ID IST3_YEAST Reviewed; 148 AA. AC P40565; D6VVT5; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 02-SEP-2026, entry version 206. DE RecName: Full=U2 snRNP component IST3; DE AltName: Full=Increased sodium tolerance protein 3; DE AltName: Full=U2 snRNP protein SNU17; GN Name=IST3; Synonyms=SNU17; OrderedLocusNames=YIR005W; ORFNames=YIB5W; 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=7762303; DOI=10.1002/yea.320110109; RA Voss H., Tamames J., Teodoru C., Valencia A., Sensen C., Wiemann S., RA Schwager C., Zimmermann J., Sander C., Ansorge W.; RT "Nucleotide sequence and analysis of the centromeric region of yeast RT chromosome IX."; RL Yeast 11:61-78(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169870; DOI=10.1038/387s084; RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C., RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., RA Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."; RL Nature 387:84-87(1997). 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 FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=11287609; DOI=10.1128/mcb.21.9.3037-3046.2001; RA Gottschalk A., Bartels C., Neubauer G., Luehrmann R., Fabrizio P.; RT "A novel yeast U2 snRNP protein, Snu17p, is required for the first RT catalytic step of splicing and for progression of spliceosome assembly."; RL Mol. Cell. Biol. 21:3037-3046(2001). RN [6] RP IDENTIFICATION IN U1.U2.U4/U6.U5 PENTA-SNRNP COMPLEX BY MASS SPECTROMETRY. 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 [7] 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 [8] RP INTERACTION WITH RDS3. RX PubMed=14517302; DOI=10.1128/mcb.23.20.7339-7349.2003; RA Wang Q., Rymond B.C.; RT "Rds3p is required for stable U2 snRNP recruitment to the splicing RT apparatus."; RL Mol. Cell. Biol. 23:7339-7349(2003). 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 FUNCTION, IDENTIFICATION IN THE RES COMPLEX BY MASS SPECTROMETRY, AND RP DISRUPTION PHENOTYPE. RX PubMed=15565172; DOI=10.1038/sj.emboj.7600482; RA Dziembowski A., Ventura A.-P., Rutz B., Caspary F., Faux C., Halgand F., RA Laprevote O., Seraphin B.; RT "Proteomic analysis identifies a new complex required for nuclear pre-mRNA RT retention and splicing."; RL EMBO J. 23:4847-4856(2004). RN [12] RP FUNCTION. RX PubMed=14973223; DOI=10.1093/nar/gkh281; RA Spingola M., Armisen J., Ares M. Jr.; RT "Mer1p is a modular splicing factor whose function depends on the conserved RT U2 snRNP protein Snu17p."; RL Nucleic Acids Res. 32:1242-1250(2004). RN [13] RP SUBUNIT. RX PubMed=16618970; DOI=10.1261/rna.50506; RA Tardiff D.F., Rosbash M.; RT "Arrested yeast splicing complexes indicate stepwise snRNP recruitment RT during in vivo spliceosome assembly."; RL RNA 12:968-979(2006). RN [14] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=23118884; DOI=10.1371/journal.pone.0047621; RA Tuo S., Nakashima K., Pringle J.R.; RT "Apparent defect in yeast bud-site selection due to a specific failure to RT splice the pre-mRNA of a regulator of cell-type-specific transcription."; RL PLoS ONE 7:e47621-e47621(2012). RN [15] {ECO:0007744|PDB:4UQT} RP STRUCTURE BY NMR OF 25-113. RX PubMed=25160624; DOI=10.1074/jbc.m114.592311; RA Tripsianes K., Friberg A., Barrandon C., Brooks M., van Tilbeurgh H., RA Seraphin B., Sattler M.; RT "A novel protein-protein interaction in the RES (REtention and Splicing) RT complex."; RL J. Biol. Chem. 289:28640-28650(2014). RN [16] {ECO:0007744|PDB:2MKC} RP STRUCTURE BY NMR OF 25-138. RX PubMed=25218446; DOI=10.1038/nsmb.2889; RA Wysoczanski P., Schneider C., Xiang S., Munari F., Trowitzsch S., RA Wahl M.C., Luhrmann R., Becker S., Zweckstetter M.; RT "Cooperative structure of the heterotrimeric pre-mRNA retention and RT splicing complex."; RL Nat. Struct. Mol. Biol. 