EXOS4_HUMAN
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 03-AUG-2022, entry version 194.
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: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}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:17545563}. Nucleus
CC {ECO:0000269|PubMed:17545563}.
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}.
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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 SMR; Q9NPD3; -.
DR BioGRID; 120007; 171.
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 iPTMnet; Q9NPD3; -.
DR MetOSite; Q9NPD3; -.
DR PhosphoSitePlus; Q9NPD3; -.
DR SwissPalm; Q9NPD3; -.
DR BioMuta; EXOSC4; -.
DR DMDM; 14285756; -.
DR SWISS-2DPAGE; Q9NPD3; -.
DR EPD; Q9NPD3; -.
DR jPOST; Q9NPD3; -.
DR MassIVE; Q9NPD3; -.
DR MaxQB; Q9NPD3; -.
DR PaxDb; Q9NPD3; -.
DR PeptideAtlas; Q9NPD3; -.
DR PRIDE; Q9NPD3; -.
DR ProteomicsDB; 81973; -.
DR Antibodypedia; 14755; 180 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 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; GIAMYDY; -.
DR OrthoDB; 1394468at2759; -.
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; 765 hits in 1061 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 130 other tissues.
DR ExpressionAtlas; Q9NPD3; baseline and differential.
DR Genevisible; Q9NPD3; HS.
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); IC: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'-exoribonuclease 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 Gene3D; 3.30.230.70; -; 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_S5_D2-typ_fold.
DR Pfam; PF01138; RNase_PH; 1.
DR Pfam; PF03725; RNase_PH_C; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55666; SSF55666; 1.
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
