domain); the interaction is direct (PubMed:10500148, CC PubMed:11135666, PubMed:12628254). {ECO:0000269|PubMed:10025403, CC ECO:0000269|PubMed:10500148, ECO:0000269|PubMed:11135666, CC ECO:0000269|PubMed:11574479, ECO:0000269|PubMed:11991638, CC ECO:0000269|PubMed:12628254, ECO:0000269|PubMed:15146077, CC ECO:0000269|PubMed:16314521, ECO:0000269|PubMed:18984161, CC ECO:0000269|PubMed:19325628, ECO:0000269|PubMed:21516107, CC ECO:0000269|PubMed:25555158, ECO:0000269|PubMed:26912367, CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, CC ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:32494006, CC ECO:0000269|PubMed:33509932, ECO:0000269|PubMed:36797247}. CC -!- INTERACTION: CC P62318; P54253: ATXN1; NbExp=3; IntAct=EBI-372789, EBI-930964; CC P62318; P54105: CLNS1A; NbExp=11; IntAct=EBI-372789, EBI-724693; CC P62318; P84090: ERH; NbExp=3; IntAct=EBI-372789, EBI-711389; CC P62318; P62310: LSM3; NbExp=5; IntAct=EBI-372789, EBI-348239; CC P62318; Q9UK45: LSM7; NbExp=3; IntAct=EBI-372789, EBI-348372; CC P62318; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-372789, EBI-741158; CC P62318; Q15428: SF3A2; NbExp=2; IntAct=EBI-372789, EBI-2462271; CC P62318; P14678: SNRPB; NbExp=8; IntAct=EBI-372789, EBI-372458; CC P62318; P08579: SNRPB2; NbExp=3; IntAct=EBI-372789, EBI-1053651; CC P62318; Q96SB4: SRPK1; NbExp=2; IntAct=EBI-372789, EBI-539478; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18984161}. CC Nucleus {ECO:0000269|PubMed:11574479, ECO:0000269|PubMed:11991638, CC ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28076346, CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166}. Note=SMN- CC mediated assembly into core snRNPs occurs in the cytosol before SMN- CC mediated transport to the nucleus to be included in spliceosomes. CC {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P62318-1; Sequence=Displayed; CC Name=2; CC IsoId=P62318-2; Sequence=VSP_056478; 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:0000269|PubMed:11747828, ECO:0000269|PubMed:17709427}. CC -!- MISCELLANEOUS: In the autoimmune disease systemic lupus erythematosus, CC antinuclear antibodies are developed with Sm specificity. CC -!- SIMILARITY: Belongs to the snRNP core protein family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U15009; AAA57034.1; -; mRNA. DR EMBL; CR456583; CAG30469.1; -; mRNA. DR EMBL; AK296173; BAG58909.1; -; mRNA. DR EMBL; AB451249; BAG70063.1; -; mRNA. DR EMBL; AB451373; BAG70187.1; -; mRNA. DR EMBL; AP000356; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471095; EAW59670.1; -; Genomic_DNA. DR EMBL; BC000457; AAH00457.1; -; mRNA. DR EMBL; BC003150; AAH03150.1; -; mRNA. DR CCDS; CCDS13828.1; -. [P62318-1] DR RefSeq; NP_001265585.1; NM_001278656.2. [P62318-1] DR RefSeq; NP_004166.1; NM_004175.5. [P62318-1] DR PDB; 1D3B; X-ray; 2.00 A; A/C/E/G/I/K=1-75. DR PDB; 3CW1; X-ray; 5.49 A; D/S/T/U=1-126. DR PDB; 3JCR; EM; 7.00 A; R/r=1-126. DR PDB; 3PGW; X-ray; 4.40 A; W/Z=1-126. DR PDB; 3VRI; X-ray; 