ID RRP46_YEAST Reviewed; 223 AA. AC P53256; Q6TQU1; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 2. DT 20-APR-2010, entry version 80. DE RecName: Full=Exosome complex component RRP46; DE AltName: Full=Ribosomal RNA-processing protein 46; GN Name=RRP46; OrderedLocusNames=YGR095C; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomyceta; OC Saccharomycotina; Saccharomycetes; Saccharomycetales; OC Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX MEDLINE=97313265; PubMed=9169869; RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., RA Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., RA Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., RA Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E., RA Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., RA Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., RA Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., RA Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., RA Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., RA Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., RA Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., RA Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., RA Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., RA Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., RA Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., RA Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., RA Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., RA Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., RA Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., RA van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., RA Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., RA Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., RA Zollner A., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."; RL Nature 387:81-84(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-67. RC STRAIN=ATCC 204511 / S288c / AB972; RA Kennedy M.C., Dietrich F.S.; RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP FUNCTION, AND IDENTIFICATION IN THE EXOSOME COMPLEX BY MASS RP SPECTROMETRY. RX MEDLINE=99396719; PubMed=10465791; 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 [4] RP INTERACTION WITH LRP1. RX MEDLINE=22721450; 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., RA Mitsakakis N., Ryan O.W., Datta N., Jojic V., Pal C., Canadien V., RA Richards D.P., Beattie B., Wu L.F., Altschuler S.J., Roweis S., RA Frey B.J., Emili A., Greenblatt J.F., Hughes T.R.; RT "A panoramic view of yeast noncoding RNA processing."; RL Cell 113:919-933(2003). RN [5] RP IDENTIFICATION OF PROBABLE INITIATION SITE. RX MEDLINE=22633889; PubMed=12748633; DOI=10.1038/nature01644; RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.; RT "Sequencing and comparison of yeast species to identify genes and RT regulatory elements."; RL Nature 423:241-254(2003). RN [6] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923954; 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 MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [8] RP LACK OF EXONUCLEASE ACTIVITY, AND SUBUNIT. 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 RT exosome."; RL Cell 127:1223-1237(2006). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION OF THE RP EXOSOME WITH RRP6 AND SKI7, 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 RT core activity."; RL Nat. Struct. Mol. Biol. 14:15-22(2007). CC -!- FUNCTION: Component of the exosome 3'->5' exoribonuclease complex CC but does not have exonuclease activity. As part of the exosome, CC required for the 3'-processing of the 7S pre-RNA to the mature CC 5.8S rRNA and for mRNA decay. CC -!- SUBUNIT: Component of the exosome multienzyme ribonuclease complex CC composed of 10 core proteins: the ring-forming non-catalytic CC subunits CSL4, MTR3, RRP4, RRP40, RRP42, RRP43, RRP45, RRP46 and CC SKI6/RRP41, and the catalytic subunit DIS3/RRP44. In the nucleus, CC exosome core is associated with at least RRP6 and LRP1/RRP47. CC Exosome nine subunit ring structure interacts with SKI7. Interacts CC with LRP1. CC -!- INTERACTION: CC P20449:DBP5; NbExp=1; IntAct=EBI-1842, EBI-5617; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. CC -!- MISCELLANEOUS: Present with 10800 molecules/cell in log phase SD CC medium. CC -!- SIMILARITY: Belongs to the RNase PH family. CC -!- CAUTION: According to PubMed:17173052 and PubMed:17174896, only CC DIS3/RRP44 subunit of the exosome core has exonuclease activity. CC -!- SEQUENCE CAUTION: CC Sequence=CAA97098.1; Type=Erroneous initiation; 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; Z72880; CAA97098.1; ALT_INIT; Genomic_DNA. DR EMBL; AY389297; AAQ97229.1; -; mRNA. DR PIR; S64390; S64390. DR RefSeq; NP_011609.2; -. DR DIP; DIP-6838N; -. DR IntAct; P53256; 26. DR MINT; MINT-614217; -. DR STRING; P53256; -. DR PeptideAtlas; P53256; -. DR Ensembl; YGR095C; YGR095C; YGR095C; Saccharomyces cerevisiae. DR GeneID; 852987; -. DR GenomeReviews; Y13135_GR; YGR095C. DR KEGG; sce:YGR095C; -. DR NMPDR; fig|4932.3.peg.2726; -. DR CYGD; YGR095c; -. DR SGD; S000003327; RRP46. DR eggNOG; fuNOG09954; -. DR HOGENOM; HBG396339; -. DR OMA; PIEPKAR; -. DR OrthoDB; EOG9VT7DM; -. DR PhylomeDB; P53256; -. DR NextBio; 972806; -. DR ArrayExpress; P53256; -. DR Genevestigator; P53256; -. DR GermOnline; YGR095C; Saccharomyces cerevisiae. DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IDA:SGD. DR GO; GO:0000176; C:nuclear exosome (RNase complex); IDA:SGD. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0000467; P:exonucleolytic trimming to generate mature ...; IMP:SGD. DR GO; GO:0070651; P:nonfunctional rRNA decay; IC:SGD. DR GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA cata...; IMP:SGD. DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA cata...; IMP:SGD. DR GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA cata...; IDA:SGD. DR GO; GO:0070478; P:nuclear-transcribed mRNA catabolic process,...; IC:SGD. DR GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process,...; IC:SGD. DR GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end pro...; IC:SGD. DR InterPro; IPR001247; ExoRNase_PH_dom1. DR InterPro; IPR015847; ExoRNase_PH_dom2. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR Pfam; PF01138; RNase_PH; 1. DR Pfam; PF03725; RNase_PH_C; 1. DR SUPFAM; SSF55666; 3_ExoRNase; 1. DR SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Exosome; Nucleus; RNA-binding; KW rRNA processing. FT CHAIN 1 223 Exosome complex component RRP46. FT /FTId=PRO_0000139978. SQ SEQUENCE 223 AA; 24407 MW; F1307E0EE4FC3133 CRC64; MSVQAEIGIL DHVDGSSEFV SQDTKVICSV TGPIEPKARQ ELPTQLALEI IVRPAKGVAT TREKVLEDKL RAVLTPLITR HCYPRQLCQI TCQILESGED EAEFSLRELS CCINAAFLAL VDAGIALNSM CASIPIAIIK DTSDIIVDPT AEQLKISLSV HTLALEFVNG GKVVKNVLLL DSNGDFNEDQ LFSLLELGEQ KCQELVTNIR RIIQDNISPR LVV //