LSM7_YEAST
ID LSM7_YEAST Reviewed; 115 AA.
AC P53905; D6W135;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm7;
GN Name=LSM7; OrderedLocusNames=YNL147W; ORFNames=N1202, N1780;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8619318; DOI=10.1002/yea.320111210;
RA Mallet L., Bussereau F., Jacquet M.;
RT "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2,
RT CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine
RT deaminase gene and 14 new open reading frames.";
RL Yeast 11:1195-1209(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8686380;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<169::aid-yea894>3.0.co;2-b;
RA Nasr F., Becam A.-M., Herbert C.J.;
RT "The sequence of 36.8 kb from the left arm of chromosome XIV reveals 24
RT complete open reading frames: 18 correspond to new genes, one of which
RT encodes a protein similar to the human myotonic dystrophy kinase.";
RL Yeast 12:169-175(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
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 [5]
RP IDENTIFICATION IN THE LSM2-LSM8 COMPLEX, AND ASSOCIATION WITH PRE-P RNA.
RX PubMed=10369684; DOI=10.1093/emboj/18.12.3451;
RA Salgado-Garrido J., Bragado-Nilsson E., Kandels-Lewis S., Seraphin B.;
RT "Sm and Sm-like proteins assemble in two related complexes of deep
RT evolutionary origin.";
RL EMBO J. 18:3451-3462(1999).
RN [6]
RP CHARACTERIZATION.
RX PubMed=10428970; DOI=10.1093/emboj/18.15.4321;
RA Mayes A.E., Verdone L., Legrain P., Beggs J.D.;
RT "Characterization of Sm-like proteins in yeast and their association with
RT U6 snRNA.";
RL EMBO J. 18:4321-4331(1999).
RN [7]
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 [8]
RP IDENTIFICATION IN THE LSM1-LSM7 COMPLEX, ASSOCIATION OF THE LSM1-LSM7
RP COMPLEX WITH PAT1 AND XRN1, FUNCTION OF THE LSM1-LSM7 COMPLEX,
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 [9]
RP FUNCTION OF THE LSM1-LSM7 COMPLEX.
RX PubMed=10761922; DOI=10.1038/35006676;
RA Tharun S., He W., Mayes A.E., Lennertz P., Beggs J.D., Parker R.;
RT "Yeast Sm-like proteins function in mRNA decapping and decay.";
RL Nature 404:515-518(2000).
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 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 [12]
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 [13]
RP IDENTIFICATION OF INTRON.
RX PubMed=17101987; DOI=10.1073/pnas.0605645103;
RA Miura F., Kawaguchi N., Sese J., Toyoda A., Hattori M., Morishita S.,
RA Ito T.;
RT "A large-scale full-length cDNA analysis to explore the budding yeast
RT transcriptome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:17846-17851(2006).
RN [14]
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 [15]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF LSM1-LSM7 COMPLEX, SUBUNIT, AND
RP INTERACTION WITH PAT1.
RX PubMed=24139796; DOI=10.1016/j.celrep.2013.10.004;
RA Sharif H., Conti E.;
RT "Architecture of the Lsm1-7-Pat1 complex: a conserved assembly in
RT eukaryotic mRNA turnover.";
RL Cell Rep. 5:283-291(2013).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF LSM1-LSM7 COMPLEX, SUBUNIT,
RP FUNCTION, RNA-BINDING, AND MUTAGENESIS OF ARG-95.
RX PubMed=24513854; DOI=10.1038/cr.2014.18;
RA Zhou L., Zhou Y., Hang J., Wan R., Lu G., Yan C., Shi Y.;
RT "Crystal structure and biochemical analysis of the heptameric Lsm1-7
RT complex.";
RL Cell Res. 24:497-500(2014).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF LSM2-LSM8 COMPLEX, SUBUNIT,
RP FUNCTION, RNA-BINDING, AND MUTAGENESIS OF ARG-95.
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 LSm protein complexes, which are involved in RNA
CC processing and may function in a chaperone-like manner. Component of
CC the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation
CC by activating the decapping step. Component of the nuclear LSM2-LSM8
CC complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8
CC associates with multiple snRNP complexes containing the U6 snRNA (U4/U6
CC snRNP, spliceosomal U4/U6.U5 snRNP, and free U6 snRNP). It binds
CC directly to the U6 snRNA and plays a role in the biogenesis and
CC stability of the U6 snRNP and U4/U6 snRNP complexes. It probably also
CC is involved in degradation of nuclear pre-mRNA by targeting them for
CC decapping. LSM7 binds specifically to the 3'-terminal U-tract of U6
CC snRNA. LSM2-LSM8 probably is involved in processing of pre-tRNAs, pre-
CC rRNAs and U3 snoRNA. LSM7, probably in a complex that contains LSM2-
CC LSM7 but not LSM1 or LSM8, associates with the precursor of the RNA
CC component of RNase P (pre-P RNA) and may be involved in maturing pre-P
CC RNA. {ECO:0000269|PubMed:10747033, ECO:0000269|PubMed:10761922,
CC ECO:0000269|PubMed:15485930, ECO:0000269|PubMed:24240276,
CC ECO:0000269|PubMed:24513854}.
CC -!- SUBUNIT: Component of the heptameric LSM1-LSM7 complex that forms a
CC seven-membered ring structure with a doughnut shape. The LSm subunits
CC are arranged in the order LSM1, LSM2, LSM3, LSM6, LSM5, LSM7 and LSM4.
