ID LSM10_MOUSE Reviewed; 122 AA. AC Q8QZX5; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 24-JAN-2024, entry version 137. DE RecName: Full=U7 snRNA-associated Sm-like protein LSm10; GN Name=Lsm10; 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 [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon, and 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 [2] RP RNA-BINDING. RX PubMed=19470752; DOI=10.1128/mcb.00296-09; RA Yang X.-C., Torres M.P., Marzluff W.F., Dominski Z.; RT "Three proteins of the U7-specific Sm ring function as the molecular ruler RT to determine the site of 3'-end processing in mammalian histone pre-mRNA."; RL Mol. Cell. Biol. 29:4045-4056(2009). CC -!- FUNCTION: Appears to function in the U7 snRNP complex that is involved CC in histone 3'-end processing (By similarity). Increases U7 snRNA levels CC but not histone 3'-end pre-mRNA processing activity, when overexpressed CC (By similarity). Required for cell cycle progression from G1 to S CC phases (By similarity). Binds specifically to U7 snRNA (By similarity). CC Binds to the downstream cleavage product (DCP) of histone pre-mRNA. CC {ECO:0000250}. CC -!- SUBUNIT: Component of the heptameric ring U7 snRNP complex, or U7 Sm CC protein core complex, at least composed of LSM10, LSM11, SNRPB, SNRPD3, CC SNRPE, SNRPF, SNRPG and U7 snRNA. Formation of the U7 snRNP is an ATP- CC dependent process mediated by a specialized SMN complex containing at CC least the Sm protein core complex and additionally, the U7-specific CC LSM10 and LSM11 proteins. Interacts with CLNS1A and SMN (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- PTM: Not methylated. Methylation is not necessary for interaction with CC SMN (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC024543; AAH24543.1; -; mRNA. DR EMBL; BC026476; AAH26476.1; -; mRNA. DR CCDS; CCDS18642.1; -. DR RefSeq; NP_001156738.1; NM_001163266.1. DR RefSeq; NP_620046.1; NM_138721.2. DR RefSeq; XP_006502749.1; XM_006502686.2. DR RefSeq; XP_006502750.1; XM_006502687.2. DR AlphaFoldDB; Q8QZX5; -. DR SMR; Q8QZX5; -. DR STRING; 10090.ENSMUSP00000061913; -. DR iPTMnet; Q8QZX5; -. DR PhosphoSitePlus; Q8QZX5; -. DR EPD; Q8QZX5; -. DR MaxQB; Q8QZX5; -. DR PaxDb; 10090-ENSMUSP00000061913; -. DR ProteomicsDB; 290178; -. DR Pumba; Q8QZX5; -. DR Antibodypedia; 17475; 95 antibodies from 17 providers. DR DNASU; 116748; -. DR Ensembl; ENSMUST00000055575.8; ENSMUSP00000061913.8; ENSMUSG00000050188.9. DR Ensembl; ENSMUST00000179323.2; ENSMUSP00000136585.2; ENSMUSG00000050188.9. DR GeneID; 116748; -. DR KEGG; mmu:116748; -. DR UCSC; uc008usk.2; mouse. DR AGR; MGI:2151045; -. DR CTD; 84967; -. DR MGI; MGI:2151045; Lsm10. DR VEuPathDB; HostDB:ENSMUSG00000050188; -. DR eggNOG; KOG3428; Eukaryota. DR GeneTree; ENSGT00510000048364; -. DR InParanoid; Q8QZX5; -. DR OMA; IADGHMT; -. DR OrthoDB; 74520at2759; -. DR PhylomeDB; Q8QZX5; -. DR TreeFam; TF332356; -. DR Reactome; R-MMU-111367; SLBP independent Processing of Histone Pre-mRNAs. DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination. DR Reactome; R-MMU-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs. DR BioGRID-ORCS; 116748; 30 hits in 80 CRISPR screens. DR PRO; PR:Q8QZX5; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; Q8QZX5; Protein. DR Bgee; ENSMUSG00000050188; Expressed in interventricular septum and 223 other cell types or tissues. DR ExpressionAtlas; Q8QZX5; baseline and differential. DR GO; GO:0015030; C:Cajal body; ISS:UniProtKB. DR GO; GO:0071254; C:cytoplasmic U snRNP body; IBA:GO_Central. DR GO; GO:0016604; C:nuclear body; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005683; C:U7 snRNP; ISS:UniProtKB. DR GO; GO:0071208; F:histone pre-mRNA DCP binding; IDA:UniProtKB. DR GO; GO:0017069; F:snRNA binding; ISO:MGI. DR GO; GO:0071209; F:U7 snRNA binding; ISO:MGI. DR GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; IBA:GO_Central. DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR CDD; cd01733; LSm10; 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 PANTHER; PTHR21196; U7 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM10; 1. DR PANTHER; PTHR21196:SF1; U7 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM10; 1. DR Pfam; PF01423; LSM; 1. DR SMART; SM00651; Sm; 1. DR SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1. DR PROSITE; PS52002; SM; 1. DR Genevisible; Q8QZX5; MM. PE 1: Evidence at protein level; KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; KW Ribonucleoprotein; RNA-binding. FT CHAIN 1..122 FT /note="U7 snRNA-associated Sm-like protein LSm10" FT /id="PRO_0000125586" FT DOMAIN 16..88 FT /note="Sm" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01346" SQ SEQUENCE 122 AA; 13881 MW; B4614D960896B828 CRC64; MALSHSVKER TISENSLIIL LQGLQGQITT VDLRDESVAR GRIDNVDAFM NIRLANVTYT DRWGHQVELD DLFVTGRNVR YVHIPDGVDI TATIEQQLQI IHRVRNFGGK GQGRREFPSK RP //