ID EXOSX_HUMAN Reviewed; 885 AA. AC Q01780; B1AKQ0; B1AKQ1; Q15158; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 27-MAR-2024, entry version 231. DE RecName: Full=Exosome complex component 10 {ECO:0000305}; DE EC=3.1.13.- {ECO:0000269|PubMed:21705430}; DE AltName: Full=Autoantigen PM/Scl 2; DE AltName: Full=P100 polymyositis-scleroderma overlap syndrome-associated autoantigen; DE AltName: Full=Polymyositis/scleroderma autoantigen 100 kDa; DE Short=PM/Scl-100; DE AltName: Full=Polymyositis/scleroderma autoantigen 2; GN Name=EXOSC10 {ECO:0000312|HGNC:HGNC:9138}; GN Synonyms=PMSCL, PMSCL2, RRP6 {ECO:0000303|PubMed:26166824}; 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] (ISOFORM 1). RC TISSUE=Placenta; RX PubMed=1383382; DOI=10.1084/jem.176.4.973; RA Bluethner M., Bautz F.A.; RT "Cloning and characterization of the cDNA coding for a polymyositis- RT scleroderma overlap syndrome-related nucleolar 100-kD protein."; RL J. Exp. Med. 176:973-980(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Thymocyte; RX PubMed=1644924; DOI=10.1172/jci115895; RA Ge Q., Frank M.B., O'Brien C., Targoff I.N.; RT "Cloning of a complementary DNA coding for the 100-kD antigenic protein of RT the PM-Scl autoantigen."; RL J. Clin. Invest. 90:559-570(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2). RX PubMed=11426320; DOI=10.1038/sj.gene.6363745; RA Stover C., Endo Y., Takahashi M., Lynch N., Constantinescu C., RA Vorup-Jensen T., Thiel S., Friedl H., Hankeln T., Hall R., Gregory S., RA Fujita T., Schwaeble W.; RT "The human gene for mannan-binding lectin-associated serine protease-2 RT (MASP-2), the effector component of the lectin route of complement RT activation, is part of a tightly linked gene cluster on chromosome 1p36.2- RT 3."; RL Genes Immun. 2:119-127(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lymph, and 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 [7] 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 [8] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271; RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., RA Greco A., Hochstrasser D.F., Diaz J.-J.; RT "Functional proteomic analysis of human nucleolus."; RL Mol. Biol. Cell 13:4100-4109(2002). RN [9] RP FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, AND SUBCELLULAR LOCATION. RX PubMed=14527413; DOI=10.1016/s1097-2765(03)00349-6; RA Lejeune F., Li X., Maquat L.E.; RT "Nonsense-mediated mRNA decay in mammalian cells involves decapping, RT deadenylating, and exonucleolytic activities."; RL Mol. Cell 12:675-687(2003). RN [10] 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 [11] RP INTERACTION WITH DHX36. RX PubMed=14731398; DOI=10.1016/s1097-2765(03)00481-7; RA Tran H., Schilling M., Wirbelauer C., Hess D., Nagamine Y.; RT "Facilitation of mRNA deadenylation and decay by the exosome-bound, DExH RT protein RHAU."; RL Mol. Cell 13:101-111(2004). RN [12] RP FUNCTION IN NUCLEAR PRE-MRNA DEGRADATION. RX PubMed=16455498; DOI=10.1016/j.molcel.2005.12.008; RA West S., Gromak N., Norbury C.J., Proudfoot N.J.; RT "Adenylation and exosome-mediated degradation of cotranscriptionally RT cleaved pre-messenger RNA in human cells."; RL Mol. Cell 21:437-443(2006). RN [13] RP INTERACTION WITH ALYREF. RX PubMed=17234882; DOI=10.1101/gad.1503107; RA Yoh S.M., Cho H., Pickle L., Evans R.M., Jones K.A.; RT "The Spt6 SH2 domain binds Ser2-P RNAPII to direct Iws1-dependent mRNA RT splicing and export."; RL Genes Dev. 21:160-174(2007). RN [14] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH C1D AND MPHOSPH6. RX PubMed=17412707; DOI=10.1093/nar/gkm082; RA Schilders G., van Dijk E., Pruijn G.J.M.; RT "C1D and hMtr4p associate with the human exosome subunit PM/Scl-100 and are RT involved in