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Protein

Nicotinamide phosphoribosyltransferase

Gene

Nampt

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

Functioni

The secreted form behaves both as a cytokine with immunomodulating properties and an adipokine with anti-diabetic properties, it has no enzymatic activity, partly because of lack of activation by ATP, which has a low level in extracellular space and plasma (By similarity). Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway. Plays a role in the modulation of circadian clock function. NAMPT-dependent oscillatory production of NAD regulates oscillation of clock target gene expression by releasing the core clock component: CLOCK-ARNTL/BMAL1 heterodimer from NAD-dependent SIRT1-mediated suppression.By similarity4 Publications

Catalytic activityi

Nicotinamide D-ribonucleotide + diphosphate = nicotinamide + 5-phospho-alpha-D-ribose 1-diphosphate.1 Publication

Kineticsi

  1. KM=0.92 µM for nicotinamide2 Publications
  1. Vmax=0.021 µmol/min/mg enzyme2 Publications

Pathwayi: NAD(+) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes nicotinamide D-ribonucleotide from 5-phospho-alpha-D-ribose 1-diphosphate and nicotinamide.
Proteins known to be involved in this subpathway in this organism are:
  1. Nicotinamide phosphoribosyltransferase (Nampt)
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 nicotinamide D-ribonucleotide from 5-phospho-alpha-D-ribose 1-diphosphate and nicotinamide, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei196DiphosphateBy similarity1
Binding sitei219Nicotinamide ribonucleotide1
Binding sitei247DiphosphateBy similarity1
Binding sitei311DiphosphateBy similarity1
Binding sitei384Nicotinamide ribonucleotide; via amide nitrogen1
Binding sitei392Nicotinamide ribonucleotide1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Glycosyltransferase, Transferase

Keywords - Biological processi

Biological rhythms, Pyridine nucleotide biosynthesis

Enzyme and pathway databases

BRENDAi2.4.2.12. 3474.
ReactomeiR-MMU-1368110. Bmal1:Clock,Npas2 activates circadian gene expression.
R-MMU-197264. Nicotinamide salvaging.
SABIO-RKQ99KQ4.
UniPathwayiUPA00253; UER00890.

Names & Taxonomyi

Protein namesi
Recommended name:
Nicotinamide phosphoribosyltransferase (EC:2.4.2.12)
Short name:
NAmPRTase
Short name:
Nampt
Alternative name(s):
Pre-B-cell colony-enhancing factor 1 homolog
Short name:
PBEF
Visfatin
Gene namesi
Name:Nampt
Synonyms:Pbef1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1929865. Nampt.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm 1 Publication
  • Secreted By similarity

  • Note: Under non-inflammatory conditions, visfatin predominantly exhibits a granular pattern within the nucleus. Secreted by endothelial cells upon IL-1beta stimulation. Abundantly secreted in milk, reaching 100-fold higher concentrations compared to maternal serum.By similarity

GO - Cellular componenti

  • cell junction Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: Reactome
  • extracellular exosome Source: MGI
  • extracellular space Source: UniProtKB-KW
  • nucleoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3259474.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002058641 – 491Nicotinamide phosphoribosyltransferaseAdd BLAST491

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei188PhosphotyrosineBy similarity1
Modified residuei472PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ99KQ4.
MaxQBiQ99KQ4.
PaxDbiQ99KQ4.
PeptideAtlasiQ99KQ4.
PRIDEiQ99KQ4.

PTM databases

iPTMnetiQ99KQ4.
PhosphoSitePlusiQ99KQ4.
SwissPalmiQ99KQ4.

Expressioni

Tissue specificityi

Ubiquitously expressed in lymphoid and non-lymphoid tissues.1 Publication

Inductioni

Expression shows a diurnal pattern of oscillation across the 24-hour light-dark cycle in liver, with a reduction in levels before the onset of the dark period (at protein level). Expression shows a diurnal pattern of oscillation in white adipose tissue (WAT), peaking at the beginning of the dark period. Up-regulated during polyclonal immune responses.2 Publications

Gene expression databases

BgeeiENSMUSG00000020572.
CleanExiMM_NAMPT.
GenevisibleiQ99KQ4. MM.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

DIPiDIP-29217N.
IntActiQ99KQ4. 2 interactors.
MINTiMINT-4123932.
STRINGi10090.ENSMUSP00000020886.

Chemistry databases

BindingDBiQ99KQ4.