21:911-918(2014). RN [17] {ECO:0007744|PDB:2MY2, ECO:0007744|PDB:2MY3} RP STRUCTURE BY NMR OF 25-138. RX PubMed=26212312; DOI=10.1038/srep12545; RA Wysoczanski P., Becker S., Zweckstetter M.; RT "Structures of intermediates during RES complex assembly."; RL Sci. Rep. 5:12545-12545(2015). RN [18] {ECO:0007744|PDB:5LQW} RP STRUCTURE BY ELECTRON MICROSCOPY (5.80 ANGSTROMS). RX PubMed=27562955; DOI=10.1126/science.aag1906; RA Rauhut R., Fabrizio P., Dybkov O., Hartmuth K., Pena V., Chari A., RA Kumar V., Lee C.T., Urlaub H., Kastner B., Stark H., Luhrmann R.; RT "Molecular architecture of the Saccharomyces cerevisiae activated RT spliceosome."; RL Science 353:1399-1405(2016). RN [19] {ECO:0007744|PDB:5GM6} RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS). RX PubMed=27445306; DOI=10.1126/science.aag0291; RA Yan C., Wan R., Bai R., Huang G., Shi Y.; RT "Structure of a yeast activated spliceosome at 3.5 A resolution."; RL Science 353:904-911(2016). RN [20] {ECO:0007744|PDB:5ZWM, ECO:0007744|PDB:5ZWO} RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS). RX PubMed=29794219; DOI=10.1126/science.aau0325; RA Bai R., Wan R., Yan C., Lei J., Shi Y.; RT "Structures of the fully assembled Saccharomyces cerevisiae spliceosome RT before activation."; RL Science 360:1423-1429(2018). CC -!- FUNCTION: Required for pre-mRNA splicing and spliceosome assembly. As CC part of the pre-mRNA retention and splicing (RES) complex, required for CC efficient splicing and nuclear retention of not properly spliced pre- CC mRNA (PubMed:11287609, PubMed:15565172). Required for MER1-activated CC splicing (PubMed:14973223). {ECO:0000269|PubMed:11287609, CC ECO:0000269|PubMed:14973223, ECO:0000269|PubMed:15565172}. CC -!- SUBUNIT: Component of the pre-mRNA retention and splicing (RES) complex CC composed of at least BUD13/CWC26, IST3/SNU17 and PML1 CC (PubMed:15565172). The heterotrimeric RES complex is organized around CC the IST3/SNU17 protein that binds to both the BUD13/CWC26 and PML1 CC subunits. The complex is a conserved, non-snRNP spliceosome-associated CC module that was shown to enhance splicing of a subset of transcripts CC (PubMed:16618970, PubMed:25160624, PubMed:25218446). Interacts with CC RDS3 (PubMed:14517302). {ECO:0000269|PubMed:14517302, CC ECO:0000269|PubMed:15565172, ECO:0000269|PubMed:16618970, CC ECO:0000269|PubMed:25160624, ECO:0000269|PubMed:25218446}. CC -!- INTERACTION: CC P40565; P46947: BUD13; NbExp=14; IntAct=EBI-25387, EBI-24073; CC P40565; Q07930: PML1; NbExp=7; IntAct=EBI-25387, EBI-27110; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- DISRUPTION PHENOTYPE: Cells have a slow growth phenotype that is CC exacerbated at 37 degrees Celsius. Deletion mutants have a significant CC pre-mRNA leakage at 25 degrees Celsius (PubMed:15565172). Displays a CC specific defect in the splicing of the MATa1 pre-mRNA CC (PubMed:23118884). {ECO:0000269|PubMed:15565172, CC ECO:0000269|PubMed:23118884}. CC -!- MISCELLANEOUS: Present with 922 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the IST3 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X79743; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z38062; CAA86207.1; -; Genomic_DNA. DR EMBL; AY558081; AAS56407.1; -; Genomic_DNA. DR EMBL; BK006942; DAA08551.1; -; Genomic_DNA. DR PIR; S48439; S48439. DR RefSeq; NP_012270.1; NM_001179527.1. DR PDB; 2MKC; NMR; -; A=25-138. DR PDB; 2MY2; NMR; -; A=25-138. DR PDB; 2MY3; NMR; -; A=25-138. DR PDB; 4UQT; NMR; -; A=25-113. DR PDB; 5GM6; EM; 3.50 A; V=1-148. DR PDB; 5LQW; EM; 5.80 A; J=1-148. DR PDB; 5ZWM; EM; 3.40 A; X=1-148. DR PDB; 5ZWO; EM; 3.90 A; X=1-148. DR AlphaFoldDB; P40565; -. DR BMRB; P40565; -. DR EMDB; EMD-6972; -. DR EMDB; EMD-6974; -. DR EMDB; EMD-9524; -. DR SMR; P40565; -. DR