1.60 A; C=54-63. DR PDB; 4PJO; X-ray; 3.30 A; A/O/a/o=1-126. DR PDB; 4WZJ; X-ray; 3.60 A; A/AA/AAA/AAAA/H/HH/HHH/HHHH/O/OO/OOO/OOOO=1-125. DR PDB; 5MQF; EM; 5.90 A; e/l=1-126. DR PDB; 5O9Z; EM; 4.50 A; W/e/l=1-126. DR PDB; 5XJC; EM; 3.60 A; a/h=1-126. DR PDB; 5YZG; EM; 4.10 A; a/h=1-126. DR PDB; 5Z56; EM; 5.10 A; a/h=1-126. DR PDB; 5Z57; EM; 6.50 A; a/h=1-126. DR PDB; 5Z58; EM; 4.90 A; a/h=1-126. DR PDB; 6AH0; EM; 5.70 A; T/e/h=1-126. DR PDB; 6AHD; EM; 3.80 A; T/g/h=1-126. DR PDB; 6FF7; EM; 4.50 A; e/l=1-126. DR PDB; 6ICZ; EM; 3.00 A; a/h=1-126. DR PDB; 6ID0; EM; 2.90 A; a/h=1-126. DR PDB; 6ID1; EM; 2.86 A; a/h=1-126. DR PDB; 6QDV; EM; 3.30 A; d/n=2-85. DR PDB; 6QW6; EM; 2.92 A; 43/53=1-126. DR PDB; 6QX9; EM; 3.28 A; 13/23/43/53=1-126. DR PDB; 6V4X; EM; 3.20 A; A=1-126. DR PDB; 6Y53; EM; 7.10 A; l=1-126. DR PDB; 6Y5Q; EM; 7.10 A; l=1-126. DR PDB; 7A5P; EM; 5.00 A; a/l=1-126. DR PDB; 7ABG; EM; 7.80 A; e/l=1-126. DR PDB; 7ABI; EM; 8.00 A; e/l=1-126. DR PDB; 7B0Y; EM; 3.60 A; i=1-126. DR PDB; 7DVQ; EM; 2.89 A; a/h=1-126. DR PDB; 7EVO; EM; 2.50 A; e=1-126. DR PDB; 7QTT; EM; 3.10 A; j=1-126. DR PDB; 7VPX; EM; 3.00 A; e/j=1-126. DR PDB; 7W59; EM; 3.60 A; a/h=1-126. DR PDB; 7W5A; EM; 3.60 A; a/h=1-126. DR PDB; 7W5B; EM; 4.30 A; a/h=1-126. DR PDB; 8C6J; EM; 2.80 A; d/n=1-126. DR PDB; 8CH6; EM; 5.90 A; 3/j=1-126. DR PDB; 8H6E; EM; 3.20 A; 2g/4g/5g=1-126. DR PDB; 8H6J; EM; 3.25 A; 2g/4g/5g=1-126. DR PDB; 8H6K; EM; 2.70 A; 2g/4g/5g=1-126. DR PDB; 8H6L; EM; 2.60 A; 2g/4g/5g=1-126. DR PDB; 8HK1; EM; 2.70 A; e=1-126. DR PDB; 8I0P; EM; 3.40 A; g/l=1-126. DR PDB; 8I0R; EM; 3.00 A; g/l=1-126. DR PDB; 8I0S; EM; 4.20 A; g/l=1-126. DR PDB; 8I0T; EM; 3.00 A; g/l=1-126. DR PDB; 8I0U; EM; 3.30 A; g/l=1-126. DR PDB; 8I0V; EM; 3.00 A; g/l=1-126. DR PDB; 8I0W; EM; 3.40 A; g/h=1-126. DR PDB; 8Q7Q; EM; 3.20 A; d=1-126. DR PDB; 8Q7V; EM; 3.80 A; d=1-126. DR PDB; 8Q7W; EM; 3.90 A; d=1-126. DR PDB; 8Q7X; EM; 4.60 A; d=1-126. DR PDB; 8Q91; EM; 3.10 A; k=1-126. DR PDB; 8QO9; EM; 5.29 A; 23/43/53=1-126. DR PDB; 8QXD; EM; 9.60 A; 23/43/53=1-126. DR PDB; 8QZS; EM; 4.10 A; 23/43/53=1-126. DR PDB; 8R08; EM; 6.10 A; 13/23/43/53=1-126. DR PDB; 8R09; EM; 4.30 A; 23/43/53=1-126. DR PDB; 8R0A; EM; 5.80 A; 23/43/53=1-126. DR PDB; 8R0B; EM; 4.40 A; 23/43/53=1-126. DR PDB; 8R7N; EM; 3.40 A; j=1-126. DR PDB; 8RC0; EM; 3.20 A; k=1-126. DR PDB; 8RM5; EM; 6.90 A; 23/43/53=1-126. DR PDB; 8RO2; EM; 3.50 A; a=1-126. DR PDB; 8Y6O; EM; 3.38 A; d/k/r=1-126. DR PDB; 8Y7E; EM; 4.66 A; h=1-126. DR PDB; 9FMD; EM; 3.30 A; a/h=1-126. DR PDB; 9GBW; EM; 3.50 A; j=1-126. DR PDB; 9GC0; EM; 3.20 A; j=1-126. DR PDB; 9GCL; EM; 3.00 A; j=1-126. DR PDB; 9N96; EM; 3.18 A; A=1-126. DR PDB; 9NB1; EM; 3.85 A; A=1-126. DR PDB; 9NH5; EM; 2.82 A; A=1-126. DR PDB; 9NH6; EM; 2.82 A; A=1-126. DR PDB; 9QEQ; EM; 3.50 A; i=1-126. DR PDB; 9R8V; EM; 8.50 A; 23/53=1-126. DR AlphaFoldDB; P62318; -. DR EMDB; EMD-10689; -. DR EMDB; EMD-11695; -. DR EMDB; EMD-11697; -. DR EMDB; EMD-11972; -. DR EMDB; EMD-14146; -. DR