LSM8_YEAST
ID LSM8_YEAST Reviewed; 109 AA.
AC P47093; D6VWJ6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm8;
GN Name=LSM8; OrderedLocusNames=YJR022W; ORFNames=J1464, YJR83.16;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-109.
RX PubMed=8619316; DOI=10.1002/yea.320111208;
RA Zagulski M., Babinska B., Gromadka R., Migdalski A., Rytka J., Sulicka J.,
RA Herbert C.J.;
RT "The sequence of 24.3 kb from chromosome X reveals five complete open
RT reading frames, all of which correspond to new genes, and a tandem
RT insertion of a Ty1 transposon.";
RL Yeast 11:1179-1186(1995).
RN [4]
RP SUBUNIT, IDENTIFICATION IN THE U4/U5/U6 TRI-SNRNP COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10449419; DOI=10.1093/emboj/18.16.4535;
RA Gottschalk A., Neubauer G., Banroques J., Mann M., Luehrmann R.,
RA Fabrizio P.;
RT "Identification by mass spectrometry and functional analysis of novel
RT proteins of the yeast [U4/U6.U5] tri-snRNP.";
RL EMBO J. 18:4535-4548(1999).
RN [5]
RP IDENTIFICATION IN THE LSM2-LSM8 COMPLEX, ASSOCIATION OF THE LSM2-LSM8
RP COMPLEX WITH U6 SNRNA, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10747033; DOI=10.1093/emboj/19.7.1661;
RA Bouveret E., Rigaut G., Shevchenko A., Wilm M., Seraphin B.;
RT "A Sm-like protein complex that participates in mRNA degradation.";
RL EMBO J. 19:1661-1671(2000).
RN [6]
RP FUNCTION IN PROCESSING OF PRE-TRNAS.
RX PubMed=12077351; DOI=10.1128/mcb.22.14.5248-5256.2002;
RA Kufel J., Allmang C., Verdone L., Beggs J.D., Tollervey D.;
RT "Lsm proteins are required for normal processing of pre-tRNAs and their
RT efficient association with La-homologous protein Lhp1p.";
RL Mol. Cell. Biol. 22:5248-5256(2002).
RN [7]
RP FUNCTION IN PROCESSING OF PRE-RRNAS.
RX PubMed=12438310; DOI=10.1074/jbc.m208856200;
RA Kufel J., Allmang C., Petfalski E., Beggs J.D., Tollervey D.;
RT "Lsm Proteins are required for normal processing and stability of ribosomal
RT RNAs.";
RL J. Biol. Chem. 278:2147-2156(2003).
RN [8]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [11]
RP FUNCTION OF THE LSM2-LSM8 COMPLEX IN NUCLEAR MRNA DEGRADATION.
RX PubMed=15485930; DOI=10.1128/mcb.24.21.9646-9657.2004;
RA Kufel J., Bousquet-Antonelli C., Beggs J.D., Tollervey D.;
RT "Nuclear pre-mRNA decapping and 5' degradation in yeast require the Lsm2-8p
RT complex.";
RL Mol. Cell. Biol. 24:9646-9657(2004).
RN [12]
RP SUBUNIT, IDENTIFICATION IN THE U4/U5/U6 TRI-SNRNP COMPLEX, AND ELECTRON
RP MICROSCOPY.
RX PubMed=18953335; DOI=10.1038/nsmb.1506;
RA Hacker I., Sander B., Golas M.M., Wolf E., Karagoz E., Kastner B.,
RA Stark H., Fabrizio P., Luhrmann R.;
RT "Localization of Prp8, Brr2, Snu114 and U4/U6 proteins in the yeast tri-
RT snRNP by electron microscopy.";
RL Nat. Struct. Mol. Biol. 15:1206-1212(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-96 OF LSM2-LSM8 COMPLEX,
RP SUBUNIT, FUNCTION, RNA-BINDING, AND MUTAGENESIS OF ARG-57.
RX PubMed=24240276; DOI=10.1038/nature12803;
RA Zhou L., Hang J., Zhou Y., Wan R., Lu G., Yin P., Yan C., Shi Y.;
RT "Crystal structures of the Lsm complex bound to the 3' end sequence of U6
RT small nuclear RNA.";
RL Nature 506:116-120(2014).
CC -!- FUNCTION: Component of the nuclear LSM2-LSM8 complex, which is involved
CC in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP
CC complexes containing the U6 snRNA (U4/U6 snRNP, spliceosomal U4/U6.U5
CC snRNP, and free U6 snRNP). It binds directly to the U6 snRNA and plays
CC a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP
CC complexes. It probably also is involved in degradation of nuclear pre-
CC mRNA by targeting them for decapping. LSM2-LSM8 probably is involved in
CC processing of pre-tRNAs, pre-rRNAs and U3 snoRNA. LSM2 is required for
CC processing of pre-tRNAs, pre-rRNAs and U3 snoRNA.
CC {ECO:0000269|PubMed:12077351, ECO:0000269|PubMed:12438310,
CC ECO:0000269|PubMed:15485930, ECO:0000269|PubMed:24240276}.