BioGRID; 34996; 406. DR ComplexPortal; CPX-1649; RES complex. DR ComplexPortal; CPX-1651; PRP19-associated complex. DR ComplexPortal; CPX-26; U2 small nuclear ribonucleoprotein complex. DR DIP; DIP-2076N; -. DR FunCoup; P40565; 919. DR IntAct; P40565; 79. DR MINT; P40565; -. DR STRING; 4932.YIR005W; -. DR iPTMnet; P40565; -. DR PaxDb; 4932-YIR005W; -. DR PeptideAtlas; P40565; -. DR EnsemblFungi; YIR005W_mRNA; YIR005W; YIR005W. DR GeneID; 854821; -. DR KEGG; sce:YIR005W; -. DR AGR; SGD:S000001444; -. DR SGD; S000001444; IST3. DR VEuPathDB; FungiDB:YIR005W; -. DR eggNOG; KOG0126; Eukaryota. DR HOGENOM; CLU_045495_5_0_1; -. DR InParanoid; P40565; -. DR OMA; CAPKPQI; -. DR OrthoDB; 2573941at2759; -. DR BioCyc; YEAST:G3O-31426-MONOMER; -. DR BioGRID-ORCS; 854821; 0 hits in 10 CRISPR screens. DR EvolutionaryTrace; P40565; -. DR PRO; PR:P40565; -. DR Proteomes; UP000002311; Chromosome IX. DR RNAct; P40565; protein. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; NAS:ComplexPortal. DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central. DR GO; GO:0000974; C:Prp19 complex; IPI:ComplexPortal. DR GO; GO:0070274; C:RES complex; IDA:SGD. DR GO; GO:0005681; C:spliceosomal complex; NAS:ComplexPortal. DR GO; GO:0005686; C:U2 snRNP; IDA:SGD. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0000349; P:generation of catalytic spliceosome for first transesterification step; IMP:SGD. DR GO; GO:0051237; P:maintenance of RNA location; IMP:ComplexPortal. DR GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:SGD. DR GO; GO:0000245; P:spliceosomal complex assembly; IMP:SGD. DR GO; GO:1903241; P:U2-type prespliceosome assembly; NAS:ComplexPortal. DR CDD; cd12411; RRM_ist3_like; 1. DR FunFam; 3.30.70.330:FF:000609; U2 snRNP component IST3; 1. DR Gene3D; 3.30.70.330; -; 1. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR051847; RNA_proc/Spliceosome_comp. DR InterPro; IPR000504; RRM_dom. DR InterPro; IPR045844; RRM_Ist3-like. DR PANTHER; PTHR45880; RNA-BINDING MOTIF PROTEIN, X-LINKED 2; 1. DR PANTHER; PTHR45880:SF1; RNA-BINDING MOTIF PROTEIN, X-LINKED 2; 1. DR Pfam; PF00076; RRM_1; 1. DR SMART; SM00360; RRM; 1. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1. DR PROSITE; PS50102; RRM; 1. DR PDBsum; 2MKC; -. DR PDBsum; 2MY2; -. DR PDBsum; 2MY3; -. DR PDBsum; 4UQT; -. DR PDBsum; 5GM6; -. DR PDBsum; 5LQW; -. DR PDBsum; 5ZWM; -. DR PDBsum; 5ZWO; -. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; mRNA processing; mRNA splicing; Nucleus; KW Reference proteome; RNA-binding; Spliceosome. FT CHAIN 1..148 FT /note="U2 snRNP component IST3" FT /id="PRO_0000081621" FT DOMAIN 31..109 FT /note="RRM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT HELIX 4..13 FT /evidence="ECO:0007829|PDB:5ZWM" FT HELIX 19..21 FT /evidence="ECO:0007829|PDB:5ZWM" FT HELIX 23..26 FT /evidence="ECO:0007829|PDB:5ZWM" FT STRAND 27..29 FT /evidence="ECO:0007829|PDB:4UQT" FT STRAND 33..37 FT /evidence="ECO:0007829|PDB:5ZWM" FT HELIX 44..50 FT /evidence="ECO:0007829|PDB:5ZWM" FT TURN 51..54 FT /evidence="ECO:0007829|PDB:5ZWM" FT STRAND 57..64 FT /evidence="ECO:0007829|PDB:5ZWM" FT TURN 66..68 FT /evidence="ECO:0007829|PDB:5ZWM" FT STRAND 71..81 FT /evidence="ECO:0007829|PDB:5ZWM" FT HELIX 83..92 FT /evidence="ECO:0007829|PDB:5ZWM" FT STRAND 103..106 FT /evidence="ECO:0007829|PDB:5ZWM" FT HELIX 110..112 FT /evidence="ECO:0007829|PDB:2MKC" FT HELIX 113..115 FT /evidence="ECO:0007829|PDB:5ZWM" FT HELIX 116..126 FT /evidence="ECO:0007829|PDB:5ZWM" FT HELIX 127..131 FT /evidence="ECO:0007829|PDB:2MY2" SQ SEQUENCE 148 AA; 17098 MW; 9D51C3043AB823D2 CRC64; MNKIQQINDK ELQSGILSPH QSWHNEYKDN AYIYIGNLNR ELTEGDILTV FSEYGVPVDV ILSRDENTGE SQGFAYLKYE DQRSTILAVD NLNGFKIGGR ALKIDHTFYR PKRSLQKYYE AVKEELDRDI VSKNNAEKLI LAKKDQPN //