ORN_RAT
ID ORN_RAT Reviewed; 237 AA.
AC Q5U1X1;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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).
CC -!- FUNCTION: 3'-to-5'exoribonuclease that preferentially degrades DNA and
CC RNA oligonucleotides composed of only two nucleotides (By similarity).
CC Binds and degrades longer oligonucleotides with a lower affinity (By
CC similarity). Plays dual roles in mitochondria, scavenging nanoRNAs
CC (small RNA oligonucleotides of <5 nucleotides) that are produced by the
CC degradosome and clearing short RNAs that are generated by RNA
CC processing (By similarity). Essential for correct initiation of
CC mitochondrial transcription, degrading mitochondrial RNA dinucleotides
CC to prevent RNA-primed transcription at non-canonical sites in the
CC mitochondrial genome (By similarity). Essential for embryonic
CC development (By similarity). {ECO:0000250|UniProtKB:Q9D8S4,
CC ECO:0000250|UniProtKB:Q9Y3B8}.
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 -!- SIMILARITY: Belongs to the oligoribonuclease family. {ECO:0000305}.
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DR EMBL; BC086420; AAH86420.1; -; mRNA.
DR RefSeq; NP_001008327.1; NM_001008326.1.
DR AlphaFoldDB; Q5U1X1; -.
DR SMR; Q5U1X1; -.
DR STRING; 10116.ENSRNOP00000050718; -.
DR iPTMnet; Q5U1X1; -.
DR PhosphoSitePlus; Q5U1X1; -.
DR jPOST; Q5U1X1; -.
DR PaxDb; Q5U1X1; -.
DR PRIDE; Q5U1X1; -.
DR Ensembl; ENSRNOT00000047633; ENSRNOP00000050718; ENSRNOG00000018939.
DR GeneID; 300689; -.
DR KEGG; rno:300689; -.
DR UCSC; RGD:1304874; rat.
DR CTD; 25996; -.
DR RGD; 1304874; Rexo2.
DR eggNOG; KOG3242; Eukaryota.
DR GeneTree; ENSGT00390000009255; -.
DR HOGENOM; CLU_064761_1_1_1; -.
DR InParanoid; Q5U1X1; -.
DR PhylomeDB; Q5U1X1; -.
DR TreeFam; TF314084; -.
DR PRO; PR:Q5U1X1; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000018939; Expressed in pancreas and 20 other tissues.
DR ExpressionAtlas; Q5U1X1; baseline and differential.
DR Genevisible; Q5U1X1; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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; ISS:UniProtKB.
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:RGD.
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:RGD.
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 2: Evidence at transcript 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_0000041952"
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:0000250|UniProtKB:Q9D8S4"
SQ SEQUENCE 237 AA; 26752 MW; 6CCC1505256EBDED CRC64;
MLGVSLGARL LRGVGGRRGQ FGARGVSEGS AAMAAGESMA QRMVWVDLEM TGLDIEKDQI
IEMACLITDS DLNILAEGPN LIIKQPDELL DSMSDWCKEH HGKSGLTKAV KESTVTLQQA
EYEFLSFVRQ QTPPGLCPLA GNSVHADKKF LDKHMPQFMK HLHYRIIDVS TVKELCRRWY
PEDYEFAPKK AASHRALDDI SESIKELQFY RNNIFKKKTD EKKRKIIENG ENEKPVS
