Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q99KQ4 (NAMPT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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. Ref.1 Ref.2

Catalytic activity

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

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.6 Ref.7

Subcellular location

Cytoplasm Ref.1.

Tissue specificity

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

Induction

Up-regulated during polyclonal immune responses. Ref.1

Sequence similarities

Belongs to the NAPRTase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.92 µM for nicotinamide Ref.1 Ref.2

Vmax=0.021 µmol/min/mg enzyme

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 491491Nicotinamide phosphoribosyltransferase
PRO_0000205864

Regions

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

Sites

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

Experimental info

Sequence conflict1701K → R in AAF43208. Ref.3
Sequence conflict1931F → S in AAF43208. Ref.3
Sequence conflict2151F → L in AAF43208. Ref.3

Secondary structure

1 ........................................................................................ 491
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q99KQ4 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: D3E522A1841297E6

FASTA49155,447
        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 KFPVTENSKG YKLLPPYLRV IQGDGVDINT 

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

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

       490 
QLNIEQDVAP H

« Hide

References

« Hide 'large scale' references
[1]"Pre-B-cell colony-enhancing factor, whose expression is up-regulated in activated lymphocytes, is a nicotinamide phosphoribosyltransferase, a cytosolic enzyme involved in NAD biosynthesis."
Rongvaux A., Shea R.J., Mulks M.H., Gigot D., Urbain J., Leo O., Andris F.
Eur. J. Immunol. 32:3225-3234(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
Tissue: T-cell.
[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, FUNCTION.
Strain: BALB/c.
Tissue: Liver.
[3]"Mus musculus pre-B-cell colony-enhancing factor (PBEF) mRNA."
Samal B.B., Sun N., Sun Y.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"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: Czech II and FVB/N.
Tissue: Mammary tumor.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-368.
Strain: C57BL/6J.
Tissue: Head.
[6]"Molecular basis for the inhibition of human NMPRTase, a novel target for anticancer agents."
Khan J.A., Tao X., Tong L.
Nat. Struct. Mol. Biol. 13:582-588(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBUNIT.
[7]"Structure of Nampt/PBEF/visfatin, a mammalian NAD+ biosynthetic enzyme."
Wang T., Zhang X., Bheda P., Revollo J.R., Imai S., Wolberger C.
Nat. Struct. Mol. Biol. 13:661-662(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH NICOTINAMIDE MONONUCLEOTIDE, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00320188.
RefSeqNP_067499.2. NM_021524.2.
UniGeneMm.489597.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GVLX-ray2.10A/B1-491[»]
2H3BX-ray1.95A/B1-491[»]
2H3DX-ray2.10A/B1-491[»]
ProteinModelPortalQ99KQ4.
SMRQ99KQ4. Positions 8-483.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29217N.
MINTMINT-4123932.
STRING10090.ENSMUSP00000020886.

PTM databases

PhosphoSiteQ99KQ4.

Proteomic databases

PaxDbQ99KQ4.
PRIDEQ99KQ4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020886; ENSMUSP00000020886; ENSMUSG00000020572.
GeneID59027.
KEGGmmu:59027.
UCSCuc007nif.2. mouse.

Organism-specific databases

CTD10135.
MGIMGI:1929865. Nampt.

Phylogenomic databases

eggNOGCOG1488.
GeneTreeENSGT00390000006647.
HOGENOMHOG000216546.
HOVERGENHBG000336.
InParanoidQ99KQ4.
KOK03462.
OMAWYPSTVA.
OrthoDBEOG40K7ZQ.

Enzyme and pathway databases

BRENDA2.4.2.12. 3474.
ReactomeREACT_109335. Circadian Clock.
REACT_24972. Circadian Clock (mouse).
SABIO-RKQ99KQ4.
UniPathwayUPA00253; UER00890.

Gene expression databases

BgeeQ99KQ4.
CleanExMM_NAMPT.
GenevestigatorQ99KQ4.
GermOnlineENSMUSG00000020572. Mus musculus.

Family and domain databases

InterProIPR015977. Nic_PRibTrfase-like.
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. Q_phspho_trans. 1 hit.
ProtoNetSearch...

Other

ChiTaRSNAMPT. mouse.
EvolutionaryTraceQ99KQ4.
NextBio314606.
SOURCESearch...

Entry information

Entry nameNAMPT_MOUSE
AccessionPrimary (citable) accession number: Q99KQ4
Secondary accession number(s): Q8C3B5, Q9JKM0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2001
Last modified: May 29, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents