SNRPA_MOUSE
ID SNRPA_MOUSE Reviewed; 287 AA.
AC Q62189; Q52LA2;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=U1 small nuclear ribonucleoprotein A;
DE Short=U1 snRNP A;
DE Short=U1-A;
DE Short=U1A;
GN Name=Snrpa; Synonyms=Rnu1a-1;
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].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=8415008; DOI=10.1093/nar/21.18.4404;
RA Bennett M.M., Baron M.A., Craft J.;
RT "Nucleotide sequence analysis of the A protein of the U1 small nuclear
RT ribonucleoprotein particle: the murine protein contains a 5' amino-terminal
RT tag.";
RL Nucleic Acids Res. 21:4404-4404(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Pancreas, Spleen, 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: Component of the spliceosomal U1 snRNP, which is essential
CC for recognition of the pre-mRNA 5' splice-site and the subsequent
CC assembly of the spliceosome. U1 snRNP is the first snRNP to interact
CC with pre-mRNA. This interaction is required for the subsequent binding
CC of U2 snRNP and the U4/U6/U5 tri-snRNP. SNRPA binds stem loop II of U1
CC snRNA. In a snRNP-free form (SF-A) may be involved in coupled pre-mRNA
CC splicing and polyadenylation process. May bind preferentially to the
CC 5'-UGCAC-3' motif on RNAs (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: U1 snRNP is composed of the 7 core Sm proteins SNRPB, SNRPD1,
CC SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric
CC protein ring on the Sm site of the small nuclear RNA to form the core
CC snRNP, and at least three U1 snRNP-specific proteins SNRNP70/U1-70K,
CC SNRPA/U1-A and SNRPC/U1-C. Interacts with SFPQ; component of a snRNP-
CC free complex with SFPQ (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRM U1 A/B'' family. {ECO:0000305}.
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DR EMBL; L15447; AAC37611.1; -; mRNA.
DR EMBL; BC003229; AAH03229.1; -; mRNA.
DR EMBL; BC094006; AAH94006.1; -; mRNA.
DR EMBL; BC096648; AAH96648.1; -; mRNA.
DR CCDS; CCDS21014.1; -.
DR PIR; S42113; S42114.
DR RefSeq; NP_001040102.1; NM_001046637.1.
DR RefSeq; NP_001272754.1; NM_001285825.1.
DR RefSeq; NP_056597.3; NM_015782.3.
DR AlphaFoldDB; Q62189; -.
DR SMR; Q62189; -.
DR BioGRID; 207327; 18.
DR IntAct; Q62189; 2.
DR STRING; 10090.ENSMUSP00000079228; -.
DR iPTMnet; Q62189; -.
DR PhosphoSitePlus; Q62189; -.
DR EPD; Q62189; -.
DR MaxQB; Q62189; -.
DR PaxDb; Q62189; -.
DR PeptideAtlas; Q62189; -.
DR PRIDE; Q62189; -.
DR ProteomicsDB; 261394; -.
DR TopDownProteomics; Q62189; -.
DR Antibodypedia; 3308; 327 antibodies from 31 providers.
DR DNASU; 53607; -.
DR Ensembl; ENSMUST00000080356; ENSMUSP00000079228; ENSMUSG00000061479.
DR Ensembl; ENSMUST00000122202; ENSMUSP00000113678; ENSMUSG00000061479.
DR Ensembl; ENSMUST00000163311; ENSMUSP00000131897; ENSMUSG00000061479.
DR GeneID; 53607; -.
DR KEGG; mmu:53607; -.
DR UCSC; uc009fvg.1; mouse.
DR CTD; 6626; -.
DR MGI; MGI:1855690; Snrpa.
DR VEuPathDB; HostDB:ENSMUSG00000061479; -.
DR eggNOG; KOG4206; Eukaryota.
DR GeneTree; ENSGT00390000007046; -.
DR HOGENOM; CLU_041869_1_3_1; -.
DR InParanoid; Q62189; -.
DR OMA; NQTIYVN; -.
DR OrthoDB; 1608132at2759; -.
DR PhylomeDB; Q62189; -.
DR TreeFam; TF313834; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 53607; 18 hits in 74 CRISPR screens.
DR ChiTaRS; Snrpa; mouse.
DR PRO; PR:Q62189; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q62189; protein.
DR Bgee; ENSMUSG00000061479; Expressed in embryonic brain and 70 other tissues.
DR ExpressionAtlas; Q62189; baseline and differential.
DR Genevisible; Q62189; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005681; C:spliceosomal complex; ISS:HGNC-UCL.
DR GO; GO:0005685; C:U1 snRNP; ISS:UniProtKB.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0030619; F:U1 snRNA binding; ISS:UniProtKB.
DR GO; GO:1990446; F:U1 snRNP binding; ISO:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:1900363; P:regulation of mRNA polyadenylation; ISO:MGI.
DR CDD; cd12477; RRM1_U1A; 1.
DR CDD; cd12480; RRM2_U1A; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034407; U1A_RRM1.
DR InterPro; IPR034409; U1A_RRM2.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Acetylation; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1..287
FT /note="U1 small nuclear ribonucleoprotein A"
FT /id="PRO_0000081888"
FT DOMAIN 16..95
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 213..287
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 106..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09012"
FT MOD_RES 157
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P09012"
SQ SEQUENCE 287 AA; 31835 MW; EEAFEC9A793759FB CRC64;
MATIATMPVP ETRANHTIYI NNLNEKIKKD ELKKSLYAIF SQFGQILDIL VSRIMKMRGQ
AFVIFKEVTS ATNALRSMQG FPFYDKPMRI QYAKTDSDII AKMKGTYVER DRKREKRKPK
SQETPAAKKA VQGGAAAPVV GAVQPVPGMP PMPQAPRIMH HMPGQPPYMP PPGMIPPPGL
APGQIPPGAM PPQQLMPGQM PPAQPLSENP PNHILFLTNL PEETNELMLS MLFNQFPGFK
EVRLVPGRHD IAFVEFDNEV QAGAARDALQ GFKITQNNAM KISFAKK
