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Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 (NMN/NaMN adenylyltransferase 1) (EC 2.7.7.1) (EC 2.7.7.18) (Nicotinamide mononucleotide adenylyltransferase 1) (NMN adenylyltransferase 1) (Nicotinate-nucleotide adenylyltransferase 1) (NaMN adenylyltransferase 1)

 NMNA1_MOUSE             Reviewed;         285 AA.
Q9EPA7; Q6B504;
09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
09-MAY-2003, sequence version 2.
07-JUN-2017, entry version 129.
RecName: Full=Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 {ECO:0000305};
Short=NMN/NaMN adenylyltransferase 1;
EC=2.7.7.1;
EC=2.7.7.18;
AltName: Full=Nicotinamide mononucleotide adenylyltransferase 1;
Short=NMN adenylyltransferase 1;
AltName: Full=Nicotinate-nucleotide adenylyltransferase 1;
Short=NaMN adenylyltransferase 1;
Name=Nmnat1; Synonyms=D4Cole1e, Nmnat;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000312|EMBL:AAG38490.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=129, C57BL/6J, and C57BL/Ola;
PubMed=11027338; DOI=10.1073/pnas.97.21.11377;
Conforti L., Tarlton A., Mack T.G.A., Mi W., Buckmaster E.A.,
Wagner D., Perry V.H., Coleman M.P.;
"A Ufd2/D4Cole1e chimeric protein and overexpression of Rbp7 in the
slow Wallerian degeneration (WldS) mouse.";
Proc. Natl. Acad. Sci. U.S.A. 97:11377-11382(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, AND
FUNCTION.
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=15381699; DOI=10.1074/jbc.M408388200;
Revollo J.R., Grimm A.A., Imai S.;
"The NAD biosynthesis pathway mediated by nicotinamide
phosphoribosyltransferase regulates Sir2 activity in mammalian
cells.";
J. Biol. Chem. 279:50754-50763(2004).
[3]
FUNCTION, AND MUTAGENESIS OF TRP-170.
PubMed=15310905; DOI=10.1126/science.1098014;
Araki T., Sasaki Y., Milbrandt J.;
"Increased nuclear NAD biosynthesis and SIRT1 activation prevent
axonal degeneration.";
Science 305:1010-1013(2004).
[4]
FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS
OF 125-ARG--LYS-128.
PubMed=16914673; DOI=10.1523/JNEUROSCI.2320-06.2006;
Sasaki Y., Araki T., Milbrandt J.;
"Stimulation of nicotinamide adenine dinucleotide biosynthetic
pathways delays axonal degeneration after axotomy.";
J. Neurosci. 26:8484-8491(2006).
-!- FUNCTION: Catalyzes the formation of NAD(+) from nicotinamide
mononucleotide (NMN) and ATP (PubMed:15381699). Can also use the
deamidated form; nicotinic acid mononucleotide (NaMN) as substrate
with the same efficiency (By similarity). Can use triazofurin
monophosphate (TrMP) as substrate (By similarity). Also catalyzes
the reverse reaction, i.e. the pyrophosphorolytic cleavage of
NAD(+) (By similarity). 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 (By similarity). Involved in
the synthesis of ATP in the nucleus, together with PARP1, PARG and
NUDT5 (By similarity). Nuclear ATP generation is required for
extensive chromatin remodeling events that are energy-consuming
(By similarity). Fails to cleave phosphorylated dinucleotides
NADP(+), NADPH and NaADP(+) (By similarity). Protects against
axonal degeneration following mechanical or toxic insults
(PubMed:15310905, PubMed:16914673). Delays axonal degeneration
after axotomy. Results in a >10-fold increase in intact neurites
72 hours after injury (PubMed:16914673).
{ECO:0000250|UniProtKB:Q9HAN9, ECO:0000269|PubMed:15310905,
ECO:0000269|PubMed:15381699, ECO:0000269|PubMed:16914673}.
-!- CATALYTIC ACTIVITY: ATP + nicotinamide ribonucleotide =
diphosphate + NAD(+). {ECO:0000250|UniProtKB:Q9HAN9}.
-!- CATALYTIC ACTIVITY: ATP + beta-nicotinate-D-ribonucleotide =
diphosphate + deamido-NAD(+).
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:Q9HAN9};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q9HAN9};
Note=Divalent metal cations. Zn(2+) confers higher activity as
compared to Mg(2+). {ECO:0000250|UniProtKB:Q9HAN9};
-!- ENZYME REGULATION: Activity is strongly inhibited by galotannin.
Inhibited by P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')-
tetraphosphate (Nap4AD). {ECO:0000250|UniProtKB:Q9HAN9}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=20.1 uM for nicotinamide mononucleotide (NMN)
{ECO:0000269|PubMed:15381699};
Vmax=34.1 umol/min/mg enzyme {ECO:0000269|PubMed:15381699};
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
nicotinamide D-ribonucleotide: step 1/1.
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-
NAD(+) from nicotinate D-ribonucleotide: step 1/1.
-!- SUBUNIT: Homohexamer. Interacts with ADPRT/PARP1.
{ECO:0000250|UniProtKB:Q9HAN9}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16914673}.
-!- DEVELOPMENTAL STAGE: Expressed throughout development and in
adulthood. {ECO:0000269|PubMed:16914673}.
-!- INDUCTION: By neuronal injury.
-!- MISCELLANEOUS: In strain C57BL/Ola, an 85 kb region on chromosome
4 containing Nmnat1 and Ube4b is triplicated. The N-terminal 70
residues of Ube4b becomes linked to the complete Nmnat1 protein
and encodes a fusion protein located in the nucleus which is
responsible for the Wallerian degeneration slow (Wlds) phenotype
characterized by delayed Wallerian degeneration of injured axons.
