ID EXOS8_HUMAN Reviewed; 276 AA. AC Q96B26; O43480; Q5TBA5; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 199. DE RecName: Full=Exosome complex component RRP43; DE AltName: Full=Exosome component 8; DE AltName: Full=Opa-interacting protein 2; DE Short=OIP-2; DE AltName: Full=Ribosomal RNA-processing protein 43; DE AltName: Full=p9; GN Name=EXOSC8; Synonyms=OIP2, RRP43; 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 [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Uterus; 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-276. RX PubMed=9466265; DOI=10.1046/j.1365-2958.1998.00670.x; RA Williams J.M., Chen G.-C., Zhu L., Rest R.F.; RT "Using the yeast two-hybrid system to identify human epithelial cell RT proteins that bind gonococcal Opa proteins: intracellular gonococci bind RT pyruvate kinase via their Opa proteins and require host pyruvate for RT growth."; RL Mol. Microbiol. 27:171-186(1998). RN [5] 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 [6] RP PROTEIN INTERACTION. RX PubMed=12419256; DOI=10.1016/s0022-2836(02)00947-6; RA Raijmakers R., Vree Egberts W., van Venrooij W.J., Pruijn G.J.M.; RT "Protein-protein interactions between human exosome components support the RT assembly of RNase PH-type subunits into a six-membered PNPase-like ring."; RL J. Mol. Biol. 323:653-663(2002). RN [7] RP PROTEIN INTERACTION. RX PubMed=15231747; DOI=10.1101/gr.2122004; RA Lehner B., Sanderson C.M.; RT "A protein interaction framework for human mRNA degradation."; RL Genome Res. 14:1315-1323(2004). 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 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 [11] 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 [12] 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 [13] RP INVOLVEMENT IN PCH1C, AND VARIANTS PCH1C VAL-2 AND THR-272. RX PubMed=24989451; DOI=10.1038/ncomms5287; RA Boczonadi V., Muller J.S., Pyle A., Munkley J., Dor T., Quartararo J., RA Ferrero I., Karcagi V., Giunta M., Polvikoski T., Birchall D., RA Princzinger A., Cinnamon Y., Lutzkendorf S., Piko H., Reza M., Florez L., RA Santibanez-Koref M., Griffin H., Schuelke M., Elpeleg O., Kalaydjieva L., RA Lochmuller H., Elliott D.J., Chinnery P.F., Edvardson S., Horvath R.; RT "EXOSC8 mutations alter mRNA metabolism and cause hypomyelination with RT spinal muscular atrophy and cerebellar hypoplasia."; RL Nat. Commun. 5:4287-4287(2014). RN [14] 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 [15] RP ERRATUM OF PUBMED:17174896. RA Liu Q., Greimann J.C., Lima C.D.; RL Cell 131:188-189(2007). RN [16] {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. EXOSC8 CC binds to ARE-containing RNAs. {ECO:0000269|PubMed:16912217, CC ECO:0000269|PubMed:17545563}. 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. Binds outer membrane protein opap from CC Neisseria gonorrhoeae. {ECO:0000269|PubMed:11719186, CC ECO:0000269|PubMed:20531389, ECO:0000269|PubMed:29906447}. CC -!