Structurei

Secondary structure

1491
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 13Combined sources3
Beta strandi14 – 16Combined sources3
Helixi17 – 24Combined sources8
Beta strandi30 – 39Combined sources10
Beta strandi56 – 59Combined sources4
Helixi62 – 69Combined sources8
Helixi77 – 91Combined sources15
Helixi98 – 108Combined sources11
Beta strandi114 – 118Combined sources5
Beta strandi123 – 126Combined sources4
Beta strandi129 – 138Combined sources10
Helixi139 – 143Combined sources5
Helixi144 – 147Combined sources4
Helixi149 – 153Combined sources5
Helixi156 – 180Combined sources25
Helixi186 – 188Combined sources3
Beta strandi189 – 192Combined sources4
Turni195 – 197Combined sources3
Helixi201 – 211Combined sources11
Turni212 – 214Combined sources3
Beta strandi216 – 219Combined sources4
Helixi222 – 230Combined sources9
Beta strandi234 – 236Combined sources3
Beta strandi238 – 240Combined sources3
Helixi247 – 251Combined sources5
Helixi255 – 257Combined sources3
Helixi258 – 268Combined sources11
Beta strandi270 – 272Combined sources3
Beta strandi274 – 277Combined sources4
Helixi283 – 288Combined sources6
Helixi289 – 294Combined sources6
Helixi296 – 299Combined sources4
Beta strandi308 – 311Combined sources4
Helixi317 – 331Combined sources15
Beta strandi348 – 352Combined sources5
Helixi358 – 370Combined sources13
Helixi375 – 377Combined sources3
Beta strandi378 – 383Combined sources6
Helixi384 – 387Combined sources4
Turni392 – 396Combined sources5
Beta strandi397 – 406Combined sources10
Beta strandi409 – 412Combined sources4
Helixi421 – 423Combined sources3
Beta strandi431 – 434Combined sources4
Beta strandi440 – 443Combined sources4
Helixi447 – 450Combined sources4
Beta strandi452 – 454Combined sources3
Beta strandi459 – 463Combined sources5
Helixi473 – 479Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GVLX-ray2.10A/B1-491[»]
2H3BX-ray1.95A/B1-491[»]
2H3DX-ray2.10A/B1-491[»]
ProteinModelPortaliQ99KQ4.
SMRiQ99KQ4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99KQ4.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni311 – 313Nicotinamide ribonucleotide binding3
Regioni353 – 354Nicotinamide ribonucleotide binding2

Sequence similaritiesi

Belongs to the NAPRTase family.Curated

Phylogenomic databases

eggNOGiENOG410IEB2. Eukaryota.
COG1488. LUCA.
GeneTreeiENSGT00390000006647.
HOGENOMiHOG000216546.
HOVERGENiHBG000336.
InParanoidiQ99KQ4.
KOiK03462.
OMAiKKFPITE.
OrthoDBiEOG091G04ZB.
PhylomeDBiQ99KQ4.
TreeFamiTF333530.

Family and domain databases

CDDicd01569. PBEF_like. 1 hit.
InterProiIPR007229. Nic_PRibTrfase-Fam.
IPR016471. Nicotinamide_PRibTrfase.
IPR002638. Quinolinate_PRibosylTrfase_C.
[Graphical view]
PANTHERiPTHR11098. PTHR11098. 1 hit.
PTHR11098:SF15. PTHR11098:SF15. 1 hit.
PfamiPF04095. NAPRTase. 1 hit.
[Graphical view]
PIRSFiPIRSF005943. NMPRT. 1 hit.
SUPFAMiSSF51690. SSF51690. 1 hit.

Sequencei

Sequence statusi: Complete.

Q99KQ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAAAEAEFN ILLATDSYKV THYKQYPPNT SKVYSYFECR EKKTENSKVR
60 70 80 90 100
KVKYEETVFY GLQYILNKYL KGKVVTKEKI QEAKEVYREH FQDDVFNERG
110 120 130 140 150
WNYILEKYDG HLPIEVKAVP EGSVIPRGNV LFTVENTDPE CYWLTNWIET
160 170 180 190 200
ILVQSWYPIT VATNSREQKK ILAKYLLETS GNLDGLEYKL HDFGYRGVSS
210 220 230 240 250
QETAGIGASA HLVNFKGTDT VAGIALIKKY YGTKDPVPGY SVPAAEHSTI
260 270 280 290 300
TAWGKDHEKD AFEHIVTQFS SVPVSVVSDS YDIYNACEKI WGEDLRHLIV
310 320 330 340 350
SRSTEAPLII RPDSGNPLDT VLKVLDILGK KFPVTENSKG YKLLPPYLRV
360 370 380 390 400
IQGDGVDINT LQEIVEGMKQ KKWSIENVSF GSGGALLQKL TRDLLNCSFK
410 420 430 440 450
CSYVVTNGLG VNVFKDPVAD PNKRSKKGRL SLHRTPAGNF VTLEEGKGDL
460 470 480 490
EEYGHDLLHT VFKNGKVTKS YSFDEVRKNA QLNIEQDVAP H
Length:491
Mass (Da):55,447
Last modified:June 1, 2001 - v1
Checksum:iD3E522A1841297E6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti170K → R in AAF43208 (Ref. 3) Curated1
Sequence conflicti193F → S in AAF43208 (Ref. 3) Curated1
Sequence conflicti215F → L in AAF43208 (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY679720 mRNA. Translation: AAT72933.1.
AF234625 mRNA. Translation: AAF43208.1.
BC004059 mRNA. Translation: AAH04059.1.
BC018358 mRNA. Translation: AAH18358.1.
AK086415 mRNA. Translation: BAC39664.1.
CCDSiCCDS25871.1.
RefSeqiNP_067499.2. NM_021524.2.
UniGeneiMm.202727.