pre-rRNA processing."; RL Nucleic Acids Res. 35:2564-2572(2007). RN [15] 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 [16] 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 [17] RP FUNCTION IN PROMPT DEGRADATION. RX PubMed=19056938; DOI=10.1126/science.1164096; RA Preker P., Nielsen J., Kammler S., Lykke-Andersen S., Christensen M.S., RA Mapendano C.K., Schierup M.H., Jensen T.H.; RT "RNA exosome depletion reveals transcription upstream of active human RT promoters."; RL Science 322:1851-1854(2008). RN [18] RP ASSOCIATION WITH THE RNA EXOSOME COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=20531386; DOI=10.1038/emboj.2010.121; RA Tomecki R., Kristiansen M.S., Lykke-Andersen S., Chlebowski A., RA Larsen K.M., Szczesny R.J., Drazkowska K., Pastula A., Andersen J.S., RA Stepien P.P., Dziembowski A., Jensen T.H.; RT "The human core exosome interacts with differentially localized processive RT RNases: hDIS3 and hDIS3L."; RL EMBO J. 29:2342-2357(2010). RN [19] 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 [20] RP FUNCTION IN NUCLEAR MRNA SURVEILLANCE. RX PubMed=20699273; DOI=10.1093/nar/gkq703; RA de Almeida S.F., Garcia-Sacristan A., Custodio N., Carmo-Fonseca M.; RT "A link between nuclear RNA surveillance, the human exosome and RNA RT polymerase II transcriptional termination."; RL Nucleic Acids Res. 38:8015-8026(2010). RN [21] 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 [22] 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 [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [24] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-583, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [25] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-583, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [26] RP IDENTIFICATION IN THE RNA EXOSOME COMPLEX. RX PubMed=26166824; DOI=10.1016/j.bbrc.2015.07.032; RA Yoshikatsu Y., Ishida Y., Sudo H., Yuasa K., Tsuji A., Nagahama M.; RT "NVL2, a nucleolar AAA-ATPase, is associated with the nuclear exosome and RT is involved in pre-rRNA processing."; RL Biochem. Biophys. Res. Commun. 464:780-786(2015). RN [27] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-826, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [28] {ECO:0000305} RP FUNCTION. RX PubMed=25632158; DOI=10.1242/jcs.158733; RA Marin-Vicente C., Domingo-Prim J., Eberle A.B., Visa N.; RT "RRP6/EXOSC10 is required for the repair of DNA double-strand breaks by RT homologous recombination."; RL J. Cell Sci. 128:1097-1107(2015). RN [29] {ECO:0000305} RP FUNCTION, INDUCTION, SUMOYLATION, AND MUTAGENESIS OF LYS-168; LYS-201 AND RP LYS-583. RX PubMed=26857222; DOI=10.1261/rna.054411.115; RA Knight J.R., Bastide A., Peretti D., Roobol A., Roobol J., Mallucci G.R., RA Smales C.M., Willis A.E.; RT "Cooling-induced SUMOylation of EXOSC10 down-regulates ribosome RT biogenesis."; RL RNA 22:623-635(2016). RN [30] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-19; LYS-583; LYS-710; LYS-826; RP LYS-833; LYS-859 AND LYS-873, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [31] {ECO:0000305} RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=31086179; DOI=10.1038/s41467-019-10153-9; RA Domingo-Prim J., Endara-Coll M., Bonath F., Jimeno S., Prados-Carvajal R., RA Friedlaender M.R., Huertas P., Visa N.; RT "EXOSC10 is required for RPA assembly and controlled DNA end resection at RT DNA double-strand breaks."; RL Nat. Commun. 