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Protein

Nicotinate phosphoribosyltransferase

Gene

Naprt

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the conversion of nicotinic acid (NA) to NA mononucleotide (NaMN). Essential for NA to increase cellular NAD levels and prevent oxidative stress of the cells (By similarity).By similarity
Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP.By similarity

Catalytic activityi

Nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O = beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate.

Pathwayi

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. nicotinate-nucleotide diphosphorylase (carboxylating) activity Source: InterPro
  3. nicotinate phosphoribosyltransferase activity Source: UniProtKB

GO - Biological processi

  1. NAD biosynthetic process Source: UniProtKB-UniPathway
  2. nicotinate nucleotide salvage Source: InterPro
  3. response to oxidative stress Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Transferase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Enzyme and pathway databases

ReactomeiREACT_211619. Nicotinamide salvaging.
UniPathwayiUPA00253; UER00457.

Names & Taxonomyi

Protein namesi
Recommended name:
Nicotinate phosphoribosyltransferase (EC:6.3.4.21)
Short name:
NAPRTase
Alternative name(s):
Nicotinate phosphoribosyltransferase domain-containing protein 1
Gene namesi
Name:Naprt
Synonyms:Naprt1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:2442664. Naprt.

Subcellular locationi

Cytoplasmcytosol By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: MGI
  4. Golgi apparatus Source: MGI
  5. nucleoplasm Source: MGI
  6. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 538538Nicotinate phosphoribosyltransferasePRO_0000315682Add
BLAST

Proteomic databases

MaxQBiQ8CC86.
PaxDbiQ8CC86.
PRIDEiQ8CC86.

PTM databases

PhosphoSiteiQ8CC86.

Expressioni

Tissue specificityi

Abundantly expressed in the small intestine, liver and kidney.1 Publication

Gene expression databases

BgeeiQ8CC86.
GenevestigatoriQ8CC86.

Interactioni

Protein-protein interaction databases

IntActiQ8CC86. 3 interactions.
MINTiMINT-1855495.

Structurei

3D structure databases

ProteinModelPortaliQ8CC86.
SMRiQ8CC86. Positions 16-522.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the NAPRTase family.Curated

Phylogenomic databases

eggNOGiCOG1488.
GeneTreeiENSGT00390000002664.
HOGENOMiHOG000001111.
HOVERGENiHBG062439.
InParanoidiQ8CC86.
KOiK00763.
OMAiGDLEYLS.
OrthoDBiEOG7N63MH.
PhylomeDBiQ8CC86.
TreeFamiTF314732.

Family and domain databases

InterProiIPR007229. Nic_PRibTrfase-Fam.
IPR006405. Nic_PRibTrfase_pncB.
IPR002638. Quinolinate_PRibosylTrfase_C.
[Graphical view]
PANTHERiPTHR11098. PTHR11098. 1 hit.
PfamiPF04095. NAPRTase. 1 hit.
[Graphical view]
PIRSFiPIRSF000484. NAPRT. 1 hit.
SUPFAMiSSF51690. SSF51690. 2 hits.
TIGRFAMsiTIGR01513. NAPRTase_put. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8CC86-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEMELDSEGR MVVRPLLTDL YQATMALGYW RAGRACEAAE FELFFRHCPF
60 70 80 90 100
GGSFALSAGL QDCMRFLRAF RLRDADVQFL ASVLPPDTDP AFFEHLRALD
110 120 130 140 150
CSGVTVRALP EGSLAFPGVP LLQVSGPLLL VQLLETPLLC LVSYASLVAT
160 170 180 190 200
NAARLRLIAG PDKKLLEMGL RRAQGPDGGF TASIYSYLGG FDSSSNTLAG
210 220 230 240 250
QLRGVPVAGT LAHSFVTSFS GSEVPPDPML APASSEGPTV DLPARVNLWL
260 270 280 290 300
KRVCLYLGLE EQEPHPGERA AFVAYALAFP RAFQGLLDSY SVRRSGLPNF
310 320 330 340 350
LAVALALGEL GYRAVGVRLD SGDLLQQAKE IRGIFRTAGA QFQMPWLESV
360 370 380 390 400
PIAVSNNIDE SELMRLAQKG SEVNVIGIGT SVVTCPKQPS MGCVYKLVSV
410 420 430 440 450
GGQPRIKLTE DPEKQTLPGS KAAFRFLGPD GSLLLDLLQL AEEPPPKAGQ
460 470 480 490 500
ELRVWPRGTQ EPCTVKPAQV EPLLRLYLQQ GQLCEPLPSL DESRRFAQQS
510 520 530
LSLLRPAHKQ LQSPAVYPVA LSEKLRALVD SLSARGPL
Length:538
Mass (Da):58,265
Last modified:March 1, 2003 - v1
Checksum:iDFD3BC809E860A9E
GO

