| Function | Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form.nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, prefers NAD(+) and NaAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less effectively. Involved in the synthesis of ATP in the nucleus, together with PARP1, PARG and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+). Also acts as a cofactor for glutamate and aspartate ADP-ribosylation by directing PARP1 catalytic activity to glutamate and aspartate residues on histones. Protects against axonal degeneration following mechanical or toxic insults. Delays axonal degeneration after axotomy.results in a >10-fold increase in intact neurites 72 hours after injury. Neural protection does not correlate with cellular NAD(+) levels but may still require enzyme activity. |
| Protein Name | Nicotinamide/Nicotinic Acid Mononucleotide Adenylyltransferase 1Nmn/Namn Adenylyltransferase 1Nicotinamide Mononucleotide Adenylyltransferase 1Nmn Adenylyltransferase 1Nicotinate-Nucleotide Adenylyltransferase 1Namn Adenylyltransferase 1 |
| Database Links | Reactome: R-MMU-196807 |
| Cellular Localisation | NucleusCytoplasmLocalizes Predominantly To The Cytoplasm |
| Alternative Protein Names | Nicotinamide/Nicotinic Acid Mononucleotide Adenylyltransferase 1 proteinNmn/Namn Adenylyltransferase 1 proteinNicotinamide Mononucleotide Adenylyltransferase 1 proteinNmn Adenylyltransferase 1 proteinNicotinate-Nucleotide Adenylyltransferase 1 proteinNamn Adenylyltransferase 1 proteinNmnat1 proteinD4Cole1e proteinNmnat protein |
Information sourced from Uniprot.org
