Nmnat2
entrez
226518
canonical
uniprot
Q8BNJ3
canonical
ensembl
ENSMUSG00000042751
resolver
ensp
ENSMUSP00000041110
resolver
ensp
ENSMUSP00000210296
resolver
enst
ENSMUST00000043313
resolver
genesymbol
Nmnat2
resolver
genesymbol_syn
Kiaa0479
resolver
uniprot
Q5HZI3
resolver
uniprot_entry
NMNA2_MOUSE
resolver
uniprot_entry
Q5HZI3_MOUSE
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:0000250|UniProtKB:Q9BZQ4}.
uniprot
proteins
amino_acid_sequence
MTETTKTHVILLACGSFNPITKGHIQMFERARDYLHKTGRFIVIGGIVSPVHDSYGKQGLVSSRHRLIMCQLAVQNSDWIRVDPWECYQDTWQTTCSVLEHHRDLMKRVTGCILSNVNTPSMTPVIGQPQHENTQPIYQNSNVPTKPTAAKILGKVGESLSRICCVRPPVERFTFVDENANLGTVMRYEEIELRILLLCGSDLLESFCIPGLWNEADMEVIVGDFGIVVVPRDAADTDRIMNHSSILRKYKNNIMVVKDDINHPMSVVSSTKSRLALQHGDGHVVDYLSQPVIDYILKSQLYINASG
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 (PubMed:20126265, PubMed:23082226). 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 (PubMed:20126265, PubMed:23082226, PubMed:25818290). Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP (By similarity). Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate but with a lower efficiency. Cannot use triazofurin monophosphate (TrMP) as substrate (By similarity). 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 (By similarity). Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+) (By similarity). 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). May be involved in the maintenance of axonal integrity (PubMed:22425156). {ECO:0000250|UniProtKB:Q9BZQ4, ECO:0000269|PubMed:20126265, ECO:0000269|PubMed:22425156, ECO:0000269|PubMed:23082226, ECO:0000269|PubMed:25818290}.
uniprot
proteins
mass_dalton
34505
uniprot
proteins
mutagenesis
MUTAGEN 151; /note="K->A: Impaired membrane association in neurons; when associated with A-155; A-162; A-167 and A-172."; MUTAGEN 155; /note="K->A: Impaired membrane association in neurons; when associated with A-151; A-162; A-167 and A-172."; MUTAGEN 162; /note="R->A: Impaired membrane association in neurons; when associated with A-151; A-155; A-167 and A-172."; MUTAGEN 164..165; /note="CC->SS: Abolished palmitoylation and membrane association in neurons."; /evidence="ECO:0000269|PubMed:23610559"; MUTAGEN 167; /note="R->A: Impaired membrane association in neurons; when associated with A-151; A-155; A-162 and A-172."; MUTAGEN 172; /note="R->A: Impaired membrane association in neurons; when associated with A-151; A-155; A-162 and A-167.
uniprot
proteins
pathway_participation
PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1. {ECO:0000250|UniProtKB:Q9BZQ4}.; PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1. {ECO:0000250|UniProtKB:Q9BZQ4}.
uniprot
proteins
post_translational_modification
PTM: Degraded in response to injured neurite (PubMed:20126265, PubMed:23610559, PubMed:23665224). Degradation is caused by polyubiquitination by MYCBP2 after recognition by FBXO45 (PubMed:23610559, PubMed:23665224). {ECO:0000269|PubMed:20126265, ECO:0000269|PubMed:23610559, ECO:0000269|PubMed:23665224}.; PTM: Palmitoylated; palmitoylation is required for membrane association. {ECO:0000269|PubMed:23610559}.
uniprot
proteins
protein_family
Eukaryotic NMN adenylyltransferase family
uniprot
proteins
pubmed
14621295
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
20126265
uniprot
proteins
pubmed
22425156
uniprot
proteins
pubmed
23082226
uniprot
proteins
pubmed
23610559
uniprot
proteins
pubmed
23665224
uniprot
proteins
pubmed
25818290
uniprot
proteins
sequence_length
307
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:23610559}; Lipid-anchor {ECO:0000269|PubMed:23610559}. Cytoplasmic vesicle membrane; Lipid-anchor {ECO:0000269|PubMed:23610559}. Cytoplasm {ECO:0000250|UniProtKB:Q9BZQ4}. Cell projection, axon {ECO:0000269|PubMed:23610559}. Note=Delivered to axons with Golgi-derived cytoplasmic vesicles. {ECO:0000269|PubMed:23610559}.
uniprot
proteins