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Q52I78

- NAMPT_PIG

UniProt

Q52I78 - NAMPT_PIG

Protein

Nicotinamide phosphoribosyltransferase

Gene

NAMPT

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 2 (24 Jan 2006)
      Previous versions | rss
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    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 By similarity.By similarity

    Catalytic activityi

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

    Pathwayi

    Sites

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

    GO - Molecular functioni

    1. nicotinamide phosphoribosyltransferase activity Source: UniProtKB-EC
    2. nicotinate-nucleotide diphosphorylase (carboxylating) activity Source: InterPro

    GO - Biological processi

    1. NAD biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Cytokine, Glycosyltransferase, Transferase

    Keywords - Biological processi

    Pyridine nucleotide biosynthesis

    Enzyme and pathway databases

    ReactomeiREACT_212440. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_221141. Nicotinamide salvaging.
    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
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Chromosome 9

    Subcellular locationi

    Nucleus By similarity. Cytoplasm By similarity. 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: UniProtKB-SubCell
    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_0000205865Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiQ52I78.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000016366.

    Structurei

    3D structure databases

    ProteinModelPortaliQ52I78.
    SMRiQ52I78. Positions 8-483.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Belongs to the NAPRTase family.Curated

    Phylogenomic databases

    eggNOGiCOG1488.
    GeneTreeiENSGT00390000006647.
    HOGENOMiHOG000216546.
    HOVERGENiHBG000336.
    KOiK03462.
    OMAiKKFPITE.
    OrthoDBiEOG7PGDQH.
    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.

    Q52I78-1 [UniParc]FASTAAdd to Basket

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    MNAAAEAEFN ILLATDSYKV THYKQYPPNT SKVYSYFECR EKKTENSKIR    50
    KVKYEETVFY GLQYILNKYL KGKVVTKEKI QEAKEVYKEH FQDDVFNEKG 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 KKWSIENIAF GSGGALLQKL TRDLLNCSFK 400
    CSYVVTNGLG INVFKDPVAD PNKRSKKGRL SLHRTPGGNF VTLEEGKGDL 450
    EEYGHDLLHT VFKNGKVTKS YSFDEVRKNA QLNIELEAAP H 491
    Length:491
    Mass (Da):55,374
    Last modified:January 24, 2006 - v2
    Checksum:iEC9CF05026B4793E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ020218 mRNA. Translation: AAY89036.1.
    DQ001974 mRNA. Translation: AAY18209.2.
    RefSeqiNP_001026963.1. NM_001031793.2.
    XP_005667778.1. XM_005667721.1.
    UniGeneiSsc.22083.

    Genome annotation databases

    EnsembliENSSSCT00000016815; ENSSSCP00000016366; ENSSSCG00000015435.
    GeneIDi595123.
    KEGGissc:595123.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ020218 mRNA. Translation: AAY89036.1 .
    DQ001974 mRNA. Translation: AAY18209.2 .
    RefSeqi NP_001026963.1. NM_001031793.2.
    XP_005667778.1. XM_005667721.1.
    UniGenei Ssc.22083.

    3D structure databases

    ProteinModelPortali Q52I78.
    SMRi Q52I78. Positions 8-483.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9823.ENSSSCP00000016366.

    Proteomic databases

    PRIDEi Q52I78.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSSSCT00000016815 ; ENSSSCP00000016366 ; ENSSSCG00000015435 .
    GeneIDi 595123.
    KEGGi ssc:595123.

    Organism-specific databases

    CTDi 10135.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00890 .
    Reactomei REACT_212440. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_221141. Nicotinamide salvaging.

    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. "Cloning and expression of porcine visfatin."
      Liu B.-H., Ding S.-T.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Chen H., Yang Z.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiNAMPT_PIG
    AccessioniPrimary (citable) accession number: Q52I78
    Secondary accession number(s): Q3I6K8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: January 24, 2006
    Last modified: October 1, 2014
    This is version 70 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3