LSM6_MOUSE
ID LSM6_MOUSE Reviewed; 80 AA.
AC P62313; Q9Y4Y8;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm6;
GN Name=Lsm6;
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=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Pancreas, Spleen, 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 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. Component of LSm protein complexes, which are involved in
CC RNA processing and may function in a chaperone-like manner,
CC facilitating the efficient association of RNA processing factors with
CC their substrates. Component of the cytoplasmic LSM1-LSM7 complex, which
CC is thought to be involved in mRNA degradation by activating the
CC decapping step in the 5'-to-3' mRNA decay pathway.
CC {ECO:0000250|UniProtKB:P62312}.
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). The U4/U6-U5
CC tri-snRNP complex is composed of the U4, U6 and U5 snRNAs and at least
CC PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB,
CC SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH,
CC SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7
CC and LSM8. LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8 form a
CC heptameric, ring-shaped subcomplex (the LSM2-8 complex) that is part of
CC the U4/U6-U5 tri-snRNP complex and the precatalytic spliceosome.
CC Component of the heptameric LSM1-LSM7 complex, which consists of LSM1,
CC LSM2, LSM3, LSM4, LSM5, LSM6 and LSM7. {ECO:0000250|UniProtKB:P62312}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62312}. Nucleus
CC {ECO:0000250|UniProtKB:P62312}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. SmF/LSm6
CC subfamily. {ECO:0000305}.
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DR EMBL; AK019126; BAB31555.1; -; mRNA.
DR EMBL; BC030427; AAH30427.1; -; mRNA.
DR CCDS; CCDS40396.1; -.
DR RefSeq; NP_001177933.1; NM_001191004.1.
DR RefSeq; NP_084421.1; NM_030145.3.
DR AlphaFoldDB; P62313; -.
DR SMR; P62313; -.
DR BioGRID; 219553; 9.
DR STRING; 10090.ENSMUSP00000049722; -.
DR iPTMnet; P62313; -.
DR PhosphoSitePlus; P62313; -.
DR SwissPalm; P62313; -.
DR EPD; P62313; -.
DR PaxDb; P62313; -.
DR PeptideAtlas; P62313; -.
DR PRIDE; P62313; -.
DR ProteomicsDB; 290179; -.
DR TopDownProteomics; P62313; -.
DR Antibodypedia; 27518; 107 antibodies from 21 providers.
DR Ensembl; ENSMUST00000051867; ENSMUSP00000049722; ENSMUSG00000031683.
DR Ensembl; ENSMUST00000130325; ENSMUSP00000119841; ENSMUSG00000031683.
DR Ensembl; ENSMUST00000146824; ENSMUSP00000148221; ENSMUSG00000031683.
DR GeneID; 78651; -.
DR KEGG; mmu:78651; -.
DR UCSC; uc009mie.2; mouse.
DR CTD; 11157; -.
DR MGI; MGI:1925901; Lsm6.
DR VEuPathDB; HostDB:ENSMUSG00000031683; -.
DR eggNOG; KOG1783; Eukaryota.
DR GeneTree; ENSGT00940000154978; -.
DR HOGENOM; CLU_076902_7_4_1; -.
DR InParanoid; P62313; -.
DR OMA; KMRRSYG; -.
DR OrthoDB; 1627235at2759; -.
DR PhylomeDB; P62313; -.
DR TreeFam; TF313751; -.
DR Reactome; R-MMU-430039; mRNA decay by 5' to 3' exoribonuclease.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 78651; 13 hits in 41 CRISPR screens.
DR ChiTaRS; Lsm6; mouse.
DR PRO; PR:P62313; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P62313; protein.
DR Bgee; ENSMUSG00000031683; Expressed in manus and 230 other tissues.
DR ExpressionAtlas; P62313; baseline and differential.
DR Genevisible; P62313; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0120115; C:Lsm2-8 complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein 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:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR GO; GO:0006402; P:mRNA catabolic process; ISO:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR016487; Lsm6/sSmF.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR PANTHER; PTHR11021; PTHR11021; 1.
DR Pfam; PF01423; LSM; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Ribonucleoprotein; RNA-binding; rRNA processing;
KW Spliceosome; tRNA processing.
FT CHAIN 1..80
FT /note="U6 snRNA-associated Sm-like protein LSm6"
FT /id="PRO_0000125576"
FT MOD_RES 59
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62312"
SQ SEQUENCE 80 AA; 9128 MW; 21167891FDE804F1 CRC64;
MSLRKQTPSD FLKQIIGRPV VVKLNSGVDY RGVLACLDGY MNIALEQTEE YVNGQLKNKY
GDAFIRGNNV LYISTQKRRM
