RUXG_YEAST
ID RUXG_YEAST Reviewed; 77 AA.
AC P40204; D6VTL2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Small nuclear ribonucleoprotein G;
DE Short=snRNP-G;
DE AltName: Full=Sm protein G;
DE Short=Sm-G;
DE Short=SmG;
GN Name=SMX2; Synonyms=SNP2; OrderedLocusNames=YFL017W-A; ORFNames=YFL017Bw;
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].
RX PubMed=3058861; DOI=10.1099/00221287-134-5-1131;
RA Ross J., Reid G.A., Dawes I.W.;
RT "The nucleotide sequence of the LPD1 gene encoding lipoamide dehydrogenase
RT in Saccharomyces cerevisiae: comparison between eukaryotic and prokaryotic
RT sequences for related enzymes and identification of potential upstream
RT control sites.";
RL J. Gen. Microbiol. 134:1131-1139(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kornfeld G.D.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INTERACTION WITH SME1.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RA Barrell B.G., Churcher C., Rajandream M.A.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
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 [9]
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 [10]
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 [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 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 [13]
RP IDENTIFICATION IN THE CWC COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11884590; DOI=10.1128/mcb.22.7.2011-2024.2002;
RA Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
RT "Proteomics analysis reveals stable multiprotein complexes in both fission
RT and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA
RT splicing factors, and snRNAs.";
RL Mol. Cell. Biol. 22:2011-2024(2002).
RN [14]
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: Plays a role in pre-mRNA splicing as a core component of the
CC spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins
CC (snRNPs), the building blocks of the spliceosome (By similarity).
CC {ECO:0000250|UniProtKB:P62308}.
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. SMX2
CC specifically interacts with SME1. Belongs to the CWC complex (or CEF1-
CC associated complex), a spliceosome sub-complex reminiscent of a late-
CC stage spliceosome composed of the U2, U5 and U6 snRNAs and at least
CC BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22,
CC CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1,
CC NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7,
CC SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2,
CC RSE1 and YJU2. Component of the U4/U6-U5 tri-snRNP complex composed of
CC the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18,
CC PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2,
CC SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and
CC DIB1. {ECO:0000269|PubMed:10449419, ECO:0000269|PubMed:11302706,
CC ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:9528767}.
CC -!- INTERACTION:
CC P40204; Q12330: SME1; NbExp=5; IntAct=EBI-637, EBI-16359;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O74966}. Cytoplasm
CC {ECO:0000250|UniProtKB:O74966}.
CC -!- MISCELLANEOUS: Present with 1400 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; M20880; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L31794; AAB63977.1; -; Genomic_DNA.
DR EMBL; D50617; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z46255; CAA86353.1; -; Genomic_DNA.
DR EMBL; AY558463; AAS56789.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12422.1; -; Genomic_DNA.
DR PIR; S48322; S48322.
DR RefSeq; NP_116636.1; NM_001180864.1.
DR PDB; 3JCM; EM; 3.80 A; X/a=1-77.
DR PDB; 5GAM; EM; 3.70 A; g=1-77.
DR PDB; 5GAN; EM; 3.60 A; g/r=1-77.
DR PDB; 5GAO; EM; 3.60 A; r=1-77.
DR PDB; 5GM6; EM; 3.50 A; j=1-77.
DR PDB; 5GMK; EM; 3.40 A; j/x=1-77.
DR PDB; 5LJ3; EM; 3.80 A; g/r=1-77.
DR PDB; 5LJ5; EM; 3.80 A; g/r=1-77.
DR PDB; 5LQW; EM; 5.80 A; g=1-77.
DR PDB; 5MPS; EM; 3.85 A; g=1-77.
DR PDB; 5MQ0; EM; 4.17 A; g/r=1-77.
DR PDB; 5NRL; EM; 7.20 A; g/r/y=1-77.
DR PDB; 5WSG; EM; 4.00 A; K/j=1-77.
DR PDB; 5Y88; EM; 3.70 A; d/k=1-77.
