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Nicotinamide phosphoribosyltransferase (NAmPRTase) (Nampt) (EC 2.4.2.12) (Pre-B-cell colony-enhancing factor 1 homolog) (PBEF) (Visfatin)

 NAMPT_RAT               Reviewed;         491 AA.
Q80Z29; Q2VT47;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
20-DEC-2017, entry version 116.
RecName: Full=Nicotinamide phosphoribosyltransferase;
Short=NAmPRTase;
Short=Nampt;
EC=2.4.2.12;
AltName: Full=Pre-B-cell colony-enhancing factor 1 homolog;
Short=PBEF;
AltName: Full=Visfatin;
Name=Nampt; Synonyms=Pbef1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=12782293; DOI=10.1016/S0014-5793(03)00476-9;
Kitani T., Okuno S., Fujisawa H.;
"Growth phase-dependent changes in the subcellular localization of
pre-B-cell colony-enhancing factor.";
FEBS Lett. 544:74-78(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Brain;
Xing J., Gao Y., Cao G., Chen J.;
"NAD biosynthesis pathway mediated by nicotinamide
phosphoribosyltransferase attenuates ischemic neuronal cell death.";
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH NICOTINAMIDE
MONONUCLEOTIDE AND FK866, AND SUBUNIT.
PubMed=16901503; DOI=10.1016/j.jmb.2006.06.082;
Kim M.-K., Lee J.H., Kim H., Park S.J., Kim S.H., Kang G.B., Lee Y.S.,
Kim J.B., Kim K.K., Suh S.W., Eom S.H.;
"Crystal structure of visfatin/pre-B cell colony-enhancing factor
1/nicotinamide phosphoribosyltransferase, free and in complex with the
anti-cancer agent FK-866.";
J. Mol. Biol. 362:66-77(2006).
-!- FUNCTION: 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. 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. {ECO:0000250|UniProtKB:P43490,
ECO:0000250|UniProtKB:Q99KQ4}.
-!- CATALYTIC ACTIVITY: Nicotinamide D-ribonucleotide + diphosphate =
nicotinamide + 5-phospho-alpha-D-ribose 1-diphosphate.
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinamide
D-ribonucleotide from 5-phospho-alpha-D-ribose 1-diphosphate and
nicotinamide: step 1/1.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16901503}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12782293}.
Cytoplasm {ECO:0000269|PubMed:12782293}. Secreted
{ECO:0000250|UniProtKB:P43490}. 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.
{ECO:0000250|UniProtKB:P43490}.
-!- TISSUE SPECIFICITY: Expressed in various tissues. At the highest
level in liver and at the second highest in heart. The amount is
higher in heart than in lung. {ECO:0000269|PubMed:12782293}.
-!- SIMILARITY: Belongs to the NAPRTase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB081730; BAC66022.1; -; mRNA.
EMBL; AY831728; AAX49410.1; -; mRNA.
EMBL; BC085681; AAH85681.1; -; mRNA.
RefSeq; NP_808789.1; NM_177928.3.
UniGene; Rn.203508; -.
PDB; 2G95; X-ray; 1.90 A; A/B=1-491.
PDB; 2G96; X-ray; 2.90 A; A/B=1-491.
PDB; 2G97; X-ray; 2.90 A; A/B=1-491.
PDB; 3G8E; X-ray; 3.00 A; A/B=1-491.
PDBsum; 2G95; -.
PDBsum; 2G96; -.
PDBsum; 2G97; -.
PDBsum; 3G8E; -.
ProteinModelPortal; Q80Z29; -.
SMR; Q80Z29; -.
STRING; 10116.ENSRNOP00000013043; -.
BindingDB; Q80Z29; -.
ChEMBL; CHEMBL3259475; -.
iPTMnet; Q80Z29; -.
PhosphoSitePlus; Q80Z29; -.
PaxDb; Q80Z29; -.
PRIDE; Q80Z29; -.
Ensembl; ENSRNOT00000013043; ENSRNOP00000013043; ENSRNOG00000009754.
GeneID; 297508; -.
KEGG; rno:297508; -.
UCSC; RGD:631365; rat.
CTD; 10135; -.
RGD; 631365; Nampt.
eggNOG; ENOG410IEB2; Eukaryota.
eggNOG; COG1488; LUCA.
GeneTree; ENSGT00390000006647; -.
HOGENOM; HOG000216546; -.
HOVERGEN; HBG000336; -.
InParanoid; Q80Z29; -.
KO; K03462; -.
OMA; VWYPITV; -.
OrthoDB; EOG091G04ZB; -.
BRENDA; 2.4.2.12; 5301.
Reactome; R-RNO-197264; Nicotinamide salvaging.
SABIO-RK; Q80Z29; -.
UniPathway; UPA00253; UER00890.
EvolutionaryTrace; Q80Z29; -.
PRO; PR:Q80Z29; -.
Proteomes; UP000002494; Chromosome 6.
Bgee; ENSRNOG00000009754; -.
ExpressionAtlas; Q80Z29; baseline and differential.
Genevisible; Q80Z29; RN.
GO; GO:0030054; C:cell junction; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005125; F:cytokine activity; IDA:RGD.
GO; GO:0008144; F:drug binding; IDA:RGD.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0047280; F:nicotinamide phosphoribosyltransferase activity; IDA:RGD.
GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0007623; P:circadian rhythm; ISO:RGD.
