ID   RRP45_YEAST             Reviewed;         305 AA.
AC   Q05636; D6VSR0;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 188.
DE   RecName: Full=Exosome complex component RRP45;
DE   AltName: Full=Ribosomal RNA-processing protein 45;
GN   Name=RRP45; OrderedLocusNames=YDR280W; ORFNames=D9954.1;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [2]
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   [3]
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   [4]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=10465791; DOI=10.1101/gad.13.16.2148;
RA   Allmang C., Petfalski E., Podtelejnikov A., Mann M., Tollervey D.,
RA   Mitchell P.;
RT   "The yeast exosome and human PM-Scl are related complexes of 3'-->5'
RT   exonucleases.";
RL   Genes Dev. 13:2148-2158(1999).
RN   [5]
RP   INTERACTION WITH LRP1.
RX   PubMed=12837249; DOI=10.1016/s0092-8674(03)00466-5;
RA   Peng W.-T., Robinson M.D., Mnaimneh S., Krogan N.J., Cagney G.,
RA   Morris Q.D., Davierwala A.P., Grigull J., Yang X., Zhang W., Mitsakakis N.,
RA   Ryan O.W., Datta N., Jojic V., Pal C., Canadien V., Richards D.P.,
RA   Beattie B., Wu L.F., Altschuler S.J., Roweis S., Frey B.J., Emili A.,
RA   Greenblatt J.F., Hughes T.R.;
RT   "A panoramic view of yeast noncoding RNA processing.";
RL   Cell 113:919-933(2003).
RN   [6]
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   [7]
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   [8]
RP   RECONSTITUTION OF THE RNA EXOSOME COMPLEX, AND LACK OF EXONUCLEASE
RP   ACTIVITY.
RX   PubMed=17174896; DOI=10.1016/j.cell.2006.10.037;
RA   Liu Q., Greimann J.C., Lima C.D.;
RT   "Reconstitution, activities, and structure of the eukaryotic RNA exosome.";
RL   Cell 127:1223-1237(2006).
RN   [9]
RP   ERRATUM OF PUBMED:17174896.
RA   Liu Q., Greimann J.C., Lima C.D.;
RL   Cell 131:188-189(2007).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION OF THE RNA EXOSOME COMPLEX,
RP   AND SUBUNIT.
RX   PubMed=17173052; DOI=10.1038/nsmb1184;
RA   Dziembowski A., Lorentzen E., Conti E., Seraphin B.;
RT   "A single subunit, Dis3, is essentially responsible for yeast exosome core
RT   activity.";
RL   Nat. Struct. Mol. Biol. 14:15-22(2007).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH SKI6 AND DIS3.
RX   PubMed=19879841; DOI=10.1016/j.cell.2009.08.042;
RA   Bonneau F., Basquin J., Ebert J., Lorentzen E., Conti E.;
RT   "The yeast exosome functions as a macromolecular cage to channel RNA
RT   substrates for degradation.";
RL   Cell 139:547-559(2009).
CC   -!- FUNCTION: Non-catalytic component of the RNA exosome complex which has
CC       3'->5' exoribonuclease activity and participates in a multitude of
CC       cellular RNA processing and degradation events. In the nucleus, the RNA
CC       exosome complex is involved in proper maturation of stable RNA species
CC       such as rRNA, snRNA and snoRNA, in the elimination of RNA processing
CC       by-products and non-coding 'pervasive' transcripts, such as antisense
CC       RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with
CC       processing defects, thereby limiting or excluding their export to the
CC       cytoplasm. In the cytoplasm, the RNA exosome complex is involved in
CC       general mRNA turnover and in RNA surveillance pathways, preventing
CC       translation of aberrant mRNAs. The catalytic inactive RNA exosome core
CC       complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the
CC       binding and presentation of RNA for ribonucleolysis, and to serve as a
CC       scaffold for the association with catalytic subunits and accessory
CC       proteins or complexes. RRP45 is part of the hexameric ring of RNase PH
CC       domain-containing subunits proposed to form a central channel which
CC       threads RNA substrates for degradation. {ECO:0000269|PubMed:10465791,
CC       ECO:0000269|PubMed:17173052}.
CC   -!- SUBUNIT: Component of the RNA exosome complex. Specifically part of the
CC       catalytically inactive RNA exosome core (Exo-9) complex which
CC       associates with catalytic subunits DIS3 and RRP6 in cytoplasmic- and
CC       nuclear-specific RNA exosome complex forms. Exo-9 is formed by a
CC       hexameric ring of RNase PH domain-containing subunits and peripheral S1
CC       domain-containing components CSL4, RRP4 and RRP40 located on the top of
CC       the ring structure. Interacts with LRP1. {ECO:0000269|PubMed:10465791,
CC       ECO:0000269|PubMed:12837249, ECO:0000269|PubMed:17173052,
CC       ECO:0000269|PubMed:19879841}.