10:2135-2135(2019). RN [32] RP INTERACTION WITH NRDE2. RX PubMed=30538148; DOI=10.1261/rna.069773.118; RA Jiao A.L., Perales R., Umbreit N.T., Haswell J.R., Piper M.E., Adams B.D., RA Pellman D., Kennedy S., Slack F.J.; RT "Human nuclear RNAi-defective 2 (NRDE2) is an essential RNA splicing RT factor."; RL RNA 25:352-363(2019). RN [33] {ECO:0000305} RP FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION. RX PubMed=32830871; DOI=10.15252/embj.2019102700; RA Kawabe Y., Mori K., Yamashita T., Gotoh S., Ikeda M.; RT "The RNA exosome complex degrades expanded hexanucleotide repeat RNA in RT C9orf72 FTLD/ALS."; RL EMBO J. 39:e102700-e102700(2020). RN [34] {ECO:0000305} RP FUNCTION, INTERACTION WITH USP36, SUBCELLULAR LOCATION, SUMOYLATION, AND RP MUTAGENESIS OF LYS-19; LYS-168; LYS-583; LYS-710; LYS-826; LYS-833; LYS-859 RP AND LYS-873. 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 [35] RP STRUCTURE BY NMR OF 483-593. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the HRDC domain of human exosome component 10."; RL Submitted (NOV-2005) to the PDB data bank. RN [36] {ECO:0007744|PDB:3SAF, ECO:0007744|PDB:3SAG, ECO:0007744|PDB:3SAH} RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 180-606 OF MUTANTS ASN-313 AND RP ALA-436 IN COMPLEX WITH MAGNESIUM, CATALYTIC ACTIVITY, COFACTOR, AND RP MUTAGENESIS OF ASP-313; GLU-315; HIS-316; ASP-371; ASP-404 AND TYR-436. RX PubMed=21705430; DOI=10.1261/rna.2763111; RA Januszyk K., Liu Q., Lima C.D.; RT "Activities of human RRP6 and structure of the human RRP6 catalytic RT domain."; RL RNA 17:1566-1577(2011). RN [37] {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). RN [38] {ECO:0007744|PDB:7MQA} RP STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=34516797; DOI=10.1126/science.abj5338; RA Singh S., Vanden Broeck A., Miller L., Chaker-Margot M., Klinge S.; RT "Nucleolar maturation of the human small subunit processome."; RL Science 373:eabj5338-eabj5338(2021). CC -!- FUNCTION: 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. Part of the small subunit (SSU) processome, first CC precursor of the small eukaryotic ribosomal subunit. During the CC assembly of the SSU processome in the nucleolus, many ribosome CC biogenesis factors, an RNA chaperone and ribosomal proteins associate CC with the nascent pre-rRNA and work in concert to generate RNA folding, CC modifications, rearrangements and cleavage as well as targeted CC degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). CC The RNA exosome may be involved in Ig class switch recombination (CSR) CC and/or Ig variable region somatic hypermutation (SHM) by targeting CC AICDA deamination activity to transcribed dsDNA substrates. In the CC cytoplasm, the RNA exosome complex is involved in general mRNA turnover CC and specifically degrades inherently unstable mRNAs containing AU-rich CC elements (AREs) within their 3' untranslated regions, and in RNA CC surveillance pathways, preventing translation of aberrant mRNAs. It CC seems to be involved in degradation of histone mRNA. EXOSC10 is CC required for nucleolar localization of C1D and probably mediates the CC association of MTREX, C1D and MPHOSPH6 with the RNA exosome involved in CC the maturation of 5.8S rRNA. Plays a role in the recruitment of CC replication protein A complex (RPA) and RAD51 to DNA double-strand CC breaks caused by irradiation, contributing to DNA repair by homologous CC recombination (PubMed:31086179, PubMed:25632158). Regulates levels of CC damage-induced RNAs in order to prevent DNA-RNA hybrid formation at DNA CC double-strand breaks and limit DNA end resection after damage CC (PubMed:31086179). Plays a role in oocyte development, maturation and CC survival (By similarity). Required for normal testis development and CC mitotic division of spermatogonia (By similarity). Plays a role in CC proper embryo development (By similarity). Required for global protein CC translation (PubMed:36912080, PubMed:26857222). Required for cell CC proliferation (PubMed:36912080). Regulates metabolism of