Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q52I78

- NAMPT_PIG

UniProt

Q52I78 - NAMPT_PIG

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Nicotinamide phosphoribosyltransferase

Gene

NAMPT

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

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. 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 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. circadian regulation of gene expression Source: UniProtKB
  2. NAD biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Glycosyltransferase, Transferase

Keywords - Biological processi

Biological rhythms, 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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  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_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.
InParanoidiQ52I78.
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

« Hide

        10         20         30         40         50
MNAAAEAEFN ILLATDSYKV THYKQYPPNT SKVYSYFECR EKKTENSKIR
60 70 80 90 100
KVKYEETVFY GLQYILNKYL KGKVVTKEKI QEAKEVYKEH FQDDVFNEKG
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 KKWSIENIAF GSGGALLQKL TRDLLNCSFK
410 420 430 440 450
CSYVVTNGLG INVFKDPVAD PNKRSKKGRL SLHRTPGGNF VTLEEGKGDL
460 470 480 490
EEYGHDLLHT VFKNGKVTKS YSFDEVRKNA QLNIELEAAP H
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.
InParanoidi Q52I78.
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 29, 2014
This is version 71 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