NUDT12

Nucleotides are involved in numerous biochemical reactions and pathways within the cell as substrates, cofactors, and effectors. Nudix hydrolases, such as NUDT12, regulate the concentrations of individual nucleotides and of nucleotide ratios in response to changing circumstances (Abdelraheim et al., 2003 [PubMed 12790796]).[supplied by OMIM

nudix (nucleoside diphosphate linked moiety X)-type motif 12

mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA (PubMed:31101919, PubMed:31875550).
The NAD-cap is present at the 5'-end of some RNAs; in contrast to the canonical N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (PubMed:31101919).
Preferentially acts on NAD-capped transcripts in response to nutrient stress (PubMed:31101919).
Also acts on free nicotinamide adenine dinucleotide molecules: hydrolyzes NAD(H) into NMN(H) and AMP, and NADPH into NMNH and 2',5'-ADP (PubMed:12790796).
May act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism in this organelle (PubMed:12790796).
Regulates the levels of circadian clock components PER1, PER2, PER3 and CRY2 in the liver (By similarity).

Circadian regulation of gene expressionISS:UniProtKB
Methylguanosine-cap decappingManual Assertion Based On ExperimentIDA:UniProtKB
mRNA catabolic processISS:UniProtKB
NAD biosynthesis via nicotinamide riboside salvage pathwayTAS:Reactome
NAD catabolic processManual Assertion Based On ExperimentIDA:UniProtKB
NAD-cap decappingManual Assertion Based On ExperimentIDA:UniProtKB
NADH metabolic processManual Assertion Based On ExperimentIBA:GO_Central
NADP catabolic processManual Assertion Based On ExperimentIDA:UniProtKB

Cytoplasm
Peroxisome
Cytoplasmic granule
Localizes to cytoplasmic granules in the presence of BLMH.