ORN_MOUSE
ID ORN_MOUSE Reviewed; 237 AA.
AC Q9D8S4;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 144.
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=Smfn;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-173, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: 3'-to-5'exoribonuclease that preferentially degrades DNA and
CC RNA oligonucleotides composed of only two nucleotides
CC (PubMed:31588022). Binds and degrades longer oligonucleotides with a
CC lower affinity (By similarity). 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 (By similarity). Essential for correct
CC initiation of mitochondrial transcription, degrading mitochondrial RNA
CC dinucleotides to prevent RNA-primed transcription at non-canonical
CC sites in the mitochondrial genome (PubMed:31588022). Essential for
CC embryonic development (PubMed:31588022). {ECO:0000250|UniProtKB:Q9Y3B8,
CC ECO:0000269|PubMed:31588022}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9Y3B8};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9Y3B8};
CC -!- SUBUNIT: Homodimer (By similarity). Homotetramer (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y3B8}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:Q9Y3B8}. Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q9Y3B8}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9Y3B8}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9Y3B8}. Nucleus {ECO:0000250|UniProtKB:Q9Y3B8}.
CC -!- DISRUPTION PHENOTYPE: Causes embryonic lethality before E8.5
CC (PubMed:31588022). Heart- and skeletal-muscle-specific knockout mice
CC show elevated concentrations of the RNA dinucleotide pApA in the
CC mitochondria purified from the heart (PubMed:31588022).
CC {ECO:0000269|PubMed:31588022}.
CC -!- SIMILARITY: Belongs to the oligoribonuclease family. {ECO:0000305}.
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DR EMBL; AK007731; BAB25219.2; -; mRNA.
DR CCDS; CCDS23154.1; -.
DR RefSeq; NP_077195.2; NM_024233.3.
DR AlphaFoldDB; Q9D8S4; -.
DR SMR; Q9D8S4; -.
DR BioGRID; 222638; 1.
DR STRING; 10090.ENSMUSP00000034524; -.
DR iPTMnet; Q9D8S4; -.
DR PhosphoSitePlus; Q9D8S4; -.
DR EPD; Q9D8S4; -.
DR MaxQB; Q9D8S4; -.
DR PaxDb; Q9D8S4; -.
DR PeptideAtlas; Q9D8S4; -.
DR PRIDE; Q9D8S4; -.
DR ProteomicsDB; 294222; -.
DR Antibodypedia; 32246; 171 antibodies from 22 providers.
DR DNASU; 104444; -.
DR Ensembl; ENSMUST00000034524; ENSMUSP00000034524; ENSMUSG00000032026.
DR GeneID; 104444; -.
DR KEGG; mmu:104444; -.
DR UCSC; uc009pia.1; mouse.
DR CTD; 25996; -.
DR MGI; MGI:1888981; Rexo2.
DR VEuPathDB; HostDB:ENSMUSG00000032026; -.
DR eggNOG; KOG3242; Eukaryota.
DR GeneTree; ENSGT00390000009255; -.
DR HOGENOM; CLU_064761_1_1_1; -.
DR InParanoid; Q9D8S4; -.
DR OMA; AFFHYRN; -.
DR OrthoDB; 1079953at2759; -.
DR PhylomeDB; Q9D8S4; -.
DR TreeFam; TF314084; -.
DR BioGRID-ORCS; 104444; 4 hits in 74 CRISPR screens.
DR PRO; PR:Q9D8S4; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9D8S4; protein.
DR Bgee; ENSMUSG00000032026; Expressed in lacrimal gland and 259 other tissues.
DR ExpressionAtlas; Q9D8S4; baseline and differential.
DR Genevisible; Q9D8S4; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008408; F:3'-5' exonuclease activity; ISS:UniProtKB.
DR GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; ISS:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; ISO:MGI.
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 Acetylation; Cytoplasm; Exonuclease; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Mitochondrion; Nuclease; Nucleus; Phosphoprotein;
KW 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_0000041951"
FT DOMAIN 43..207
FT /note="Exonuclease"
FT ACT_SITE 194
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B8"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B8"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B8"
FT BINDING 49
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B8"
FT BINDING 147
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B8"
FT BINDING 199
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B8"
FT SITE 53
FT /note="Important for dinucleotide binding"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B8"
FT SITE 96
FT /note="Important for dinucleotide binding"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B8"
FT SITE 164
FT /note="Important for dinucleotide binding"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B8"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B8"
FT MOD_RES 122
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B8"
FT MOD_RES 173
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
SQ SEQUENCE 237 AA; 26739 MW; 6CCC1505257B5DED CRC64;
MLGVSLGARL LRGVGGRRGQ FGARGVSEGS AAMAAGESMA QRMVWVDLEM TGLDIEKDQI
IEMACLITDS DLNILAEGPN LIIKQPDELL DSMSDWCKEH HGKSGLTKAV KESTVTLQQA
EYEFLSFVRQ QTPPGLCPLA GNSVHADKKF LDKHMPQFMK HLHYRIIDVS TVKELCRRWY
PEDYEFAPKK AASHRALDDI SESIKELQFY RNNIFKKKTD EKKRKIIENG ETEKPVS