- INTERACTION: CC Q96B26; Q8WTP8: AEN; NbExp=3; IntAct=EBI-371922, EBI-8637627; CC Q96B26; P15336: ATF2; NbExp=3; IntAct=EBI-371922, EBI-1170906; CC Q96B26; Q6P5X5: C22orf39; NbExp=3; IntAct=EBI-371922, EBI-7317823; CC Q96B26; Q8NE01: CNNM3; NbExp=3; IntAct=EBI-371922, EBI-741032; CC Q96B26; Q86Y22: COL23A1; NbExp=3; IntAct=EBI-371922, EBI-373279; CC Q96B26; P20674: COX5A; NbExp=3; IntAct=EBI-371922, EBI-715032; CC Q96B26; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-371922, EBI-742054; CC Q96B26; Q9BVJ7: DUSP23; NbExp=12; IntAct=EBI-371922, EBI-724940; CC Q96B26; Q9Y3B2: EXOSC1; NbExp=7; IntAct=EBI-371922, EBI-371892; CC Q96B26; Q9NQT5: EXOSC3; NbExp=5; IntAct=EBI-371922, EBI-371866; CC Q96B26; Q9NQT4: EXOSC5; NbExp=22; IntAct=EBI-371922, EBI-371876; CC Q96B26; Q96B26: EXOSC8; NbExp=5; IntAct=EBI-371922, EBI-371922; CC Q96B26; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-371922, EBI-7225287; CC Q96B26; Q86YD7: FAM90A1; NbExp=6; IntAct=EBI-371922, EBI-6658203; CC Q96B26; Q9NU39: FOXD4L1; NbExp=3; IntAct=EBI-371922, EBI-11320806; CC Q96B26; Q14331: FRG1; NbExp=3; IntAct=EBI-371922, EBI-2515248; CC Q96B26; P55040: GEM; NbExp=3; IntAct=EBI-371922, EBI-744104; CC Q96B26; Q9GZV7: HAPLN2; NbExp=3; IntAct=EBI-371922, EBI-11956675; CC Q96B26; P17482: HOXB9; NbExp=3; IntAct=EBI-371922, EBI-745290; CC Q96B26; Q0VD86: INCA1; NbExp=3; IntAct=EBI-371922, EBI-6509505; CC Q96B26; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-371922, EBI-2556193; CC Q96B26; Q14654: KCNJ11; NbExp=3; IntAct=EBI-371922, EBI-2866553; CC Q96B26; P61968: LMO4; NbExp=3; IntAct=EBI-371922, EBI-2798728; CC Q96B26; Q8TBB1: LNX1; NbExp=6; IntAct=EBI-371922, EBI-739832; CC Q96B26; Q9Y4Z0: LSM4; NbExp=3; IntAct=EBI-371922, EBI-372521; CC Q96B26; Q96GV9: MACIR; NbExp=3; IntAct=EBI-371922, EBI-2350695; CC Q96B26; Q8NDC4: MORN4; NbExp=3; IntAct=EBI-371922, EBI-10269566; CC Q96B26; Q8WVZ3: MORN4; NbExp=3; IntAct=EBI-371922, EBI-10277137; CC Q96B26; Q9NP98: MYOZ1; NbExp=3; IntAct=EBI-371922, EBI-744402; CC Q96B26; Q14511-2: NEDD9; NbExp=3; IntAct=EBI-371922, EBI-11746523; CC Q96B26; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-371922, EBI-741158; CC Q96B26; Q01804: OTUD4; NbExp=6; IntAct=EBI-371922, EBI-1054396; CC Q96B26; Q96BD5: PHF21A; NbExp=3; IntAct=EBI-371922, EBI-745085; CC Q96B26; O75928-2: PIAS2; NbExp=3; IntAct=EBI-371922, EBI-348567; CC Q96B26; Q8WUT1: POLDIP3; NbExp=3; IntAct=EBI-371922, EBI-10276663; CC Q96B26; Q9Y272: RASD1; NbExp=3; IntAct=EBI-371922, EBI-740818; CC Q96B26; Q04864: REL; NbExp=3; IntAct=EBI-371922, EBI-307352; CC Q96B26; P40937: RFC5; NbExp=3; IntAct=EBI-371922, EBI-712376; CC Q96B26; O95059: RPP14; NbExp=3; IntAct=EBI-371922, EBI-366542; CC Q96B26; Q9BVN2: RUSC1; NbExp=6; IntAct=EBI-371922, EBI-6257312; CC Q96B26; P28702-3: RXRB; NbExp=3; IntAct=EBI-371922, EBI-16429492; CC Q96B26; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-371922, EBI-10269374; CC Q96B26; O95863: SNAI1; NbExp=3; IntAct=EBI-371922, EBI-1045459; CC Q96B26; P14678-2: SNRPB; NbExp=3; IntAct=EBI-371922, EBI-372475; CC Q96B26; P09234: SNRPC; NbExp=3; IntAct=EBI-371922, EBI-766589; CC Q96B26; Q5TAL4: SNRPC; NbExp=3; IntAct=EBI-371922, EBI-10246938; CC Q96B26; O14512: SOCS7; NbExp=3; IntAct=EBI-371922, EBI-1539606; CC Q96B26; Q9H0A9-2: SPATC1L; NbExp=3; IntAct=EBI-371922, EBI-11995806; CC Q96B26; Q15560: TCEA2; NbExp=3; IntAct=EBI-371922, EBI-710310; CC Q96B26; Q86VL0: TCEA2; NbExp=3; IntAct=EBI-371922, EBI-10259904; CC Q96B26; Q01664: TFAP4; NbExp=6; IntAct=EBI-371922, EBI-2514218; CC Q96B26; Q9BRA2: TXNDC17; NbExp=6; IntAct=EBI-371922, EBI-1055906; CC Q96B26; O14530: TXNDC9; NbExp=6; IntAct=EBI-371922, EBI-707554; CC Q96B26; O75604: USP2; NbExp=3; IntAct=EBI-371922, EBI-743272; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17545563}. Nucleus CC {ECO:0000269|PubMed:17545563}. Nucleus, nucleolus {ECO:0000250}. CC -!