EMDB; EMD-16452; -. DR EMDB; EMD-16658; -. DR EMDB; EMD-18229; -. DR EMDB; EMD-18234; -. DR EMDB; EMD-18235; -. DR EMDB; EMD-18237; -. DR EMDB; EMD-18267; -. DR EMDB; EMD-18529; -. DR EMDB; EMD-18718; -. DR EMDB; EMD-18781; -. DR EMDB; EMD-18786; -. DR EMDB; EMD-18787; -. DR EMDB; EMD-18788; -. DR EMDB; EMD-18789; -. DR EMDB; EMD-18984; -. DR EMDB; EMD-19041; -. DR EMDB; EMD-19349; -. DR EMDB; EMD-19399; -. DR EMDB; EMD-21050; -. DR EMDB; EMD-30875; -. DR EMDB; EMD-31334; -. DR EMDB; EMD-32074; -. DR EMDB; EMD-32317; -. DR EMDB; EMD-32319; -. DR EMDB; EMD-32321; -. DR EMDB; EMD-34500; -. DR EMDB; EMD-34505; -. DR EMDB; EMD-34507; -. DR EMDB; EMD-34508; -. DR EMDB; EMD-34841; -. DR EMDB; EMD-35105; -. DR EMDB; EMD-35107; -. DR EMDB; EMD-35108; -. DR EMDB; EMD-35109; -. DR EMDB; EMD-35110; -. DR EMDB; EMD-35111; -. DR EMDB; EMD-35113; -. DR EMDB; EMD-3545; -. DR EMDB; EMD-3766; -. DR EMDB; EMD-38993; -. DR EMDB; EMD-39013; -. DR EMDB; EMD-4525; -. DR EMDB; EMD-4658; -. DR EMDB; EMD-4665; -. DR EMDB; EMD-49161; -. DR EMDB; EMD-49206; -. DR EMDB; EMD-49402; -. DR EMDB; EMD-49403; -. DR EMDB; EMD-51223; -. DR EMDB; EMD-51226; -. DR EMDB; EMD-51233; -. DR EMDB; EMD-53087; -. DR EMDB; EMD-53843; -. DR EMDB; EMD-6721; -. DR EMDB; EMD-6864; -. DR EMDB; EMD-6889; -. DR EMDB; EMD-6890; -. DR EMDB; EMD-6891; -. DR EMDB; EMD-9621; -. DR EMDB; EMD-9624; -. DR EMDB; EMD-9645; -. DR EMDB; EMD-9646; -. DR EMDB; EMD-9647; -. DR SMR; P62318; -. DR BioGRID; 112518; 495. DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-2392; U1 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-2539; U2 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-26417; U4 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-26421; U5 small nuclear ribonucleoprotein complete complex. DR ComplexPortal; CPX-26429; Major Spliceosomal Pre-B complex. DR ComplexPortal; CPX-26435; Major Spliceosomal B complex. DR ComplexPortal; CPX-26441; Major Spliceosomal Pre-B-act complex. DR ComplexPortal; CPX-26448; Major Spliceosomal B-act-I complex. DR ComplexPortal; CPX-26450; Major Spliceosomal B-act-II complex. DR ComplexPortal; CPX-26451; Major Spliceosomal B-act-III complex. DR ComplexPortal; CPX-26454; Major Spliceosomal B-act-IV complex. DR ComplexPortal; CPX-26458; Major Spliceosomal Post-B-act complex. DR ComplexPortal; CPX-26463; Major Spliceosomal C complex. DR ComplexPortal; CPX-26465; Major Spliceosomal Pre-C*-I complex. DR ComplexPortal; CPX-26467; Major Spliceosomal Pre-C*-II complex. DR ComplexPortal; CPX-26472; Major Spliceosomal C* complex. DR ComplexPortal; CPX-26479; Major Post-catalytic P Spliceosome complex. DR ComplexPortal; CPX-26480; Intron Lariat Spliceosome, type 1 complex. DR ComplexPortal; CPX-26481; Intron Lariat Spliceosome, type 2 complex. DR ComplexPortal; CPX-26485; U11 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-26487; U12 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-26489; U11/U12 di-small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-26495; U4atac small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-26502; U4atac/U6atac.U5 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-26506; Minor Spliceosomal Pre-B complex. DR ComplexPortal; CPX-26509; Minor Spliceosomal B-act complex. DR ComplexPortal; CPX-26552; U5 small nuclear ribonucleoprotein complex, AAR2 variant. DR ComplexPortal; CPX-2705; U7 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-6033; Sm complex. DR CORUM; P62318; -. DR DIP; DIP-31216N; -. DR FunCoup; P62318; 2961. DR IntAct; P62318; 187. DR NDEx; IQUERY-CP-SNRPD3; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000215829; -. DR BindingDB; P62318; -. DR ChEMBL; CHEMBL5725034; -. DR CarbonylDB; P62318; -. DR GlyGen; P62318; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P62318; -. DR MetOSite; P62318; -. DR PhosphoSitePlus; P62318; -. DR SwissPalm; P62318; -. DR BioMuta; SNRPD3; -. DR DMDM; 51338667; -. DR jPOST; P62318; -. DR MassIVE; P62318; -. DR PaxDb; 9606-ENSP00000215829; -. DR PeptideAtlas; P62318; -. DR ProteomicsDB; 4397; -. DR ProteomicsDB; 57393; -. [P62318-1] DR Pumba; P62318; -. DR TopDownProteomics; P62318-1; -. [P62318-1] DR ABCD; P62318; 7 sequenced antibodies. DR Antibodypedia; 216; 269 antibodies from 36 providers. DR DNASU; 6634; -. DR Ensembl; ENST00000215829.8; ENSP00000215829.3; ENSG00000100028.13. [P62318-1] DR Ensembl; ENST00000402849.5; ENSP00000385266.1; ENSG00000100028.13. [P62318-2] DR Ensembl; ENST00000404603.5; ENSP00000456090.1; ENSG00000286070.2. [P62318-1] DR Ensembl; ENST00000652248.1; ENSP00000499210.1; ENSG00000286070.2. [P62318-1] DR Ensembl; ENST00000865614.1; ENSP00000535673.1; ENSG00000100028.13. [P62318-1] DR Ensembl; ENST00000865615.1; ENSP00000535674.1; ENSG00000100028.13. [P62318-1] DR Ensembl; ENST00000865616.1; ENSP00000535675.1; ENSG00000100028.13. [P62318-1] DR Ensembl; ENST00000865617.1; ENSP00000535676.1; ENSG00000100028.13. [P62318-1] DR Ensembl; ENST00000865618.1; ENSP00000535677.1; ENSG00000100028.13. [P62318-1] DR Ensembl; ENST00000940750.1; ENSP00000610809.1; ENSG00000100028.13. [P62318-1] DR Ensembl; ENST00000940752.1; ENSP00000610811.1; ENSG00000100028.13. [P62318-1] DR Ensembl; ENST00000972066.1; ENSP00000642125.1; ENSG00000100028.13. [P62318-1] DR GeneID; 6634; -. DR KEGG; hsa:6634; -. DR MANE-Select; ENST00000215829.8; ENSP00000215829.3; NM_004175.5; NP_004166.1. DR UCSC; uc003aam.3; human. [P62318-1] DR AGR; HGNC:11160; -. DR ClinPGx; PA36001; -. DR CTD; 6634; -. DR DisGeNET; 6634; -. DR GeneCards; SNRPD3; -. DR HGNC; HGNC:11160; SNRPD3. DR HPA; ENSG00000100028; Low tissue specificity. DR MIM; 601062; gene. DR OpenTargets; ENSG00000100028; -. DR VEuPathDB; HostDB:ENSG00000100028; -. DR eggNOG; KOG3172; Eukaryota. DR GeneTree; ENSGT00610000086153; -. DR HOGENOM; CLU_099537_1_0_1; -. DR InParanoid; P62318; -. DR OMA; AGRGKXA; -. DR OrthoDB; 6425924at2759; -. DR PAN-GO; P62318; 11 GO annotations based on evolutionary models. DR PhylomeDB; P62318; -. DR PathwayCommons; P62318; -. DR Reactome; R-HSA-111367; SLBP independent Processing of Histone Pre-mRNAs. DR Reactome; R-HSA-191859; snRNP Assembly. