ID EXOS4_HUMAN Reviewed; 245 AA. AC Q9NPD3; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 203. DE RecName: Full=Exosome complex component RRP41; DE AltName: Full=Exosome component 4; DE AltName: Full=Ribosomal RNA-processing protein 41; DE AltName: Full=p12A; GN Name=EXOSC4; Synonyms=RRP41, SKI6; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION. RX PubMed=11110791; DOI=10.1074/jbc.m007603200; RA Brouwer R., Allmang C., Raijmakers R., van Aarssen Y., Egberts W.V., RA Petfalski E., van Venrooij W.J., Tollervey D., Pruijn G.J.M.; RT "Three novel components of the human exosome."; RL J. Biol. Chem. 276:6177-6184(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RA Bienvenut W.V.; RL Submitted (OCT-2004) to UniProtKB. RN [6] RP CHARACTERIZATION. 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE RNA EXOSOME RP CORE COMPLEX. RX PubMed=11719186; DOI=10.1016/s0092-8674(01)00578-5; RA Chen C.-Y., Gherzi R., Ong S.-E., Chan E.L., Raijmakers R., Pruijn G.J.M., RA Stoecklin G., Moroni C., Mann M., Karin M.; RT "AU binding proteins recruit the exosome to degrade ARE-containing mRNAs."; RL Cell 107:451-464(2001). RN [8] RP FUNCTION IN ARE-CONTAINING MRNA-BINDING. RX PubMed=16912217; DOI=10.1261/rna.144606; RA Anderson J.R., Mukherjee D., Muthukumaraswamy K., Moraes K.C., Wilusz C.J., RA Wilusz J.; RT "Sequence-specific RNA binding mediated by the RNase PH domain of RT components of the exosome."; RL RNA 12:1810-1816(2006). RN [9] RP FUNCTION IN MRNA DEGRADATION, AND SUBCELLULAR LOCATION. RX PubMed=17545563; DOI=10.1261/rna.575107; RA van Dijk E.L., Schilders G., Pruijn G.J.; RT "Human cell growth requires a functional cytoplasmic exosome, which is RT involved in various mRNA decay pathways."; RL RNA 13:1027-1035(2007). RN [10] RP FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY. RX PubMed=18172165; DOI=10.1101/gad.1622708; RA Mullen T.E., Marzluff W.F.; RT "Degradation of histone mRNA requires oligouridylation followed by RT decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to RT 5'."; RL Genes Dev. 22:50-65(2008). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP IDENTIFICATION IN THE RNA EXOSOME COMPLEX, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=20531389; DOI=10.1038/emboj.2010.122; RA Staals R.H., Bronkhorst A.W., Schilders G., Slomovic S., Schuster G., RA Heck A.J., Raijmakers R., Pruijn G.J.; RT "Dis3-like 1: a novel exoribonuclease associated with the human exosome."; RL EMBO J. 29:2358-2367(2010). RN [13] RP FUNCTION IN RRNA MATURATION. RX PubMed=20368444; DOI=10.1073/pnas.0910621107; RA Slomovic S., Fremder E., Staals R.H., Pruijn G.J., Schuster G.; RT "Addition of poly(A) and poly(A)-rich tails during RNA degradation in the RT cytoplasm of human cells."; RL Proc. Natl. Acad. Sci. U.S.A. 107:7407-7412(2010). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] RP FUNCTION IN DEAMINATION OF TRANSCRIBED DNA SUBSTRATE. RX PubMed=21255825; DOI=10.1016/j.cell.2011.01.001; RA Basu U., Meng F.L., Keim C., Grinstein V., Pefanis E., Eccleston J., RA Zhang T., Myers D., Wasserman C.R., Wesemann D.R., Januszyk K., RA Gregory R.I., Deng H., Lima C.D., Alt F.W.; RT "The RNA exosome targets the AID cytidine deaminase to both strands of RT transcribed duplex DNA substrates."; RL Cell 144:353-363(2011). RN [16] RP INTERACTION WITH DDX60. RX PubMed=21791617; DOI=10.1128/mcb.01368-10; RA Miyashita M., Oshiumi H., Matsumoto M., Seya T.; RT "DDX60, a DEXD/H box helicase, is a novel antiviral factor promoting RIG-I- RT like receptor-mediated signaling."; RL Mol. Cell. Biol. 31:3802-3819(2011). