ID ORN_HUMAN Reviewed; 237 AA. AC Q9Y3B8; B2R532; Q32Q18; Q53FT1; Q6FIC6; Q9UFY7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 3. DT 24-JAN-2024, entry version 189. DE RecName: Full=Oligoribonuclease, mitochondrial; DE EC=3.1.15.-; DE AltName: Full=RNA exonuclease 2 homolog; DE AltName: Full=Small fragment nuclease; DE Flags: Precursor; GN Name=REXO2; Synonyms=SFN, SMFN; ORFNames=CGI-114; 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 MRNA] (ISOFORM 2). RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Kidney; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skeletal muscle; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Kidney proximal tubule; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and Placenta; 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 [8] RP FUNCTION (ISOFORM 3), BIOPHYSICOCHEMICAL PROPERTIES (ISOFORM 3), COFACTOR RP (ISOFORM 3), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF RP ASP-136 (ISOFORM 3), AND CATALYTIC ACTIVITY (ISOFORM 3). RX PubMed=10851236; DOI=10.1074/jbc.m002672200; RA Nguyen L.H., Erzberger J.P., Root J., Wilson D.M. III; RT "The human homolog of Escherichia coli Orn degrades small single-stranded RT RNA and DNA oligomers."; RL J. Biol. Chem. 275:25900-25906(2000). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-122, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [10] RP FUNCTION (ISOFORM 3), ACTIVITY REGULATION (ISOFORM 3), AND CATALYTIC RP ACTIVITY (ISOFORM 3). RX PubMed=16682444; DOI=10.1093/nar/gkl247; RA Mechold U., Ogryzko V., Ngo S., Danchin A.; RT "Oligoribonuclease is a common downstream target of lithium-induced pAp RT accumulation in Escherichia coli and human cells."; RL Nucleic Acids Res. 34:2364-2373(2006). 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 IDENTIFICATION BY MASS SPECTROMETRY [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 IDENTIFICATION BY 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 [14] RP FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE INITIATION (ISOFORM 3), RP SUBUNIT, AND CATALYTIC ACTIVITY. RX PubMed=23741365; DOI=10.1371/journal.pone.0064670; RA Bruni F., Gramegna P., Oliveira J.M., Lightowlers R.N., RA Chrzanowska-Lightowlers Z.M.; RT "REXO2 is an oligoribonuclease active in human mitochondria."; RL PLoS ONE 8:E64670-E64670(2013). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [18] RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 39-216 OF WILD-TYPE AND MUTANT RP HIS-199 IN COMPLEX WITH PAPA AND DADA, FUNCTION, CATALYTIC ACTIVITY, RP SUBUNIT, MUTAGENESIS OF ASP-47; GLU-49; ASP-147; ARG-178; TRP-179; HIS-194 RP AND ASP-199, METAL-BINDING SITES, COFACTOR, AND ACTIVE SITE. RX PubMed=31588022; DOI=10.1016/j.molcel.2019.09.010; RA Nicholls T.J., Spahr H., Jiang S., Siira S.J., Koolmeister C., Sharma S., RA Kauppila J.H.K., Jiang M., Kaever V., Rackham O., Chabes A., Falkenberg M., RA Filipovska A., Larsson N.G., Gustafsson C.M.; RT "Dinucleotide Degradation by REXO2 Maintains Promoter Specificity in RT Mammalian Mitochondria."; RL Mol. Cell 76:784-796(2019). RN [19] RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 33-218 IN COMPLEX WITH RNA AND RP DNA, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF HIS-194 AND RP ASP-199, METAL-BINDING SITES, COFACTOR, AND ACTIVE SITE. RX PubMed=30926754; DOI=10.1261/rna.070557.119; RA Chu L.Y., Agrawal