- DISEASE: Pontocerebellar hypoplasia 1C (PCH1C) [MIM:616081]: A severe CC autosomal recessive neurodegenerative disease characterized by CC cerebellar and corpus callosum hypoplasia, abnormal myelination of the CC central nervous system, and spinal motor neuron disease. Affected CC individuals manifest failure to thrive, severe muscle weakness, CC spasticity and psychomotor retardation. Vision and hearing are CC impaired. {ECO:0000269|PubMed:24989451}. Note=The disease is caused by CC variants affecting the gene represented in this entry. EXOSC8 CC dysfunction causes myelin disruption through an imbalanced supply of CC myelin proteins due to dysregulation of their ARE-containing mRNAs CC (PubMed:24989451). {ECO:0000269|PubMed:24989451}. 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 -!- SEQUENCE CAUTION: CC Sequence=EAX08581.1; Type=Erroneous gene model prediction; Evidence={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; AL138706; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471075; EAX08581.1; ALT_SEQ; Genomic_DNA. DR EMBL; BC020773; AAH20773.1; -; mRNA. DR EMBL; AF025438; AAC39558.1; -; mRNA. DR CCDS; CCDS31958.1; -. DR RefSeq; NP_852480.1; NM_181503.2. DR PDB; 2NN6; X-ray; 3.35 A; C=1-276. DR PDB; 6D6Q; EM; 3.45 A; C=1-276. DR PDB; 6D6R; EM; 3.45 A; C=1-276. DR PDB; 6H25; EM; 3.80 A; C=1-276. DR PDBsum; 2NN6; -. DR PDBsum; 6D6Q; -. DR PDBsum; 6D6R; -. DR PDBsum; 6H25; -. DR AlphaFoldDB; Q96B26; -. DR EMDB; EMD-0127; -. DR EMDB; EMD-0128; -. DR EMDB; EMD-7808; -. DR EMDB; EMD-7809; -. DR SMR; Q96B26; -. DR BioGRID; 116468; 202. 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; Q96B26; -. DR DIP; DIP-31133N; -. DR IntAct; Q96B26; 99. DR MINT; Q96B26; -. DR STRING; 9606.ENSP00000374354; -. DR GlyGen; Q96B26; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q96B26; -. DR PhosphoSitePlus; Q96B26; -. DR SwissPalm; Q96B26; -. DR BioMuta; EXOSC8; -. DR DMDM; 21759409; -. DR EPD; Q96B26; -. DR jPOST; Q96B26; -. DR MassIVE; Q96B26; -. DR MaxQB; Q96B26; -. DR PaxDb; 9606-ENSP00000374354; -. DR PeptideAtlas; Q96B26; -. DR ProteomicsDB; 76038; -. DR Pumba; Q96B26; -. DR TopDownProteomics; Q96B26; -. DR Antibodypedia; 23142; 169 antibodies from 27 providers. DR DNASU; 11340; -. DR Ensembl; ENST00000389704.4; ENSP00000374354.3; ENSG00000120699.14. DR GeneID; 11340; -. DR KEGG; hsa:11340; -. DR MANE-Select; ENST00000389704.4; ENSP00000374354.3; NM_181503.3; NP_852480.1. DR UCSC; uc001uwa.5; human. DR AGR; HGNC:17035; -. DR CTD; 11340; -. DR DisGeNET; 11340; -. DR GeneCards; EXOSC8; -. DR HGNC; HGNC:17035; EXOSC8. DR HPA; ENSG00000120699; Low tissue specificity. DR MalaCards; EXOSC8; -. DR MIM; 606019; gene. DR MIM; 616081; phenotype. DR neXtProt; NX_Q96B26; -. DR OpenTargets; ENSG00000120699; -. DR Orphanet; 2254; Pontocerebellar hypoplasia type 1. DR PharmGKB; PA134922251; -. DR VEuPathDB; HostDB:ENSG00000120699; -. DR eggNOG; KOG1613; Eukaryota. DR GeneTree; ENSGT00950000183130; -. DR HOGENOM; CLU_038194_3_1_1; -. DR InParanoid; Q96B26; -. DR OMA; RIWYQPP; -. DR OrthoDB; 21598at2759; -. DR PhylomeDB; Q96B26; -. DR TreeFam; TF320415; -. DR PathwayCommons; Q96B26; -. 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; Q96B26; -. DR SIGNOR; Q96B26; -. DR BioGRID-ORCS; 11340; 744 hits in 1184 CRISPR screens. DR EvolutionaryTrace; Q96B26; -. DR GeneWiki; Exosome_component_8; -. DR GenomeRNAi; 11340; -. DR Pharos; Q96B26; Tbio. DR PRO; PR:Q96B26; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q96B26; Protein. DR Bgee; ENSG00000120699; Expressed in ventricular zone and 209 other cell types or tissues. DR ExpressionAtlas; Q96B26; baseline and differential. DR GO; GO:0005694; C:chromosome; IDA:HPA. 