RUXF_YEAST
ID RUXF_YEAST Reviewed; 86 AA.
AC P54999; D6W4I2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Small nuclear ribonucleoprotein F;
DE Short=snRNP-F;
DE AltName: Full=Sm protein F;
DE Short=Sm-F;
DE Short=SmF;
GN Name=SMX3; OrderedLocusNames=YPR182W; ORFNames=P9705.4;
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=7744014; DOI=10.1002/j.1460-2075.1995.tb07200.x;
RA Seraphin B.;
RT "Sm and Sm-like proteins belong to a large family: identification of
RT proteins of the U6 as well as the U1, U2, U4 and U5 snRNPs.";
RL EMBO J. 14:2089-2099(1995).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 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 [8]
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 [9]
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 [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 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
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).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF WILD-TYPE AND MUTANT SER-75.
RX PubMed=12618433; DOI=10.1074/jbc.m211826200;
RA Collins B.M., Cubeddu L., Naidoo N., Harrop S.J., Kornfeld G.D.,
RA Dawes I.W., Curmi P.M., Mabbutt B.C.;
RT "Homomeric ring assemblies of eukaryotic Sm proteins have affinity for both
RT RNA and DNA. Crystal structure of an oligomeric complex of yeast SmF.";
RL J. Biol. Chem. 278:17291-17298(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:P62306}.
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. SMX3
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 P54999; Q12330: SME1; NbExp=6; IntAct=EBI-770, EBI-16359;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O59734}. Cytoplasm
CC {ECO:0000250|UniProtKB:O59734}.
CC -!- MISCELLANEOUS: Present with 2570 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. SmF/LSm6
CC subfamily. {ECO:0000305}.
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DR EMBL; X82778; CAA58022.1; -; Genomic_DNA.
DR EMBL; U25842; AAB68115.1; -; Genomic_DNA.
DR EMBL; AY558049; AAS56375.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11598.1; -; Genomic_DNA.
DR PIR; S55055; S55055.
DR RefSeq; NP_015508.1; NM_001184279.1.
DR PDB; 1N9R; X-ray; 2.80 A; A/B/C/D/E/F/G=1-86.
DR PDB; 1N9S; X-ray; 3.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-86.
DR PDB; 3JCM; EM; 3.80 A; W/Z=1-86.
DR PDB; 5GAM; EM; 3.70 A; f=1-86.
DR PDB; 5GAN; EM; 3.60 A; f/q=1-86.
DR PDB; 5GAO; EM; 3.60 A; q=1-86.
DR PDB; 5GM6; EM; 3.50 A; h=1-86.
DR PDB; 5GMK; EM; 3.40 A; h/w=1-86.
DR PDB; 5LJ3; EM; 3.80 A; f/q=1-86.
DR PDB; 5LJ5; EM; 3.80 A; f/q=1-86.
DR PDB; 5LQW; EM; 5.80 A; f=1-86.
DR PDB; 5MPS; EM; 3.85 A; f=1-86.
DR PDB; 5MQ0; EM; 4.17 A; f/q=1-86.
DR PDB; 5NRL; EM; 7.20 A; f/q/x=1-86.
DR PDB; 5WSG; EM; 4.00 A; H/h=1-86.
DR PDB; 5Y88; EM; 3.70 A; c/j=1-86.
DR PDB; 5YLZ; EM; 3.60 A; c/j=1-86.
DR PDB; 5ZWM; EM; 3.40 A; U/f/j=1-86.
DR PDB; 5ZWN; EM; 3.30 A; f=1-86.
DR PDB; 5ZWO; EM; 3.90 A; U/f/j=1-86.
DR PDB; 6BK8; EM; 3.30 A; b/m=1-86.
DR PDB; 6EXN; EM; 3.70 A; f/q=1-86.
DR PDB; 6G90; EM; 4.00 A; f/x=1-86.
DR PDB; 6J6G; EM; 3.20 A; h/w=1-86.
DR PDB; 6J6H; EM; 3.60 A; h/w=1-86.
DR PDB; 6J6N; EM; 3.86 A; h/w=1-86.
DR PDB; 6J6Q; EM; 3.70 A; h/w=1-86.
DR PDB; 6N7P; EM; 3.60 A; P=1-86.
DR PDB; 6N7R; EM; 3.20 A; P=1-86.
DR PDB; 6N7X; EM; 3.60 A; P=1-86.
DR PDB; 7B9V; EM; 2.80 A; f/q=1-86.
DR PDB; 7OQB; EM; 9.00 A; x=1-86.
DR PDB; 7OQC; EM; 4.10 A; f=1-86.
DR PDB; 7OQE; EM; 5.90 A; f/x=1-86.
DR PDBsum; 1N9R; -.
DR PDBsum; 1N9S; -.
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; P54999; -.
DR SMR; P54999; -.
DR BioGRID; 36354; 571.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
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-1634N; -.
DR IntAct; P54999; 45.
DR MINT; P54999; -.
DR STRING; 4932.YPR182W; -.
DR MaxQB; P54999; -.
DR PaxDb; P54999; -.
DR PRIDE; P54999; -.
DR EnsemblFungi; YPR182W_mRNA; YPR182W; YPR182W.
DR GeneID; 856312; -.
DR KEGG; sce:YPR182W; -.
DR SGD; S000006386; SMX3.
DR VEuPathDB; FungiDB:YPR182W; -.
DR eggNOG; KOG3482; Eukaryota.
DR GeneTree; ENSGT00940000154818; -.
DR HOGENOM; CLU_076902_12_3_1; -.
DR InParanoid; P54999; -.
DR OMA; VKLKWGH; -.
DR BioCyc; YEAST:G3O-34307-MON; -.
DR EvolutionaryTrace; P54999; -.
DR PRO; PR:P54999; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P54999; 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:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0005685; C:U1 snRNP; IDA:SGD.
DR GO; GO:0005686; C:U2 snRNP; 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:0008266; F:poly(U) RNA binding; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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; 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; cd01722; Sm_F; 1.
DR InterPro; IPR016487; Lsm6/sSmF.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR034100; Sm_F.
DR PANTHER; PTHR11021; PTHR11021; 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..86
FT /note="Small nuclear ribonucleoprotein F"
FT /id="PRO_0000125544"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:1N9R"
FT STRAND 25..33
FT /evidence="ECO:0007829|PDB:1N9R"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:1N9R"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1N9R"
FT STRAND 51..60
FT /evidence="ECO:0007829|PDB:1N9R"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:1N9R"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:1N9R"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1N9R"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:1N9R"
SQ SEQUENCE 86 AA; 9660 MW; 1640D3237597B2D8 CRC64;
MSESSDISAM QPVNPKPFLK GLVNHRVGVK LKFNSTEYRG TLVSTDNYFN LQLNEAEEFV
AGVSHGTLGE IFIRCNNVLY IRELPN
