[1]	NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. DOI=10.1016/S0014-5793(03)00476-9; PubMed=12782293 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

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 (By similarity).
CATALYTIC ACTIVITY: Nicotinamide D-ribonucleotide + diphosphate = nicotinamide + 5-phospho-alpha-D-ribose 1-diphosphate.
PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinamide ribonucleotide from 5-phospho-alpha-D-ribose 1-diphosphate and nicotinamide: step 1/1 .
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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.
SIMILARITY: Belongs to the NAPRTase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB081730; BAC66022.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY831728; AAX49410.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC085681; AAH85681.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00230979; -.

NP_808789.1; -.

3D structure databases

PDB

2G95; X-ray; 1.90 A; A/B=1-491.	[ExPASy / RCSB / EBI]
2G96; X-ray; 2.90 A; A/B=1-491.	[ExPASy / RCSB / EBI]
2G97; X-ray; 2.90 A; A/B=1-491.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2G95; -.
2G96; -.
2G97; -.

ModBase

Q80Z29.

Enzyme and pathway databases

BRENDA

2.4.2.12; 248.

Organism-specific databases

RGD

631365; Nampt.

Gene expression databases

ArrayExpress

Q80Z29; -.

GermOnline

ENSRNOG00000009754; Rattus norvegicus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from RGD).
GO:0005634;	Cellular component: nucleus (inferred from direct assay from RGD).
GO:0008144;	Molecular function: drug binding (inferred from direct assay from RGD).
GO:0047280;	Molecular function: nicotinamide phosphoribosyltransferase activity (inferred from direct assay from RGD).
GO:0042803;	Molecular function: protein homodimerization activity (inferred from direct assay from RGD).
GO:0007049;	Biological process: cell cycle (inferred from physical interaction from RGD).
GO:0007565;	Biological process: female pregnancy (inferred from expression pattern from RGD).
GO:0019363;	Biological process: pyridine nucleotide biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0014070;	Biological process: response to organic cyclic substance (inferred from expression pattern from RGD).
QuickGo view.

Family and domain databases

InterPro

IPR015977; Nic_PRibTrfase-like.
IPR016471; Nicotinamide_PRibTrfase.
Graphical view of domain structure.

Pfam

PF04095; NAPRTase; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF005943; NMPRT; 1.

Proteomic databases

PRIDE

Q80Z29; -.

Genome annotation databases

GeneID

297508; -.

KEGG

rno:297508; -.

Phylogenomic databases

HOVERGEN

Q80Z29; -.

Other

642340; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cytoplasm; Glycosyltransferase; Nucleus; Phosphoprotein; Pyridine nucleotide biosynthesis; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 491`	`491`	`Nicotinamide phosphoribosyltransferase.`	`PRO_0000205866`
`MOD_RES`	`34 34`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`188 188`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`398 398`		`Phosphoserine (By similarity).`
`HELIX`	`11 13`	`3`
`HELIX`	`17 24`	`8`
`STRAND`	`30 39`	`10`
`STRAND`	`56 58`	`3`
`HELIX`	`62 69`	`8`
`HELIX`	`77 91`	`15`
`HELIX`	`98 108`	`11`
`STRAND`	`114 118`	`5`
`STRAND`	`124 138`	`15`
`HELIX`	`139 143`	`5`
`HELIX`	`144 147`	`4`
`HELIX`	`149 153`	`5`
`HELIX`	`156 180`	`25`
`HELIX`	`186 188`	`3`
`STRAND`	`189 192`	`4`
`HELIX`	`195 197`	`3`
`HELIX`	`201 211`	`11`
`TURN`	`212 214`	`3`
`STRAND`	`217 219`	`3`
`HELIX`	`222 230`	`9`
`STRAND`	`238 240`	`3`
`HELIX`	`247 250`	`4`
`HELIX`	`251 253`	`3`
`HELIX`	`255 257`	`3`
`HELIX`	`258 268`	`11`
`STRAND`	`274 278`	`5`
`HELIX`	`283 288`	`6`
`HELIX`	`289 294`	`6`
`HELIX`	`296 299`	`4`
`STRAND`	`308 311`	`4`
`HELIX`	`317 331`	`15`
`STRAND`	`348 352`	`5`
`HELIX`	`358 370`	`13`
`HELIX`	`375 377`	`3`
`STRAND`	`378 383`	`6`
`HELIX`	`384 387`	`4`
`HELIX`	`392 394`	`3`
`STRAND`	`397 406`	`10`
`STRAND`	`409 411`	`3`
`STRAND`	`431 434`	`4`
`STRAND`	`440 443`	`4`
`HELIX`	`447 450`	`4`
`STRAND`	`459 463`	`5`
`HELIX`	`473 479`	`7`

Sequence information

Length: 491 AA [This is the length of the unprocessed precursor]

Molecular weight: 55438 Da [This is the MW of the unprocessed precursor]

CRC64: 78F526F0D3F579FC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNAAAEAEFN ILLATDSYKV THYKQYPPNT SKVYSYFECR EKKTENSKVR KVKYEETVFY 

        70         80         90        100        110        120 
GLQYILNKYL KGKVVTKEKI QEAKEVYREH FQDDVFNERG WNYILEKYDG HLPIEVKAVP 

       130        140        150        160        170        180 
EGSVIPRGNV LFTVENTDPE CYWLTNWIET ILVQSWYPIT VATNSREQKK ILAKYLLETS 

       190        200        210        220        230        240 
GNLDGLEYKL HDFGYRGVSS QETAGIGASA HLVNFKGTDT VAGIALIKKY YGTKDPVPGY 

       250        260        270        280        290        300 
SVPAAEHSTI TAWGKDHEKD AFEHIVTQFS SVPVSVVSDS YDIYNACEKI WGEDLRHLIV 

       310        320        330        340        350        360 
SRSTEAPLII RPDSGNPLDT VLKVLDILGK KFPVSENSKG YKLLPPYLRV IQGDGVDINT 

       370        380        390        400        410        420 
LQEIVEGMKQ KKWSIENVSF GSGGALLQKL TRDLLNCSFK CSYVVTNGLG VNVFKDPVAD 

       430        440        450        460        470        480 
PNKRSKKGRL SLHRTPAGTF VTLEEGKGDL EEYGHDLLHT VFKNGKVTKS YSFDEVRKNA 

       490 
QLNMEQDVAP H

Q80Z29 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools