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Q9EPA7 (NMNA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nicotinamide mononucleotide adenylyltransferase 1

Short name=NMN adenylyltransferase 1
EC=2.7.7.1
Alternative name(s):
Nicotinate-nucleotide adenylyltransferase 1
Short name=NaMN adenylyltransferase 1
EC=2.7.7.18
Gene names
Name:Nmnat1
Synonyms:D4Cole1e, Nmnat
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length285 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Fails to cleave phosphorylated dinucleotides NADP+, NADPH and NAADP+ By similarity. 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. Ref.3 Ref.4

Catalytic activity

ATP + nicotinamide ribonucleotide = diphosphate + NAD+. UniProtKB Q9HAN9

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

Cofactor

Divalent metal cations. Zinc confers higher activity than magnesium By similarity.

Enzyme regulation

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

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.

Subunit structure

Homohexamer. Interacts with ADPRT/PARP1 By similarity. UniProtKB Q9HAN9

Subcellular location

Nucleus Ref.4.

Developmental stage

Expressed throughout development and in adulthood. Ref.4

Induction

By neuronal injury.

Post-translational modification

Phosphorylated By similarity. UniProtKB Q9HAN9

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.

Sequence similarities

Belongs to the eukaryotic NMN adenylyltransferase family.

Biophysicochemical properties

Kinetic parameters:

KM=20.1 µM for nicotinamide mononucleotide (NMN) Ref.2

Vmax=34.1 µmol/min/mg enzyme

Sequence caution

The sequence AAG17285.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAG17286.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAG38490.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 285285Nicotinamide mononucleotide adenylyltransferase 1
PRO_0000135013

Regions

Nucleotide binding15 – 2410ATP Potential
Nucleotide binding223 – 2286ATP Potential
Motif123 – 1297Nuclear localization signal Potential

Sites

Binding site161Substrate By similarity
Binding site551Substrate By similarity
Binding site1591Substrate By similarity

Experimental info

Mutagenesis125 – 1284RKRK → AAAA: Locates to the cytoplasm. Has no affect on enzyme activity or axonal protection. Ref.4
Mutagenesis1701W → A: Decrease in enzyme activity. Has no axonal protective effect. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9EPA7 [UniParc].

Last modified May 9, 2003. Version 2.
Checksum: 2769D42E894EB84F

FASTA28532,355
        10         20         30         40         50         60 
MDSSKKTEVV LLACGSFNPI TNMHLRLFEL AKDYMHATGK YSVIKGIISP VGDAYKKKGL 

        70         80         90        100        110        120 
IPAHHRIIMA ELATKNSHWV EVDTWESLQK EWVETVKVLR YHQEKLATGS CSYPQSSPAL 

       130        140        150        160        170        180 
EKPGRKRKWA DQKQDSSPQK PQEPKPTGVP KVKLLCGADL LESFSVPNLW KMEDITQIVA 

       190        200        210        220        230        240 
NFGLICITRA GSDAQKFIYE SDVLWRHQSN IHLVNEWITN DISSTKIRRA LRRGQSIRYL 

       250        260        270        280 
VPDLVQEYIE KHELYNTESE GRNAGVTLAP LQRNAAEAKH NHSTL 

« Hide

References

[1]"A Ufd2/D4Cole1e chimeric protein and overexpression of Rbp7 in the slow Wallerian degeneration (WldS) mouse."
Conforti L., Tarlton A., Mack T.G.A., Mi W., Buckmaster E.A., Wagner D., Perry V.H., Coleman M.P.
Proc. Natl. Acad. Sci. U.S.A. 97:11377-11382(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: 129, C57BL/6J and C57BL/Ola.
[2]"The NAD biosynthesis pathway mediated by nicotinamide phosphoribosyltransferase regulates Sir2 activity in mammalian cells."
Revollo J.R., Grimm A.A., Imai S.
J. Biol. Chem. 279:50754-50763(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES.
Strain: BALB/c.
Tissue: Liver.
[3]"Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration."
Araki T., Sasaki Y., Milbrandt J.
Science 305:1010-1013(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF TRP-170.
[4]"Stimulation of nicotinamide adenine dinucleotide biosynthetic pathways delays axonal degeneration after axotomy."
Sasaki Y., Araki T., Milbrandt J.
J. Neurosci. 26:8484-8491(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, MUTAGENESIS OF 125-ARG--LYS-128.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_597679.1. NM_133435.1.
XP_006539168.1. XM_006539105.1.
UniGeneMm.76062.

3D structure databases

ProteinModelPortalQ9EPA7.
SMRQ9EPA7. Positions 6-276.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000030845.

PTM databases

PhosphoSiteQ9EPA7.

Proteomic databases

PaxDbQ9EPA7.
PRIDEQ9EPA7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030845; ENSMUSP00000030845; ENSMUSG00000028992.
ENSMUST00000105693; ENSMUSP00000101318; ENSMUSG00000028992.
GeneID66454.
KEGGmmu:66454.
UCSCuc008vwj.1. mouse.

Organism-specific databases

CTD64802.
MGIMGI:1913704. Nmnat1.

Phylogenomic databases

eggNOGCOG1057.
GeneTreeENSGT00530000063189.
HOGENOMHOG000216047.
HOVERGENHBG052640.
InParanoidQ9EPA7.
KOK06210.
OMAVDPWEAF.
PhylomeDBQ9EPA7.
TreeFamTF315035.

Enzyme and pathway databases

BRENDA2.7.7.1. 3474.
SABIO-RKQ9EPA7.
UniPathwayUPA00253; UER00600.

Gene expression databases

ArrayExpressQ9EPA7.
BgeeQ9EPA7.
CleanExMM_NMNAT1.
GenevestigatorQ9EPA7.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
InterProIPR004821. Cyt_trans-like.
IPR005248. NAMN_adtrnsfrase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR12039. PTHR12039. 1 hit.
PfamPF01467. CTP_transf_2. 1 hit.
[Graphical view]
TIGRFAMsTIGR00482. TIGR00482. 1 hit.
ProtoNetSearch...

Other

ChiTaRSNMNAT1. mouse.
NextBio321736.
PROQ9EPA7.
SOURCESearch...

Entry information

Entry nameNMNA1_MOUSE
AccessionPrimary (citable) accession number: Q9EPA7
Secondary accession number(s): Q6B504
Entry history
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: May 9, 2003
Last modified: April 16, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot