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Q99KQ4

- NAMPT_MOUSE

UniProt

Q99KQ4 - NAMPT_MOUSE

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Protein

Nicotinamide phosphoribosyltransferase

Gene

Nampt

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

Vmax=0.021 µmol/min/mg enzyme2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei196 – 1961DiphosphateBy similarity
Binding sitei219 – 2191Nicotinamide ribonucleotide
Binding sitei247 – 2471DiphosphateBy similarity
Binding sitei311 – 3111DiphosphateBy similarity
Binding sitei384 – 3841Nicotinamide ribonucleotide; via amide nitrogen
Binding sitei392 – 3921Nicotinamide ribonucleotide

GO - Molecular functioni

  1. drug binding Source: Ensembl
  2. nicotinamide phosphoribosyltransferase activity Source: MGI
  3. nicotinate-nucleotide diphosphorylase (carboxylating) activity Source: InterPro

GO - Biological processi

  1. circadian regulation of gene expression Source: UniProtKB
  2. circadian rhythm Source: UniProtKB
  3. female pregnancy Source: Ensembl
  4. NAD biosynthetic process Source: MGI
  5. positive regulation of smooth muscle cell proliferation Source: Ensembl
  6. response to organic cyclic compound Source: Ensembl
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.
ReactomeiREACT_115781. Bmal1:Clock,Npas2 activates circadian gene expression.
REACT_198620. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_211619. 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
ProteomesiUP000000589: 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

  1. cytoplasm Source: MGI
  2. extracellular space Source: UniProtKB-KW
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 491491Nicotinamide phosphoribosyltransferasePRO_0000205864Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ99KQ4.
PaxDbiQ99KQ4.
PRIDEiQ99KQ4.

PTM databases

PhosphoSiteiQ99KQ4.

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

BgeeiQ99KQ4.
CleanExiMM_NAMPT.
GenevestigatoriQ99KQ4.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

1
491
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 133
Beta strandi14 – 163
Helixi17 – 248
Beta strandi30 – 3910
Beta strandi56 – 594
Helixi62 – 698
Helixi77 – 9115
Helixi98 – 10811
Beta strandi114 – 1185
Beta strandi123 – 1264
Beta strandi129 – 13810
Helixi139 – 1435
Helixi144 – 1474
Helixi149 – 1535
Helixi156 – 18025
Helixi186 – 1883
Beta strandi189 – 1924
Turni195 – 1973
Helixi201 – 21111
Turni212 – 2143
Beta strandi216 – 2194
Helixi222 – 2309
Beta strandi234 – 2363
Beta strandi238 – 2403
Helixi247 – 2515
Helixi255 – 2573
Helixi258 – 26811
Beta strandi270 – 2723
Beta strandi274 – 2774
Helixi283 – 2886
Helixi289 – 2946
Helixi296 – 2994
Beta strandi308 – 3114
Helixi317 – 33115
Beta strandi348 – 3525
Helixi358 – 37013
Helixi375 – 3773
Beta strandi378 – 3836
Helixi384 – 3874
Turni392 – 3965
Beta strandi397 – 40610
Beta strandi409 – 4124
Helixi421 – 4233
Beta strandi431 – 4344
Beta strandi440 – 4434
Helixi447 – 4504
Beta strandi452 – 4543
Beta strandi459 – 4635
Helixi473 – 4797

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GVLX-ray2.10A/B1-491[»]
2H3BX-ray1.95A/B1-491[»]
2H3DX-ray2.10A/B1-491[»]
ProteinModelPortaliQ99KQ4.
SMRiQ99KQ4. Positions 8-483.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99KQ4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni311 – 3133Nicotinamide ribonucleotide binding
Regioni353 – 3542Nicotinamide ribonucleotide binding

Sequence similaritiesi

Belongs to the NAPRTase family.Curated

Phylogenomic databases

eggNOGiCOG1488.
GeneTreeiENSGT00390000006647.
HOGENOMiHOG000216546.
HOVERGENiHBG000336.
InParanoidiQ99KQ4.
KOiK03462.
OMAiKKFPITE.
OrthoDBiEOG7PGDQH.
PhylomeDBiQ99KQ4.
TreeFamiTF333530.

Family and domain databases

InterProiIPR007229. Nic_PRibTrfase-Fam.
IPR016471. Nicotinamide_PRibTrfase.
IPR002638. Quinolinate_PRibosylTrfase_C.
[Graphical view]
PANTHERiPTHR11098. PTHR11098. 1 hit.
PTHR11098:SF2. PTHR11098:SF2. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti170 – 1701K → R in AAF43208. 1 PublicationCurated
Sequence conflicti193 – 1931F → S in AAF43208. 1 PublicationCurated
Sequence conflicti215 – 2151F → L in AAF43208. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS25871.1.
RefSeqi NP_067499.2. NM_021524.2.
UniGenei Mm.202727.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2GVL X-ray 2.10 A/B 1-491 [» ]
2H3B X-ray 1.95 A/B 1-491 [» ]
2H3D X-ray 2.10 A/B 1-491 [» ]
ProteinModelPortali Q99KQ4.
SMRi Q99KQ4. Positions 8-483.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29217N.
IntActi Q99KQ4. 2 interactions.
MINTi MINT-4123932.
STRINGi 10090.ENSMUSP00000020886.

PTM databases

PhosphoSitei Q99KQ4.

Proteomic databases

MaxQBi Q99KQ4.
PaxDbi Q99KQ4.
PRIDEi Q99KQ4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020886 ; ENSMUSP00000020886 ; ENSMUSG00000020572 .
GeneIDi 59027.
KEGGi mmu:59027.
UCSCi uc007nif.2. mouse.

Organism-specific databases

CTDi 10135.
MGIi MGI:1929865. Nampt.

Phylogenomic databases

eggNOGi COG1488.
GeneTreei ENSGT00390000006647.
HOGENOMi HOG000216546.
HOVERGENi HBG000336.
InParanoidi Q99KQ4.
KOi K03462.
OMAi KKFPITE.
OrthoDBi EOG7PGDQH.
PhylomeDBi Q99KQ4.
TreeFami TF333530.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00890 .
BRENDAi 2.4.2.12. 3474.
Reactomei REACT_115781. Bmal1:Clock,Npas2 activates circadian gene expression.
REACT_198620. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_211619. Nicotinamide salvaging.
SABIO-RK Q99KQ4.

Miscellaneous databases

ChiTaRSi NAMPT. mouse.
EvolutionaryTracei Q99KQ4.
NextBioi 314606.
PROi Q99KQ4.
SOURCEi Search...

Gene expression databases

Bgeei Q99KQ4.
CleanExi MM_NAMPT.
Genevestigatori Q99KQ4.

Family and domain databases

InterProi IPR007229. Nic_PRibTrfase-Fam.
IPR016471. Nicotinamide_PRibTrfase.
IPR002638. Quinolinate_PRibosylTrfase_C.
[Graphical view ]
PANTHERi PTHR11098. PTHR11098. 1 hit.
PTHR11098:SF2. PTHR11098:SF2. 1 hit.
Pfami PF04095. NAPRTase. 1 hit.
[Graphical view ]
PIRSFi PIRSF005943. NMPRT. 1 hit.
SUPFAMi SSF51690. SSF51690. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: FUNCTION, INDUCTION.
  7. "Circadian control of the NAD+ salvage pathway by CLOCK-SIRT1."
    Nakahata Y., Sahar S., Astarita G., Kaluzova M., Sassone-Corsi P.
    Science 324:654-657(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "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.
  9. "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.

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: October 29, 2014
This is version 117 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

External Data

Dasty 3