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Q80Z29 (NAMPT_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 87. 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 phosphoribosyltransferase

Short name=NAmPRTase
Short name=Nampt
EC=2.4.2.12
Alternative name(s):
Pre-B-cell colony-enhancing factor 1 homolog
Short name=PBEF
Visfatin
Gene names
Name:Nampt
Synonyms:Pbef1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity.

Catalytic activity

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

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; nicotinamide D-ribonucleotide from 5-phospho-alpha-D-ribose 1-diphosphate and nicotinamide: step 1/1.

Subunit structure

Homodimer. Ref.4

Subcellular location

Nucleus. Cytoplasm. 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. Ref.1

Tissue specificity

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. Ref.1

Sequence similarities

Belongs to the NAPRTase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 491491Nicotinamide phosphoribosyltransferase
PRO_0000205866

Regions

Region311 – 3133Nicotinamide ribonucleotide binding
Region353 – 3542Nicotinamide ribonucleotide binding

Sites

Binding site1961Diphosphate By similarity
Binding site2191Nicotinamide ribonucleotide By similarity
Binding site2471Diphosphate By similarity
Binding site3111Diphosphate By similarity
Binding site3841Nicotinamide ribonucleotide; via amide nitrogen
Binding site3921Nicotinamide ribonucleotide

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Secondary structure

.......................................................................................... 491
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q80Z29 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 78F526F0D3F579FC

FASTA49155,438
        10         20         30         40         50         60 
MNAAAEAEFN ILLATDSYKV THYKQYPPNT SKVYSYFECR EKKTENSKVR KVKYEETVFY 

        70         80         90        100        110        120 
GLQYILNKYL KGKVVTKEKI QEAKEVYREH FQDDVFNERG WNYILEKYDG HLPIEVKAVP 

       130        140        150        160        170        180 
EGSVIPRGNV LFTVENTDPE CYWLTNWIET ILVQSWYPIT VATNSREQKK ILAKYLLETS 

       190        200        210        220        230        240 
GNLDGLEYKL HDFGYRGVSS QETAGIGASA HLVNFKGTDT VAGIALIKKY YGTKDPVPGY 

       250        260        270        280        290        300 
SVPAAEHSTI TAWGKDHEKD AFEHIVTQFS SVPVSVVSDS YDIYNACEKI WGEDLRHLIV 

       310        320        330        340        350        360 
SRSTEAPLII RPDSGNPLDT VLKVLDILGK KFPVSENSKG YKLLPPYLRV IQGDGVDINT 

       370        380        390        400        410        420 
LQEIVEGMKQ KKWSIENVSF GSGGALLQKL TRDLLNCSFK CSYVVTNGLG VNVFKDPVAD 

       430        440        450        460        470        480 
PNKRSKKGRL SLHRTPAGTF VTLEEGKGDL EEYGHDLLHT VFKNGKVTKS YSFDEVRKNA 

       490 
QLNMEQDVAP H 

« Hide

References

« Hide 'large scale' references
[1]"Growth phase-dependent changes in the subcellular localization of pre-B-cell colony-enhancing factor."
Kitani T., Okuno S., Fujisawa H.
FEBS Lett. 544:74-78(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"NAD biosynthesis pathway mediated by nicotinamide phosphoribosyltransferase attenuates ischemic neuronal cell death."
Xing J., Gao Y., Cao G., Chen J.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Brain.
[3]"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].
Tissue: Heart.
[4]"Crystal structure of visfatin/pre-B cell colony-enhancing factor 1/nicotinamide phosphoribosyltransferase, free and in complex with the anti-cancer agent FK-866."
Kim M.-K., Lee J.H., Kim H., Park S.J., Kim S.H., Kang G.B., Lee Y.S., Kim J.B., Kim K.K., Suh S.W., Eom S.H.
J. Mol. Biol. 362:66-77(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH NICOTINAMIDE MONONUCLEOTIDE AND FK866, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB081730 mRNA. Translation: BAC66022.1.
AY831728 mRNA. Translation: AAX49410.1.
BC085681 mRNA. Translation: AAH85681.1.
RefSeqNP_808789.1. NM_177928.3.
UniGeneRn.203508.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2G95X-ray1.90A/B1-491[»]
2G96X-ray2.90A/B1-491[»]
2G97X-ray2.90A/B1-491[»]
3G8EX-ray3.00A/B1-491[»]
ProteinModelPortalQ80Z29.
SMRQ80Z29. Positions 9-483.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ80Z29.

Proteomic databases

PaxDbQ80Z29.
PRIDEQ80Z29.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000013043; ENSRNOP00000013043; ENSRNOG00000009754.
GeneID297508.
KEGGrno:297508.
UCSCRGD:631365. rat.

Organism-specific databases

CTD10135.
RGD631365. Nampt.

Phylogenomic databases

eggNOGCOG1488.
GeneTreeENSGT00390000006647.
HOGENOMHOG000216546.
HOVERGENHBG000336.
KOK03462.
OMAKKFPITE.
OrthoDBEOG7PGDQH.

Enzyme and pathway databases

BRENDA2.4.2.12. 5301.
SABIO-RKQ80Z29.
UniPathwayUPA00253; UER00890.

Gene expression databases

GenevestigatorQ80Z29.

Family and domain databases

InterProIPR007229. Nic_PRibTrfase-Fam.
IPR016471. Nicotinamide_PRibTrfase.
IPR002638. Quinolinate_PRibosylTrfase_C.
[Graphical view]
PANTHERPTHR11098:SF2. PTHR11098:SF2. 1 hit.
PfamPF04095. NAPRTase. 1 hit.
[Graphical view]
PIRSFPIRSF005943. NMPRT. 1 hit.
SUPFAMSSF51690. SSF51690. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ80Z29.
NextBio642340.
PROQ80Z29.

Entry information

Entry nameNAMPT_RAT
AccessionPrimary (citable) accession number: Q80Z29
Secondary accession number(s): Q2VT47
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 87 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways