RSMN_MOUSE
ID RSMN_MOUSE Reviewed; 240 AA.
AC P63163; P14648; P17135;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Small nuclear ribonucleoprotein-associated protein N;
DE Short=snRNP-N;
DE AltName: Full=Sm protein D;
DE Short=Sm-D;
DE AltName: Full=Sm protein N;
DE Short=Sm-N;
DE Short=SmN;
DE AltName: Full=Tissue-specific-splicing protein;
GN Name=Snrpn; Synonyms=Smn;
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].
RX PubMed=1754402; DOI=10.1093/nar/19.23.6642;
RA Gerrelli D., Sharp N.G., Latchman D.S.;
RT "Cloning and sequencing of a mouse embryonal carcinoma cell mRNA encoding
RT the tissue specific RNA splicing protein SmN.";
RL Nucleic Acids Res. 19:6642-6642(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=8510173; DOI=10.1006/jmcc.1993.1038;
RA Gerrelli D., Grimaldi K., Horn D., Mahadeva U., Sharpe N., Latchman D.S.;
RT "The cardiac form of the tissue-specific SmN protein is identical to the
RT brain and embryonic forms of the protein.";
RL J. Mol. Cell. Cardiol. 25:321-329(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hippocampus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary tumor;
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=10318933; DOI=10.1073/pnas.96.10.5616;
RA Gray T.A., Saitoh S., Nicholls R.D.;
RT "An imprinted, mammalian bicistronic transcript encodes two independent
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:5616-5621(1999).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-108 AND ARG-172, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: May be involved in tissue-specific alternative RNA processing
CC events.
CC -!- SUBUNIT: Interacts with TDRD3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in brain and embryonic stem (ES) cells.
CC {ECO:0000269|PubMed:10318933}.
CC -!- MISCELLANEOUS: Encoded on a bicistronic transcript that code for two
CC proteins, SNRPN and SNURF.
CC -!- SIMILARITY: Belongs to the snRNP SmB/SmN family. {ECO:0000305}.
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DR EMBL; X62648; CAA44517.1; -; mRNA.
DR EMBL; X63730; CAA45273.1; -; mRNA.
DR EMBL; S62288; AAB27138.1; -; mRNA.
DR EMBL; AK013607; BAB28927.1; -; mRNA.
DR EMBL; BC019589; AAH19589.1; -; mRNA.
DR EMBL; BC024880; AAH24880.1; -; mRNA.
DR CCDS; CCDS39974.1; -.
DR PIR; S20068; S20068.
DR RefSeq; NP_001076430.1; NM_001082961.1.
DR RefSeq; NP_001076431.1; NM_001082962.1.
DR RefSeq; NP_038698.1; NM_013670.3.
DR AlphaFoldDB; P63163; -.
DR SMR; P63163; -.
DR BioGRID; 203381; 3.
DR IntAct; P63163; 1.
DR STRING; 10090.ENSMUSP00000096003; -.
DR iPTMnet; P63163; -.
DR PhosphoSitePlus; P63163; -.
DR SwissPalm; P63163; -.
DR PaxDb; P63163; -.
DR PeptideAtlas; P63163; -.
DR PRIDE; P63163; -.
DR ProteomicsDB; 256784; -.
DR Antibodypedia; 22280; 162 antibodies from 26 providers.
DR DNASU; 20646; -.
DR Ensembl; ENSMUST00000059305; ENSMUSP00000055941; ENSMUSG00000102252.
DR Ensembl; ENSMUST00000098402; ENSMUSP00000096003; ENSMUSG00000102252.
DR GeneID; 20646; -.
DR KEGG; mmu:20646; -.
DR UCSC; uc009heq.3; mouse.
DR CTD; 6638; -.
DR MGI; MGI:98347; Snrpn.
DR VEuPathDB; HostDB:ENSMUSG00000102252; -.
DR eggNOG; KOG3168; Eukaryota.
DR GeneTree; ENSGT00940000158222; -.
DR HOGENOM; CLU_076902_1_0_1; -.
DR InParanoid; P63163; -.
DR OMA; FAPQRPG; -.
DR OrthoDB; 1630470at2759; -.
DR PhylomeDB; P63163; -.
DR TreeFam; TF314232; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 20646; 3 hits in 78 CRISPR screens.
DR ChiTaRS; Snrpn; mouse.
DR PRO; PR:P63163; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P63163; protein.
DR Bgee; ENSMUSG00000102252; Expressed in dentate gyrus of hippocampal formation granule cell and 260 other tissues.
DR ExpressionAtlas; P63163; baseline and differential.
DR Genevisible; P63163; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; TAS:MGI.
DR GO; GO:0005685; C:U1 snRNP; IBA:GO_Central.
DR GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
DR GO; GO:0005687; C:U4 snRNP; IBA:GO_Central.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IBA:GO_Central.
DR GO; GO:0005682; C:U5 snRNP; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0009725; P:response to hormone; IEA:Ensembl.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR017131; snRNP-assoc_SmB/SmN.
DR Pfam; PF01423; LSM; 1.
DR PIRSF; PIRSF037187; snRNP_SmB/SmN; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
PE 1: Evidence at protein level;
KW Methylation; Nucleus; Reference proteome; Repeat; Ribonucleoprotein;
KW RNA-binding.
FT CHAIN 1..240
FT /note="Small nuclear ribonucleoprotein-associated protein
FT N"
FT /id="PRO_0000125524"
FT REPEAT 175..181
FT REPEAT 191..196
FT REPEAT 216..221
FT REPEAT 222..228
FT REPEAT 230..236
FT REGION 163..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..236
FT /note="Repeat-rich region"
FT COMPBIAS 169..240
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 108
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14678"
FT MOD_RES 108
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14678"
FT MOD_RES 108
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 112
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14678"
FT MOD_RES 112
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14678"
FT MOD_RES 112
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14678"
FT MOD_RES 147
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P14678"
FT MOD_RES 172
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 240 AA; 24614 MW; 9A176D043561474C CRC64;
MTVGKSSKML QHIDYRMRCI LQDGRIFIGT FKAFDKHMNL ILCDCDEFRK IKPKNAKQPE
REEKRVLGLV LLRGENLVSM TVEGPPPKDT GIARVPLAGA AGGPGVGRAA GRGVPAGVPI
PQAPAGLAGP VRGVGGPSQQ VMTPQGRGTV AAAAVAATAS IAGAPTQYPP GRGTPPPPVG
RATPPPGIMA PPPGMRPPMG PPIGLPPARG TPIGMPPPGM RPPPPGIRGP PPPGMRPPRP
