ID   LSM1_BOVIN              Reviewed;         133 AA.
AC   Q5E9Z8;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm1;
GN   Name=LSM1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
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   -!- 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}.
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DR   EMBL; BT020738; AAX08755.1; -; mRNA.
DR   EMBL; BT020771; AAX08788.1; -; mRNA.
DR   EMBL; BT020779; AAX08796.1; -; mRNA.
DR   RefSeq; NP_001017952.1; NM_001017952.1.
DR   AlphaFoldDB; Q5E9Z8; -.
DR   SMR; Q5E9Z8; -.
DR   STRING; 9913.ENSBTAP00000002113; -.
DR   PaxDb; Q5E9Z8; -.
DR   PRIDE; Q5E9Z8; -.
DR   Ensembl; ENSBTAT00000002113; ENSBTAP00000002113; ENSBTAG00000001612.
DR   GeneID; 535447; -.
DR   KEGG; bta:535447; -.
DR   CTD; 27257; -.
DR   VEuPathDB; HostDB:ENSBTAG00000001612; -.
DR   VGNC; VGNC:31050; LSM1.
DR   eggNOG; KOG1782; Eukaryota.
DR   GeneTree; ENSGT00730000111133; -.
DR   HOGENOM; CLU_076902_0_1_1; -.
DR   InParanoid; Q5E9Z8; -.
DR   OMA; FMVRGEN; -.
DR   OrthoDB; 1508864at2759; -.
DR   TreeFam; TF105846; -.
DR   Proteomes; UP000009136; Chromosome 27.
DR   Bgee; ENSBTAG00000001612; Expressed in oocyte and 107 other tissues.
DR   ExpressionAtlas; Q5E9Z8; baseline.
DR   GO; GO:1990726; C:Lsm1-7-Pat1 complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0000932; C:P-body; IBA:GO_Central.
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; IEA:Ensembl.
DR   GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
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; IEA:Ensembl.
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   2: Evidence at transcript 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_0000245167"
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;  15193 MW;  FF798D6A9447037A CRC64;
     MNYMPGTASL IEDIDKKHLV LLRDGRTLIG FLRSIDQFAN LVLHQTVERI HVGKKYGDIP
     RGIFVVRGEN VVLLGEIDLE KESDTPLQQV SIEEILEEQR VEQQTKLEAE KLKVQALKDR
     GLSIPRADTL EEY