CC   -!- INTERACTION:
CC       Q05636; P53859: CSL4; NbExp=15; IntAct=EBI-1810, EBI-1731;
CC       Q05636; P46948: SKI6; NbExp=11; IntAct=EBI-1810, EBI-1788;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus,
CC       nucleolus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 4800 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000305}.
CC   -!- CAUTION: According to PubMed:17173052 and PubMed:17174896, only
CC       DIS3/RRP44 subunit of the exosome core has exonuclease activity.
CC       {ECO:0000305}.
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DR   EMBL; U51030; AAB64446.1; -; Genomic_DNA.
DR   EMBL; AY557748; AAS56074.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12120.1; -; Genomic_DNA.
DR   PIR; S70136; S70136.
DR   RefSeq; NP_010566.1; NM_001180588.1.
DR   PDB; 2WP8; X-ray; 3.00 A; A=1-305.
DR   PDB; 4IFD; X-ray; 2.80 A; A=2-305.
DR   PDB; 4OO1; X-ray; 3.30 A; A=1-305.
DR   PDB; 5C0W; X-ray; 4.60 A; A=1-305.
DR   PDB; 5C0X; X-ray; 3.81 A; A=1-305.
DR   PDB; 5G06; EM; 4.20 A; A=1-305.
DR   PDB; 5JEA; X-ray; 2.65 A; A=1-305.
DR   PDB; 5K36; X-ray; 3.10 A; A=1-305.
DR   PDB; 5OKZ; X-ray; 3.20 A; A/K/U/e=1-305.
DR   PDB; 5VZJ; X-ray; 3.30 A; A=1-305.
DR   PDB; 6FSZ; EM; 4.60 A; AA=3-305.
DR   PDB; 6LQS; EM; 3.80 A; R5=1-305.
DR   PDB; 7AJT; EM; 4.60 A; EB=1-305.
DR   PDB; 7AJU; EM; 3.80 A; EB=1-305.
DR   PDB; 7D4I; EM; 4.00 A; R5=1-305.
DR   PDBsum; 2WP8; -.
DR   PDBsum; 4IFD; -.
DR   PDBsum; 4OO1; -.
DR   PDBsum; 5C0W; -.
DR   PDBsum; 5C0X; -.
DR   PDBsum; 5G06; -.
DR   PDBsum; 5JEA; -.
DR   PDBsum; 5K36; -.
DR   PDBsum; 5OKZ; -.
DR   PDBsum; 5VZJ; -.
DR   PDBsum; 6FSZ; -.
DR   PDBsum; 6LQS; -.
DR   PDBsum; 7AJT; -.
DR   PDBsum; 7AJU; -.
DR   PDBsum; 7D4I; -.
DR   AlphaFoldDB; Q05636; -.
DR   EMDB; EMD-0952; -.
DR   EMDB; EMD-11807; -.
DR   EMDB; EMD-11808; -.
DR   EMDB; EMD-30574; -.
DR   EMDB; EMD-4301; -.
DR   SMR; Q05636; -.
DR   BioGRID; 32333; 145.
DR   ComplexPortal; CPX-599; Nuclear/nucleolar exosome complex, DIS3-RRP6 variant.
DR   ComplexPortal; CPX-603; Cytoplasmic exosome complex, DIS3 variant.
DR   DIP; DIP-2084N; -.
DR   IntAct; Q05636; 30.
DR   MINT; Q05636; -.
DR   STRING; 4932.YDR280W; -.
DR   MaxQB; Q05636; -.
DR   PaxDb; 4932-YDR280W; -.
DR   PeptideAtlas; Q05636; -.
DR   EnsemblFungi; YDR280W_mRNA; YDR280W; YDR280W.
DR   GeneID; 851874; -.
DR   KEGG; sce:YDR280W; -.
DR   AGR; SGD:S000002688; -.
DR   SGD; S000002688; RRP45.
DR   VEuPathDB; FungiDB:YDR280W; -.
DR   eggNOG; KOG1614; Eukaryota.
DR   GeneTree; ENSGT00950000183130; -.
DR   HOGENOM; CLU_038194_0_0_1; -.
DR   InParanoid; Q05636; -.
DR   OMA; GPQFENG; -.
DR   OrthoDB; 128403at2759; -.
DR   BioCyc; YEAST:G3O-29845-MONOMER; -.
DR   Reactome; R-SCE-429958; mRNA decay by 3' to 5' exoribonuclease.
DR   Reactome; R-SCE-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR   Reactome; R-SCE-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR   Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   BioGRID-ORCS; 851874; 7 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; Q05636; -.
DR   PRO; PR:Q05636; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q05636; Protein.
DR   GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IDA:SGD.
DR   GO; GO:0000178; C:exosome (RNase complex); IPI:ComplexPortal.
DR   GO; GO:0000176; C:nuclear exosome (RNase complex); IDA:SGD.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0043928; P:exonucleolytic catabolism of deadenylated mRNA; IBA:GO_Central.