DR PDB; 5YLZ; EM; 3.60 A; d/k=1-77.
DR PDB; 5ZWM; EM; 3.40 A; V/g/k=1-77.
DR PDB; 5ZWN; EM; 3.30 A; g=1-77.
DR PDB; 5ZWO; EM; 3.90 A; V/g/k=1-77.
DR PDB; 6BK8; EM; 3.30 A; d/n=1-77.
DR PDB; 6EXN; EM; 3.70 A; g/r=1-77.
DR PDB; 6G90; EM; 4.00 A; g/y=1-77.
DR PDB; 6J6G; EM; 3.20 A; j/x=1-77.
DR PDB; 6J6H; EM; 3.60 A; j/x=1-77.
DR PDB; 6J6N; EM; 3.86 A; j/x=1-77.
DR PDB; 6J6Q; EM; 3.70 A; j/x=1-77.
DR PDB; 6N7P; EM; 3.60 A; Q=1-77.
DR PDB; 6N7R; EM; 3.20 A; Q=1-77.
DR PDB; 6N7X; EM; 3.60 A; Q=1-77.
DR PDB; 7B9V; EM; 2.80 A; g/r=1-77.
DR PDB; 7DCO; EM; 2.50 A; g/k=1-77.
DR PDB; 7OQB; EM; 9.00 A; y=1-77.
DR PDB; 7OQC; EM; 4.10 A; g=1-77.
DR PDB; 7OQE; EM; 5.90 A; g/y=1-77.
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; 7DCO; -.
DR PDBsum; 7OQB; -.
DR PDBsum; 7OQC; -.
DR PDBsum; 7OQE; -.
DR AlphaFoldDB; P40204; -.
DR SMR; P40204; -.
DR BioGRID; 31129; 61.
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-6683N; -.
DR IntAct; P40204; 57.
DR MINT; P40204; -.
DR STRING; 4932.YFL017W-A; -.
DR MaxQB; P40204; -.
DR PaxDb; P40204; -.
DR PRIDE; P40204; -.
DR TopDownProteomics; P40204; -.
DR EnsemblFungi; YFL017W-A_mRNA; YFL017W-A; YFL017W-A.
DR GeneID; 850528; -.
DR KEGG; sce:YFL017W-A; -.
DR SGD; S000002965; SMX2.
DR VEuPathDB; FungiDB:YFL017W-A; -.
DR eggNOG; KOG1780; Eukaryota.
DR GeneTree; ENSGT00940000176059; -.
DR HOGENOM; CLU_076902_10_1_1; -.
DR InParanoid; P40204; -.
DR OMA; LGMCVIR; -.
DR BioCyc; YEAST:G3O-30503-MON; -.
DR PRO; PR:P40204; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P40204; protein.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
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:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0034719; C:SMN-Sm protein complex; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0097526; C:spliceosomal tri-snRNP complex; IBA:GO_Central.
DR GO; GO:0005685; C:U1 snRNP; IDA:SGD.
DR GO; GO:0005689; C:U12-type spliceosomal complex; IBA:GO_Central.
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: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; IPI:ComplexPortal.
DR GO; GO:0000245; P:spliceosomal complex assembly; IC:ComplexPortal.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IC:ComplexPortal.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; IC:ComplexPortal.
DR CDD; cd01719; Sm_G; 1.
DR InterPro; IPR044641; Lsm7/SmG-like.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR034098; Sm_G.
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; Direct protein sequencing; mRNA processing;
KW mRNA splicing; Nucleus; Reference proteome; Ribonucleoprotein; RNA-binding;
KW Spliceosome.
FT CHAIN 1..77
FT /note="Small nuclear ribonucleoprotein G"
FT /id="PRO_0000125552"
FT TURN 8..12
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:6J6G"
SQ SEQUENCE 77 AA; 8482 MW; 5C6208B8C5A9AB33 CRC64;
MVSTPELKKY MDKKILLNIN GSRKVAGILR GYDIFLNVVL DDAMEINGED PANNHQLGLQ
TVIRGNSIIS LEALDAI