S., Chen Y.P., Yang W.Z., Yuan H.S.; RT "Structural insights into nanoRNA degradation by human Rexo2."; RL RNA 25:737-746(2019). RN [20] RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) IN COMPLEX WITH RNA, FUNCTION, RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), AND RP MUTAGENESIS OF ASP-49; LEU-53; TRP-96; GLU-146; ASP-147; TYR-164; TRP-179 RP AND PHE-215. RX PubMed=32365187; DOI=10.1093/nar/gkaa302; RA Szewczyk M., Malik D., Borowski L.S., Czarnomska S.D., Kotrys A.V., RA Klosowska-Kosicka K., Nowotny M., Szczesny R.J.; RT "Human REXO2 controls short mitochondrial RNAs generated by mtRNA RT processing and decay machinery to prevent accumulation of double-stranded RT RNA."; RL Nucleic Acids Res. 48:5572-5590(2020). CC -!- FUNCTION: 3'-to-5'exoribonuclease that preferentially degrades DNA and CC RNA oligonucleotides composed of only two nucleotides (PubMed:31588022, CC PubMed:30926754, PubMed:32365187, PubMed:23741365). Binds and degrades CC longer oligonucleotides with a lower affinity (PubMed:31588022, CC PubMed:30926754, PubMed:32365187). Plays dual roles in mitochondria, CC scavenging nanoRNAs (small RNA oligonucleotides of <5 nucleotides) that CC are produced by the degradosome and clearing short RNAs that are CC generated by RNA processing (PubMed:31588022, PubMed:30926754, CC PubMed:32365187). Essential for correct initiation of mitochondrial CC transcription, degrading mitochondrial RNA dinucleotides to prevent CC RNA-primed transcription at non-canonical sites in the mitochondrial CC genome (PubMed:31588022). Essential for embryonic development (By CC similarity). {ECO:0000250|UniProtKB:Q9D8S4, CC ECO:0000269|PubMed:23741365, ECO:0000269|PubMed:30926754, CC ECO:0000269|PubMed:31588022, ECO:0000269|PubMed:32365187}. CC -!- FUNCTION: [Isoform 3]: 3'-to-5'exoribonuclease that preferentially CC degrades DNA and RNA oligonucleotides composed of only two nucleotides. CC {ECO:0000269|PubMed:10851236, ECO:0000269|PubMed:16682444}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:10851236}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:10851236, ECO:0000269|PubMed:30926754, CC ECO:0000269|PubMed:31588022}; CC -!- ACTIVITY REGULATION: [Isoform 3]: Inhibited by adenosine 3',5'- CC bisphosphate. {ECO:0000269|PubMed:16682444}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 3]: CC Kinetic parameters: CC KM=1.56 uM for RNA {ECO:0000269|PubMed:10851236}; CC KM=1.51 uM for DNA {ECO:0000269|PubMed:10851236}; CC Temperature dependence: CC Optimum temperature is 50 degrees Celsius. CC {ECO:0000269|PubMed:10851236}; CC -!- SUBUNIT: Homodimer (PubMed:31588022, PubMed:30926754, PubMed:32365187). CC Homotetramer (PubMed:23741365). {ECO:0000269|PubMed:23741365, CC ECO:0000269|PubMed:30926754, ECO:0000269|PubMed:31588022, CC ECO:0000269|PubMed:32365187}. CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space CC {ECO:0000269|PubMed:23741365}. Mitochondrion matrix CC {ECO:0000269|PubMed:23741365}. Mitochondrion CC {ECO:0000269|PubMed:32365187}. Cytoplasm {ECO:0000269|PubMed:23741365, CC ECO:0000269|PubMed:32365187}. Nucleus {ECO:0000269|PubMed:32365187}. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm CC {ECO:0000269|PubMed:32365187}. Nucleus {ECO:0000269|PubMed:32365187}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=3; CC Name=1; Synonyms=Sfn-alpha {ECO:0000303|PubMed:10851236}; CC IsoId=Q9Y3B8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y3B8-2; Sequence=VSP_003775; CC Name=3; Synonyms=Sfn {ECO:0000303|PubMed:10851236}; CC IsoId=Q9Y3B8-3; Sequence=VSP_054954; CC -!