-!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG17285.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAG17286.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAG38490.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF260924; AAG17285.1; ALT_INIT; mRNA.
EMBL; AF260925; AAG17286.1; ALT_INIT; mRNA.
EMBL; AF260927; AAG38490.1; ALT_INIT; Genomic_DNA.
EMBL; AY679721; AAT76443.1; -; mRNA.
CCDS; CCDS18960.1; -.
RefSeq; NP_597679.1; NM_133435.1.
RefSeq; XP_006539168.1; XM_006539105.3.
UniGene; Mm.76062; -.
ProteinModelPortal; Q9EPA7; -.
SMR; Q9EPA7; -.
IntAct; Q9EPA7; 1.
STRING; 10090.ENSMUSP00000030845; -.
iPTMnet; Q9EPA7; -.
PhosphoSitePlus; Q9EPA7; -.
EPD; Q9EPA7; -.
MaxQB; Q9EPA7; -.
PaxDb; Q9EPA7; -.
PRIDE; Q9EPA7; -.
Ensembl; ENSMUST00000030845; ENSMUSP00000030845; ENSMUSG00000028992.
Ensembl; ENSMUST00000105693; ENSMUSP00000101318; ENSMUSG00000028992.
GeneID; 66454; -.
KEGG; mmu:66454; -.
UCSC; uc008vwj.1; mouse.
CTD; 64802; -.
MGI; MGI:1913704; Nmnat1.
eggNOG; KOG3199; Eukaryota.
eggNOG; COG1057; LUCA.
GeneTree; ENSGT00530000063189; -.
HOGENOM; HOG000216047; -.
HOVERGEN; HBG052640; -.
InParanoid; Q9EPA7; -.
KO; K06210; -.
OMA; DHFDHEI; -.
OrthoDB; EOG091G0JTI; -.
PhylomeDB; Q9EPA7; -.
TreeFam; TF315035; -.
BRENDA; 2.7.7.1; 3474.
Reactome; R-MMU-196807; Nicotinate metabolism.
SABIO-RK; Q9EPA7; -.
UniPathway; UPA00253; UER00332.
UniPathway; UPA00253; UER00600.
PRO; PR:Q9EPA7; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028992; -.
CleanEx; MM_NMNAT1; -.
ExpressionAtlas; Q9EPA7; baseline and differential.
Genevisible; Q9EPA7; MM.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IDA:MGI.
GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IDA:MGI.
GO; GO:0034628; P:'de novo' NAD biosynthetic process from aspartate; IBA:GO_Central.
GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; ISS:UniProtKB.
GO; GO:0009435; P:NAD biosynthetic process; IDA:MGI.
GO; GO:0009611; P:response to wounding; IDA:MGI.
Gene3D; 3.40.50.620; -; 1.
InterPro; IPR004821; Cyt_trans-like.
InterPro; IPR005248; NadD/NMNAT.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
Pfam; PF01467; CTP_transf_like; 1.
TIGRFAMs; TIGR00482; TIGR00482; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Magnesium; NAD; Nucleotide-binding;
Nucleotidyltransferase; Nucleus; Phosphoprotein;
Pyridine nucleotide biosynthesis; Reference proteome; Transferase;
Zinc.
CHAIN 1 285 Nicotinamide/nicotinic acid
mononucleotide adenylyltransferase 1.
/FTId=PRO_0000135013.
NP_BIND 15 17 ATP. {ECO:0000250|UniProtKB:Q96T66,
ECO:0000250|UniProtKB:Q9HAN9}.
NP_BIND 157 159 ATP. {ECO:0000250|UniProtKB:Q96T66}.
NP_BIND 225 228 ATP. {ECO:0000250|UniProtKB:Q96T66}.
REGION 55 57 Substrate binding.
{ECO:0000250|UniProtKB:Q9HAN9}.
REGION 92 95 Substrate binding.
{ECO:0000250|UniProtKB:Q9HAN9}.
REGION 169 170 Substrate binding.
{ECO:0000250|UniProtKB:Q9HAN9}.
MOTIF 123 129 Nuclear localization signal.
{ECO:0000255}.
BINDING 24 24 ATP. {ECO:0000250|UniProtKB:Q96T66}.
BINDING 58 58 ATP. {ECO:0000250|UniProtKB:Q96T66}.
MOD_RES 117 117 Phosphoserine.
{ECO:0000250|UniProtKB:Q9HAN9}.
MUTAGEN 125 128 RKRK->AAAA: Locates to the cytoplasm. Has
no affect on enzyme activity or axonal
protection.
{ECO:0000269|PubMed:16914673}.
MUTAGEN 170 170 W->A: Decrease in enzyme activity. Has no
axonal protective effect.
{ECO:0000269|PubMed:15310905}.
SEQUENCE 285 AA; 32355 MW; 2769D42E894EB84F CRC64;
MDSSKKTEVV LLACGSFNPI TNMHLRLFEL AKDYMHATGK YSVIKGIISP VGDAYKKKGL
IPAHHRIIMA ELATKNSHWV EVDTWESLQK EWVETVKVLR YHQEKLATGS CSYPQSSPAL
EKPGRKRKWA DQKQDSSPQK PQEPKPTGVP KVKLLCGADL LESFSVPNLW KMEDITQIVA
NFGLICITRA GSDAQKFIYE SDVLWRHQSN IHLVNEWITN DISSTKIRRA LRRGQSIRYL
VPDLVQEYIE KHELYNTESE GRNAGVTLAP LQRNAAEAKH NHSTL


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