C9orf72- CC derived repeat RNA that can be translated into toxic dipeptide repeat CC proteins (PubMed:32830871). {ECO:0000250|UniProtKB:P56960, CC ECO:0000269|PubMed:14527413, ECO:0000269|PubMed:16455498, CC ECO:0000269|PubMed:17412707, ECO:0000269|PubMed:17545563, CC ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:19056938, CC ECO:0000269|PubMed:20368444, ECO:0000269|PubMed:20699273, CC ECO:0000269|PubMed:25632158, ECO:0000269|PubMed:26857222, CC ECO:0000269|PubMed:31086179, ECO:0000269|PubMed:32830871, CC ECO:0000269|PubMed:34516797, ECO:0000269|PubMed:36912080}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:21705430}; CC -!- ACTIVITY REGULATION: Arginine-rich dipeptide repeat proteins expressed CC from C9orf72-derived repeat RNA interact with EXOSC10 and inhibit its CC ability to promote degradation of this RNA. CC {ECO:0000269|PubMed:32830871}. CC -!- SUBUNIT: Component of the RNA exosome complex (PubMed:20531389, CC PubMed:26166824, PubMed:29906447). The catalytically inactive RNA CC exosome core (Exo-9) complex is believed to associate with catalytic CC subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear- CC specific RNA exosome complex forms (PubMed:20531389). Part of the small CC subunit (SSU) processome, composed of more than 70 proteins and the RNA CC chaperone small nucleolar RNA (snoRNA) U3 (PubMed:34516797). Interacts CC with C1D and MPHOSPH6 (PubMed:17412707). Interacts with ALYREF/THOC4 CC (PubMed:17234882). Interacts with MTREX; the interaction mediates the CC association of MTREX with nuclear RNA exosomes (PubMed:26166824). CC Interacts with DHX36; this interaction occurs in a RNase-insensitive CC manner (PubMed:14731398). Interacts with NRDE2 (PubMed:30538148). CC Interacts (via C-terminus) with USP36 (via C-terminus); the interaction CC is facilitated by the association with RNA and promotes sumoylation of CC EXOSC10 (PubMed:36912080). {ECO:0000269|PubMed:14731398, CC ECO:0000269|PubMed:17234882, ECO:0000269|PubMed:17412707, CC ECO:0000269|PubMed:20531389, ECO:0000269|PubMed:26166824, CC ECO:0000269|PubMed:29906447, ECO:0000269|PubMed:30538148, CC ECO:0000269|PubMed:34516797, ECO:0000269|PubMed:36912080}. CC -!- INTERACTION: CC Q01780; Q13901: C1D; NbExp=5; IntAct=EBI-358236, EBI-3844053; CC Q01780; P17844: DDX5; NbExp=3; IntAct=EBI-358236, EBI-351962; CC Q01780; Q9Y2L1: DIS3; NbExp=4; IntAct=EBI-358236, EBI-373539; CC Q01780; Q9NPD3: EXOSC4; NbExp=5; IntAct=EBI-358236, EBI-371823; CC Q01780; Q9NQT4: EXOSC5; NbExp=4; IntAct=EBI-358236, EBI-371876; CC Q01780; Q99547: MPHOSPH6; NbExp=4; IntAct=EBI-358236, EBI-373187; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20531386}. Nucleus CC {ECO:0000269|PubMed:36912080}. Nucleus, nucleolus CC {ECO:0000269|PubMed:20531386, ECO:0000269|PubMed:31086179, CC ECO:0000269|PubMed:32830871, ECO:0000269|PubMed:34516797, CC ECO:0000269|PubMed:36912080}. Nucleus, nucleoplasm CC {ECO:0000269|PubMed:32830871, ECO:0000269|PubMed:36912080}. CC Note=Strongly enriched in the nucleolus and a small amount has been CC found in cytoplasm supporting the existence of a nucleolar RNA exosome CC complex form (PubMed:20531386, PubMed:34516797). Arginine-rich CC dipeptide repeat proteins expressed from C9orf72-derived repeat RNA CC cause diffuse nuclear misdistribution of EXOSC10 (PubMed:32830871). CC Relocates to the DNA double-strand breaks in response to irradiation CC (PubMed:31086179). {ECO:0000269|PubMed:20531386, CC ECO:0000269|PubMed:31086179, ECO:0000269|PubMed:32830871, CC ECO:0000269|PubMed:34516797}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q01780-1; Sequence=Displayed; CC Name=2; CC IsoId=Q01780-2; Sequence=VSP_004362; CC -!- INDUCTION: Down-regulated by mild hypothermia (at protein level). CC {ECO:0000269|PubMed:26857222}. CC -!