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [19] RP X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS), LACK OF CATALYTIC ACTIVITY, AND RP RECONSTITUTION OF THE RNA EXOSOME CORE COMPLEX. 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 [20] RP ERRATUM OF PUBMED:17174896. RA Liu Q., Greimann J.C., Lima C.D.; RL Cell 131:188-189(2007). RN [21] {ECO:0000305} RP SUBCELLULAR LOCATION. RX PubMed=36912080; DOI=10.1093/nar/gkad140; RA Chen Y., Li Y., Dai R.S., Savage J.C., Shinde U., Klimek J., David L.L., RA Young E.A., Hafner M., Sears R.C., Sun X.X., Dai M.S.; RT "The ubiquitin-specific protease USP36 SUMOylates EXOSC10 and promotes the RT nucleolar RNA exosome function in rRNA processing."; RL Nucleic Acids Res. 51:3934-3949(2023). RN [22] {ECO:0007744|PDB:6D6Q, ECO:0007744|PDB:6D6R} RP STRUCTURE BY ELECTRON MICROSCOPY (3.45 ANGSTROMS), AND SUBUNIT. RX PubMed=29906447; DOI=10.1016/j.cell.2018.05.041; RA Weick E.M., Puno M.R., Januszyk K., Zinder J.C., DiMattia M.A., Lima C.D.; RT "Helicase-Dependent RNA Decay Illuminated by a Cryo-EM Structure of a Human RT Nuclear RNA Exosome-MTR4 Complex."; RL Cell 173:1663-1677.e21(2018). 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 promoter-upstream transcripts (PROMPTs), and of mRNAs CC with processing defects, thereby limiting or excluding their export to CC the cytoplasm. The RNA exosome may be involved in Ig class switch CC recombination (CSR) and/or Ig variable region somatic hypermutation CC (SHM) by targeting AICDA deamination activity to transcribed dsDNA CC substrates. In the cytoplasm, the RNA exosome complex is involved in CC general mRNA turnover and specifically degrades inherently unstable CC mRNAs containing AU-rich elements (AREs) within their 3' untranslated CC regions, and in RNA surveillance pathways, preventing translation of CC aberrant mRNAs. It seems to be involved in degradation of histone mRNA. CC The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) CC is proposed to play a pivotal role in the binding and presentation of CC RNA for ribonucleolysis, and to serve as a scaffold for the association CC with catalytic subunits and accessory proteins or complexes. EXOSC4 CC binds to ARE-containing RNAs. {ECO:0000269|PubMed:16912217, CC ECO:0000269|PubMed:17545563, ECO:0000269|PubMed:18172165, CC ECO:0000269|PubMed:20368444, ECO:0000269|PubMed:21255825}. CC -!- SUBUNIT: Component of the RNA exosome complex (PubMed:29906447). CC Specifically part of the catalytically inactive RNA exosome core (Exo- CC 9) complex which is believed to associate with catalytic subunits CC EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA CC exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH CC domain-containing subunits specifically containing the heterodimers CC EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and peripheral S1 CC domain-containing components EXOSC1, EXOSC2 and EXOSC3 located on the CC top of the ring structure. Interacts with DDX60. CC {ECO:0000269|PubMed:11719186, ECO:0000269|PubMed:20531389, CC ECO:0000269|PubMed:21791617, ECO:0000269|PubMed:29906447}. CC -!- INTERACTION: CC Q9NPD3; Q9Y3B2: EXOSC1; NbExp=9; IntAct=EBI-371823, EBI-371892; CC Q9NPD3; Q01780: EXOSC10; NbExp=5; IntAct=EBI-371823, EBI-358236; CC Q9NPD3; Q13868: EXOSC2; NbExp=8; IntAct=EBI-371823, EBI-301735; CC Q9NPD3; Q9NQT5: EXOSC3; NbExp=7; IntAct=EBI-371823, EBI-371866; CC Q9NPD3; Q15024: EXOSC7; NbExp=6; IntAct=EBI-371823, EBI-371841; CC Q9NPD3; Q06265: EXOSC9; NbExp=7; IntAct=EBI-371823, EBI-347966; CC Q9NPD3; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-371823, EBI-739832; CC Q9NPD3; P56282: POLE2; NbExp=5; IntAct=EBI-371823, EBI-713847; CC Q9NPD3; O00560: SDCBP; NbExp=3; IntAct=EBI-371823, EBI-727004; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17545563, CC ECO:0000269|PubMed:36912080}. Nucleus, nucleolus CC {ECO:0000269|PubMed:17545563, ECO:0000269|PubMed:36912080}. Nucleus CC {ECO:0000269|PubMed:17545563, ECO:0000269|PubMed:36912080}. Nucleus, CC nucleoplasm {ECO:0000269|PubMed:36912080}. CC -!