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:0000178; C:exosome (RNase complex); IDA:UniProtKB. DR GO; GO:0001650; C:fibrillar center; IDA:HPA. 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:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:GO_Central. 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); IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0034475; P:U4 snRNA 3'-end processing; IBA:GO_Central. DR GO; GO:0034476; P:U5 snRNA 3'-end processing; IBA:GO_Central. DR CDD; cd11369; RNase_PH_RRP43; 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; IPR033196; Rrp43. DR PANTHER; PTHR11097:SF9; EXOSOME COMPLEX COMPONENT RRP43; 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. DR SWISS-2DPAGE; Q96B26; -. DR Genevisible; Q96B26; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Disease variant; Exosome; KW Neurodegeneration; Nucleus; Reference proteome; RNA-binding; KW rRNA processing. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..276 FT /note="Exosome complex component RRP43" FT /id="PRO_0000139967" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22814378" FT VARIANT 2 FT /note="A -> V (in PCH1C; dbSNP:rs606231285)" FT /evidence="ECO:0000269|PubMed:24989451" FT /id="VAR_072558" FT VARIANT 272 FT /note="S -> T (in PCH1C; dbSNP:rs36027220)" FT /evidence="ECO:0000269|PubMed:24989451" FT /id="VAR_072559" FT CONFLICT 265..276 FT /note="LMDEVIKSMKPK -> TDG (in Ref. 4; AAC39558)" FT /evidence="ECO:0000305" FT HELIX 11..19 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 37..39 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 43..53 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 56..66 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 71..73 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 80..84 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 87..89 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:2NN6" FT HELIX 100..116 FT /evidence="ECO:0007829|PDB:2NN6" FT HELIX 121..124 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 126..128 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 133..143 FT /evidence="ECO:0007829|PDB:2NN6" FT HELIX 150..161 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 164..171 FT /evidence="ECO:0007829|PDB:6D6Q" FT STRAND 172..175 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 176..186 FT /evidence="ECO:0007829|PDB:6D6Q" FT STRAND 194..200 FT /evidence="ECO:0007829|PDB:2NN6" FT TURN 202..204 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 207..209 FT /evidence="ECO:0007829|PDB:2NN6" FT TURN 212..216 FT /evidence="ECO:0007829|PDB:2NN6" FT STRAND 219..226 FT /evidence="ECO:0007829|PDB:2NN6" FT TURN 228..230 FT /evidence="ECO:0007829|PDB:6D6Q" FT STRAND 232..238 FT /evidence="ECO:0007829|PDB:2NN6" FT HELIX 245..267 FT /evidence="ECO:0007829|PDB:2NN6" FT TURN 268..273 FT /evidence="ECO:0007829|PDB:2NN6" SQ SEQUENCE 276 AA; 30040 MW; FC8F5BAE74A1FF55 CRC64; MAAGFKTVEP LEYYRRFLKE NCRPDGRELG EFRTTTVNIG SISTADGSAL VKLGNTTVIC GVKAEFAAPS TDAPDKGYVV PNVDLPPLCS SRFRSGPPGE EAQVASQFIA DVIENSQIIQ KEDLCISPGK LVWVLYCDLI CLDYDGNILD ACTFALLAAL KNVQLPEVTI NEETALAEVN LKKKSYLNIR THPVATSFAV FDDTLLIVDP TGEEEHLATG TLTIVMDEEG KLCCLHKPGG SGLTGAKLQD CMSRAVTRHK EVKKLMDEVI KSMKPK //