- PTM: Sumoylated by USP36; sumoylation does not significantly affect CC EXOSC10 nucleolar localization and association with core exosome and CC USP36, but regulates the nucleolar RNA exosome activity in rRNA CC processing by promoting binding of EXOSC10 to pre-rRNAs CC (PubMed:36912080). Effects of sumoylation on EXOSC10 levels vary CC between different studies (PubMed:26857222, PubMed:36912080). CC Sumoylation of EXOSC10 is required for the modulation of EXOSC10 CC effects on cellular protein translation and cell proliferation CC (PubMed:36912080). Sumoylation is promoted by mild hypothermia CC (PubMed:26857222). {ECO:0000269|PubMed:26857222, CC ECO:0000269|PubMed:36912080}. CC -!- SIMILARITY: Belongs to the exosome component 10/RRP6 family. CC {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; X66113; CAA46904.1; -; mRNA. DR EMBL; L01457; AAB59352.1; -; mRNA. DR EMBL; AJ300188; CAC15569.1; -; Genomic_DNA. DR EMBL; AL109811; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471130; EAW71679.1; -; Genomic_DNA. DR EMBL; BC039901; AAH39901.1; -; mRNA. DR EMBL; BC073788; AAH73788.1; -; mRNA. DR CCDS; CCDS126.1; -. [Q01780-2] DR CCDS; CCDS30584.1; -. [Q01780-1] DR PIR; A43920; A43920. DR PIR; JH0796; JH0796. DR RefSeq; NP_001001998.1; NM_001001998.2. [Q01780-1] DR RefSeq; NP_002676.1; NM_002685.3. [Q01780-2] DR PDB; 2CPR; NMR; -; A=483-593. DR PDB; 3SAF; X-ray; 2.50 A; A/B=180-606. DR PDB; 3SAG; X-ray; 2.70 A; A/B=180-606. DR PDB; 3SAH; X-ray; 2.65 A; A/B=180-606. DR PDB; 6D6Q; EM; 3.45 A; J=1-648, J=705-804. DR PDB; 6D6R; EM; 3.45 A; J=1-648, J=705-804. DR PDB; 7MQA; EM; 2.70 A; NV=1-885. DR PDBsum; 2CPR; -. DR PDBsum; 3SAF; -. DR PDBsum; 3SAG; -. DR PDBsum; 3SAH; -. DR PDBsum; 6D6Q; -. DR PDBsum; 6D6R; -. DR PDBsum; 7MQA; -. DR AlphaFoldDB; Q01780; -. DR EMDB; EMD-0127; -. DR EMDB; EMD-14515; -. DR EMDB; EMD-23938; -. DR EMDB; EMD-7808; -. DR EMDB; EMD-7809; -. DR EMDB; EMD-7818; -. DR EMDB; EMD-7819; -. DR SMR; Q01780; -. DR BioGRID; 111403; 212. DR ComplexPortal; CPX-476; Nuclear exosome complex, DIS3-EXOSC10 variant. DR ComplexPortal; CPX-591; Nucleolar exosome complex, EXOSC10 variant. DR ComplexPortal; CPX-600; Cytoplasmic exosome complex, DIS3L-EXOSC10 variant. DR CORUM; Q01780; -. DR DIP; DIP-31249N; -. DR IntAct; Q01780; 88. DR MINT; Q01780; -. DR STRING; 9606.ENSP00000366135; -. DR GlyGen; Q01780; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q01780; -. DR MetOSite; Q01780; -. DR PhosphoSitePlus; Q01780; -. DR SwissPalm; Q01780; -. DR BioMuta; EXOSC10; -. DR DMDM; 8928564; -. DR EPD; Q01780; -. DR jPOST; Q01780; -. DR MassIVE; Q01780; -. DR MaxQB; Q01780; -. DR PaxDb; 9606-ENSP00000366135; -. DR PeptideAtlas; Q01780; -. DR ProteomicsDB; 57986; -. [Q01780-1] DR ProteomicsDB; 57987; -. [Q01780-2] DR Pumba; Q01780; -. DR Antibodypedia; 13683; 228 antibodies from 30 providers. DR DNASU; 5394; -. DR Ensembl; ENST00000304457.11; ENSP00000307307.7; ENSG00000171824.14. [Q01780-2] DR Ensembl; ENST00000376936.9; ENSP00000366135.4; ENSG00000171824.14. [Q01780-1] DR GeneID; 5394; -. DR KEGG; hsa:5394; -. DR MANE-Select; ENST00000376936.9; ENSP00000366135.4; NM_001001998.3; NP_001001998.1. DR UCSC; uc001asa.4; human. [Q01780-1] DR AGR; HGNC:9138; -. DR CTD; 5394; -. DR DisGeNET; 5394; -. DR GeneCards; EXOSC10; -. DR HGNC; HGNC:9138; EXOSC10. DR HPA; ENSG00000171824; Low tissue specificity. DR MIM; 605960; gene. DR neXtProt; NX_Q01780; -. DR OpenTargets; ENSG00000171824; -. DR PharmGKB; PA33464; -. DR VEuPathDB; HostDB:ENSG00000171824; -. DR eggNOG; KOG2206; Eukaryota. DR GeneTree; ENSGT00390000015408; -. DR HOGENOM; CLU_010129_1_1_1; -. DR InParanoid; Q01780; -. DR OMA; NIMRPQM; -. DR OrthoDB; 2880475at2759; -. DR