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Protein

Nicotinamide phosphoribosyltransferase

Gene

Nampt

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. 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. 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 similarity

Catalytic activityi

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

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 ribonucleotideBy similarity1
Binding sitei247DiphosphateBy similarity1
Binding sitei311DiphosphateBy similarity1
Binding sitei384Nicotinamide ribonucleotide; via amide nitrogen1
Binding sitei392Nicotinamide ribonucleotide1

GO - Molecular functioni

  • cytokine activity Source: RGD
  • drug binding Source: RGD
  • nicotinamide phosphoribosyltransferase activity Source: RGD
  • nicotinate-nucleotide diphosphorylase (carboxylating) activity Source: InterPro
  • protein homodimerization activity Source: RGD

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. 5301.
ReactomeiR-RNO-197264. Nicotinamide salvaging.
SABIO-RKQ80Z29.
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi631365. Nampt.

Subcellular locationi

  • Nucleus 1 Publication
  • 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: Ensembl
  • cytoplasm Source: RGD
  • extracellular exosome Source: Ensembl
  • extracellular space Source: UniProtKB-KW
  • nucleoplasm Source: Ensembl
  • nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3259475.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002058661 – 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

PaxDbiQ80Z29.
PRIDEiQ80Z29.

PTM databases

iPTMnetiQ80Z29.
PhosphoSitePlusiQ80Z29.

Expressioni

Tissue specificityi

Expressed in various tissues. At the highest level in liver and at the second highest in heart. The amount is higher in heart than in lung.1 Publication

Gene expression databases

BgeeiENSRNOG00000009754.
ExpressionAtlasiQ80Z29. baseline and differential.
GenevisibleiQ80Z29. RN.

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • cytokine activity Source: RGD
  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000013043.

Chemistry databases

BindingDBiQ80Z29.

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 – 58Combined sources3
Helixi62 – 69Combined sources8
Beta strandi71 – 73Combined sources3
Helixi77 – 91Combined sources15
Helixi98 – 108Combined sources11
Beta strandi114 – 118Combined sources5
Beta strandi124 – 138Combined sources15
Helixi139 – 143Combined sources5
Helixi144 – 147Combined sources4
Helixi149 – 153Combined sources5
Helixi156 – 180Combined sources25
Helixi186 – 188Combined sources3
Beta strandi189 – 192Combined sources4
Helixi195 – 197Combined sources3
Beta strandi198 – 200Combined sources3
Helixi201 – 211Combined sources11
Turni212 – 214Combined sources3
Beta strandi217 – 219Combined sources3
Helixi222 – 230Combined sources9
Beta strandi234 – 236Combined sources3
Beta strandi238 – 240Combined sources3
Helixi247 – 250Combined sources4
Helixi251 – 253Combined sources3
Helixi255 – 257Combined sources3
Helixi258 – 268Combined sources11
Beta strandi270 – 272Combined sources3
Beta strandi274 – 278Combined sources5
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
Helixi392 – 394Combined sources3
Beta strandi397 – 406Combined sources10
Beta strandi409 – 411Combined sources3
Helixi421 – 423Combined sources3
Beta strandi431 – 434Combined sources4
Beta strandi440 – 443Combined sources4
Helixi447 – 450Combined sources4
Beta strandi453 – 455Combined 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
2G95X-ray1.90A/B1-491[»]
2G96X-ray2.90A/B1-491[»]
2G97X-ray2.90A/B1-491[»]
3G8EX-ray3.00A/B1-491[»]
ProteinModelPortaliQ80Z29.
SMRiQ80Z29.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ80Z29.

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.
InParanoidiQ80Z29.
KOiK03462.
OMAiKKFPITE.
OrthoDBiEOG091G04ZB.

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.

Q80Z29-1 [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 KFPVSENSKG YKLLPPYLRV
360 370 380 390 400
IQGDGVDINT LQEIVEGMKQ KKWSIENVSF GSGGALLQKL TRDLLNCSFK
410 420 430 440 450
CSYVVTNGLG VNVFKDPVAD PNKRSKKGRL SLHRTPAGTF VTLEEGKGDL
460 470 480 490
EEYGHDLLHT VFKNGKVTKS YSFDEVRKNA QLNMEQDVAP H
Length:491
Mass (Da):55,438
Last modified:June 1, 2003 - v1
Checksum:i78F526F0D3F579FC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB081730 mRNA. Translation: BAC66022.1.
AY831728 mRNA. Translation: AAX49410.1.
BC085681 mRNA. Translation: AAH85681.1.
RefSeqiNP_808789.1. NM_177928.3.
UniGeneiRn.203508.

Genome annotation databases

EnsembliENSRNOT00000013043; ENSRNOP00000013043; ENSRNOG00000009754.
GeneIDi297508.
KEGGirno:297508.
UCSCiRGD:631365. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB081730 mRNA. Translation: BAC66022.1.
AY831728 mRNA. Translation: AAX49410.1.
BC085681 mRNA. Translation: AAH85681.1.
RefSeqiNP_808789.1. NM_177928.3.
UniGeneiRn.203508.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2G95X-ray1.90A/B1-491[»]
2G96X-ray2.90A/B1-491[»]
2G97X-ray2.90A/B1-491[»]
3G8EX-ray3.00A/B1-491[»]
ProteinModelPortaliQ80Z29.
SMRiQ80Z29.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000013043.

Chemistry databases

BindingDBiQ80Z29.
ChEMBLiCHEMBL3259475.

PTM databases

iPTMnetiQ80Z29.
PhosphoSitePlusiQ80Z29.

Proteomic databases

PaxDbiQ80Z29.
PRIDEiQ80Z29.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000013043; ENSRNOP00000013043; ENSRNOG00000009754.
GeneIDi297508.
KEGGirno:297508.
UCSCiRGD:631365. rat.

Organism-specific databases

CTDi10135.
RGDi631365. Nampt.

Phylogenomic databases

eggNOGiENOG410IEB2. Eukaryota.
COG1488. LUCA.
GeneTreeiENSGT00390000006647.
HOGENOMiHOG000216546.
HOVERGENiHBG000336.
InParanoidiQ80Z29.
KOiK03462.
OMAiKKFPITE.
OrthoDBiEOG091G04ZB.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00890.
BRENDAi2.4.2.12. 5301.
ReactomeiR-RNO-197264. Nicotinamide salvaging.
SABIO-RKQ80Z29.

Miscellaneous databases

EvolutionaryTraceiQ80Z29.
PROiQ80Z29.

Gene expression databases

BgeeiENSRNOG00000009754.
ExpressionAtlasiQ80Z29. baseline and differential.
GenevisibleiQ80Z29. RN.

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_RAT
AccessioniPrimary (citable) accession number: Q80Z29
Secondary accession number(s): Q2VT47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 107 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.