NAMPT_RAT
ID NAMPT_RAT Reviewed; 491 AA.
AC Q80Z29; Q2VT47;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12782293; DOI=10.1016/s0014-5793(03)00476-9;
RA Kitani T., Okuno S., Fujisawa H.;
RT "Growth phase-dependent changes in the subcellular localization of pre-B-
RT cell colony-enhancing factor.";
RL FEBS Lett. 544:74-78(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Xing J., Gao Y., Cao G., Chen J.;
RT "NAD biosynthesis pathway mediated by nicotinamide
RT phosphoribosyltransferase attenuates ischemic neuronal cell death.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH NICOTINAMIDE
RP MONONUCLEOTIDE AND FK866, AND SUBUNIT.
RX PubMed=16901503; DOI=10.1016/j.jmb.2006.06.082;
RA Kim M.-K., Lee J.H., Kim H., Park S.J., Kim S.H., Kang G.B., Lee Y.S.,
RA Kim J.B., Kim K.K., Suh S.W., Eom S.H.;
RT "Crystal structure of visfatin/pre-B cell colony-enhancing factor
RT 1/nicotinamide phosphoribosyltransferase, free and in complex with the
RT anti-cancer agent FK-866.";
RL J. Mol. Biol. 362:66-77(2006).
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. NAMPT-dependent oscillatory production of NAD
CC regulates oscillation of clock target gene expression by releasing the
CC core clock component: CLOCK-ARNTL/BMAL1 heterodimer from NAD-dependent
CC SIRT1-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:0000269|PubMed:16901503}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12782293}. Cytoplasm
CC {ECO:0000269|PubMed:12782293}. Secreted {ECO:0000250|UniProtKB:P43490}.
CC Note=Under non-inflammatory conditions, visfatin predominantly exhibits
CC a granular pattern within the nucleus. Secreted by endothelial cells
CC upon IL-1beta stimulation. Abundantly secreted in milk, reaching 100-
CC fold higher concentrations compared to maternal serum.
CC {ECO:0000250|UniProtKB:P43490}.
CC -!- TISSUE SPECIFICITY: Expressed in various tissues. At the highest level
CC in liver and at the second highest in heart. The amount is higher in
CC heart than in lung. {ECO:0000269|PubMed:12782293}.
CC -!- SIMILARITY: Belongs to the NAPRTase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB081730; BAC66022.1; -; mRNA.
DR EMBL; AY831728; AAX49410.1; -; mRNA.
DR EMBL; BC085681; AAH85681.1; -; mRNA.
DR RefSeq; NP_808789.1; NM_177928.3.
DR PDB; 2G95; X-ray; 1.90 A; A/B=1-491.
DR PDB; 2G96; X-ray; 2.90 A; A/B=1-491.
DR PDB; 2G97; X-ray; 2.90 A; A/B=1-491.
DR PDB; 3G8E; X-ray; 3.00 A; A/B=1-491.
DR PDBsum; 2G95; -.
DR PDBsum; 2G96; -.
DR PDBsum; 2G97; -.
DR PDBsum; 3G8E; -.
DR AlphaFoldDB; Q80Z29; -.
DR SMR; Q80Z29; -.
DR STRING; 10116.ENSRNOP00000013043; -.
DR BindingDB; Q80Z29; -.
DR ChEMBL; CHEMBL3259475; -.
DR iPTMnet; Q80Z29; -.
DR PhosphoSitePlus; Q80Z29; -.
DR jPOST; Q80Z29; -.
DR PaxDb; Q80Z29; -.
DR PRIDE; Q80Z29; -.
DR Ensembl; ENSRNOT00000013043; ENSRNOP00000013043; ENSRNOG00000009754.
DR GeneID; 297508; -.
DR KEGG; rno:297508; -.
DR UCSC; RGD:631365; rat.
DR CTD; 10135; -.
DR RGD; 631365; Nampt.
DR eggNOG; ENOG502QSGN; Eukaryota.
DR GeneTree; ENSGT00940000153456; -.
DR HOGENOM; CLU_012550_2_0_1; -.
DR InParanoid; Q80Z29; -.
DR OMA; TFGFAMK; -.
DR OrthoDB; 446086at2759; -.
DR BRENDA; 2.4.2.12; 5301.