PhylomeDB; Q01780; -. DR TreeFam; TF105991; -. DR PathwayCommons; Q01780; -. DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR SignaLink; Q01780; -. DR SIGNOR; Q01780; -. DR BioGRID-ORCS; 5394; 505 hits in 1167 CRISPR screens. DR ChiTaRS; EXOSC10; human. DR EvolutionaryTrace; Q01780; -. DR GeneWiki; Exosome_component_10; -. DR GenomeRNAi; 5394; -. DR Pharos; Q01780; Tbio. DR PRO; PR:Q01780; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q01780; Protein. DR Bgee; ENSG00000171824; Expressed in cerebellar hemisphere and 203 other cell types or tissues. DR ExpressionAtlas; Q01780; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); NAS:ComplexPortal. 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:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0000176; C:nuclear exosome (RNase complex); IDA:UniProtKB. DR GO; GO:0101019; C:nucleolar exosome (RNase complex); NAS:ComplexPortal. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032040; C:small-subunit processome; IDA:UniProtKB. DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IMP:BHF-UCL. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0004532; F:RNA exonuclease activity; IDA:UniProtKB. DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central. DR GO; GO:0070034; F:telomerase RNA binding; IC:BHF-UCL. DR GO; GO:0071034; P:CUT catabolic process; IMP:UniProtKB. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. 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:0071044; P:histone mRNA catabolic process; IMP:UniProtKB. DR GO; GO:0000460; P:maturation of 5.8S rRNA; IMP:UniProtKB. DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IMP:BHF-UCL. DR GO; GO:0071028; P:nuclear mRNA surveillance; IMP:UniProtKB. DR GO; GO:0071040; P:nuclear polyadenylation-dependent antisense transcript catabolic process; IBA:GO_Central. DR GO; GO:0071039; P:nuclear polyadenylation-dependent CUT catabolic process; IBA:GO_Central. DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IMP:UniProtKB. DR GO; GO:0071036; P:nuclear polyadenylation-dependent snoRNA catabolic process; IBA:GO_Central. DR GO; GO:0071037; P:nuclear polyadenylation-dependent snRNA catabolic process; IBA:GO_Central. DR GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IBA:GO_Central. DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:UniProtKB. DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW. DR GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IBA:GO_Central. DR GO; GO:1905746; P:positive regulation of mRNA cis splicing, via spliceosome; IEA:Ensembl. DR GO; GO:1904872; P:regulation of telomerase RNA localization to Cajal body; IMP:BHF-UCL. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB. DR GO; GO:0006401; P:RNA catabolic process; IDA:ComplexPortal. DR GO; GO:0006396; P:RNA processing; IDA:ComplexPortal. DR GO; GO:0006364; P:rRNA processing; TAS:Reactome. DR CDD; cd06147; Rrp6p_like_exo; 1. DR Gene3D; 1.10.150.80; HRDC domain; 1. DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1. DR InterPro; IPR002562; 3'-5'_exonuclease_dom. DR InterPro; IPR012588; Exosome-assoc_fac_Rrp6_N. DR InterPro; IPR010997; HRDC-like_sf. DR InterPro; IPR002121; HRDC_dom. DR InterPro; IPR044876; HRDC_dom_sf. DR InterPro; IPR012337; RNaseH-like_sf. DR InterPro; IPR036397; RNaseH_sf. DR InterPro; IPR045092; Rrp6-like. DR InterPro; IPR049559; Rrp6p-like_exo. DR PANTHER; PTHR12124:SF47; EXOSOME COMPONENT 10; 1. DR PANTHER; PTHR12124; POLYMYOSITIS/SCLERODERMA AUTOANTIGEN-RELATED; 1. DR Pfam; PF01612; DNA_pol_A_exo1; 1. DR Pfam; PF00570; HRDC; 1. DR Pfam; PF08066; PMC2NT; 1. DR SMART; SM00474; 35EXOc; 1. DR SMART; SM00341; HRDC; 1. DR SUPFAM; SSF47819; HRDC-like; 1. DR SUPFAM; SSF53098; Ribonuclease H-like; 1. DR PROSITE; PS50967; HRDC; 1. DR