CC Except for LSM1, where a C-terminal helix crosses the ring structure to
CC form additional interactions with LSM3 and LSM6, each subunit interacts
CC only with its two neighboring subunits. The LSM1-LSM7 complex interacts
CC with PAT1; within the complex PAT1 has direct interactions with LSM2
CC and LSM3. 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. A complex comprising
CC LSM2-LSM7 without LSM1 or LSM8 may exist. Component of the spliceosome
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:10369684,
CC ECO:0000269|PubMed:10449419, ECO:0000269|PubMed:10747033,
CC ECO:0000269|PubMed:24139796, ECO:0000269|PubMed:24240276,
CC ECO:0000269|PubMed:24513854}.
CC -!- INTERACTION:
CC P53905; P38203: LSM2; NbExp=6; IntAct=EBI-141, EBI-180;
CC P53905; P25644: PAT1; NbExp=3; IntAct=EBI-141, EBI-204;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3070 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=CAA86879.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA96030.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z46843; CAA86879.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z71423; CAA96030.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006947; DAA10401.1; -; Genomic_DNA.
DR PIR; S55137; S55137.
DR RefSeq; NP_014252.2; NM_001182985.1.
DR PDB; 3JCM; EM; 3.80 A; g=1-115.
DR PDB; 4C8Q; X-ray; 3.70 A; G=1-115.
DR PDB; 4C92; X-ray; 2.30 A; G=1-115.
DR PDB; 4M75; X-ray; 2.95 A; F/M=1-115.
DR PDB; 4M77; X-ray; 3.11 A; F/M=1-115.
DR PDB; 4M78; X-ray; 2.79 A; F/M=1-115.
DR PDB; 4M7A; X-ray; 2.78 A; F/M=1-115.
DR PDB; 4M7D; X-ray; 2.60 A; F/M=1-115.
DR PDB; 5GAN; EM; 3.60 A; 7=1-115.
DR PDB; 5NRL; EM; 7.20 A; 7=1-115.
DR PDB; 5VSU; X-ray; 3.10 A; G=1-115.
DR PDB; 5ZWM; EM; 3.40 A; y=1-115.
DR PDB; 5ZWO; EM; 3.90 A; y=1-115.
DR PDB; 6ASO; X-ray; 2.71 A; G=1-115.
DR PDBsum; 3JCM; -.
DR PDBsum; 4C8Q; -.
DR PDBsum; 4C92; -.
DR PDBsum; 4M75; -.
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; P53905; -.
DR SMR; P53905; -.
DR BioGRID; 35681; 787.
DR ComplexPortal; CPX-112; LSM1-7-PAT1 complex.
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 ComplexPortal; CPX-45; LSM1-7 complex.
DR ComplexPortal; CPX-46; LSM2-7 complex.
DR DIP; DIP-1419N; -.
DR IntAct; P53905; 26.
DR MINT; P53905; -.
DR STRING; 4932.YNL147W; -.
DR MaxQB; P53905; -.
DR PaxDb; P53905; -.
DR PRIDE; P53905; -.
DR EnsemblFungi; YNL147W_mRNA; YNL147W; YNL147W.
DR GeneID; 855575; -.
DR KEGG; sce:YNL147W; -.
DR SGD; S000005091; LSM7.
DR VEuPathDB; FungiDB:YNL147W; -.
DR eggNOG; KOG1781; Eukaryota.
DR GeneTree; ENSGT00510000047872; -.
DR HOGENOM; CLU_076902_3_2_1; -.
DR InParanoid; P53905; -.
DR OMA; ICPADGM; -.
DR BioCyc; YEAST:G3O-33165-MON; -.
DR Reactome; R-SCE-430039; mRNA decay by 5' to 3' exoribonuclease.
DR PRO; PR:P53905; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53905; protein.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:1990726; C:Lsm1-7-Pat1 complex; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0000932; C:P-body; IDA:ComplexPortal.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; IPI:SGD.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0097526; C:spliceosomal tri-snRNP complex; IBA:GO_Central.
DR GO; GO:0005689; C:U12-type spliceosomal complex; IBA:GO_Central.
DR GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
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:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IMP:ComplexPortal.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IMP:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IMP:ComplexPortal.
DR GO; GO:0008033; P:tRNA processing; IMP:ComplexPortal.
DR CDD; cd01729; LSm7; 1.
DR DisProt; DP01261; -.
DR InterPro; IPR017132; Lsm7.
DR InterPro; IPR044641; Lsm7/SmG-like.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR PANTHER; PTHR10553; PTHR10553; 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..115
FT /note="U6 snRNA-associated Sm-like protein LSm7"
FT /id="PRO_0000125581"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 95
FT /note="R->A: Slightly reduces affinity for poly-U RNA
FT ends."
FT /evidence="ECO:0000269|PubMed:24240276,
FT ECO:0000269|PubMed:24513854"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:4C92"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:4C92"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:4M7A"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:4C92"
FT STRAND 61..69
FT /evidence="ECO:0007829|PDB:4C92"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:4C92"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:4C92"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:4C92"
SQ SEQUENCE 115 AA; 13006 MW; EA1D019FC5D1B5C5 CRC64;
MHQQHSKSEN KPQQQRKKFE GPKREAILDL AKYKDSKIRV KLMGGKLVIG VLKGYDQLMN
LVLDDTVEYM SNPDDENNTE LISKNARKLG LTVIRGTILV SLSSAEGSDV LYMQK