DR   GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0071028; P:nuclear mRNA surveillance; IBA:GO_Central.
DR   GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IBA:GO_Central.
DR   GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IMP:SGD.
DR   GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IDA:SGD.
DR   GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IBA:GO_Central.
DR   GO; GO:0006401; P:RNA catabolic process; IDA:ComplexPortal.
DR   GO; GO:0006396; P:RNA processing; IDA:ComplexPortal.
DR   GO; GO:0034473; P:U1 snRNA 3'-end processing; IMP:SGD.
DR   GO; GO:0034475; P:U4 snRNA 3'-end processing; IMP:SGD.
DR   GO; GO:0034476; P:U5 snRNA 3'-end processing; IMP:SGD.
DR   CDD; cd11368; RNase_PH_RRP45; 1.
DR   Gene3D; 3.30.230.70; GHMP Kinase, N-terminal domain; 1.
DR   InterPro; IPR001247; ExoRNase_PH_dom1.
DR   InterPro; IPR015847; ExoRNase_PH_dom2.
DR   InterPro; IPR036345; ExoRNase_PH_dom2_sf.
DR   InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR033100; Rrp45.
DR   PANTHER; PTHR11097:SF14; EXOSOME COMPLEX COMPONENT RRP45; 1.
DR   PANTHER; PTHR11097; EXOSOME COMPLEX EXONUCLEASE RIBOSOMAL RNA PROCESSING PROTEIN; 1.
DR   Pfam; PF01138; RNase_PH; 1.
DR   Pfam; PF03725; RNase_PH_C; 1.
DR   SUPFAM; SSF55666; Ribonuclease PH domain 2-like; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Exosome; Nucleus; Reference proteome; RNA-binding;
KW   rRNA processing.
FT   CHAIN           1..305
FT                   /note="Exosome complex component RRP45"
FT                   /id="PRO_0000139974"
FT   HELIX           9..20
FT                   /evidence="ECO:0007829|PDB:5JEA"
FT   STRAND          36..40
FT                   /evidence="ECO:0007829|PDB:5JEA"
FT   STRAND          46..51
FT                   /evidence="ECO:0007829|PDB:5JEA"
FT   STRAND          54..65
FT                   /evidence="ECO:0007829|PDB:5JEA"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:5OKZ"
FT   STRAND          76..80
FT                   /evidence="ECO:0007829|PDB:5JEA"
FT   HELIX           85..87
FT                   /evidence="ECO:0007829|PDB:4IFD"
FT   HELIX           99..112
FT                   /evidence="ECO:0007829|PDB:5JEA"
FT   TURN            113..116
FT                   /evidence="ECO:0007829|PDB:5JEA"
FT   STRAND          123..126
FT                   /evidence="ECO:0007829|PDB:5JEA"
FT   TURN            127..129
FT                   /evidence="ECO:0007829|PDB:5JEA"
FT   STRAND          130..142
FT                   /evidence="ECO:0007829|PDB:5JEA"
FT   HELIX           147..161
FT                   /evidence="ECO:0007829|PDB:5JEA"
FT   STRAND          167..170
FT                   /evidence="ECO:0007829|PDB:5JEA"
FT   STRAND          173..176
FT                   /evidence="ECO:0007829|PDB:5JEA"
FT   TURN            179..181
FT                   /evidence="ECO:0007829|PDB:5JEA"
FT   STRAND          194..201
FT                   /evidence="ECO:0007829|PDB:5JEA"
FT   HELIX           206..211
FT                   /evidence="ECO:0007829|PDB:5JEA"
FT   STRAND          218..222
FT                   /evidence="ECO:0007829|PDB:5JEA"
FT   HELIX           225..228
FT                   /evidence="ECO:0007829|PDB:5JEA"
FT   STRAND          232..239
FT                   /evidence="ECO:0007829|PDB:5JEA"
FT   STRAND          243..257
FT                   /evidence="ECO:0007829|PDB:5JEA"
FT   HELIX           258..298
FT                   /evidence="ECO:0007829|PDB:5JEA"
FT   STRAND          299..302
FT                   /evidence="ECO:0007829|PDB:2WP8"
SQ   SEQUENCE   305 AA;  33962 MW;  65C9DB5A63678F2D CRC64;
     MAKDIEISAS ESKFILEALR QNYRLDGRSF DQFRDVEITF GKEFGDVSVK MGNTKVHCRI
     SCQIAQPYED RPFEGLFVIS TEISPMAGSQ FENGNITGED EVLCSRIIEK SVRRSGALDV
     EGLCIVAGSK CWAVRADVHF LDCDGGFIDA SCIAVMAGLM HFKKPDITVH GEQIIVHPVN
     EREPVPLGIL HIPICVTFSF FNPQDTEENI KGETNSEISI IDATLKEELL RDGVLTVTLN
     KNREVVQVSK AGGLPMDALT LMKCCHEAYS IIEKITDQIL QLLKEDSEKR NKYAAMLTSE
     NAREI
//