- TISSUE SPECIFICITY: Highly expressed in the heart and at lower levels CC in the lymph nodes, brain, lung, liver, spleen and thymus. CC {ECO:0000269|PubMed:10851236}. CC -!- DEVELOPMENTAL STAGE: Expressed in fetal liver, lung and kidney. CC {ECO:0000269|PubMed:10851236}. CC -!- SIMILARITY: Belongs to the oligoribonuclease family. {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; AF151872; AAD34109.1; -; mRNA. DR EMBL; AL110239; CAB53690.1; -; mRNA. DR EMBL; AK312042; BAG34979.1; -; mRNA. DR EMBL; CR533500; CAG38531.1; -; mRNA. DR EMBL; AK223200; BAD96920.1; -; mRNA. DR EMBL; CH471065; EAW67250.1; -; Genomic_DNA. DR EMBL; BC105024; AAI05025.1; -; mRNA. DR EMBL; BC105026; AAI05027.1; -; mRNA. DR EMBL; BC107887; AAI07888.1; -; mRNA. DR EMBL; BC143701; AAI43702.1; -; mRNA. DR CCDS; CCDS8371.1; -. [Q9Y3B8-1] DR PIR; T14770; T14770. DR RefSeq; NP_056338.2; NM_015523.3. [Q9Y3B8-1] DR PDB; 6J7Y; X-ray; 2.20 A; A/B=34-218. DR PDB; 6J7Z; X-ray; 2.00 A; A/B=33-218. DR PDB; 6J80; X-ray; 1.81 A; A/B=38-216. DR PDB; 6N6I; X-ray; 1.43 A; A/B=33-237. DR PDB; 6N6J; X-ray; 1.32 A; A/B=33-237. DR PDB; 6N6K; X-ray; 1.42 A; A/B=33-237. DR PDB; 6RCI; X-ray; 2.00 A; A/B=39-216. DR PDB; 6RCL; X-ray; 1.97 A; A/B=39-216. DR PDB; 6RCN; X-ray; 2.25 A; A/B=39-216. DR PDB; 6STY; X-ray; 3.15 A; A/B/D/E=1-237. DR PDBsum; 6J7Y; -. DR PDBsum; 6J7Z; -. DR PDBsum; 6J80; -. DR PDBsum; 6N6I; -. DR PDBsum; 6N6J; -. DR PDBsum; 6N6K; -. DR PDBsum; 6RCI; -. DR PDBsum; 6RCL; -. DR PDBsum; 6RCN; -. DR PDBsum; 6STY; -. DR AlphaFoldDB; Q9Y3B8; -. DR SMR; Q9Y3B8; -. DR BioGRID; 117473; 37. DR STRING; 9606.ENSP00000480535; -. DR GlyGen; Q9Y3B8; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9Y3B8; -. DR MetOSite; Q9Y3B8; -. DR PhosphoSitePlus; Q9Y3B8; -. DR SwissPalm; Q9Y3B8; -. DR BioMuta; REXO2; -. DR DMDM; 116242694; -. DR EPD; Q9Y3B8; -. DR jPOST; Q9Y3B8; -. DR MassIVE; Q9Y3B8; -. DR MaxQB; Q9Y3B8; -. DR PaxDb; 9606-ENSP00000265881; -. DR PeptideAtlas; Q9Y3B8; -. DR ProteomicsDB; 86006; -. [Q9Y3B8-1] DR ProteomicsDB; 86007; -. [Q9Y3B8-2] DR Pumba; Q9Y3B8; -. DR Antibodypedia; 32246; 196 antibodies from 23 providers. DR DNASU; 25996; -. DR Ensembl; ENST00000265881.10; ENSP00000265881.5; ENSG00000076043.11. [Q9Y3B8-1] DR GeneID; 25996; -. DR KEGG; hsa:25996; -. DR MANE-Select; ENST00000265881.10; ENSP00000265881.5; NM_015523.4; NP_056338.2. DR UCSC; uc001poy.4; human. [Q9Y3B8-1] DR AGR; HGNC:17851; -. DR CTD; 25996; -. DR DisGeNET; 25996; -. DR GeneCards; REXO2; -. DR HGNC; HGNC:17851; REXO2. DR HPA; ENSG00000076043; Low tissue specificity. DR MIM; 607149; gene. DR neXtProt; NX_Q9Y3B8; -. DR OpenTargets; ENSG00000076043; -. DR PharmGKB; PA142671085; -. DR VEuPathDB; HostDB:ENSG00000076043; -. DR eggNOG; KOG3242; Eukaryota. DR GeneTree; ENSGT00390000009255; -. DR InParanoid; Q9Y3B8; -. DR OMA; AFFHYRN; -. DR OrthoDB; 5474140at2759; -. DR PhylomeDB; Q9Y3B8; -. DR TreeFam; TF314084; -. DR BRENDA; 3.1.13.3; 2681. DR PathwayCommons; Q9Y3B8; -. DR Reactome; R-HSA-9836573; Mitochondrial RNA degradation. DR BioGRID-ORCS; 25996; 172 hits in 1176 CRISPR screens. DR ChiTaRS; REXO2; human. DR GeneWiki; REXO2; -. DR GenomeRNAi; 25996; -. DR Pharos; Q9Y3B8; Tbio. DR