DR Reactome; R-RNO-197264; Nicotinamide salvaging.
DR SABIO-RK; Q80Z29; -.
DR UniPathway; UPA00253; UER00890.
DR EvolutionaryTrace; Q80Z29; -.
DR PRO; PR:Q80Z29; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000009754; Expressed in skeletal muscle tissue and 19 other tissues.
DR ExpressionAtlas; Q80Z29; baseline and differential.
DR Genevisible; Q80Z29; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0005125; F:cytokine activity; IDA:RGD.
DR GO; GO:1901363; F:heterocyclic compound binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IDA:RGD.
DR GO; GO:0047280; F:nicotinamide phosphoribosyltransferase activity; IDA:RGD.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IEP:RGD.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IEP:RGD.
DR GO; GO:0090650; P:cellular response to oxygen-glucose deprivation; IEP:RGD.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEP:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0001774; P:microglial cell activation; IMP:RGD.
DR GO; GO:0009435; P:NAD biosynthetic process; ISO:RGD.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP:RGD.
DR GO; GO:2000773; P:negative regulation of cellular senescence; IDA:RGD.
DR GO; GO:0070997; P:neuron death; IEP:RGD.
DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISO:RGD.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0014916; P:regulation of lung blood pressure; IMP:RGD.
DR GO; GO:1905377; P:response to D-galactose; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Biological rhythms; Cytokine; Cytoplasm;
KW Glycosyltransferase; Nucleus; Phosphoprotein;
KW Pyridine nucleotide biosynthesis; Reference proteome; Secreted;
KW Transferase.
FT CHAIN 1..491
FT /note="Nicotinamide phosphoribosyltransferase"
FT /id="PRO_0000205866"
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 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 BINDING 384
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT BINDING 392
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
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"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:2G95"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:2G96"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:2G95"
FT STRAND 30..39
FT /evidence="ECO:0007829|PDB:2G95"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:2G95"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:2G97"
FT HELIX 77..91
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:2G95"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:2G95"
FT STRAND 124..138
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 139..143
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 149..153
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 156..180
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:2G95"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:2G95"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:2G96"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:2G95"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:2G95"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 222..230
FT /evidence="ECO:0007829|PDB:2G95"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:2G97"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 258..268
FT /evidence="ECO:0007829|PDB:2G95"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:2G96"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 283..288
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:2G95"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 317..331
FT /evidence="ECO:0007829|PDB:2G95"
FT STRAND 348..352
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 358..370
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:2G95"
FT STRAND 378..383
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:2G95"
FT STRAND 397..406
FT /evidence="ECO:0007829|PDB:2G95"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:2G96"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:2G95"
FT STRAND 440..443
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 447..450
FT /evidence="ECO:0007829|PDB:2G95"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:2G97"
FT STRAND 459..463
FT /evidence="ECO:0007829|PDB:2G95"
FT HELIX 473..479
FT /evidence="ECO:0007829|PDB:2G95"
SQ SEQUENCE 491 AA; 55438 MW; 78F526F0D3F579FC CRC64;
MNAAAEAEFN ILLATDSYKV THYKQYPPNT SKVYSYFECR EKKTENSKVR KVKYEETVFY
GLQYILNKYL KGKVVTKEKI QEAKEVYREH FQDDVFNERG WNYILEKYDG HLPIEVKAVP
EGSVIPRGNV LFTVENTDPE CYWLTNWIET ILVQSWYPIT VATNSREQKK ILAKYLLETS
GNLDGLEYKL HDFGYRGVSS QETAGIGASA HLVNFKGTDT VAGIALIKKY YGTKDPVPGY
SVPAAEHSTI TAWGKDHEKD AFEHIVTQFS SVPVSVVSDS YDIYNACEKI WGEDLRHLIV
SRSTEAPLII RPDSGNPLDT VLKVLDILGK KFPVSENSKG YKLLPPYLRV IQGDGVDINT
LQEIVEGMKQ KKWSIENVSF GSGGALLQKL TRDLLNCSFK CSYVVTNGLG VNVFKDPVAD
PNKRSKKGRL SLHRTPAGTF VTLEEGKGDL EEYGHDLLHT VFKNGKVTKS YSFDEVRKNA
QLNMEQDVAP H
