ORN_HUMAN
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 03-AUG-2022, entry version 181.
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}.
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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; 32.
DR STRING; 9606.ENSP00000265881; -.
DR GlyGen; Q9Y3B8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y3B8; -.
DR MetOSite; Q9Y3B8; -.
DR PhosphoSitePlus; Q9Y3B8; -.
DR BioMuta; REXO2; -.
DR DMDM; 116242694; -.
DR EPD; Q9Y3B8; -.
DR jPOST; Q9Y3B8; -.
DR MassIVE; Q9Y3B8; -.
DR MaxQB; Q9Y3B8; -.
DR PaxDb; Q9Y3B8; -.
DR PeptideAtlas; Q9Y3B8; -.
DR PRIDE; Q9Y3B8; -.
DR ProteomicsDB; 86006; -. [Q9Y3B8-1]
DR ProteomicsDB; 86007; -. [Q9Y3B8-2]
DR Antibodypedia; 32246; 171 antibodies from 22 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 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; 1079953at2759; -.
DR PhylomeDB; Q9Y3B8; -.
DR TreeFam; TF314084; -.
DR BRENDA; 3.1.13.3; 2681.
DR PathwayCommons; Q9Y3B8; -.
DR BioGRID-ORCS; 25996; 158 hits in 1097 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 200 other tissues.
DR ExpressionAtlas; Q9Y3B8; baseline and differential.
DR Genevisible; Q9Y3B8; HS.
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:UniProtKB.
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'-exodeoxyribonuclease activity; IDA:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease 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; -; 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; PTHR11046; 1.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
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 3'-
FT to-5'exoribonuclease activity; when associated with R-179
FT or A-179."
FT /evidence="ECO:0000269|PubMed:31588022"
FT MUTAGEN 179
FT /note="W->A: Disruption of homodimerization and loss of 3'-
FT to-5'exoribonuclease activity; when associated with A-178
FT 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 3'-
FT to-5'exoribonuclease activity; when associated with 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 3'-
FT to-5'exoribonuclease activity; when associated with 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