PRO; PR:Q9Y3B8; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q9Y3B8; Protein. DR Bgee; ENSG00000076043; Expressed in secondary oocyte and 202 other cell types or tissues. DR ExpressionAtlas; Q9Y3B8; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; IDA:HPA. DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB. DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0008408; F:3'-5' exonuclease activity; IDA:MGI. DR GO; GO:0008296; F:3'-5'-DNA exonuclease activity; IDA:UniProtKB. DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IDA:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IDA:MGI. DR GO; GO:0009117; P:nucleotide metabolic process; TAS:ProtInc. DR CDD; cd06135; Orn; 1. DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1. DR HAMAP; MF_00045; Oligoribonuclease; 1. DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3. DR InterPro; IPR022894; Oligoribonuclease. DR InterPro; IPR012337; RNaseH-like_sf. DR InterPro; IPR036397; RNaseH_sf. DR PANTHER; PTHR11046; OLIGORIBONUCLEASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR11046:SF0; OLIGORIBONUCLEASE, MITOCHONDRIAL; 1. DR Pfam; PF00929; RNase_T; 1. DR SMART; SM00479; EXOIII; 1. DR SUPFAM; SSF53098; Ribonuclease H-like; 1. DR Genevisible; Q9Y3B8; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative initiation; Cytoplasm; Exonuclease; KW Hydrolase; Magnesium; Manganese; Metal-binding; Mitochondrion; Nuclease; KW Nucleus; Phosphoprotein; Reference proteome; Transit peptide. FT TRANSIT 1..25 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 26..237 FT /note="Oligoribonuclease, mitochondrial" FT /id="PRO_0000020273" FT DOMAIN 43..207 FT /note="Exonuclease" FT ACT_SITE 194 FT /evidence="ECO:0000269|PubMed:30926754, FT ECO:0000269|PubMed:31588022" FT BINDING 47 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:30926754, FT ECO:0000269|PubMed:31588022, ECO:0007744|PDB:6J7Y, FT ECO:0007744|PDB:6RCN" FT BINDING 47 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:30926754, FT ECO:0000269|PubMed:31588022, ECO:0007744|PDB:6J7Y, FT ECO:0007744|PDB:6RCN" FT BINDING 49 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:30926754, FT ECO:0000269|PubMed:31588022, ECO:0007744|PDB:6J7Y, FT ECO:0007744|PDB:6RCN" FT BINDING 147 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:30926754, FT ECO:0000269|PubMed:31588022, ECO:0007744|PDB:6RCN" FT BINDING 199 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:30926754, FT ECO:0007744|PDB:6J7Y" FT SITE 53 FT /note="Important for dinucleotide binding" FT /evidence="ECO:0000269|PubMed:30926754, FT ECO:0000269|PubMed:32365187" FT SITE 96 FT /note="Important for dinucleotide binding" FT /evidence="ECO:0000269|PubMed:30926754, FT ECO:0000269|PubMed:32365187" FT SITE 164 FT /note="Important for dinucleotide binding" FT /evidence="ECO:0000269|PubMed:30926754, FT ECO:0000269|PubMed:32365187" FT MOD_RES 92 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 122 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15592455" FT MOD_RES 173 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9D8S4" FT VAR_SEQ 1..38 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10810093" FT /id="VSP_003775" FT VAR_SEQ 1..32 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_054954" FT MUTAGEN 47 FT /note="D->A: Loss of 3'-to-5'exoribonuclease activity." FT /evidence="ECO:0000269|PubMed:31588022" FT