CC -!- SUBUNIT: Component of the heptameric LSM2-LSM8 complex that forms a
CC seven-membered ring structure with a doughnut shape; an RNA strand can
CC pass through the hole in the center of the ring structure. The LSm
CC subunits are arranged in the order LSM8, LSM2, LSM3, LSM6, LSM5, LSM7
CC and LSM4. LSM2-LSM8 associates with PAT1 and XRN1. Component of the
CC U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at
CC least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66,
CC SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4,
CC LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1. {ECO:0000269|PubMed:10449419,
CC ECO:0000269|PubMed:10747033, ECO:0000269|PubMed:18953335,
CC ECO:0000269|PubMed:24240276}.
CC -!- INTERACTION:
CC P47093; Q99181: HSH49; NbExp=3; IntAct=EBI-313, EBI-8579;
CC P47093; P38203: LSM2; NbExp=10; IntAct=EBI-313, EBI-180;
CC P47093; P40070: LSM4; NbExp=3; IntAct=EBI-313, EBI-188;
CC P47093; Q06406: LSM6; NbExp=4; IntAct=EBI-313, EBI-196;
CC P47093; P49960: PRP24; NbExp=3; IntAct=EBI-313, EBI-212;
CC P47093; P20053: PRP4; NbExp=3; IntAct=EBI-313, EBI-219;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1440 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA60945.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA89547.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X87611; CAA60945.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z49522; CAA89547.1; ALT_INIT; Genomic_DNA.
DR EMBL; X87297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006943; DAA08812.1; -; Genomic_DNA.
DR PIR; S55211; S55211.
DR RefSeq; NP_012556.2; NM_001181680.1.
DR PDB; 3JCM; EM; 3.80 A; b=1-109.
DR PDB; 4M77; X-ray; 3.11 A; A/H=1-109.
DR PDB; 4M78; X-ray; 2.79 A; A/H=1-96.
DR PDB; 4M7A; X-ray; 2.78 A; A/H=1-96.
DR PDB; 4M7D; X-ray; 2.60 A; A/H=1-96.
DR PDB; 5GAN; EM; 3.60 A; 8=1-109.
DR PDB; 5NRL; EM; 7.20 A; 8=1-109.
DR PDB; 5VSU; X-ray; 3.10 A; H=1-109.
DR PDB; 5ZWM; EM; 3.40 A; z=1-109.
DR PDB; 5ZWO; EM; 3.90 A; z=1-109.
DR PDB; 6ASO; X-ray; 2.71 A; H=1-109.
DR PDBsum; 3JCM; -.
DR PDBsum; 4M77; -.
DR PDBsum; 4M78; -.
DR PDBsum; 4M7A; -.
DR PDBsum; 4M7D; -.
DR PDBsum; 5GAN; -.
DR PDBsum; 5NRL; -.
DR PDBsum; 5VSU; -.
DR PDBsum; 5ZWM; -.
DR PDBsum; 5ZWO; -.
DR PDBsum; 6ASO; -.
DR AlphaFoldDB; P47093; -.
DR SMR; P47093; -.
DR BioGRID; 33776; 472.
DR ComplexPortal; CPX-24; U6 small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-25; U4/U6.U5 tri-small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-32; U4/U6 small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-44; LSM2-8 complex.
DR DIP; DIP-903N; -.
DR IntAct; P47093; 77.
DR MINT; P47093; -.
DR STRING; 4932.YJR022W; -.
DR MaxQB; P47093; -.
DR PaxDb; P47093; -.
DR PRIDE; P47093; -.
DR EnsemblFungi; YJR022W_mRNA; YJR022W; YJR022W.
DR GeneID; 853479; -.
DR KEGG; sce:YJR022W; -.
DR SGD; S000003783; LSM8.
DR VEuPathDB; FungiDB:YJR022W; -.
DR eggNOG; KOG1784; Eukaryota.
DR HOGENOM; CLU_076902_8_1_1; -.
DR InParanoid; P47093; -.
DR BioCyc; YEAST:G3O-31662-MON; -.
DR ChiTaRS; LSM8; yeast.
DR PRO; PR:P47093; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47093; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0071001; C:U4/U6 snRNP; IC:ComplexPortal.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:SGD.
DR GO; GO:0005688; C:U6 snRNP; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR GO; GO:0016070; P:RNA metabolic process; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IMP:ComplexPortal.
DR GO; GO:0008033; P:tRNA processing; IMP:ComplexPortal.
DR CDD; cd01727; LSm8; 1.
DR DisProt; DP01401; -.
DR InterPro; IPR034103; Lsm8.
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 3D-structure; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Ribonucleoprotein; RNA-binding; rRNA processing;
KW Spliceosome; tRNA processing.
FT CHAIN 1..109
FT /note="U6 snRNA-associated Sm-like protein LSm8"
FT /id="PRO_0000203088"
FT MUTAGEN 57
FT /note="R->A: Reduces affinity for poly-U RNA ends."
FT /evidence="ECO:0000269|PubMed:24240276"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:4M7D"
FT STRAND 11..17
FT /evidence="ECO:0007829|PDB:4M7D"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:5VSU"
FT STRAND 22..30
FT /evidence="ECO:0007829|PDB:4M7D"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:4M7D"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:4M7D"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:4M7D"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:4M7D"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:4M7D"
FT HELIX 97..106
FT /evidence="ECO:0007829|PDB:6ASO"
SQ SEQUENCE 109 AA; 12385 MW; B6E37F585B6292EA CRC64;
MSATLKDYLN KRVVIIKVDG ECLIASLNGF DKNTNLFITN VFNRISKEFI CKAQLLRGSE
IALVGLIDAE NDDSLAPIDE KKVPMLKDTK NKIENEHVIW EKVYESKTK