SWISS-2DPAGE; Q01780; -. DR Genevisible; Q01780; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; DNA damage; DNA repair; KW Exonuclease; Exosome; Hydrolase; Isopeptide bond; Magnesium; Metal-binding; KW Nonsense-mediated mRNA decay; Nuclease; Nucleus; Phosphoprotein; KW Reference proteome; RNA-binding; rRNA processing; Ubl conjugation. FT CHAIN 1..885 FT /note="Exosome complex component 10" FT /id="PRO_0000087133" FT DOMAIN 289..455 FT /note="3'-5' exonuclease" FT /evidence="ECO:0000255" FT DOMAIN 503..583 FT /note="HRDC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00328" FT REGION 776..885 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 776..814 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 825..846 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 313 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:21705430, FT ECO:0007744|PDB:3SAF, ECO:0007744|PDB:3SAG, FT ECO:0007744|PDB:3SAH" FT BINDING 313 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:21705430, FT ECO:0007744|PDB:3SAH" FT BINDING 315 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:21705430, FT ECO:0007744|PDB:3SAH" FT BINDING 371 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:21705430, FT ECO:0007744|PDB:3SAF, ECO:0007744|PDB:3SAG, FT ECO:0007744|PDB:3SAH" FT BINDING 440 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:21705430, FT ECO:0007744|PDB:3SAH" FT SITE 583 FT /note="Not ubiquitinated" FT /evidence="ECO:0000269|PubMed:36912080" FT MOD_RES 821 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 19 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 583 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000269|PubMed:36912080, FT ECO:0007744|PubMed:25114211" FT CROSSLNK 583 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000269|PubMed:36912080, FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733" FT CROSSLNK 710 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 826 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 833 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 859 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 873 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 695..719 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:1644924" FT /id="VSP_004362" FT MUTAGEN 19 FT /note="K->R: No effect on sumoylation by USP36." FT /evidence="ECO:0000269|PubMed:36912080" FT MUTAGEN 168 FT /note="K->R: No effect on sumoylation by USP36. Reduces FT sumoylation levels and increases steady-state expression; FT when associated with R-201 and R-583." FT /evidence="ECO:0000269|PubMed:26857222, FT ECO:0000269|PubMed:36912080" FT MUTAGEN 201 FT /note="K->R: Reduces sumoylation levels and increases FT steady-state expression; when associated with R-168 and FT R-583." FT /evidence="ECO:0000269|PubMed:26857222" FT MUTAGEN 313 FT /note="D->N: Abolishes exoribonuclease activity." FT /evidence="ECO:0000269|PubMed:21705430" FT MUTAGEN 315 FT /note="E->Q: Abolishes exoribonuclease activity." FT /evidence="ECO:0000269|PubMed:21705430" FT MUTAGEN 316 FT /note="H->A: Slightly reduces exoribonuclease activity." FT /evidence="ECO:0000269|PubMed:21705430" FT MUTAGEN 371 FT /note="D->N: Abolishes exoribonuclease activity." FT /evidence="ECO:0000269|PubMed:21705430" FT MUTAGEN 404 FT /note="D->A: Increases exoribonuclease activity." FT /evidence="ECO:0000269|PubMed:21705430" FT MUTAGEN 436 FT /note="Y->A: Significantly reduces exoribonuclease FT activity." FT /evidence="ECO:0000269|PubMed:21705430" FT MUTAGEN 583 FT /note="K->R: Reduces sumoylation by USP36. Significantly FT attenuates binding to pre-rRNA across the 5.8S-ITS2 and FT 18S-ITS1 junctions. Reduces sumoylation levels and FT increases steady-state expression; when associated with