MUTAGEN 49 FT /note="E->A: Loss of 3'-to-5'exoribonuclease activity." FT /evidence="ECO:0000269|PubMed:31588022, FT ECO:0000269|PubMed:32365187" FT MUTAGEN 53 FT /note="L->A: Loss of 3'-to-5'exoribonuclease activity." FT /evidence="ECO:0000269|PubMed:32365187" FT MUTAGEN 96 FT /note="W->A: Loss of 3'-to-5'exoribonuclease activity." FT /evidence="ECO:0000269|PubMed:32365187" FT MUTAGEN 146 FT /note="E->A: No effect on 3'-to-5'exoribonuclease FT activity." FT /evidence="ECO:0000269|PubMed:32365187" FT MUTAGEN 147 FT /note="D->A: Loss of 3'-to-5'exoribonuclease activity." FT /evidence="ECO:0000269|PubMed:31588022, FT ECO:0000269|PubMed:32365187" FT MUTAGEN 164 FT /note="Y->A: Loss of 3'-to-5'exoribonuclease activity." FT /evidence="ECO:0000269|PubMed:32365187" FT MUTAGEN 178 FT /note="R->A: Disruption of homodimerization and loss of FT 3'-to-5'exoribonuclease activity; when associated with FT R-179 or A-179." FT /evidence="ECO:0000269|PubMed:31588022" FT MUTAGEN 179 FT /note="W->A: Disruption of homodimerization and loss of FT 3'-to-5'exoribonuclease activity; when associated with FT A-178 or A-215." FT /evidence="ECO:0000269|PubMed:31588022, FT ECO:0000269|PubMed:32365187" FT MUTAGEN 179 FT /note="W->R: Disruption of homodimerization and loss of FT 3'-to-5'exoribonuclease activity; when associated with FT A-178." FT /evidence="ECO:0000269|PubMed:31588022" FT MUTAGEN 194 FT /note="H->A: Loss of 3'-to-5'exoribonuclease activity." FT /evidence="ECO:0000269|PubMed:30926754, FT ECO:0000269|PubMed:31588022" FT MUTAGEN 199 FT /note="D->A: Loss of 3'-to-5'exoribonuclease activity." FT /evidence="ECO:0000269|PubMed:30926754, FT ECO:0000269|PubMed:31588022" FT MUTAGEN 215 FT /note="F->A: Disruption of homodimerization and loss of FT 3'-to-5'exoribonuclease activity; when associated with FT A-179." FT /evidence="ECO:0000269|PubMed:32365187" FT CONFLICT 103 FT /note="K -> R (in Ref. 2; CAB53690 and 4; CAG38531)" FT /evidence="ECO:0000305" FT HELIX 37..40 FT /evidence="ECO:0007829|PDB:6N6J" FT STRAND 43..51 FT /evidence="ECO:0007829|PDB:6N6J" FT TURN 55..57 FT /evidence="ECO:0007829|PDB:6N6J" FT STRAND 60..68 FT /evidence="ECO:0007829|PDB:6N6J" FT STRAND 74..82 FT /evidence="ECO:0007829|PDB:6N6J" FT HELIX 87..91 FT /evidence="ECO:0007829|PDB:6N6J" FT HELIX 95..103 FT /evidence="ECO:0007829|PDB:6N6J" FT HELIX 106..112 FT /evidence="ECO:0007829|PDB:6N6J" FT HELIX 117..131 FT /evidence="ECO:0007829|PDB:6N6J" FT TURN 134..136 FT /evidence="ECO:0007829|PDB:6N6J" FT STRAND 139..141 FT /evidence="ECO:0007829|PDB:6N6J" FT HELIX 144..154 FT /evidence="ECO:0007829|PDB:6N6J" FT HELIX 156..160 FT /evidence="ECO:0007829|PDB:6N6J" FT STRAND 166..168 FT /evidence="ECO:0007829|PDB:6N6J" FT HELIX 169..179 FT /evidence="ECO:0007829|PDB:6N6J" FT HELIX 181..184 FT /evidence="ECO:0007829|PDB:6N6J" FT HELIX 196..214 FT /evidence="ECO:0007829|PDB:6N6J" FT HELIX 221..229 FT /evidence="ECO:0007829|PDB:6N6J" FT MUTAGEN Q9Y3B8-3:136 FT /note="D->A: 50% reduction in 3'-to-5'exoribonuclease FT activity." FT /evidence="ECO:0000269|PubMed:10851236" SQ SEQUENCE 237 AA; 26833 MW; A0343A8918B11B82 CRC64; MLGGSLGSRL LRGVGGSHGR FGARGVREGG AAMAAGESMA QRMVWVDLEM TGLDIEKDQI IEMACLITDS DLNILAEGPN LIIKQPDELL DSMSDWCKEH HGKSGLTKAV KESTITLQQA EYEFLSFVRQ QTPPGLCPLA GNSVHEDKKF LDKYMPQFMK HLHYRIIDVS TVKELCRRWY PEEYEFAPKK AASHRALDDI SESIKELQFY RNNIFKKKID EKKRKIIENG ENEKTVS //