LSM1_MOUSE
ID LSM1_MOUSE Reviewed; 133 AA.
AC Q8VC85;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm1;
GN Name=Lsm1;
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 TISSUE=Liver;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Pancreas, 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 a role in the degradation of histone mRNAs, the only
CC eukaryotic mRNAs that are not polyadenylated (By similarity). Probably
CC also part of an LSm subunits-containing complex involved in the general
CC process of mRNA degradation (By similarity).
CC {ECO:0000250|UniProtKB:O15116, ECO:0000250|UniProtKB:P47017}.
CC -!- SUBUNIT: Interacts with SLBP; interaction with SLBP occurs when histone
CC mRNA is being rapidly degraded during the S phase (By similarity). LSm
CC subunits form a heteromer with a donut shape (By similarity).
CC {ECO:0000250|UniProtKB:O15116, ECO:0000250|UniProtKB:P47017}.
CC -!- INTERACTION:
CC Q8VC85; Q7TMF2: Eri1; NbExp=3; IntAct=EBI-16026183, EBI-16026214;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15116}.
CC Cytoplasm, P-body {ECO:0000250|UniProtKB:O15116}.
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; BC021460; AAH21460.1; -; mRNA.
DR CCDS; CCDS22202.1; -.
DR RefSeq; NP_080308.1; NM_026032.1.
DR AlphaFoldDB; Q8VC85; -.
DR SMR; Q8VC85; -.
DR BioGRID; 212017; 11.
DR DIP; DIP-60113N; -.
DR IntAct; Q8VC85; 1.
DR STRING; 10090.ENSMUSP00000041022; -.
DR iPTMnet; Q8VC85; -.
DR PhosphoSitePlus; Q8VC85; -.
DR REPRODUCTION-2DPAGE; Q8VC85; -.
DR EPD; Q8VC85; -.
DR MaxQB; Q8VC85; -.
DR PaxDb; Q8VC85; -.
DR PRIDE; Q8VC85; -.
DR ProteomicsDB; 292046; -.
DR Antibodypedia; 10914; 328 antibodies from 29 providers.
DR DNASU; 67207; -.
DR Ensembl; ENSMUST00000038421; ENSMUSP00000041022; ENSMUSG00000037296.
DR GeneID; 67207; -.
DR KEGG; mmu:67207; -.
DR UCSC; uc009lgz.1; mouse.
DR CTD; 27257; -.
DR MGI; MGI:1914457; Lsm1.
DR VEuPathDB; HostDB:ENSMUSG00000037296; -.
DR eggNOG; KOG1782; Eukaryota.
DR GeneTree; ENSGT00730000111133; -.
DR HOGENOM; CLU_076902_0_1_1; -.
DR InParanoid; Q8VC85; -.
DR OMA; FMVRGEN; -.
DR OrthoDB; 1508864at2759; -.
DR PhylomeDB; Q8VC85; -.
DR TreeFam; TF105846; -.
DR Reactome; R-MMU-430039; mRNA decay by 5' to 3' exoribonuclease.
DR BioGRID-ORCS; 67207; 8 hits in 72 CRISPR screens.
DR ChiTaRS; Lsm1; mouse.
DR PRO; PR:Q8VC85; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8VC85; protein.
DR Bgee; ENSMUSG00000037296; Expressed in renal corpuscle and 260 other tissues.
DR ExpressionAtlas; Q8VC85; baseline and differential.
DR Genevisible; Q8VC85; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:1990726; C:Lsm1-7-Pat1 complex; IBA:GO_Central.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:MGI.
DR GO; GO:0000932; C:P-body; IDA:MGI.
DR GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR GO; GO:0036002; F:pre-mRNA binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000339; F:RNA cap binding; IBA:GO_Central.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
DR GO; GO:0071044; P:histone mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0016070; P:RNA metabolic process; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
DR CDD; cd01728; LSm1; 1.
DR InterPro; IPR034104; Lsm1.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR044642; PTHR15588.
DR PANTHER; PTHR15588; PTHR15588; 1.
DR Pfam; PF01423; LSM; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; mRNA processing; mRNA splicing; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; RNA-binding.
FT CHAIN 1..133
FT /note="U6 snRNA-associated Sm-like protein LSm1"
FT /id="PRO_0000125555"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15116"
FT MOD_RES 129
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15116"
SQ SEQUENCE 133 AA; 15236 MW; 92A34D7205CE036F CRC64;
MNYMPGTASL IEDIDKKHLV LLRDGRTLIG FLRSIDQFAN LVLHQTVERI HVGKKYGDIP
RGIFVVRGEN VVLLGEIDLE KESDTPLQQV SIEEILEEQR VQQQTRLEAE KLKVQTLKDR
GLSIPRADTL DEY