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000305}. CC -!- CAUTION: The six exosome core subunits containing a RNase PH-domain are CC not phosphorolytically active. {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; AF281133; AAF82134.1; -; mRNA. DR EMBL; AK000598; BAA91279.1; -; mRNA. DR EMBL; AC109322; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC002777; AAH02777.1; -; mRNA. DR CCDS; CCDS6414.1; -. DR RefSeq; NP_061910.1; NM_019037.2. DR PDB; 2NN6; X-ray; 3.35 A; B=2-245. DR PDB; 6D6Q; EM; 3.45 A; B=1-245. DR PDB; 6D6R; EM; 3.45 A; B=1-245. DR PDB; 6H25; EM; 3.80 A; B=1-245. DR PDBsum; 2NN6; -. DR PDBsum; 6D6Q; -. DR PDBsum; 6D6R; -. DR PDBsum; 6H25; -. DR AlphaFoldDB; Q9NPD3; -. DR EMDB; EMD-0127; -. DR EMDB; EMD-0128; -. DR EMDB; EMD-14515; -. DR EMDB; EMD-7808; -. DR EMDB; EMD-7809; -. DR SMR; Q9NPD3; -. DR BioGRID; 120007; 198. DR ComplexPortal; CPX-476; Nuclear exosome complex, DIS3-EXOSC10 variant. DR ComplexPortal; CPX-591; Nucleolar exosome complex, EXOSC10 variant. DR ComplexPortal; CPX-592; Cytoplasmic exosome complex, DIS3L variant. DR ComplexPortal; CPX-593; Exosome complex, DIS3 variant. DR ComplexPortal; CPX-600; Cytoplasmic exosome complex, DIS3L-EXOSC10 variant. DR CORUM; Q9NPD3; -. DR DIP; DIP-31165N; -. DR IntAct; Q9NPD3; 70. DR MINT; Q9NPD3; -. DR STRING; 9606.ENSP00000315476; -. DR MoonDB; Q9NPD3; Predicted. DR GlyGen; Q9NPD3; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NPD3; -. DR MetOSite; Q9NPD3; -. DR PhosphoSitePlus; Q9NPD3; -. DR SwissPalm; Q9NPD3; -. DR BioMuta; EXOSC4; -. DR DMDM; 14285756; -. DR EPD; Q9NPD3; -. DR jPOST; Q9NPD3; -. DR MassIVE; Q9NPD3; -. DR MaxQB; Q9NPD3; -. DR PaxDb; 9606-ENSP00000315476; -. DR PeptideAtlas; Q9NPD3; -. DR ProteomicsDB; 81973; -. DR Pumba; Q9NPD3; -. DR Antibodypedia; 14755; 201 antibodies from 27 providers. DR DNASU; 54512; -. DR Ensembl; ENST00000316052.6; ENSP00000315476.4; ENSG00000178896.9. DR GeneID; 54512; -. DR KEGG; hsa:54512; -. DR MANE-Select; ENST00000316052.6; ENSP00000315476.4; NM_019037.3; NP_061910.1. DR UCSC; uc003zau.4; human. DR AGR; HGNC:18189; -. DR CTD; 54512; -. DR DisGeNET; 54512; -. DR GeneCards; EXOSC4; -. DR HGNC; HGNC:18189; EXOSC4. DR HPA; ENSG00000178896; Tissue enhanced (testis). DR MIM; 606491; gene. DR neXtProt; NX_Q9NPD3; -. DR OpenTargets; ENSG00000178896; -. DR PharmGKB; PA134867931; -. DR VEuPathDB; HostDB:ENSG00000178896; -. DR eggNOG; KOG1068; Eukaryota. DR GeneTree; ENSGT00940000153348; -. DR HOGENOM; CLU_063514_0_0_1; -. DR InParanoid; Q9NPD3; -. DR OMA; RVICTAT; -. DR OrthoDB; 202892at2759; -. DR PhylomeDB; Q9NPD3; -. DR TreeFam; TF313915; -. DR PathwayCommons; Q9NPD3; -. DR Reactome; R-HSA-380994; ATF4 activates genes in response to endoplasmic reticulum stress. DR Reactome; R-HSA-429958; mRNA decay by 3' to 5' exoribonuclease. DR Reactome; R-HSA-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA. DR Reactome; R-HSA-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA. DR Reactome; R-HSA-450604; KSRP (KHSRP) binds and destabilizes mRNA. DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR SignaLink; Q9NPD3; -. DR SIGNOR; Q9NPD3; -. DR BioGRID-ORCS; 54512; 802 hits in 1142 CRISPR screens. DR ChiTaRS; EXOSC4; human. DR EvolutionaryTrace; Q9NPD3; -. DR GeneWiki; Exosome_component_4; -. DR GenomeRNAi; 54512; -. DR Pharos; Q9NPD3; Tbio. DR PRO; PR:Q9NPD3; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q9NPD3; Protein. DR Bgee; ENSG00000178896; Expressed in left testis and 132 other cell types or tissues. DR ExpressionAtlas; Q9NPD3; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0000791; C:euchromatin; IMP:UniProtKB. DR GO; GO:0000178; C:exosome (RNase complex); IDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0000176; C:nuclear exosome (RNase complex); IBA:GO_Central. DR GO; GO:0101019; C:nucleolar exosome (RNase complex); NAS:ComplexPortal. DR GO; GO:0005730; C:nucleolus; IDA:ComplexPortal. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; NAS:UniProtKB. DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:GO_Central. DR GO; GO:0051607; P:defense response to virus; IMP:MGI. DR GO; GO:0045006; P:DNA deamination; IDA:UniProtKB. DR GO; GO:0071044; P:histone mRNA catabolic process; IMP:UniProtKB. DR GO; GO:0000460; P:maturation of 5.8S rRNA; IMP:UniProtKB. DR GO; GO:0071028; P:nuclear mRNA surveillance; IMP:UniProtKB. DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:UniProtKB. DR GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IBA:GO_Central. DR GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IBA:GO_Central. DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB. DR GO; GO:0006401; P:RNA catabolic process; IDA:ComplexPortal. DR GO; GO:0006396; P:RNA processing; IDA:ComplexPortal. DR GO; GO:0016075; P:rRNA catabolic process; IBA:GO_Central. DR GO; GO:0006364; P:rRNA processing; NAS:UniProtKB. DR GO; GO:0034475; P:U4 snRNA 3'-end processing; IBA:GO_Central. DR CDD; cd11370; RNase_PH_RRP41; 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 PANTHER; PTHR11953; EXOSOME COMPLEX COMPONENT; 1. DR PANTHER; PTHR11953:SF0; EXOSOME COMPLEX COMPONENT RRP41; 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. DR SWISS-2DPAGE; Q9NPD3; -. DR Genevisible; Q9NPD3; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Exosome; KW Nucleus; Reference proteome; RNA-binding; rRNA processing. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT CHAIN 2..245 FT /note="Exosome complex component RRP41" FT /id="PRO_0000139958" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT STRAND 14..17 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 25..30 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 32..45 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 47..57 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 60..62 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 67..69 FT /evidence="ECO:0007829|PDB:6D6Q" FT STRAND 72..78 FT /evidence="ECO:0007829|PDB:2NN6" FT TURN 80..82 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 83..85 FT /evidence="ECO:0007829|PDB:2NN6" FT TURN 89..91 FT /evidence="ECO:0007829|PDB:2NN6" FT HELIX 94..109 FT /evidence="ECO:0007829|PDB:2NN6" FT HELIX 113..115 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 119..129 FT /evidence="ECO:0007829|PDB:2NN6" FT HELIX 134..148 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 158..165 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 168..172 FT /evidence="ECO:0007829|PDB:2NN6" FT HELIX 175..178 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 185..189 FT /evidence="ECO:0007829|PDB:2NN6" FT TURN 191..193 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 198..201 FT /evidence="ECO:0007829|PDB:2NN6" FT HELIX 210..239 FT /evidence="ECO:0007829|PDB:2NN6" SQ SEQUENCE 245 AA; 26383 MW; 7A24E97897DAF313 CRC64; MAGLELLSDQ GYRVDGRRAG ELRKIQARMG VFAQADGSAY IEQGNTKALA VVYGPHEIRG SRARALPDRA LVNCQYSSAT FSTGERKRRP HGDRKSCEMG LQLRQTFEAA ILTQLHPRSQ IDIYVQVLQA DGGTYAACVN AATLAVLDAG IPMRDFVCAC SAGFVDGTAL ADLSHVEEAA GGPQLALALL PASGQIALLE MDARLHEDHL ERVLEAAAQA ARDVHTLLDR VVRQHVREAS ILLGD //