IST3_YEAST
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 03-AUG-2022, entry version 190.
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;
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).
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 nuclear pre-mRNA retention and efficient splicing. Required for MER1-
CC activated splicing. {ECO:0000269|PubMed:11287609,
CC ECO:0000269|PubMed:14973223, ECO:0000269|PubMed:15565172}.
CC -!- SUBUNIT: Component of the 45S U1.U2.U4/U6.U5 penta-snRNP particle, a
CC subcomplex of the spliceosome. 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. Belongs to the pre-mRNA retention and splicing (RES)
CC complex composed of at least BUD13, IST3 and PML1. Subunit of the U2
CC snRNP. Interacts with RDS3. {ECO:0000269|PubMed:11287609,
CC ECO:0000269|PubMed:11804584, ECO:0000269|PubMed:11884590,
CC ECO:0000269|PubMed:14517302, ECO:0000269|PubMed:15565172}.
CC -!- INTERACTION:
CC P40565; P46947: BUD13; NbExp=13; IntAct=EBI-25387, EBI-24073;
CC P40565; Q07930: PML1; NbExp=5; 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. {ECO:0000269|PubMed:15565172}.
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}.
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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 PDBsum; 2MKC; -.
DR PDBsum; 2MY2; -.
DR PDBsum; 2MY3; -.
DR PDBsum; 4UQT; -.
DR PDBsum; 5GM6; -.
DR PDBsum; 5LQW; -.
DR PDBsum; 5ZWM; -.
DR PDBsum; 5ZWO; -.
DR AlphaFoldDB; P40565; -.
DR BMRB; P40565; -.
DR SMR; P40565; -.
DR BioGRID; 34996; 402.
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 IntAct; P40565; 27.
DR MINT; P40565; -.
DR STRING; 4932.YIR005W; -.
DR MaxQB; P40565; -.
DR PaxDb; P40565; -.
DR PRIDE; P40565; -.
DR EnsemblFungi; YIR005W_mRNA; YIR005W; YIR005W.
DR GeneID; 854821; -.
DR KEGG; sce:YIR005W; -.
DR SGD; S000001444; IST3.
DR VEuPathDB; FungiDB:YIR005W; -.
DR eggNOG; KOG0126; Eukaryota.
DR GeneTree; ENSGT00890000139472; -.
DR HOGENOM; CLU_045495_5_0_1; -.
DR InParanoid; P40565; -.
DR OMA; GGKKSWH; -.
DR BioCyc; YEAST:G3O-31426-MON; -.
DR PRO; PR:P40565; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40565; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR GO; GO:0070274; C:RES complex; IDA:SGD.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0005686; C:U2 snRNP; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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; IC:ComplexPortal.
DR CDD; cd12411; RRM_ist3_like; 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; IPR000504; RRM_dom.
DR InterPro; IPR045844; RRM_Ist3-like.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
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 STRAND 27..29
FT /evidence="ECO:0007829|PDB:4UQT"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:2MKC"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:2MKC"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:2MKC"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:2MKC"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:2MKC"
FT STRAND 71..81
FT /evidence="ECO:0007829|PDB:2MKC"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:2MKC"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:2MKC"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:2MY3"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:2MKC"
SQ SEQUENCE 148 AA; 17098 MW; 9D51C3043AB823D2 CRC64;
MNKIQQINDK ELQSGILSPH QSWHNEYKDN AYIYIGNLNR ELTEGDILTV FSEYGVPVDV
ILSRDENTGE SQGFAYLKYE DQRSTILAVD NLNGFKIGGR ALKIDHTFYR PKRSLQKYYE
AVKEELDRDI VSKNNAEKLI LAKKDQPN
