ID L5LS28_MYODS Unreviewed; 133 AA.
AC L5LS28;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm1 {ECO:0000256|RuleBase:RU365047};
GN Name=LSM1 {ECO:0000256|RuleBase:RU365047};
GN ORFNames=MDA_GLEAN10024929 {ECO:0000313|EMBL:ELK28857.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK28857.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- FUNCTION: Plays a role in the degradation of histone mRNAs, the only
CC eukaryotic mRNAs that are not polyadenylated. Probably also part of an
CC LSm subunits-containing complex involved in the general process of mRNA
CC degradation. {ECO:0000256|RuleBase:RU365047}.
CC -!- SUBUNIT: Interacts with SLBP; interaction with SLBP occurs when histone
CC mRNA is being rapidly degraded during the S phase. LSm subunits form a
CC heteromer with a donut shape. {ECO:0000256|RuleBase:RU365047}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU365047}.
CC Cytoplasm, P-body {ECO:0000256|RuleBase:RU365047}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family.
CC {ECO:0000256|ARBA:ARBA00006850, ECO:0000256|RuleBase:RU365047}.
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DR EMBL; KB108646; ELK28857.1; -; Genomic_DNA.
DR RefSeq; XP_006765645.1; XM_006765582.2.
DR AlphaFoldDB; L5LS28; -.
DR GeneID; 102762740; -.
DR KEGG; myd:102762740; -.
DR CTD; 27257; -.
DR eggNOG; KOG1782; Eukaryota.
DR OrthoDB; 1113423at2759; -.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0000339; F:RNA cap binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IEA:InterPro.
DR CDD; cd01728; LSm1; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR InterPro; IPR034104; Lsm1.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR044642; PTHR15588.
DR InterPro; IPR047575; Sm.
DR InterPro; IPR001163; Sm_dom_euk/arc.
DR PANTHER; PTHR15588; LSM1; 1.
DR PANTHER; PTHR15588:SF8; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM1; 1.
DR Pfam; PF01423; LSM; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR PROSITE; PS52002; SM; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|RuleBase:RU365047};
KW mRNA processing {ECO:0000256|RuleBase:RU365047};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Ribonucleoprotein {ECO:0000256|RuleBase:RU365047};
KW RNA-binding {ECO:0000256|RuleBase:RU365047}.
FT DOMAIN 5..80
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
FT COILED 93..120
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 133 AA; 15208 MW; F091D0DA9447037A CRC64;
MNYMPGTASL IEDIDKKHLV LLRDGRTLIG FLRSIDQFAN LVLHQTVERI HVGKKYGDIP
RGIFVVRGEN VVLLGEIDLE KESDTPLQQV SIEEILEEQR VEQQTKLENE KLKVQALKDR
GLSVPRADTL DEY
//
