Q52I78 (NAMPT_PIG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nicotinamide phosphoribosyltransferase
Short name=NAmPRTase
Short name=Nampt
EC=2.4.2.12

Alternative name(s):
Pre-B-cell colony-enhancing factor 1 homolog
Short name=PBEF
Visfatin

Gene names

Name:	NAMPT
Synonyms:	PBEF1

Organism

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	491 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (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 D-ribonucleotide from 5-phospho-alpha-D-ribose 1-diphosphate and nicotinamide: step 1/1.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the NAPRTase family.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Cytoplasm
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	NAD biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	nicotinamide phosphoribosyltransferase activity Inferred from electronic annotation. Source: EC nicotinate phosphoribosyltransferase activity Inferred from electronic annotation. Source: InterPro nicotinate-nucleotide diphosphorylase (carboxylating) activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 491	491	Nicotinamide phosphoribosyltransferase		PRO_0000205865
Regions
	Region	311 – 313	3	Nicotinamide ribonucleotide binding By similarity
	Region	353 – 354	2	Nicotinamide ribonucleotide binding By similarity
Sites
	Binding site	196	1	Diphosphate By similarity
	Binding site	219	1	Nicotinamide ribonucleotide By similarity
	Binding site	247	1	Diphosphate By similarity
	Binding site	311	1	Diphosphate By similarity
	Binding site	384	1	Nicotinamide ribonucleotide; via amide nitrogen By similarity
	Binding site	392	1	Nicotinamide ribonucleotide By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q52I78 [UniParc]. Last modified January 24, 2006. Version 2. Checksum: EC9CF05026B4793E	FASTA	491	55,374
	10 20 30 40 50 60 MNAAAEAEFN ILLATDSYKV THYKQYPPNT SKVYSYFECR EKKTENSKIR KVKYEETVFY 70 80 90 100 110 120 GLQYILNKYL KGKVVTKEKI QEAKEVYKEH FQDDVFNEKG 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 KFPVTENSKG YKLLPPYLRV IQGDGVDINT 370 380 390 400 410 420 LQEIVEGMKQ KKWSIENIAF GSGGALLQKL TRDLLNCSFK CSYVVTNGLG INVFKDPVAD 430 440 450 460 470 480 PNKRSKKGRL SLHRTPGGNF VTLEEGKGDL EEYGHDLLHT VFKNGKVTKS YSFDEVRKNA 490 QLNIELEAAP H

References

[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].

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ020218 mRNA. Translation: AAY89036.1. DQ001974 mRNA. Translation: AAY18209.2.
RefSeq	NP_001026963.1. NM_001031793.2.
UniGene	Ssc.22083.
3D structure databases
ProteinModelPortal	Q52I78.
SMR	Q52I78. Positions 8-483.
ModBase	Search...
Protein-protein interaction databases
STRING	9823.ENSSSCP00000016366.
Proteomic databases
PRIDE	Q52I78.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSSSCT00000016815; ENSSSCP00000016366; ENSSSCG00000015435.
GeneID	595123.
KEGG	ssc:595123.
Organism-specific databases
CTD	10135.
Phylogenomic databases
eggNOG	COG1488.
GeneTree	ENSGT00390000006647.
HOGENOM	HOG000216546.
HOVERGEN	HBG000336.
KO	K03462.
OMA	WYPSTVA.
OrthoDB	EOG40K7ZQ.
Enzyme and pathway databases
UniPathway	UPA00253; UER00890.
Gene expression databases
ArrayExpress	Q52I78.
Family and domain databases
InterPro	IPR015977. Nic_PRibTrfase-like. IPR016471. Nicotinamide_PRibTrfase. IPR002638. Quinolinate_PRibosylTrfase_C. [Graphical view]
PANTHER	PTHR11098:SF2. PTHR11098:SF2. 1 hit.
Pfam	PF04095. NAPRTase. 1 hit. [Graphical view]
PIRSF	PIRSF005943. NMPRT. 1 hit.
SUPFAM	SSF51690. Q_phspho_trans. 1 hit.
ProtoNet	Search...

Entry information

Entry name

NAMPT_PIG

Accession

Primary (citable) accession number: Q52I78
Secondary accession number(s): Q3I6K8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	January 24, 2006
Last modified:	April 3, 2013
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program