EXOS8_HUMAN
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 03-AUG-2022, entry version 190.
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};
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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 SMR; Q96B26; -.
DR BioGRID; 116468; 181.
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 SWISS-2DPAGE; Q96B26; -.
DR EPD; Q96B26; -.
DR jPOST; Q96B26; -.
DR MassIVE; Q96B26; -.
DR MaxQB; Q96B26; -.
DR PaxDb; Q96B26; -.
DR PeptideAtlas; Q96B26; -.
DR PRIDE; Q96B26; -.
DR ProteomicsDB; 76038; -.
DR TopDownProteomics; Q96B26; -.
DR Antibodypedia; 23142; 150 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 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; RWILADP; -.
DR OrthoDB; 1210090at2759; -.
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; 713 hits in 1102 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 207 other tissues.
DR ExpressionAtlas; Q96B26; baseline and differential.
DR Genevisible; Q96B26; HS.
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); 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: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:0016075; P:rRNA catabolic process; IBA:GO_Central.
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 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 InterPro; IPR033196; Rrp43.
DR PANTHER; PTHR11097:SF9; PTHR11097:SF9; 1.
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; 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
