ID   RSMN_BOVIN              Reviewed;         240 AA.
AC   Q17QN3; A6QL65;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Small nuclear ribonucleoprotein-associated protein N;
DE            Short=snRNP-N;
DE   AltName: Full=Sm protein N;
DE            Short=Sm-N;
DE            Short=SmN;
GN   Name=SNRPN;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Basal ganglia, and Fetal pons;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in tissue-specific alternative RNA processing
CC       events. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with TDRD3. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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; BC118260; AAI18261.1; -; mRNA.
DR   EMBL; BC147854; AAI47855.1; -; mRNA.
DR   RefSeq; NP_001073265.1; NM_001079797.1.
DR   AlphaFoldDB; Q17QN3; -.
DR   SMR; Q17QN3; -.
DR   STRING; 9913.ENSBTAP00000010856; -.
DR   PaxDb; Q17QN3; -.
DR   PRIDE; Q17QN3; -.
DR   Ensembl; ENSBTAT00000010856; ENSBTAP00000010856; ENSBTAG00000008251.
DR   GeneID; 780877; -.
DR   KEGG; bta:780877; -.
DR   CTD; 6638; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008251; -.
DR   VGNC; VGNC:35082; SNRPN.
DR   eggNOG; KOG3168; Eukaryota.
DR   GeneTree; ENSGT00940000158222; -.
DR   HOGENOM; CLU_076902_1_0_1; -.
DR   InParanoid; Q17QN3; -.
DR   OMA; FAPQRPG; -.
DR   OrthoDB; 1630470at2759; -.
DR   TreeFam; TF314232; -.
DR   Proteomes; UP000009136; Chromosome 21.
DR   Bgee; ENSBTAG00000008251; Expressed in hypothalamus and 109 other tissues.
DR   ExpressionAtlas; Q17QN3; 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; IEA:Ensembl.
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   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   2: Evidence at transcript 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_0000249873"
FT   REPEAT          175..181
FT   REPEAT          191..196
FT   REPEAT          216..221
FT   REPEAT          222..228
FT   REPEAT          230..236
FT   REGION          165..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          175..236
FT                   /note="Repeat-rich region"
FT   COMPBIAS        179..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:0000250|UniProtKB:P63163"
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:0000250|UniProtKB:P63162"
SQ   SEQUENCE   240 AA;  24622 MW;  817B1A02EFCBF748 CRC64;
     MTVGKSSKML QHIDYRMRCI LQDGRIFIGT FKAFDKHMNL ILCDCDEFRK IKPKNAKQPE
     REEKRVLGLV LLRGENLVSM TVEGPPPKDT GIARVPLAGA AGGPGVGRAA GRGVPAGVPI
     PQAPAGLAGP VRGVGGPSQQ VMTPQGRGTV AAAAVAATAS IAGAPTQYPP GRGTAPTPVG
     RATPPPGIMA PPPGMRPPMG PPIGLPPTRG TPIGMPPPGM RPPPPGIRGP PPPGMRPPRP