LSM1_YEAST
ID LSM1_YEAST Reviewed; 172 AA.
AC P47017; D6VW62;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Sm-like protein LSm1;
DE AltName: Full=SPB8 protein;
GN Name=LSM1; Synonyms=SPB8; OrderedLocusNames=YJL124C; ORFNames=J0714;
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 96604 / S288c / FY1679;
RX PubMed=8948101;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1471::aid-yea30>3.0.co;2-4;
RA Cziepluch C., Kordes E., Pujol A., Jauniaux J.-C.;
RT "Sequencing analysis of a 40.2 kb fragment of yeast chromosome X reveals 19
RT open reading frames including URA2 (5' end), TRK1, PBS2, SPT10, GCD14,
RT RPE1, PHO86, NCA3, ASF1, CCT7, GZF3, two tRNA genes, three remnant delta
RT elements and a Ty4 transposon.";
RL Yeast 12:1471-1474(1996).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP CHARACTERIZATION.
RX PubMed=9710590; DOI=10.1128/mcb.18.9.5062;
RA Boeck R., Lapeyre B., Brown C.E., Sachs A.B.;
RT "Capped mRNA degradation intermediates accumulate in the yeast spb8-2
RT mutant.";
RL Mol. Cell. Biol. 18:5062-5072(1998).
RN [6]
RP IDENTIFICATION IN THE LSM1-LSM7 COMPLEX, ASSOCIATION OF THE LSM1-LSM7
RP COMPLEX WITH PAT1 AND XRN1, FUNCTION OF THE LSM1-LSM7 COMPLEX, AND
RP 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 [7]
RP FUNCTION, AND INTERACTION WITH PAT1.
RX PubMed=10913177; DOI=10.1128/mcb.20.16.5939-5946.2000;
RA Bonnerot C., Boeck R., Lapeyre B.;
RT "The two proteins Pat1p (Mrt1p) and Spb8p interact in vivo, are required
RT for mRNA decay, and are functionally linked to Pab1p.";
RL Mol. Cell. Biol. 20:5939-5946(2000).
RN [8]
RP FUNCTION OF THE LSM1-LSM7 COMPLEX, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH PAT1.
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 [9]
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 [10]
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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 27-172 OF LSM1-LSM7 COMPLEX,
RP SUBUNIT, AND 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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF LSM1-LSM7 COMPLEX, SUBUNIT,
RP FUNCTION, RNA-BINDING, AND MUTAGENESIS OF ARG-105.
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).
CC -!- FUNCTION: Component of the cytoplasmic LSM1-LSM7 complex which is
CC involved in mRNA degradation by activating the decapping step. The
CC LSM1-LSM7 complex binds RNA with a preference for poly-U ends.
CC {ECO:0000269|PubMed:10747033, ECO:0000269|PubMed:10761922,
CC ECO:0000269|PubMed:10913177, ECO:0000269|PubMed:24513854}.
CC -!- SUBUNIT: Component of the heptameric LSM1-LSM7 complex that forms a
CC seven-membered ring structure with a donut shape. The LSm subunits are
CC 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. {ECO:0000269|PubMed:10747033, ECO:0000269|PubMed:10761922,
CC ECO:0000269|PubMed:10913177, ECO:0000269|PubMed:24139796,
CC ECO:0000269|PubMed:24513854}.
CC -!- INTERACTION:
CC P47017; P39517: DHH1; NbExp=2; IntAct=EBI-174, EBI-158;
CC P47017; P38203: LSM2; NbExp=6; IntAct=EBI-174, EBI-180;
CC P47017; P57743: LSM3; NbExp=4; IntAct=EBI-174, EBI-10227;
CC P47017; P40070: LSM4; NbExp=4; IntAct=EBI-174, EBI-188;
CC P47017; P40089: LSM5; NbExp=6; IntAct=EBI-174, EBI-10236;
CC P47017; Q06406: LSM6; NbExp=3; IntAct=EBI-174, EBI-196;
CC P47017; P25644: PAT1; NbExp=5; IntAct=EBI-174, EBI-204;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10761922}. Cytoplasm
CC {ECO:0000269|PubMed:10761922}. Cytoplasm, P-body
CC {ECO:0000305|PubMed:10913177}.
CC -!- MISCELLANEOUS: Present with 3490 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {ECO:0000305}.
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DR EMBL; Z49399; CAA89419.1; -; Genomic_DNA.
DR EMBL; AY558307; AAS56633.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08678.1; -; Genomic_DNA.
DR PIR; S56905; S56905.
DR RefSeq; NP_012411.1; NM_001181557.1.
DR PDB; 4C8Q; X-ray; 3.70 A; A=45-145.
DR PDB; 4C92; X-ray; 2.30 A; A=27-172.
DR PDB; 4M75; X-ray; 2.95 A; A/H=30-172.
DR PDBsum; 4C8Q; -.
DR PDBsum; 4C92; -.
DR PDBsum; 4M75; -.
DR AlphaFoldDB; P47017; -.
DR SMR; P47017; -.
DR BioGRID; 33632; 1108.
DR ComplexPortal; CPX-112; LSM1-7-PAT1 complex.
DR ComplexPortal; CPX-45; LSM1-7 complex.
DR DIP; DIP-1330N; -.
DR IntAct; P47017; 43.
DR MINT; P47017; -.
DR STRING; 4932.YJL124C; -.
DR MoonDB; P47017; Predicted.
DR iPTMnet; P47017; -.
DR MaxQB; P47017; -.
DR PaxDb; P47017; -.
DR PRIDE; P47017; -.
DR EnsemblFungi; YJL124C_mRNA; YJL124C; YJL124C.
DR GeneID; 853318; -.
DR KEGG; sce:YJL124C; -.
DR SGD; S000003660; LSM1.
DR VEuPathDB; FungiDB:YJL124C; -.
DR eggNOG; KOG1782; Eukaryota.
DR GeneTree; ENSGT00730000111133; -.
DR HOGENOM; CLU_076902_0_1_1; -.
DR InParanoid; P47017; -.
DR OMA; FMVRGEN; -.
DR BioCyc; YEAST:G3O-31575-MON; -.
DR Reactome; R-SCE-430039; mRNA decay by 5' to 3' exoribonuclease.
DR PRO; PR:P47017; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47017; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:1990726; C:Lsm1-7-Pat1 complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000932; C:P-body; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000339; F:RNA cap binding; IMP:SGD.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IMP:SGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IMP:SGD.
DR GO; GO:0016070; P:RNA metabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; mRNA processing; Nucleus; Reference proteome;
KW Ribonucleoprotein; RNA-binding.
FT CHAIN 1..172
FT /note="Sm-like protein LSm1"
FT /id="PRO_0000125553"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 105
FT /note="R->A: Slightly reduces affinity for poly-U RNA
FT ends."
FT /evidence="ECO:0000269|PubMed:24513854"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:4M75"
FT STRAND 48..58
FT /evidence="ECO:0007829|PDB:4C92"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:4C92"
FT STRAND 77..88
FT /evidence="ECO:0007829|PDB:4C92"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:4C92"
FT STRAND 93..104
FT /evidence="ECO:0007829|PDB:4C92"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:4C92"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:4C92"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:4C92"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:4C92"
FT HELIX 132..158
FT /evidence="ECO:0007829|PDB:4C92"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:4C92"
SQ SEQUENCE 172 AA; 20307 MW; 2632FA5288E178A2 CRC64;
MSANSKDRNQ SNQDAKRQQQ NFPKKISEGE ADLYLDQYNF TTTAAIVSSV DRKIFVLLRD
GRMLFGVLRT FDQYANLILQ DCVERIYFSE ENKYAEEDRG IFMIRGENVV MLGEVDIDKE
DQPLEAMERI PFKEAWLTKQ KNDEKRFKEE THKGKKMARH GIVYDFHKSD MY