Sequence cautioni

The sequence BAC33575.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC33575.1 differs from that shown. Reason: Erroneous termination at position 517. Translated as Tyr.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti518 – 5181P → T in BAC33575 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY214331 mRNA. Translation: AAP69609.1.
AK033661 mRNA. Translation: BAC28414.1.
AK049157 mRNA. Translation: BAC33575.1. Sequence problems.
AK159127 mRNA. Translation: BAE34841.1.
AK170518 mRNA. Translation: BAE41854.1.
BC058800 mRNA. Translation: AAH58800.1.
CCDSiCCDS27552.1.
RefSeqiNP_766195.2. NM_172607.3.
UniGeneiMm.288368.

Genome annotation databases

EnsembliENSMUST00000023237; ENSMUSP00000023237; ENSMUSG00000022574.
GeneIDi223646.
KEGGimmu:223646.
UCSCiuc007whi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY214331 mRNA. Translation: AAP69609.1.
AK033661 mRNA. Translation: BAC28414.1.
AK049157 mRNA. Translation: BAC33575.1. Sequence problems.
AK159127 mRNA. Translation: BAE34841.1.
AK170518 mRNA. Translation: BAE41854.1.
BC058800 mRNA. Translation: AAH58800.1.
CCDSiCCDS27552.1.
RefSeqiNP_766195.2. NM_172607.3.
UniGeneiMm.288368.

3D structure databases

ProteinModelPortaliQ8CC86.
SMRiQ8CC86. Positions 16-522.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8CC86. 3 interactions.
MINTiMINT-1855495.

PTM databases

PhosphoSiteiQ8CC86.

Proteomic databases

MaxQBiQ8CC86.
PaxDbiQ8CC86.
PRIDEiQ8CC86.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023237; ENSMUSP00000023237; ENSMUSG00000022574.
GeneIDi223646.
KEGGimmu:223646.
UCSCiuc007whi.1. mouse.

Organism-specific databases

CTDi93100.
MGIiMGI:2442664. Naprt.

Phylogenomic databases

eggNOGiCOG1488.
GeneTreeiENSGT00390000002664.
HOGENOMiHOG000001111.
HOVERGENiHBG062439.
InParanoidiQ8CC86.
KOiK00763.
OMAiGDLEYLS.
OrthoDBiEOG7N63MH.
PhylomeDBiQ8CC86.
TreeFamiTF314732.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00457.
ReactomeiREACT_211619. Nicotinamide salvaging.

Miscellaneous databases

NextBioi376772.
PROiQ8CC86.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CC86.
GenevestigatoriQ8CC86.

Family and domain databases

InterProiIPR007229. Nic_PRibTrfase-Fam.
IPR006405. Nic_PRibTrfase_pncB.
IPR002638. Quinolinate_PRibosylTrfase_C.
[Graphical view]
PANTHERiPTHR11098. PTHR11098. 1 hit.
PfamiPF04095. NAPRTase. 1 hit.
[Graphical view]
PIRSFiPIRSF000484. NAPRT. 1 hit.
SUPFAMiSSF51690. SSF51690. 2 hits.
TIGRFAMsiTIGR01513. NAPRTase_put. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis and molecular evolution of the eukaryotic nicotinate phosphoribosyltransferase family."
    Huang C.-H., Peng J., Chen Y.
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Cecum.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Colon.
  4. "Elevation of cellular NAD levels by nicotinic acid and involvement of nicotinic acid phosphoribosyltransferase in human cells."
    Hara N., Yamada K., Shibata T., Osago H., Hashimoto T., Tsuchiya M.
    J. Biol. Chem. 282:24574-24582(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiPNCB_MOUSE
AccessioniPrimary (citable) accession number: Q8CC86
Secondary accession number(s): Q8C7W2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 1, 2003
Last modified: March 4, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.