RUXE_YEAST
ID RUXE_YEAST Reviewed; 94 AA.
AC Q12330; D6W2L6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Small nuclear ribonucleoprotein E;
DE Short=snRNP-E;
DE AltName: Full=Sm protein E;
DE Short=Sm-E;
DE Short=SmE;
GN Name=SME1; OrderedLocusNames=YOR159C;
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], AND FUNCTION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8918241; DOI=10.1016/0378-1119(96)00230-2;
RA Bordonne R., Tarassov I.A.;
RT "The yeast SME1 gene encodes the homologue of the human E core protein.";
RL Gene 176:111-117(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / FY1678;
RX PubMed=9046089;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<73::aid-yea52>3.0.co;2-m;
RA Bordonne R., Camasses A., Madania A., Poch O., Tarassov I.A., Winsor B.,
RA Martin R.P.;
RT "Analysis of a 35.6 kb region on the right arm of Saccharomyces cerevisiae
RT chromosome XV.";
RL Yeast 13:73-83(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 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 [6]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=9012791; DOI=10.1073/pnas.94.2.385;
RA Neubauer G., Gottschalk A., Fabrizio P., Seraphin B., Luehrmann R.,
RA Mann M.;
RT "Identification of the proteins of the yeast U1 small nuclear
RT ribonucleoprotein complex by mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:385-390(1997).
RN [7]
RP INTERACTION WITH SMX2 AND SMX3.
RX PubMed=9528767; DOI=10.1128/mcb.18.4.1956;
RA Camasses A., Bragado-Nilsson E., Martin R., Seraphin B., Bordonne R.;
RT "Interactions within the yeast Sm core complex: from proteins to amino
RT acids.";
RL Mol. Cell. Biol. 18:1956-1966(1998).
RN [8]
RP RNA-BINDING.
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 [9]
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 [10]
RP CHARACTERIZATION OF THE SPLICEOSOME.
RX PubMed=11804584; DOI=10.1016/s1097-2765(02)00436-7;
RA Stevens S.W., Ryan D.E., Ge H.Y., Moore R.E., Young M.K., Lee T.D.,
RA Abelson J.;
RT "Composition and functional characterization of the yeast spliceosomal
RT penta-snRNP.";
RL Mol. Cell 9:31-44(2002).
RN [11]
RP SUBUNIT.
RX PubMed=11302706; DOI=10.1006/jmbi.2001.4549;
RA Walke S., Bragado-Nilsson E., Seraphin B., Nagai K.;
RT "Stoichiometry of the Sm proteins in yeast spliceosomal snRNPs supports the
RT heptamer ring model of the core domain.";
RL J. Mol. Biol. 308:49-58(2001).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=11027265; DOI=10.1128/mcb.20.21.7943-7954.2000;
RA Bordonne R.;
RT "Functional characterization of nuclear localization signals in yeast Sm
RT proteins.";
RL Mol. Cell. Biol. 20:7943-7954(2000).
RN [13]
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).
CC -!- FUNCTION: Involved in pre-mRNA splicing. Binds and is required for the
CC stability of snRNA U1, U2, U4 and U5 which contain a highly conserved
CC structural motif called the Sm binding site. Involved in cap
CC modification. {ECO:0000269|PubMed:8918241}.
CC -!- SUBUNIT: Component of the Sm core complex, present in spliceosomal
CC snRNP U1, U2, U4/U6 and U5. The core complex contains SMB1, SMD1, SMD2,
CC SMD3, SME1, SMX3 and SMX2 (Sm proteins B, D1, D2, D3, E, F and G,
CC respectively), and is probably a heptameric ring structure. SME1
CC specifically interacts with SMX2 and SMX3. Component of the U4/U6-U5
CC tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least
CC 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:11302706, ECO:0000269|PubMed:9528767}.
CC -!- INTERACTION:
CC Q12330; P40204: SMX2; NbExp=5; IntAct=EBI-16359, EBI-637;
CC Q12330; P54999: SMX3; NbExp=6; IntAct=EBI-16359, EBI-770;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11027265}. Nucleus
CC {ECO:0000269|PubMed:11027265}.
CC -!- MISCELLANEOUS: Present with 556 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; X92449; CAA63198.1; -; Genomic_DNA.
DR EMBL; U55020; AAC49645.1; -; Genomic_DNA.
DR EMBL; Z75067; CAA99365.1; -; Genomic_DNA.
DR EMBL; AY558029; AAS56355.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10932.1; -; Genomic_DNA.
DR PIR; S67047; S67047.
DR RefSeq; NP_014802.3; NM_001183578.3.
DR PDB; 3JCM; EM; 3.80 A; V/Y=1-94.
DR PDB; 5GAM; EM; 3.70 A; e=1-94.
DR PDB; 5GAN; EM; 3.60 A; e/p=1-94.
DR PDB; 5GAO; EM; 3.60 A; p=1-94.
DR PDB; 5GM6; EM; 3.50 A; i=1-94.
DR PDB; 5GMK; EM; 3.40 A; i/u=1-94.
DR PDB; 5LJ3; EM; 3.80 A; e/p=1-94.
DR PDB; 5LJ5; EM; 3.80 A; e/p=1-94.
DR PDB; 5LQW; EM; 5.80 A; e=1-94.
DR PDB; 5MPS; EM; 3.85 A; e=1-94.
DR PDB; 5MQ0; EM; 4.17 A; e/p=1-94.
DR PDB; 5NRL; EM; 7.20 A; e/p/w=1-94.
DR PDB; 5WSG; EM; 4.00 A; G/i=1-94.
DR PDB; 5Y88; EM; 3.70 A; b/i=1-94.
