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Protein

Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3

Gene

Nmnat3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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. Can also use GTP and ITP as nucleotide donors. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD+. For the pyrophosphorolytic activity, can use NAD+, NADH, NaAD, nicotinic acid adenine dinucleotide phosphate (NHD), nicotinamide guanine dinucleotide (NGD) as substrates. Fails to cleave phosphorylated dinucleotides NADP+, NADPH and NaADP+. Protects against axonal degeneration following injury.1 Publication

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Divalent metal cations. Mg2+ confers the highest activity.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

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 2 (Nmnat2), Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 (Nmnat1), Nicotinamide-nucleotide adenylyltransferase (Nmnat2), Nicotinamide-nucleotide adenylyltransferase (Nmnat2), Nicotinamide-nucleotide adenylyltransferase (Nmnat1), Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3 (Nmnat3), Nicotinamide-nucleotide adenylyltransferase
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 2 (Nmnat2), Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 (Nmnat1), 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei22 – 221ATPBy similarity
Binding sitei56 – 561ATPBy similarity
Binding sitei139 – 1391ATP; shared with dimeric partnerBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 153ATPBy similarity
Nucleotide bindingi134 – 1363ATPBy similarity
Nucleotide bindingi202 – 2054ATPBy similarity

GO - Molecular functioni

GO - Biological processi

  • 'de novo' NAD biosynthetic process from aspartate Source: GO_Central
  • NAD biosynthetic process Source: MGI
  • response to wounding Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

ATP-binding, NAD, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.7.1. 3474.
ReactomeiR-MMU-196807. Nicotinate metabolism.
UniPathwayiUPA00253; UER00332.
UPA00253; UER00600.

Names & Taxonomyi

Protein namesi
Recommended name:
Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3Curated (EC:2.7.7.1, EC:2.7.7.18)
Short name:
NMN/NaMN adenylyltransferase 3
Alternative name(s):
Nicotinamide-nucleotide adenylyltransferase 3
Short name:
NMN adenylyltransferase 3
Nicotinate-nucleotide adenylyltransferase 3
Short name:
NaMN adenylyltransferase 3
Gene namesi
Name:Nmnat3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1921330. Nmnat3.

Subcellular locationi

  • Mitochondrion 1 Publication

GO - Cellular componenti

  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 245245Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3PRO_0000135017Add
BLAST

Proteomic databases

MaxQBiQ99JR6.
PaxDbiQ99JR6.
PeptideAtlasiQ99JR6.
PRIDEiQ99JR6.

PTM databases

iPTMnetiQ99JR6.
PhosphoSiteiQ99JR6.

Expressioni

Developmental stagei

Expressed throughout development and in adulthood.1 Publication

Gene expression databases

BgeeiQ99JR6.
CleanExiMM_NMNAT3.
ExpressionAtlasiQ99JR6. baseline and differential.
GenevisibleiQ99JR6. MM.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000035031.

Structurei

3D structure databases

ProteinModelPortaliQ99JR6.
SMRiQ99JR6. Positions 3-232.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 553Substrate bindingBy similarity
Regioni90 – 934Substrate bindingBy similarity
Regioni146 – 1472Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3199. Eukaryota.
COG1057. LUCA.
GeneTreeiENSGT00530000063189.
HOGENOMiHOG000216047.
HOVERGENiHBG052640.
InParanoidiQ99JR6.
KOiK06210.
OMAiGMYQVIQ.
PhylomeDBiQ99JR6.
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_like. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00482. TIGR00482. 1 hit.

Sequencei

Sequence statusi: Complete.

Q99JR6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNRIPVVLL ACGSFNPITN MHLRLFEVAR DHLHQTGRYQ VIEGIISPVN
60 70 80 90 100
DSYGKKDLVA SHHRVAMARL ALQTSDWIRV DPWESEQAQW METVKVLRHH
110 120 130 140 150
HRELLRSSAQ MDGPDPSKTP SASAALPELK LLCGADVLKT FQTPNLWKDT
160 170 180 190 200
HIQEIVEKFG LVCVSRSGHD PERYISDSPI LQQFQHNIHL AREPVLNEIS
210 220 230 240
ATYVRKALGQ GQSVKYLLPE AVITYIRDQG LYINDGSWKG KGKTG
Length:245
Mass (Da):27,703
Last modified:June 1, 2001 - v1
Checksum:iE46D50D81CD150BB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC005737 mRNA. Translation: AAH05737.1.
BC092086 mRNA. Translation: AAH92086.1.
CCDSiCCDS23423.1.
RefSeqiNP_653116.1. NM_144533.2.
XP_006511565.1. XM_006511502.2.
XP_006511566.1. XM_006511503.2.
XP_006511567.1. XM_006511504.2.
XP_011241128.1. XM_011242826.1.
XP_011241129.1. XM_011242827.1.
UniGeneiMm.294082.

Genome annotation databases

EnsembliENSMUST00000112935; ENSMUSP00000108557; ENSMUSG00000032456.
GeneIDi74080.
KEGGimmu:74080.
UCSCiuc009rdh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC005737 mRNA. Translation: AAH05737.1.
BC092086 mRNA. Translation: AAH92086.1.
CCDSiCCDS23423.1.
RefSeqiNP_653116.1. NM_144533.2.
XP_006511565.1. XM_006511502.2.
XP_006511566.1. XM_006511503.2.
XP_006511567.1. XM_006511504.2.
XP_011241128.1. XM_011242826.1.
XP_011241129.1. XM_011242827.1.
UniGeneiMm.294082.

3D structure databases

ProteinModelPortaliQ99JR6.
SMRiQ99JR6. Positions 3-232.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000035031.

PTM databases

iPTMnetiQ99JR6.
PhosphoSiteiQ99JR6.

Proteomic databases

MaxQBiQ99JR6.
PaxDbiQ99JR6.
PeptideAtlasiQ99JR6.
PRIDEiQ99JR6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000112935; ENSMUSP00000108557; ENSMUSG00000032456.
GeneIDi74080.
KEGGimmu:74080.
UCSCiuc009rdh.1. mouse.

Organism-specific databases

CTDi349565.
MGIiMGI:1921330. Nmnat3.

Phylogenomic databases

eggNOGiKOG3199. Eukaryota.
COG1057. LUCA.
GeneTreeiENSGT00530000063189.
HOGENOMiHOG000216047.
HOVERGENiHBG052640.
InParanoidiQ99JR6.
KOiK06210.
OMAiGMYQVIQ.
PhylomeDBiQ99JR6.
TreeFamiTF315035.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00332.
UPA00253; UER00600.
BRENDAi2.7.7.1. 3474.
ReactomeiR-MMU-196807. Nicotinate metabolism.

Miscellaneous databases

PROiQ99JR6.
SOURCEiSearch...

Gene expression databases

BgeeiQ99JR6.
CleanExiMM_NMNAT3.
ExpressionAtlasiQ99JR6. baseline and differential.
GenevisibleiQ99JR6. MM.

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_like. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00482. TIGR00482. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney.
  2. "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.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Spleen and Testis.

Entry informationi

Entry nameiNMNA3_MOUSE
AccessioniPrimary (citable) accession number: Q99JR6
Secondary accession number(s): Q58E37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.