LSM4_MOUSE
ID LSM4_MOUSE Reviewed; 137 AA.
AC Q9QXA5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm4;
GN Name=Lsm4;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10629062; DOI=10.1128/mcb.20.3.1055-1062.2000;
RA Hirsch E., Oohashi T., Ahmad M., Stamm S., Faessler R.;
RT "Peri-implantation lethality in mice lacking the Sm motif-containing
RT protein Lsm4.";
RL Mol. Cell. Biol. 20:1055-1062(2000).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, 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: Plays role in pre-mRNA splicing as component of the U4/U6-U5
CC tri-snRNP complex that is involved in spliceosome assembly, and as
CC component of the precatalytic spliceosome (spliceosome B complex). The
CC heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract
CC of U6 snRNA. {ECO:0000250|UniProtKB:Q9Y4Z0}.
CC -!- SUBUNIT: Component of the precatalytic spliceosome (spliceosome B
CC complex). Component of the U4/U6-U5 tri-snRNP complex, a building block
CC of the precatalytic spliceosome (spliceosome B complex). The U4/U6-U5
CC tri-snRNP complex is composed of the U4, U6 and U5 snRNAs and at least
CC PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB,
CC SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH,
CC SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7
CC and LSM8. LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8 form a
CC heptameric, ring-shaped subcomplex (the LSM2-8 complex) that is part of
CC the U4/U6-U5 tri-snRNP complex and the precatalytic spliceosome.
CC {ECO:0000250|UniProtKB:Q9Y4Z0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10629062}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10629062}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {ECO:0000305}.
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DR EMBL; AJ249439; CAB65729.1; -; mRNA.
DR RefSeq; NP_056631.2; NM_015816.4.
DR AlphaFoldDB; Q9QXA5; -.
DR SMR; Q9QXA5; -.
DR BioGRID; 206115; 8.
DR DIP; DIP-60115N; -.
DR IntAct; Q9QXA5; 1.
DR iPTMnet; Q9QXA5; -.
DR PhosphoSitePlus; Q9QXA5; -.
DR SwissPalm; Q9QXA5; -.
DR EPD; Q9QXA5; -.
DR MaxQB; Q9QXA5; -.
DR PaxDb; Q9QXA5; -.
DR PRIDE; Q9QXA5; -.
DR ProteomicsDB; 252536; -.
DR DNASU; 50783; -.
DR GeneID; 50783; -.
DR KEGG; mmu:50783; -.
DR CTD; 25804; -.
DR MGI; MGI:1354692; Lsm4.
DR eggNOG; KOG3293; Eukaryota.
DR InParanoid; Q9QXA5; -.
DR OrthoDB; 1571169at2759; -.
DR Reactome; R-MMU-430039; mRNA decay by 5' to 3' exoribonuclease.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 50783; 29 hits in 111 CRISPR screens.
DR ChiTaRS; Lsm4; mouse.
DR PRO; PR:Q9QXA5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9QXA5; protein.
DR GO; GO:0005737; C:cytoplasm; ISS:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0120115; C:Lsm2-8 complex; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISS:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005681; C:spliceosomal complex; ISS:MGI.
DR GO; GO:0097526; C:spliceosomal tri-snRNP complex; IBA:GO_Central.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISS:UniProtKB.
DR GO; GO:0005688; C:U6 snRNP; IBA:GO_Central.
DR GO; GO:0042731; F:PH domain binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0017070; F:U6 snRNA binding; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IEA:InterPro.
DR GO; GO:0033962; P:P-body assembly; IBA:GO_Central.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IBA:GO_Central.
DR CDD; cd01723; LSm4; 1.
DR InterPro; IPR034101; Lsm4.
DR InterPro; IPR027141; LSm4/Sm_D1/D3.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR PANTHER; PTHR23338; PTHR23338; 1.
DR Pfam; PF01423; LSM; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
PE 1: Evidence at protein level;
KW Acetylation; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1..137
FT /note="U6 snRNA-associated Sm-like protein LSm4"
FT /id="PRO_0000125565"
FT REGION 82..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4Z0"
SQ SEQUENCE 137 AA; 15076 MW; A917E16E61467940 CRC64;
MLPLSLLKTA QNHPMLVELK NGETYNGHLV SCDNWMNINL REVICTSRDG DKFWRMPECY
IRGSTIKYLR IPDEIIDMVR EEAAKGRGRG GPQQKQQKGR GMGGAGRGVF GGRGRGGIPG
AGRGQPEKKP GRQAGKQ