FT R-168 and R-201." FT /evidence="ECO:0000269|PubMed:26857222, FT ECO:0000269|PubMed:36912080" FT MUTAGEN 710 FT /note="K->R: No effect on sumoylation by USP36." FT /evidence="ECO:0000269|PubMed:36912080" FT MUTAGEN 826 FT /note="K->R: No effect on sumoylation by USP36." FT /evidence="ECO:0000269|PubMed:36912080" FT MUTAGEN 833 FT /note="K->R: No effect on sumoylation by USP36." FT /evidence="ECO:0000269|PubMed:36912080" FT MUTAGEN 859 FT /note="K->R: No effect on sumoylation by USP36." FT /evidence="ECO:0000269|PubMed:36912080" FT MUTAGEN 873 FT /note="K->R: No effect on sumoylation by USP36." FT /evidence="ECO:0000269|PubMed:36912080" FT HELIX 183..186 FT /evidence="ECO:0007829|PDB:3SAF" FT STRAND 194..196 FT /evidence="ECO:0007829|PDB:3SAF" FT HELIX 214..216 FT /evidence="ECO:0007829|PDB:3SAF" FT HELIX 218..220 FT /evidence="ECO:0007829|PDB:3SAF" FT STRAND 253..255 FT /evidence="ECO:0007829|PDB:3SAF" FT HELIX 259..263 FT /evidence="ECO:0007829|PDB:3SAF" FT HELIX 269..272 FT /evidence="ECO:0007829|PDB:3SAF" FT HELIX 283..285 FT /evidence="ECO:0007829|PDB:3SAF" FT STRAND 288..291 FT /evidence="ECO:0007829|PDB:3SAF" FT HELIX 294..304 FT /evidence="ECO:0007829|PDB:3SAF" FT STRAND 308..317 FT /evidence="ECO:0007829|PDB:3SAF" FT STRAND 325..332 FT /evidence="ECO:0007829|PDB:3SAF" FT STRAND 337..341 FT /evidence="ECO:0007829|PDB:3SAF" FT TURN 342..345 FT /evidence="ECO:0007829|PDB:3SAF" FT HELIX 346..352 FT /evidence="ECO:0007829|PDB:3SAF" FT HELIX 353..356 FT /evidence="ECO:0007829|PDB:3SAF" FT STRAND 361..367 FT /evidence="ECO:0007829|PDB:3SAF" FT HELIX 369..379 FT /evidence="ECO:0007829|PDB:3SAF" FT STRAND 384..388 FT /evidence="ECO:0007829|PDB:3SAF" FT HELIX 389..395 FT /evidence="ECO:0007829|PDB:3SAF" FT HELIX 403..411 FT /evidence="ECO:0007829|PDB:3SAF" FT TURN 418..421 FT /evidence="ECO:0007829|PDB:3SAF" FT HELIX 431..442 FT /evidence="ECO:0007829|PDB:3SAF" FT HELIX 444..458 FT /evidence="ECO:0007829|PDB:3SAF" FT STRAND 461..463 FT /evidence="ECO:0007829|PDB:3SAH" FT HELIX 464..476 FT /evidence="ECO:0007829|PDB:3SAF" FT HELIX 490..492 FT /evidence="ECO:0007829|PDB:3SAF" FT HELIX 493..496 FT /evidence="ECO:0007829|PDB:3SAF" FT STRAND 497..500 FT /evidence="ECO:0007829|PDB:2CPR" FT HELIX 504..524 FT /evidence="ECO:0007829|PDB:3SAF" FT HELIX 528..531 FT /evidence="ECO:0007829|PDB:3SAF" FT HELIX 534..543 FT /evidence="ECO:0007829|PDB:3SAF" FT HELIX 548..552 FT /evidence="ECO:0007829|PDB:3SAF" FT STRAND 555..557 FT /evidence="ECO:0007829|PDB:3SAH" FT HELIX 560..564 FT /evidence="ECO:0007829|PDB:3SAF" FT HELIX 566..577 FT /evidence="ECO:0007829|PDB:3SAF" FT HELIX 583..586 FT /evidence="ECO:0007829|PDB:3SAF" FT STRAND 636..638 FT /evidence="ECO:0007829|PDB:6D6Q" SQ SEQUENCE 885 AA; 100831 MW; A37BDC8F49BF2E57 CRC64; MAPPSTREPR VLSATSATKS DGEMVLPGFP DADSFVKFAL GSVVAVTKAS GGLPQFGDEY DFYRSFPGFQ AFCETQGDRL LQCMSRVMQY HGCRSNIKDR SKVTELEDKF DLLVDANDVI LERVGILLDE ASGVNKNQQP VLPAGLQVPK TVVSSWNRKA AEYGKKAKSE TFRLLHAKNI IRPQLKFREK IDNSNTPFLP KIFIKPNAQK PLPQALSKER RERPQDRPED LDVPPALADF IHQQRTQQVE QDMFAHPYQY ELNHFTPADA VLQKPQPQLY RPIEETPCHF ISSLDELVEL NEKLLNCQEF AVDLEHHSYR SFLGLTCLMQ ISTRTEDFII DTLELRSDMY ILNESLTDPA IVKVFHGADS DIEWLQKDFG LYVVNMFDTH QAARLLNLGR HSLDHLLKLY CNVDSNKQYQ LADWRIRPLP EEMLSYARDD THYLLYIYDK MRLEMWERGN GQPVQLQVVW QRSRDICLKK FIKPIFTDES YLELYRKQKK HLNTQQLTAF QLLFAWRDKT ARREDESYGY VLPNHMMLKI AEELPKEPQG IIACCNPVPP LVRQQINEMH LLIQQAREMP LLKSEVAAGV KKSGPLPSAE RLENVLFGPH DCSHAPPDGY PIIPTSGSVP VQKQASLFPD EKEDNLLGTT CLIATAVITL FNEPSAEDSK KGPLTVAQKK AQNIMESFEN PFRMFLPSLG HRAPVSQAAK FDPSTKIYEI SNRWKLAQVQ VQKDSKEAVK KKAAEQTAAR EQAKEACKAA AEQAISVRQQ VVLENAAKKR ERATSDPRTT EQKQEKKRLK ISKKPKDPEP PEKEFTPYDY SQSDFKAFAG NSKSKVSSQF DPNKQTPSGK KCIAAKKIKQ SVGNKSMSFP TGKSDRGFRY NWPQR //