Nudt16
entrez
75686
canonical
uniprot
Q6P3D0
canonical
ensembl
ENSMUSG00000032565
resolver
ensp
ENSMUSP00000035179
resolver
ensp
ENSMUSP00000349015
resolver
enst
ENSMUST00000035179
resolver
genesymbol
Nudt16
resolver
uniprot
Q9D716
resolver
uniprot_entry
NUD16_MOUSE
resolver
uniprot_sec
Q9D716
resolver
amino_acid_sequence
MEGHRKVELSEALALGPDWRHACHALLYAPDPRKLFGRIPMRFAVLMQMRFDGRLGFPGGFVDAQDSCLEDGLNRELREELGEAMSAFRVERSDYRSSHIAARPRVVAHFYAKRLTLEQLQAVEARAPQAKDHGLEVLGLVRVPLYVLRDGEGGLPAFLENSFIGAAREQLLEALQDLKLLDPGIIAKLKIPDSK
uniprot
proteins
ec_number
3.6.1.62
uniprot
proteins
ec_number
3.6.1.64
uniprot
proteins
function
FUNCTION: RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the RNA. Also catalyzes the cleavage of the cap structure on mRNAs. Does not hydrolyze cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with less efficiencies. Has broad substrate specificity with manganese or cobalt as cofactor and can act on various RNA species. Binds to the U8 snoRNA; metal is not required for RNA-binding. May play a role in the regulation of snoRNAs and mRNAs degradation (By similarity). Also acts as a phosphatase; hydrolyzes the non-canonical purine nucleotides inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as well as guanosine diphosphate (GDP), deoxyguanosine diphosphate (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and deoxyinosine triphosphate (ITP) to their respective monophosphate derivatives and does not distinguish between the deoxy- and ribose forms. The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP. Binds strongly to GTP, ITP and XTP. Participates in the hydrolysis of dIDP/IDP and probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. Exhibits decapping activity towards NAD-capped RNAs and FAD-capped RNAs (By similarity). Exhibits decapping activity towards dpCoA-capped RNAs in vitro (PubMed:32432673). {ECO:0000250|UniProtKB:Q96DE0, ECO:0000269|PubMed:20081199, ECO:0000269|PubMed:20385596, ECO:0000269|PubMed:21070968, ECO:0000269|PubMed:32432673}.
uniprot
proteins
mass_dalton
21825
uniprot
proteins
protein_family
NUDT16 subfamily
uniprot
proteins
protein_family
Nudix hydrolase family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
20081199
uniprot
proteins
pubmed
20385596
uniprot
proteins
pubmed
21070968
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
32432673
uniprot
proteins
sequence_length
195
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96DE0}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q6TEC1}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q6TEC1}. Cytoplasm {ECO:0000250|UniProtKB:Q96DE0}. Note=Localized predominantly in the cytoplasm. Localized in nucleolus, and in a minor proportion in distinct foci in the nucleoplasm. {ECO:0000250|UniProtKB:Q6TEC1, ECO:0000250|UniProtKB:Q96DE0}.
uniprot
proteins