DR PDB; 5YLZ; EM; 3.60 A; b/i=1-94.
DR PDB; 5ZWM; EM; 3.40 A; T/e/i=1-94.
DR PDB; 5ZWN; EM; 3.30 A; e=1-94.
DR PDB; 5ZWO; EM; 3.90 A; T/e/i=1-94.
DR PDB; 6BK8; EM; 3.30 A; c/l=1-94.
DR PDB; 6EXN; EM; 3.70 A; e/p=1-94.
DR PDB; 6G90; EM; 4.00 A; e/w=1-94.
DR PDB; 6J6G; EM; 3.20 A; i/u=1-94.
DR PDB; 6J6H; EM; 3.60 A; i/u=1-94.
DR PDB; 6J6N; EM; 3.86 A; i/u=1-94.
DR PDB; 6J6Q; EM; 3.70 A; i/u=1-94.
DR PDB; 6N7P; EM; 3.60 A; O=1-94.
DR PDB; 6N7R; EM; 3.20 A; O=1-94.
DR PDB; 6N7X; EM; 3.60 A; O=1-94.
DR PDB; 7B9V; EM; 2.80 A; e/p=1-94.
DR PDB; 7OQB; EM; 9.00 A; w=1-93.
DR PDB; 7OQC; EM; 4.10 A; e=1-94.
DR PDB; 7OQE; EM; 5.90 A; e/w=1-94.
DR PDBsum; 3JCM; -.
DR PDBsum; 5GAM; -.
DR PDBsum; 5GAN; -.
DR PDBsum; 5GAO; -.
DR PDBsum; 5GM6; -.
DR PDBsum; 5GMK; -.
DR PDBsum; 5LJ3; -.
DR PDBsum; 5LJ5; -.
DR PDBsum; 5LQW; -.
DR PDBsum; 5MPS; -.
DR PDBsum; 5MQ0; -.
DR PDBsum; 5NRL; -.
DR PDBsum; 5WSG; -.
DR PDBsum; 5Y88; -.
DR PDBsum; 5YLZ; -.
DR PDBsum; 5ZWM; -.
DR PDBsum; 5ZWN; -.
DR PDBsum; 5ZWO; -.
DR PDBsum; 6BK8; -.
DR PDBsum; 6EXN; -.
DR PDBsum; 6G90; -.
DR PDBsum; 6J6G; -.
DR PDBsum; 6J6H; -.
DR PDBsum; 6J6N; -.
DR PDBsum; 6J6Q; -.
DR PDBsum; 6N7P; -.
DR PDBsum; 6N7R; -.
DR PDBsum; 6N7X; -.
DR PDBsum; 7B9V; -.
DR PDBsum; 7OQB; -.
DR PDBsum; 7OQC; -.
DR PDBsum; 7OQE; -.
DR AlphaFoldDB; Q12330; -.
DR SMR; Q12330; -.
DR BioGRID; 34555; 157.
DR ComplexPortal; CPX-23; U1 small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-25; U4/U6.U5 tri-small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-26; U2 small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-29; U5 small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-30; U5 small nuclear ribonucleoprotein complex, AAR2 variant.
DR ComplexPortal; CPX-31; U4 small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-32; U4/U6 small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-43; Sm complex.
DR DIP; DIP-1633N; -.
DR IntAct; Q12330; 16.
DR MINT; Q12330; -.
DR STRING; 4932.YOR159C; -.
DR iPTMnet; Q12330; -.
DR MaxQB; Q12330; -.
DR PaxDb; Q12330; -.
DR PRIDE; Q12330; -.
DR EnsemblFungi; YOR159C_mRNA; YOR159C; YOR159C.
DR GeneID; 854330; -.
DR KEGG; sce:YOR159C; -.
DR SGD; S000005685; SME1.
DR VEuPathDB; FungiDB:YOR159C; -.
DR eggNOG; KOG1774; Eukaryota.
DR GeneTree; ENSGT00390000012818; -.
DR HOGENOM; CLU_125186_1_0_1; -.
DR InParanoid; Q12330; -.
DR OMA; TIWLYEQ; -.
DR BioCyc; YEAST:G3O-33676-MON; -.
DR PRO; PR:Q12330; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12330; protein.
DR GO; GO:0000243; C:commitment complex; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0005685; C:U1 snRNP; IDA:SGD.
DR GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR GO; GO:0071004; C:U2-type prespliceosome; IDA:SGD.
DR GO; GO:0005687; C:U4 snRNP; IPI: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:0005682; C:U5 snRNP; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:1990935; F:splicing factor binding; IPI:SGD.
DR GO; GO:0036261; P:7-methylguanosine cap hypermethylation; IMP:ComplexPortal.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; IC:ComplexPortal.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR GO; GO:0000245; P:spliceosomal complex assembly; IC:ComplexPortal.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IBA:GO_Central.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; IC:ComplexPortal.
DR CDD; cd01718; Sm_E; 1.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR027078; snRNP-E.
DR PANTHER; PTHR11193; PTHR11193; 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; Direct protein sequencing; mRNA processing;
KW mRNA splicing; Nucleus; Reference proteome; Ribonucleoprotein; RNA-binding;
KW Spliceosome.
FT CHAIN 1..94
FT /note="Small nuclear ribonucleoprotein E"
FT /id="PRO_0000125535"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 52..61
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:6J6G"
SQ SEQUENCE 94 AA; 10375 MW; B76D72DA8456F3B5 CRC64;
MSNKVKTKAM VPPINCIFNF LQQQTPVTIW LFEQIGIRIK GKIVGFDEFM NVVIDEAVEI
PVNSADGKED VEKGTPLGKI LLKGDNITLI TSAD
