REXO2
entrez
25996
canonical
uniprot
Q9Y3B8
canonical
ensembl
ENSG00000076043
resolver
ensp
ENSP00000265881
resolver
genesymbol
REXO2
resolver
genesymbol_syn
SFN
resolver
genesymbol_syn
SMFN
resolver
hgnc
HGNC:17851
resolver
uniprot
B2R532
resolver
uniprot
Q32Q18
resolver
uniprot
Q53FT1
resolver
uniprot
Q6FIC6
resolver
uniprot
Q9UFY7
resolver
uniprot_entry
ORN_HUMAN
resolver
uniprot_sec
B2R532
resolver
uniprot_sec
Q32Q18
resolver
uniprot_sec
Q53FT1
resolver
uniprot_sec
Q6FIC6
resolver
uniprot_sec
Q9UFY7
resolver
activity_regulation
ACTIVITY REGULATION: [Isoform 3]: Inhibited by adenosine 3',5'-bisphosphate. {ECO:0000269|PubMed:16682444}.
uniprot
proteins
amino_acid_sequence
MLGGSLGSRLLRGVGGSHGRFGARGVREGGAAMAAGESMAQRMVWVDLEMTGLDIEKDQIIEMACLITDSDLNILAEGPNLIIKQPDELLDSMSDWCKEHHGKSGLTKAVKESTITLQQAEYEFLSFVRQQTPPGLCPLAGNSVHEDKKFLDKYMPQFMKHLHYRIIDVSTVKELCRRWYPEEYEFAPKKAASHRALDDISESIKELQFYRNNIFKKKIDEKKRKIIENGENEKTVS
uniprot
proteins
ec_number
3.1.15.-
uniprot
proteins
function
FUNCTION: 3'-to-5'exoribonuclease that preferentially degrades DNA and RNA oligonucleotides composed of only two nucleotides (PubMed:23741365, PubMed:30926754, PubMed:31588022, PubMed:32365187). Binds and degrades longer oligonucleotides with a lower affinity (PubMed:30926754, PubMed:31588022, PubMed:32365187). Plays dual roles in mitochondria, scavenging nanoRNAs (small RNA oligonucleotides of <5 nucleotides) that are produced by the degradosome and clearing short RNAs that are generated by RNA processing (PubMed:30926754, PubMed:31588022, PubMed:32365187). Essential for correct initiation of mitochondrial transcription, degrading mitochondrial RNA dinucleotides to prevent RNA-primed transcription at non-canonical sites in the mitochondrial genome (PubMed:31588022). Essential for embryonic development (By similarity). {ECO:0000250|UniProtKB:Q9D8S4, ECO:0000269|PubMed:23741365, ECO:0000269|PubMed:30926754, ECO:0000269|PubMed:31588022, ECO:0000269|PubMed:32365187}.; FUNCTION: [Isoform 3]: 3'-to-5'exoribonuclease that preferentially degrades DNA and RNA oligonucleotides composed of only two nucleotides. {ECO:0000269|PubMed:10851236, ECO:0000269|PubMed:16682444}.
uniprot
proteins
mass_dalton
26833
uniprot
proteins
mutagenesis
MUTAGEN 47; /note="D->A: Loss of 3'-to-5'exoribonuclease activity."; /evidence="ECO:0000269|PubMed:31588022"; MUTAGEN 49; /note="E->A: Loss of 3'-to-5'exoribonuclease activity."; /evidence="ECO:0000269|PubMed:31588022, ECO:0000269|PubMed:32365187"; MUTAGEN 53; /note="L->A: Loss of 3'-to-5'exoribonuclease activity."; /evidence="ECO:0000269|PubMed:32365187"; MUTAGEN 96; /note="W->A: Loss of 3'-to-5'exoribonuclease activity."; /evidence="ECO:0000269|PubMed:32365187"; MUTAGEN 146; /note="E->A: No effect on 3'-to-5'exoribonuclease activity."; /evidence="ECO:0000269|PubMed:32365187"; MUTAGEN 147; /note="D->A: Loss of 3'-to-5'exoribonuclease activity."; /evidence="ECO:0000269|PubMed:31588022, ECO:0000269|PubMed:32365187"; MUTAGEN 164; /note="Y->A: Loss of 3'-to-5'exoribonuclease activity."; /evidence="ECO:0000269|PubMed:32365187"; MUTAGEN 178; /note="R->A: Disruption of homodimerization and loss of 3'-to-5'exoribonuclease activity; when associated with R-179 or A-179."; /evidence="ECO:0000269|PubMed:31588022"; MUTAGEN 179; /note="W->A: Disruption of homodimerization and loss of 3'-to-5'exoribonuclease activity; when associated with A-178 or A-215."; /evidence="ECO:0000269|PubMed:31588022, ECO:0000269|PubMed:32365187"; MUTAGEN 179; /note="W->R: Disruption of homodimerization and loss of 3'-to-5'exoribonuclease activity; when associated with A-178."; /evidence="ECO:0000269|PubMed:31588022"; MUTAGEN 194; /note="H->A: Loss of 3'-to-5'exoribonuclease activity."; /evidence="ECO:0000269|PubMed:30926754, ECO:0000269|PubMed:31588022"; MUTAGEN 199; /note="D->A: Loss of 3'-to-5'exoribonuclease activity."; /evidence="ECO:0000269|PubMed:30926754, ECO:0000269|PubMed:31588022"; MUTAGEN 215; /note="F->A: Disruption of homodimerization and loss of 3'-to-5'exoribonuclease activity; when associated with A-179."; /evidence="ECO:0000269|PubMed:32365187"; MUTAGEN Q9Y3B8-3:136; /note="D->A: 50% reduction in 3'-to-5'exoribonuclease activity."; /evidence="ECO:0000269|PubMed:10851236
uniprot
proteins
protein_family
Oligoribonuclease family
uniprot
proteins
pubmed
10810093
uniprot
proteins
pubmed
10851236
uniprot
proteins
pubmed
11230166
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
16682444
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23741365
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
30926754
uniprot
proteins
pubmed
31588022
uniprot
proteins
pubmed
32365187
uniprot
proteins
sequence_length
237
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:23741365}. Mitochondrion matrix {ECO:0000269|PubMed:23741365}. Mitochondrion {ECO:0000269|PubMed:32365187}. Cytoplasm {ECO:0000269|PubMed:23741365, ECO:0000269|PubMed:32365187}. Nucleus {ECO:0000269|PubMed:32365187}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:32365187}. Nucleus {ECO:0000269|PubMed:32365187}.
uniprot
proteins