NAMPT_PIG
ID NAMPT_PIG Reviewed; 491 AA.
AC Q52I78; Q3I6K8;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Nicotinamide phosphoribosyltransferase;
DE Short=NAmPRTase;
DE Short=Nampt;
DE EC=2.4.2.12 {ECO:0000250|UniProtKB:Q99KQ4};
DE AltName: Full=Pre-B-cell colony-enhancing factor 1 homolog;
DE Short=PBEF;
DE AltName: Full=Visfatin;
GN Name=NAMPT; Synonyms=PBEF1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu B.-H., Ding S.-T.;
RT "Cloning and expression of porcine visfatin.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chen H., Yang Z.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the condensation of nicotinamide with 5-
CC phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an
CC intermediate in the biosynthesis of NAD. It is the rate limiting
CC component in the mammalian NAD biosynthesis pathway. The secreted form
CC behaves both as a cytokine with immunomodulating properties and an
CC adipokine with anti-diabetic properties, it has no enzymatic activity,
CC partly because of lack of activation by ATP, which has a low level in
CC extracellular space and plasma. Plays a role in the modulation of
CC circadian clock function. Plays a role in the modulation of circadian
CC clock function. NAMPT-dependent oscillatory production of NAD regulates
CC oscillation of clock target gene expression by releasing the core clock
CC component: CLOCK-ARNTL/BMAL1 heterodimer from NAD-dependent SIRT1-
CC mediated suppression. {ECO:0000250|UniProtKB:P43490,
CC ECO:0000250|UniProtKB:Q99KQ4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-nicotinamide D-ribonucleotide + diphosphate = 5-phospho-
CC alpha-D-ribose 1-diphosphate + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16149, ChEBI:CHEBI:14649, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.12;
CC Evidence={ECO:0000250|UniProtKB:Q99KQ4};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16151;
CC Evidence={ECO:0000250|UniProtKB:Q99KQ4};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinamide D-
CC ribonucleotide from 5-phospho-alpha-D-ribose 1-diphosphate and
CC nicotinamide: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P43490}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P43490}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q99KQ4}. Secreted
CC {ECO:0000250|UniProtKB:P43490}. Note=Under non-inflammatory conditions,
CC visfatin predominantly exhibits a granular pattern within the nucleus.
CC Secreted by endothelial cells upon IL-1beta stimulation. Abundantly
CC secreted in milk, reaching 100-fold higher concentrations compared to
CC maternal serum. {ECO:0000250|UniProtKB:P43490}.
CC -!- SIMILARITY: Belongs to the NAPRTase family. {ECO:0000305}.
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DR EMBL; DQ020218; AAY89036.1; -; mRNA.
DR EMBL; DQ001974; AAY18209.2; -; mRNA.
DR RefSeq; NP_001026963.1; NM_001031793.2.
DR RefSeq; XP_005667778.1; XM_005667721.2.
DR AlphaFoldDB; Q52I78; -.
DR SMR; Q52I78; -.
DR STRING; 9823.ENSSSCP00000016366; -.
DR PaxDb; Q52I78; -.
DR PeptideAtlas; Q52I78; -.
DR PRIDE; Q52I78; -.
DR Ensembl; ENSSSCT00000016815; ENSSSCP00000016366; ENSSSCG00000015435.
DR Ensembl; ENSSSCT00015027285; ENSSSCP00015010680; ENSSSCG00015020619.
DR Ensembl; ENSSSCT00025073146; ENSSSCP00025031692; ENSSSCG00025052770.
DR Ensembl; ENSSSCT00030036653; ENSSSCP00030016758; ENSSSCG00030026152.
DR Ensembl; ENSSSCT00035085702; ENSSSCP00035035670; ENSSSCG00035063648.
DR Ensembl; ENSSSCT00040104251; ENSSSCP00040047452; ENSSSCG00040075208.
DR Ensembl; ENSSSCT00045063220; ENSSSCP00045044570; ENSSSCG00045036681.
