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   27-MAR-2024, entry version 152.
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; 4.
DR   IntAct; P63163; 1.
DR   STRING; 10090.ENSMUSP00000096003; -.
DR   iPTMnet; P63163; -.
DR   PhosphoSitePlus; P63163; -.
DR   SwissPalm; P63163; -.
DR   PaxDb; 10090-ENSMUSP00000096003; -.
DR   PeptideAtlas; P63163; -.
DR   ProteomicsDB; 256784; -.
DR   Pumba; P63163; -.
DR   Antibodypedia; 22280; 179 antibodies from 26 providers.
DR   DNASU; 20646; -.
DR   Ensembl; ENSMUST00000059305.17; ENSMUSP00000055941.11; ENSMUSG00000102252.6.
DR   Ensembl; ENSMUST00000098402.5; ENSMUSP00000096003.4; ENSMUSG00000102252.6.
DR   GeneID; 20646; -.
DR   KEGG; mmu:20646; -.
DR   UCSC; uc009heq.3; mouse.
DR   AGR; MGI:98347; -.
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; MGTTKMV; -.
DR   OrthoDB; 5475294at2759; -.
DR   PhylomeDB; P63163; -.
DR   TreeFam; TF314232; -.
DR   Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR   BioGRID-ORCS; 20646; 3 hits in 83 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 263 other cell types or tissues.
DR   ExpressionAtlas; P63163; baseline and differential.
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; ISO:MGI.
DR   GO; GO:0005686; C:U2 snRNP; ISO:MGI.
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   CDD; cd01717; Sm_B; 1.
DR   Gene3D; 2.30.30.100; -; 1.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR047575; Sm.
DR   InterPro; IPR001163; Sm_dom_euk/arc.
DR   InterPro; IPR017131; snRNP-assoc_SmB/SmN.
DR   PANTHER; PTHR10701:SF0; SMALL NUCLEAR RIBONUCLEOPROTEIN-ASSOCIATED PROTEIN B; 1.
DR   PANTHER; PTHR10701; SMALL NUCLEAR RIBONUCLEOPROTEIN-ASSOCIATED PROTEIN B AND N; 1.
DR   Pfam; PF01423; LSM; 1.
DR   PIRSF; PIRSF037187; snRNP_SmB/SmN; 1.
DR   SMART; SM00651; Sm; 1.
DR   SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR   PROSITE; PS52002; SM; 1.
DR   Genevisible; P63163; MM.
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   DOMAIN          4..86
FT                   /note="Sm"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01346"
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
//