Genome annotation databases

EnsembliENSMUST00000020886; ENSMUSP00000020886; ENSMUSG00000020572.
GeneIDi59027.
KEGGimmu:59027.
UCSCiuc007nif.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY679720 mRNA. Translation: AAT72933.1.
AF234625 mRNA. Translation: AAF43208.1.
BC004059 mRNA. Translation: AAH04059.1.
BC018358 mRNA. Translation: AAH18358.1.
AK086415 mRNA. Translation: BAC39664.1.
CCDSiCCDS25871.1.
RefSeqiNP_067499.2. NM_021524.2.
UniGeneiMm.202727.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GVLX-ray2.10A/B1-491[»]
2H3BX-ray1.95A/B1-491[»]
2H3DX-ray2.10A/B1-491[»]
ProteinModelPortaliQ99KQ4.
SMRiQ99KQ4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29217N.
IntActiQ99KQ4. 2 interactors.
MINTiMINT-4123932.
STRINGi10090.ENSMUSP00000020886.

Chemistry databases

BindingDBiQ99KQ4.
ChEMBLiCHEMBL3259474.

PTM databases

iPTMnetiQ99KQ4.
PhosphoSitePlusiQ99KQ4.
SwissPalmiQ99KQ4.

Proteomic databases

EPDiQ99KQ4.
MaxQBiQ99KQ4.
PaxDbiQ99KQ4.
PeptideAtlasiQ99KQ4.
PRIDEiQ99KQ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020886; ENSMUSP00000020886; ENSMUSG00000020572.
GeneIDi59027.
KEGGimmu:59027.
UCSCiuc007nif.2. mouse.

Organism-specific databases

CTDi10135.
MGIiMGI:1929865. Nampt.

Phylogenomic databases

eggNOGiENOG410IEB2. Eukaryota.
COG1488. LUCA.
GeneTreeiENSGT00390000006647.
HOGENOMiHOG000216546.
HOVERGENiHBG000336.
InParanoidiQ99KQ4.
KOiK03462.
OMAiKKFPITE.
OrthoDBiEOG091G04ZB.
PhylomeDBiQ99KQ4.
TreeFamiTF333530.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00890.
BRENDAi2.4.2.12. 3474.
ReactomeiR-MMU-1368110. Bmal1:Clock,Npas2 activates circadian gene expression.
R-MMU-197264. Nicotinamide salvaging.
SABIO-RKQ99KQ4.

Miscellaneous databases

ChiTaRSiNampt. mouse.
EvolutionaryTraceiQ99KQ4.
PROiQ99KQ4.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000020572.
CleanExiMM_NAMPT.
GenevisibleiQ99KQ4. MM.

Family and domain databases

CDDicd01569. PBEF_like. 1 hit.
InterProiIPR007229. Nic_PRibTrfase-Fam.
IPR016471. Nicotinamide_PRibTrfase.
IPR002638. Quinolinate_PRibosylTrfase_C.
[Graphical view]
PANTHERiPTHR11098. PTHR11098. 1 hit.
PTHR11098:SF15. PTHR11098:SF15. 1 hit.
PfamiPF04095. NAPRTase. 1 hit.
[Graphical view]
PIRSFiPIRSF005943. NMPRT. 1 hit.
SUPFAMiSSF51690. SSF51690. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNAMPT_MOUSE
AccessioniPrimary (citable) accession number: Q99KQ4
Secondary accession number(s): Q8C3B5, Q9JKM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2001
Last modified: November 2, 2016
This is version 134 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.