Nmnat2 - nicotinamide nucleotide adenylyltransferase 2 (Norway rat)
Gene
Symbol
Taxonomy
Dates
- Create:2016-09-14
- Modify:2025-01-26
Description
Predicted to enable nicotinamide-nucleotide adenylyltransferase activity; nicotinate-nucleotide adenylyltransferase activity; and protein ADP-ribosyltransferase-substrate adaptor activity. Involved in NAD biosynthetic process and cellular response to angiotensin. Predicted to be located in several cellular components, including cytosol; late endosome; and trans-Golgi network. Predicted to be active in Golgi apparatus. Biomarker of hypertrophic cardiomyopathy. Orthologous to human NMNAT2 (nicotinamide nucleotide adenylyltransferase 2).
- nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- NMN adenylyltransferase 2
- NMN/NaMN adenylyltransferase 2
- naMN adenylyltransferase 1
- naMN adenylyltransferase 2
- nicotinamide mononucleotide adenylyltransferase 2
- nicotinate-nucleotide adenylyltransferase 1
- nicotinate-nucleotide adenylyltransferase 2
Nicotinamide/nicotinate-nucleotide adenylyltransferase that acts as an axon maintenance factor (By similarity). Axon survival factor required for the maintenance of healthy axons: acts by delaying Wallerian axon degeneration, an evolutionarily conserved process that drives the loss of damaged axons (By similarity). Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate but with a lower efficiency. Cannot use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity prefers NAD(+), NADH and NaAD as substrates and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less effectively. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+). Also acts as an activator of ADP-ribosylation by supporting the catalytic activity of PARP16 and promoting mono-ADP-ribosylation of ribosomes by PARP16 (By similarity).
Highly accurate protein structure prediction with AlphaFold. Nature. 2021 Aug;596(7873):583-589. DOI:10.1038/s41586-021-03819-2. PMID:34265844; PMCID:PMC8371605
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