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Q99KQ4

- NAMPT_MOUSE

UniProt

Q99KQ4 - NAMPT_MOUSE

Protein

Nicotinamide phosphoribosyltransferase

Gene

Nampt

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    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.By similarity3 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. female pregnancy Source: Ensembl
    2. NAD biosynthetic process Source: MGI
    3. positive regulation of smooth muscle cell proliferation Source: Ensembl
    4. response to organic cyclic compound Source: Ensembl

    Keywords - Molecular functioni

    Cytokine, Glycosyltransferase, Transferase

    Keywords - Biological processi

    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.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. extracellular space Source: UniProtKB-KW
    3. nucleus Source: UniProtKB-SubCell

    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

    Up-regulated during polyclonal immune responses.1 Publication

    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

    MNAAAEAEFN ILLATDSYKV THYKQYPPNT SKVYSYFECR EKKTENSKVR    50
    KVKYEETVFY GLQYILNKYL KGKVVTKEKI QEAKEVYREH FQDDVFNERG 100
    WNYILEKYDG HLPIEVKAVP EGSVIPRGNV LFTVENTDPE CYWLTNWIET 150
    ILVQSWYPIT VATNSREQKK ILAKYLLETS GNLDGLEYKL HDFGYRGVSS 200
    QETAGIGASA HLVNFKGTDT VAGIALIKKY YGTKDPVPGY SVPAAEHSTI 250
    TAWGKDHEKD AFEHIVTQFS SVPVSVVSDS YDIYNACEKI WGEDLRHLIV 300
    SRSTEAPLII RPDSGNPLDT VLKVLDILGK KFPVTENSKG YKLLPPYLRV 350
    IQGDGVDINT LQEIVEGMKQ KKWSIENVSF GSGGALLQKL TRDLLNCSFK 400
    CSYVVTNGLG VNVFKDPVAD PNKRSKKGRL SLHRTPAGNF VTLEEGKGDL 450
    EEYGHDLLHT VFKNGKVTKS YSFDEVRKNA QLNIEQDVAP H 491
    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

    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. "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.
    7. "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.
    8. "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 1, 2014
    This is version 116 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