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Q9EPA7

- NMNA1_MOUSE

UniProt

Q9EPA7 - NMNA1_MOUSE

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Protein

Nicotinamide mononucleotide adenylyltransferase 1

Gene

Nmnat1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity2 Publications

Catalytic activityi

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

Cofactori

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

Enzyme regulationi

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

Kineticsi

  1. KM=20.1 µM for nicotinamide mononucleotide (NMN)1 Publication

Vmax=34.1 µmol/min/mg enzyme1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei16 – 161SubstrateBy similarity
Binding sitei55 – 551SubstrateBy similarity
Binding sitei159 – 1591SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 2410ATPSequence Analysis
Nucleotide bindingi223 – 2286ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. nicotinamide-nucleotide adenylyltransferase activity Source: UniProtKB
  3. nicotinate-nucleotide adenylyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. NAD biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, NAD, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi2.7.7.1. 3474.
ReactomeiREACT_209575. Nicotinate metabolism.
SABIO-RKQ9EPA7.
UniPathwayiUPA00253; UER00600.

Names & Taxonomyi

Protein namesi
Recommended name:
Nicotinamide mononucleotide adenylyltransferase 1 (EC:2.7.7.1)
Short name:
NMN adenylyltransferase 1
Alternative name(s):
Nicotinate-nucleotide adenylyltransferase 1 (EC:2.7.7.18)
Short name:
NaMN adenylyltransferase 1
Gene namesi
Name:Nmnat1
Synonyms:D4Cole1e, Nmnat
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1913704. Nmnat1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi125 – 1284RKRK → AAAA: Locates to the cytoplasm. Has no affect on enzyme activity or axonal protection. 1 Publication
Mutagenesisi170 – 1701W → A: Decrease in enzyme activity. Has no axonal protective effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 285285Nicotinamide mononucleotide adenylyltransferase 1PRO_0000135013Add
BLAST

Post-translational modificationi

Phosphorylated.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9EPA7.
PaxDbiQ9EPA7.
PRIDEiQ9EPA7.

PTM databases

PhosphoSiteiQ9EPA7.

Expressioni

Developmental stagei

Expressed throughout development and in adulthood.1 Publication

Inductioni

By neuronal injury.

Gene expression databases

BgeeiQ9EPA7.
CleanExiMM_NMNAT1.
ExpressionAtlasiQ9EPA7. baseline and differential.
GenevestigatoriQ9EPA7.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000030845.

Structurei

3D structure databases

ProteinModelPortaliQ9EPA7.
SMRiQ9EPA7. Positions 6-276.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi123 – 1297Nuclear localization signalSequence Analysis

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1057.
GeneTreeiENSGT00530000063189.
HOGENOMiHOG000216047.
HOVERGENiHBG052640.
InParanoidiQ9EPA7.
KOiK06210.
OMAiHRVAMCQ.
PhylomeDBiQ9EPA7.
TreeFamiTF315035.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR004821. Cyt_trans-like.
IPR005248. NAMN_adtrnsfrase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR12039. PTHR12039. 1 hit.
PfamiPF01467. CTP_transf_2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00482. TIGR00482. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Sequence cautioni

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 databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006539105.1.
UniGeneiMm.76062.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS18960.1.
RefSeqi NP_597679.1. NM_133435.1.
XP_006539168.1. XM_006539105.1.
UniGenei Mm.76062.

3D structure databases

ProteinModelPortali Q9EPA7.
SMRi Q9EPA7. Positions 6-276.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000030845.

PTM databases

PhosphoSitei Q9EPA7.

Proteomic databases

MaxQBi Q9EPA7.
PaxDbi Q9EPA7.
PRIDEi Q9EPA7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000030845 ; ENSMUSP00000030845 ; ENSMUSG00000028992 .
ENSMUST00000105693 ; ENSMUSP00000101318 ; ENSMUSG00000028992 .
GeneIDi 66454.
KEGGi mmu:66454.
UCSCi uc008vwj.1. mouse.

Organism-specific databases

CTDi 64802.
MGIi MGI:1913704. Nmnat1.

Phylogenomic databases

eggNOGi COG1057.
GeneTreei ENSGT00530000063189.
HOGENOMi HOG000216047.
HOVERGENi HBG052640.
InParanoidi Q9EPA7.
KOi K06210.
OMAi HRVAMCQ.
PhylomeDBi Q9EPA7.
TreeFami TF315035.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00600 .
BRENDAi 2.7.7.1. 3474.
Reactomei REACT_209575. Nicotinate metabolism.
SABIO-RK Q9EPA7.

Miscellaneous databases

ChiTaRSi NMNAT1. mouse.
NextBioi 321736.
PROi Q9EPA7.
SOURCEi Search...

Gene expression databases

Bgeei Q9EPA7.
CleanExi MM_NMNAT1.
ExpressionAtlasi Q9EPA7. baseline and differential.
Genevestigatori Q9EPA7.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
InterProi IPR004821. Cyt_trans-like.
IPR005248. NAMN_adtrnsfrase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view ]
PANTHERi PTHR12039. PTHR12039. 1 hit.
Pfami PF01467. CTP_transf_2. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00482. TIGR00482. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiNMNA1_MOUSE
AccessioniPrimary (citable) accession number: Q9EPA7
Secondary accession number(s): Q6B504
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: May 9, 2003
Last modified: October 29, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3