LSM4_CAEEL
ID LSM4_CAEEL Reviewed; 123 AA.
AC Q19952;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Probable U6 snRNA-associated Sm-like protein LSm4;
GN Name=lsm-4; ORFNames=F32A5.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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). LSM2, LSM3,
CC LSM4, LSM5, LSM6, LSM7 and LSM8 form a heptameric, ring-shaped
CC subcomplex (the LSM2-8 complex) that is part of the U4/U6-U5 tri-snRNP
CC complex and the precatalytic spliceosome.
CC {ECO:0000250|UniProtKB:Q9Y4Z0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y4Z0}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {ECO:0000305}.
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DR EMBL; FO080735; CCD66279.1; -; Genomic_DNA.
DR PIR; T16234; T16234.
DR RefSeq; NP_495514.1; NM_063113.4.
DR AlphaFoldDB; Q19952; -.
DR SMR; Q19952; -.
DR BioGRID; 39529; 14.
DR IntAct; Q19952; 1.
DR STRING; 6239.F32A5.7; -.
DR EPD; Q19952; -.
DR PaxDb; Q19952; -.
DR PeptideAtlas; Q19952; -.
DR EnsemblMetazoa; F32A5.7.1; F32A5.7.1; WBGene00003078.
DR GeneID; 174193; -.
DR KEGG; cel:CELE_F32A5.7; -.
DR UCSC; F32A5.7; c. elegans.
DR CTD; 3772280; -.
DR WormBase; F32A5.7; CE01277; WBGene00003078; lsm-4.
DR eggNOG; KOG3293; Eukaryota.
DR GeneTree; ENSGT00610000086173; -.
DR HOGENOM; CLU_099537_2_2_1; -.
DR InParanoid; Q19952; -.
DR OMA; RAEMNKN; -.
DR OrthoDB; 1561576at2759; -.
DR PhylomeDB; Q19952; -.
DR Reactome; R-CEL-430039; mRNA decay by 5' to 3' exoribonuclease.
DR Reactome; R-CEL-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q19952; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00003078; Expressed in embryo and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
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: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 3: Inferred from homology;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1..123
FT /note="Probable U6 snRNA-associated Sm-like protein LSm4"
FT /id="PRO_0000125566"
FT REGION 85..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 123 AA; 13593 MW; B3EB874B67705109 CRC64;
MVLPLSLLKT AQNHPMLVEL KNGETYNGHL KACDSWMNIH LVDVIFTSKD GDKFFKMSEA
YVRGSTIKYL RIPETVVDLV KTEVNEVRRQ QQREQSRGRG GGRGGRGGHR GGGGNRGGRG
GAR