DR Ensembl; ENSSSCT00050050316; ENSSSCP00050021045; ENSSSCG00050037351.
DR Ensembl; ENSSSCT00055050900; ENSSSCP00055040693; ENSSSCG00055025329.
DR Ensembl; ENSSSCT00060100116; ENSSSCP00060043441; ENSSSCG00060072321.
DR Ensembl; ENSSSCT00065059675; ENSSSCP00065025888; ENSSSCG00065043557.
DR Ensembl; ENSSSCT00070043855; ENSSSCP00070036932; ENSSSCG00070022024.
DR GeneID; 595123; -.
DR KEGG; ssc:595123; -.
DR CTD; 10135; -.
DR VGNC; VGNC:90573; NAMPT.
DR eggNOG; ENOG502QSGN; Eukaryota.
DR GeneTree; ENSGT00940000153456; -.
DR HOGENOM; CLU_012550_2_0_1; -.
DR InParanoid; Q52I78; -.
DR OrthoDB; 446086at2759; -.
DR TreeFam; TF333530; -.
DR Reactome; R-SSC-197264; Nicotinamide salvaging.
DR UniPathway; UPA00253; UER00890.
DR Proteomes; UP000008227; Chromosome 9.
DR Proteomes; UP000314985; Chromosome 9.
DR Bgee; ENSSSCG00000015435; Expressed in muscle tissue and 44 other tissues.
DR ExpressionAtlas; Q52I78; baseline and differential.
DR Genevisible; Q52I78; SS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0047280; F:nicotinamide phosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
DR CDD; cd01569; PBEF_like; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR041529; DUF5598.
DR InterPro; IPR041525; N/Namide_PRibTrfase.
DR InterPro; IPR016471; Nicotinamide_PRibTrfase.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR PANTHER; PTHR43816; PTHR43816; 1.
DR Pfam; PF18127; NAMPT_N; 1.
DR Pfam; PF04095; NAPRTase; 1.
DR PIRSF; PIRSF005943; NMPRT; 1.
DR SUPFAM; SSF51690; SSF51690; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Biological rhythms; Cytokine; Cytoplasm; Glycosyltransferase;
KW Nucleus; Phosphoprotein; Pyridine nucleotide biosynthesis;
KW Reference proteome; Secreted; Transferase.
FT CHAIN 1..491
FT /note="Nicotinamide phosphoribosyltransferase"
FT /id="PRO_0000205865"
FT BINDING 196
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000250"
FT BINDING 311..313
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000250"
FT BINDING 353..354
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P43490"
FT MOD_RES 188
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P43490"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43490"
SQ SEQUENCE 491 AA; 55374 MW; EC9CF05026B4793E CRC64;
MNAAAEAEFN ILLATDSYKV THYKQYPPNT SKVYSYFECR EKKTENSKIR KVKYEETVFY
GLQYILNKYL KGKVVTKEKI QEAKEVYKEH FQDDVFNEKG WNYILEKYDG HLPIEVKAVP
EGSVIPRGNV LFTVENTDPE CYWLTNWIET ILVQSWYPIT VATNSREQKK ILAKYLLETS
GNLDGLEYKL HDFGYRGVSS QETAGIGASA HLVNFKGTDT VAGIALIKKY YGTKDPVPGY
SVPAAEHSTI TAWGKDHEKD AFEHIVTQFS SVPVSVVSDS YDIYNACEKI WGEDLRHLIV
SRSTEAPLII RPDSGNPLDT VLKVLDILGK KFPVTENSKG YKLLPPYLRV IQGDGVDINT
LQEIVEGMKQ KKWSIENIAF GSGGALLQKL TRDLLNCSFK CSYVVTNGLG INVFKDPVAD
PNKRSKKGRL SLHRTPGGNF VTLEEGKGDL EEYGHDLLHT VFKNGKVTKS YSFDEVRKNA
QLNIELEAAP H