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway. DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination. DR Reactome; R-HSA-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs. DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery. DR Reactome; R-HSA-9770562; mRNA Polyadenylation. DR Reactome; R-HSA-9918481; Dengue Virus-Host Interactions. DR Reactome; R-HSA-9943411; CHD1 and CHD2 subfamily. DR SignaLink; P62318; -. DR SIGNOR; P62318; -. DR Agora; ENSG00000100028; -. DR BioGRID-ORCS; 6634; 834 hits in 1135 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; B5B9A610; PML body. DR ChiTaRS; SNRPD3; human. DR EvolutionaryTrace; P62318; -. DR GeneWiki; SNRPD3; -. DR GenomeRNAi; 6634; -. DR Pharos; P62318; Tbio. DR PRO; PR:P62318; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; P62318; protein. DR Bgee; ENSG00000100028; Expressed in ganglionic eminence and 114 other cell types or tissues. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0000243; C:commitment complex; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0034709; C:methylosome; IDA:UniProtKB. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0034715; C:pICln-Sm protein complex; IDA:UniProtKB. DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IPI:ComplexPortal. DR GO; GO:0071020; C:post-spliceosomal complex; IPI:ComplexPortal. DR GO; GO:0071011; C:precatalytic spliceosome; IPI:ComplexPortal. DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; TAS:ProtInc. DR GO; GO:0034719; C:SMN-Sm protein complex; IDA:UniProtKB. DR GO; GO:0005681; C:spliceosomal complex; IPI:ComplexPortal. DR GO; GO:0097526; C:spliceosomal tri-snRNP complex; IBA:GO_Central. DR GO; GO:0005697; C:telomerase holoenzyme complex; IDA:BHF-UCL. DR GO; GO:0005685; C:U1 snRNP; IDA:UniProtKB. DR GO; GO:0034693; C:U11/U12 snRNP; IPI:ComplexPortal. DR GO; GO:0071018; C:U12-type catalytic step 2 spliceosome; IPI:ComplexPortal. DR GO; GO:0071016; C:U12-type precatalytic spliceosome; IPI:ComplexPortal. DR GO; GO:0005689; C:U12-type spliceosomal complex; IDA:UniProtKB. DR GO; GO:0005686; C:U2 snRNP; IBA:GO_Central. DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IPI:ComplexPortal. DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB. DR GO; GO:0005684; C:U2-type spliceosomal complex; IDA:UniProtKB. DR GO; GO:0005687; C:U4 snRNP; IDA:UniProtKB. DR GO; GO:0071001; C:U4/U6 snRNP; NAS:ComplexPortal. DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:UniProtKB. DR GO; GO:0005690; C:U4atac snRNP; NAS:ComplexPortal. DR GO; GO:0071002; C:U4atac/U6atac snRNP; NAS:ComplexPortal. DR GO; GO:0071009; C:U4atac/U6atac x U5 tri-snRNP complex; NAS:ComplexPortal. DR GO; GO:0005682; C:U5 snRNP; IBA:GO_Central. DR GO; GO:0005683; C:U7 snRNP; IDA:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0071208; F:histone pre-mRNA DCP binding; ISS:UniProtKB. DR GO; GO:0003723; F:RNA binding; IPI:BHF-UCL. DR GO; GO:0070034; F:telomerase RNA binding; IPI:BHF-UCL. DR GO; GO:0071209; F:U7 snRNA binding; IPI:BHF-UCL. DR GO; GO:0036261; P:7-methylguanosine cap hypermethylation; NAS:ComplexPortal. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; NAS:ComplexPortal. DR GO; GO:0071045; P:nuclear histone mRNA catabolic process; NAS:ComplexPortal. DR GO; GO:0006479; P:protein methylation; IDA:MGI. DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc. DR GO; GO:0000245; P:spliceosomal complex assembly; NAS:ComplexPortal. DR GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB. DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; NAS:ComplexPortal. DR GO; GO:0000388; P:spliceosome conformational change to release U4 (or U4atac) and U1 (or U11); NAS:ComplexPortal. DR GO; GO:1903241; P:U2-type prespliceosome assembly; NAS:ComplexPortal. DR CDD; cd01721; Sm_D3; 1. DR DisProt; DP01704; -. DR FunFam; 2.30.30.100:FF:000002; Small nuclear ribonucleoprotein Sm D3; 1. DR Gene3D; 2.30.30.100; -; 1. DR IDEAL; IID00161; -. DR InterPro; IPR027141; LSm4/Sm_D1/D3. DR InterPro; IPR010920; LSM_dom_sf. DR InterPro; IPR047575; Sm. DR InterPro; IPR001163; Sm_dom_euk/arc. DR InterPro; IPR034099; SmD3. DR PANTHER; PTHR23338; SMALL NUCLEAR RIBONUCLEOPROTEIN SM; 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 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Direct protein sequencing; Methylation; mRNA processing; mRNA splicing; KW Nucleus; Proteomics identification; Reference proteome; Repeat; KW Ribonucleoprotein; RNA-binding; Spliceosome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..126 FT /note="Small nuclear ribonucleoprotein Sm D3" FT /id="PRO_0000122214" FT DOMAIN 5..77 FT /note="Sm" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01346" 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; required for FT interaction with SMN1" FT /evidence="ECO:0000269|PubMed:12628254" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:19413330" FT VAR_SEQ 107..126 FT /note="VAARGRGRGMGRGNIFQKRR -> GYLSSLEWVLVHIC (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056478" FT HELIX 6..12 FT /evidence="ECO:0007829|PDB:1D3B" FT TURN 13..15 FT /evidence="ECO:0007829|PDB:1D3B" FT STRAND 16..22 FT /evidence="ECO:0007829|PDB:1D3B" FT STRAND 23..25 FT /evidence="ECO:0007829|PDB:9N96" FT STRAND 27..35 FT /evidence="ECO:0007829|PDB:1D3B" FT STRAND 37..39 FT /evidence="ECO:0007829|PDB:8Q91" FT STRAND 41..49 FT /evidence="ECO:0007829|PDB:1D3B" FT TURN 50..53 FT /evidence="ECO:0007829|PDB:8C6J" FT STRAND 55..63 FT /evidence="ECO:0007829|PDB:1D3B" FT HELIX 65..67 FT /evidence="ECO:0007829|PDB:1D3B" FT STRAND 68..73 FT /evidence="ECO:0007829|PDB:1D3B" FT STRAND 77..81 FT /evidence="ECO:0007829|PDB:7EVO" SQ SEQUENCE 126 AA; 13916 MW; 59A6E78E860AA3E0 CRC64; MSIGVPIKVL HEAEGHIVTC ETNTGEVYRG KLIEAEDNMN CQMSNITVTY RDGRVAQLEQ VYIRGSKIRF LILPDMLKNA PMLKSMKNKN QGSGAGRGKA AILKAQVAAR GRGRGMGRGN IFQKRR //