GO; GO:0007565; P:female pregnancy; IEP:RGD.
GO; GO:0009435; P:NAD biosynthetic process; ISO:RGD.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISO:RGD.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISO:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
CDD; cd01569; PBEF_like; 1.
InterPro; IPR007229; Nic_PRibTrfase-Fam.
InterPro; IPR016471; Nicotinamide_PRibTrfase.
InterPro; IPR036068; Nicotinate_pribotase_like_C.
PANTHER; PTHR43816; PTHR43816; 1.
Pfam; PF04095; NAPRTase; 1.
PIRSF; PIRSF005943; NMPRT; 1.
SUPFAM; SSF51690; SSF51690; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Biological rhythms; Complete proteome;
Cytokine; Cytoplasm; Glycosyltransferase; Nucleus; Phosphoprotein;
Pyridine nucleotide biosynthesis; Reference proteome; Secreted;
Transferase.
CHAIN 1 491 Nicotinamide phosphoribosyltransferase.
/FTId=PRO_0000205866.
REGION 311 313 Nicotinamide ribonucleotide binding.
REGION 353 354 Nicotinamide ribonucleotide binding.
BINDING 196 196 Diphosphate. {ECO:0000250}.
BINDING 219 219 Nicotinamide ribonucleotide.
{ECO:0000250}.
BINDING 247 247 Diphosphate. {ECO:0000250}.
BINDING 311 311 Diphosphate. {ECO:0000250}.
BINDING 384 384 Nicotinamide ribonucleotide; via amide
nitrogen.
BINDING 392 392 Nicotinamide ribonucleotide.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P43490}.
MOD_RES 188 188 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43490}.
MOD_RES 472 472 Phosphoserine.
{ECO:0000250|UniProtKB:P43490}.
HELIX 11 13 {ECO:0000244|PDB:2G95}.
STRAND 14 16 {ECO:0000244|PDB:2G96}.
HELIX 17 24 {ECO:0000244|PDB:2G95}.
STRAND 30 39 {ECO:0000244|PDB:2G95}.
STRAND 56 58 {ECO:0000244|PDB:2G95}.
HELIX 62 69 {ECO:0000244|PDB:2G95}.
STRAND 71 73 {ECO:0000244|PDB:2G97}.
HELIX 77 91 {ECO:0000244|PDB:2G95}.
HELIX 98 108 {ECO:0000244|PDB:2G95}.
STRAND 114 118 {ECO:0000244|PDB:2G95}.
STRAND 124 138 {ECO:0000244|PDB:2G95}.
HELIX 139 143 {ECO:0000244|PDB:2G95}.
HELIX 144 147 {ECO:0000244|PDB:2G95}.
HELIX 149 153 {ECO:0000244|PDB:2G95}.
HELIX 156 180 {ECO:0000244|PDB:2G95}.
HELIX 186 188 {ECO:0000244|PDB:2G95}.
STRAND 189 192 {ECO:0000244|PDB:2G95}.
HELIX 195 197 {ECO:0000244|PDB:2G95}.
STRAND 198 200 {ECO:0000244|PDB:2G96}.
HELIX 201 211 {ECO:0000244|PDB:2G95}.
TURN 212 214 {ECO:0000244|PDB:2G95}.
STRAND 217 219 {ECO:0000244|PDB:2G95}.
HELIX 222 230 {ECO:0000244|PDB:2G95}.
STRAND 234 236 {ECO:0000244|PDB:2G97}.
STRAND 238 240 {ECO:0000244|PDB:2G95}.
HELIX 247 250 {ECO:0000244|PDB:2G95}.
HELIX 251 253 {ECO:0000244|PDB:2G95}.
HELIX 255 257 {ECO:0000244|PDB:2G95}.
HELIX 258 268 {ECO:0000244|PDB:2G95}.
STRAND 270 272 {ECO:0000244|PDB:2G96}.
STRAND 274 278 {ECO:0000244|PDB:2G95}.
HELIX 283 288 {ECO:0000244|PDB:2G95}.
HELIX 289 294 {ECO:0000244|PDB:2G95}.
HELIX 296 299 {ECO:0000244|PDB:2G95}.
STRAND 308 311 {ECO:0000244|PDB:2G95}.
HELIX 317 331 {ECO:0000244|PDB:2G95}.
STRAND 348 352 {ECO:0000244|PDB:2G95}.
HELIX 358 370 {ECO:0000244|PDB:2G95}.
HELIX 375 377 {ECO:0000244|PDB:2G95}.
STRAND 378 383 {ECO:0000244|PDB:2G95}.
HELIX 384 387 {ECO:0000244|PDB:2G95}.
HELIX 392 394 {ECO:0000244|PDB:2G95}.
STRAND 397 406 {ECO:0000244|PDB:2G95}.
STRAND 409 411 {ECO:0000244|PDB:2G95}.
HELIX 421 423 {ECO:0000244|PDB:2G96}.
STRAND 431 434 {ECO:0000244|PDB:2G95}.
STRAND 440 443 {ECO:0000244|PDB:2G95}.
HELIX 447 450 {ECO:0000244|PDB:2G95}.
STRAND 453 455 {ECO:0000244|PDB:2G97}.
STRAND 459 463 {ECO:0000244|PDB:2G95}.
HELIX 473 479 {ECO:0000244|PDB:2G95}.
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


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