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Protein

Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1

Gene

Nmnat1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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).By similarity3 Publications

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.

Catalytic activityi

ATP + nicotinamide ribonucleotide = diphosphate + NAD+.By similarity
ATP + beta-nicotinate-D-ribonucleotide = diphosphate + deamido-NAD+.

Cofactori

Zn2+By similarity, Mg2+By similarityNote: Divalent metal cations. Zn2+ confers higher activity as compared to Mg2+.By similarity

Activity regulationi

Activity is strongly inhibited by galotannin. Inhibited by P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')-tetraphosphate (Nap4AD).By similarity

Kineticsi

  1. KM=20.1 µM for nicotinamide mononucleotide (NMN)1 Publication
  1. Vmax=34.1 µmol/min/mg enzyme1 Publication

Pathwayi: NAD(+) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes NAD(+) from nicotinamide D-ribonucleotide.
Proteins known to be involved in this subpathway in this organism are:
  1. Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 (Nmnat1), Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 (Nmnat2), Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3 (Nmnat3), Nicotinamide-nucleotide adenylyltransferase, Nicotinamide-nucleotide adenylyltransferase (Nmnat1)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes NAD(+) from nicotinamide D-ribonucleotide, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Pathwayi: NAD(+) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes deamido-NAD(+) from nicotinate D-ribonucleotide.
Proteins known to be involved in this subpathway in this organism are:
  1. Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 (Nmnat1), Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 (Nmnat2), Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3 (Nmnat3)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes deamido-NAD(+) from nicotinate D-ribonucleotide, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei24ATPBy similarity1
Binding sitei58ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi15 – 17ATPBy similarity3
Nucleotide bindingi157 – 159ATPBy similarity3
Nucleotide bindingi225 – 228ATPBy similarity4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionNucleotidyltransferase, Transferase
Biological processPyridine nucleotide biosynthesis
LigandATP-binding, Magnesium, NAD, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi2.7.7.1 3474
ReactomeiR-MMU-196807 Nicotinate metabolism
SABIO-RKiQ9EPA7
UniPathwayi
UPA00253;UER00332

UPA00253;UER00600

Names & Taxonomyi

Protein namesi
Recommended name:
Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1Curated (EC:2.7.7.1, EC:2.7.7.18)
Short name:
NMN/NaMN adenylyltransferase 1
Alternative name(s):
Nicotinamide mononucleotide adenylyltransferase 1
Short name:
NMN adenylyltransferase 1
Nicotinate-nucleotide adenylyltransferase 1
Short name:
NaMN adenylyltransferase 1
Gene namesi
Name:Nmnat1
Synonyms:D4Cole1e, Nmnat
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1913704 Nmnat1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi125 – 128RKRK → AAAA: Locates to the cytoplasm. Has no effect on enzyme activity or axonal protection. 1 Publication4
Mutagenesisi170W → A: Decrease in enzyme activity. Has no axonal protective effect. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001350131 – 285Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1Add BLAST285

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei117PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9EPA7
MaxQBiQ9EPA7
PaxDbiQ9EPA7
PRIDEiQ9EPA7

PTM databases

iPTMnetiQ9EPA7
PhosphoSitePlusiQ9EPA7

Expressioni

Developmental stagei

Expressed throughout development and in adulthood.1 Publication

Inductioni

By neuronal injury.

Gene expression databases

BgeeiENSMUSG00000028992 Expressed in 209 organ(s), highest expression level in ear
CleanExiMM_NMNAT1
ExpressionAtlasiQ9EPA7 baseline and differential
GenevisibleiQ9EPA7 MM

Interactioni

Subunit structurei

Homohexamer. Interacts with ADPRT/PARP1.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi211485, 1 interactor
IntActiQ9EPA7, 1 interactor
STRINGi10090.ENSMUSP00000030845

Structurei

3D structure databases

ProteinModelPortaliQ9EPA7
SMRiQ9EPA7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni55 – 57Substrate bindingBy similarity3
Regioni92 – 95Substrate bindingBy similarity4
Regioni169 – 170Substrate bindingBy similarity2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi123 – 129Nuclear localization signalSequence analysis7

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3199 Eukaryota
COG1057 LUCA
GeneTreeiENSGT00530000063189
HOGENOMiHOG000216047
HOVERGENiHBG052640
InParanoidiQ9EPA7
KOiK06210
OMAiVCITRAG
OrthoDBiEOG091G0JTI
PhylomeDBiQ9EPA7
TreeFamiTF315035

Family and domain databases

InterProiView protein in InterPro
IPR004821 Cyt_trans-like
IPR005248 NadD/NMNAT
PfamiView protein in Pfam
PF01467 CTP_transf_like, 1 hit
TIGRFAMsiTIGR00482 TIGR00482, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q9EPA7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDSSKKTEVV LLACGSFNPI TNMHLRLFEL AKDYMHATGK YSVIKGIISP
60 70 80 90 100
VGDAYKKKGL IPAHHRIIMA ELATKNSHWV EVDTWESLQK EWVETVKVLR
110 120 130 140 150
YHQEKLATGS CSYPQSSPAL EKPGRKRKWA DQKQDSSPQK PQEPKPTGVP
160 170 180 190 200
KVKLLCGADL LESFSVPNLW KMEDITQIVA NFGLICITRA GSDAQKFIYE
210 220 230 240 250
SDVLWRHQSN IHLVNEWITN DISSTKIRRA LRRGQSIRYL VPDLVQEYIE
260 270 280
KHELYNTESE GRNAGVTLAP LQRNAAEAKH NHSTL
Length:285
Mass (Da):32,355
Last modified:May 9, 2003 - v2
Checksum:i2769D42E894EB84F
GO

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B0QZL2B0QZL2_MOUSE
Nicotinamide/nicotinic acid mononuc...
Nmnat1
149Annotation score:
B1AS01B1AS01_MOUSE
Nicotinamide/nicotinic acid mononuc...
Nmnat1
37Annotation score:

Sequence cautioni

The sequence AAG17285 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAG17286 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAG38490 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF260924 mRNA Translation: AAG17285.1 Different initiation.
AF260925 mRNA Translation: AAG17286.1 Different initiation.
AF260927 Genomic DNA Translation: AAG38490.1 Different initiation.
AY679721 mRNA Translation: AAT76443.1
CCDSiCCDS18960.1
RefSeqiNP_597679.1, NM_133435.1
XP_006539168.1, XM_006539105.3
UniGeneiMm.76062

Genome annotation databases

EnsembliENSMUST00000030845; ENSMUSP00000030845; ENSMUSG00000028992
ENSMUST00000105693; ENSMUSP00000101318; ENSMUSG00000028992
GeneIDi66454
KEGGimmu:66454
UCSCiuc008vwj.1 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF260924 mRNA Translation: AAG17285.1 Different initiation.
AF260925 mRNA Translation: AAG17286.1 Different initiation.
AF260927 Genomic DNA Translation: AAG38490.1 Different initiation.
AY679721 mRNA Translation: AAT76443.1
CCDSiCCDS18960.1
RefSeqiNP_597679.1, NM_133435.1
XP_006539168.1, XM_006539105.3
UniGeneiMm.76062

3D structure databases

ProteinModelPortaliQ9EPA7
SMRiQ9EPA7
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211485, 1 interactor
IntActiQ9EPA7, 1 interactor
STRINGi10090.ENSMUSP00000030845

PTM databases

iPTMnetiQ9EPA7
PhosphoSitePlusiQ9EPA7

Proteomic databases

EPDiQ9EPA7
MaxQBiQ9EPA7
PaxDbiQ9EPA7
PRIDEiQ9EPA7

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030845; ENSMUSP00000030845; ENSMUSG00000028992
ENSMUST00000105693; ENSMUSP00000101318; ENSMUSG00000028992
GeneIDi66454
KEGGimmu:66454
UCSCiuc008vwj.1 mouse

Organism-specific databases

CTDi64802
MGIiMGI:1913704 Nmnat1

Phylogenomic databases

eggNOGiKOG3199 Eukaryota
COG1057 LUCA
GeneTreeiENSGT00530000063189
HOGENOMiHOG000216047
HOVERGENiHBG052640
InParanoidiQ9EPA7
KOiK06210
OMAiVCITRAG
OrthoDBiEOG091G0JTI
PhylomeDBiQ9EPA7
TreeFamiTF315035

Enzyme and pathway databases

UniPathwayi
UPA00253;UER00332

UPA00253;UER00600

BRENDAi2.7.7.1 3474
ReactomeiR-MMU-196807 Nicotinate metabolism
SABIO-RKiQ9EPA7

Miscellaneous databases

ChiTaRSiNmnat1 mouse
PROiPR:Q9EPA7
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000028992 Expressed in 209 organ(s), highest expression level in ear
CleanExiMM_NMNAT1
ExpressionAtlasiQ9EPA7 baseline and differential
GenevisibleiQ9EPA7 MM

Family and domain databases

InterProiView protein in InterPro
IPR004821 Cyt_trans-like
IPR005248 NadD/NMNAT
PfamiView protein in Pfam
PF01467 CTP_transf_like, 1 hit
TIGRFAMsiTIGR00482 TIGR00482, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiNMNA1_MOUSE
AccessioniPrimary (citable) accession number: Q9EPA7
Secondary accession number(s): Q6B504
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: May 9, 2003
Last modified: November 7, 2018
This is version 133 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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