NMNAT2
entrez
23057
canonical
uniprot
Q9BZQ4
canonical
ensembl
ENSG00000157064
resolver
ensp
ENSP00000287713
resolver
ensp
ENSP00000294868
resolver
genesymbol
NMNAT2
resolver
genesymbol_syn
C1orf15
resolver
genesymbol_syn
KIAA0479
resolver
hgnc
HGNC:16789
resolver
uniprot
O75067
resolver
uniprot
Q5T1Q3
resolver
uniprot
Q8WU99
resolver
uniprot
Q96QW1
resolver
uniprot_entry
NMNA2_HUMAN
resolver
uniprot_sec
O75067
resolver
uniprot_sec
Q5T1Q3
resolver
uniprot_sec
Q8WU99
resolver
uniprot_sec
Q96QW1
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by P1-(adenosine-5')-P3-(nicotinamide-riboside-5')-triphosphate (Np3AD) and P1-(adenosine-5')-P4-(nicotinamide-riboside-5')-tetraphosphate (Np4AD). {ECO:0000269|PubMed:17402747}.
uniprot
proteins
amino_acid_sequence
MTETTKTHVILLACGSFNPITKGHIQMFERARDYLHKTGRFIVIGGIVSPVHDSYGKQGLVSSRHRLIMCQLAVQNSDWIRVDPWECYQDTWQTTCSVLEHHRDLMKRVTGCILSNVNTPSMTPVIGQPQNETPQPIYQNSNVATKPTAAKILGKVGESLSRICCVRPPVERFTFVDENANLGTVMRYEEIELRILLLCGSDLLESFCIPGLWNEADMEVIVGDFGIVVVPRDAADTDRIMNHSSILRKYKNNIMVVKDDINHPMSVVSSTKSRLALQHGDGHVVDYLSQPVIDYILKSQLYINASG
uniprot
proteins
ec_number
2.7.7.1
uniprot
proteins
ec_number
2.7.7.18
uniprot
proteins
function
FUNCTION: 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 (PubMed:16118205, PubMed:17402747). Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate but with a lower efficiency (PubMed:16118205, PubMed:17402747). Cannot use triazofurin monophosphate (TrMP) as substrate (PubMed:16118205, PubMed:17402747). Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+) (PubMed:16118205, PubMed:17402747). For the pyrophosphorolytic activity prefers NAD(+), NADH and NaAD as substrates and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less effectively (PubMed:16118205, PubMed:17402747). Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+) (PubMed:16118205, PubMed:17402747). Also acts as an activator of ADP-ribosylation by supporting the catalytic activity of PARP16 and promoting mono-ADP-ribosylation of ribosomes by PARP16 (PubMed:34314702). May be involved in the maintenance of axonal integrity (By similarity). {ECO:0000250|UniProtKB:Q8BNJ3, ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747, ECO:0000269|PubMed:34314702}.
uniprot
proteins
mass_dalton
34439
uniprot
proteins
mutagenesis
MUTAGEN 24; /note="H->A: Reduces activity by 95%."; /evidence="ECO:0000269|PubMed:14516279"; MUTAGEN 24; /note="H->D: Abolished nicotinamide-nucleotide adenylyltransferase activity; abolished ability to promote mono-ADP-ribosylation of ribosomes."; /evidence="ECO:0000269|PubMed:34314702"; MUTAGEN 92; /note="W->G: Abolished nicotinamide-nucleotide adenylyltransferase activity; abolished ability to promote mono-ADP-ribosylation of ribosomes."; /evidence="ECO:0000269|PubMed:14516279, ECO:0000269|PubMed:34314702
uniprot
proteins
pathway_participation
PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1. {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}.; PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1. {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}.
uniprot
proteins
post_translational_modification
PTM: Degraded in response to injured neurite (By similarity). Degradation is caused by polyubiquitination by MYCBP2 after recognition by FBXO45 (PubMed:29643511, PubMed:29997255). {ECO:0000250|UniProtKB:Q8BNJ3, ECO:0000269|PubMed:29643511, ECO:0000269|PubMed:29997255}.; PTM: Palmitoylated; palmitoylation is required for membrane association. {ECO:0000250|UniProtKB:Q8BNJ3}.
uniprot
proteins
protein_family
Eukaryotic NMN adenylyltransferase family
uniprot
proteins
pubmed
11318611
uniprot
proteins
pubmed
12359228
uniprot
proteins
pubmed
14516279
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16118205
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17402747
uniprot
proteins
pubmed
29643511
uniprot
proteins
pubmed
29997255
uniprot
proteins
pubmed
34314702
uniprot
proteins
pubmed
9455484
uniprot
proteins
sequence_length
307
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:16118205}; Lipid-anchor {ECO:0000250|UniProtKB:Q8BNJ3}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q8BNJ3}; Lipid-anchor {ECO:0000250|UniProtKB:Q8BNJ3}. Cytoplasm {ECO:0000269|PubMed:16118205}. Cell projection, axon {ECO:0000250|UniProtKB:Q8BNJ3}. Note=Delivered to axons with Golgi-derived cytoplasmic vesicles. {ECO:0000250|UniProtKB:Q8BNJ3}.
uniprot
proteins