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Reviewed, UniProtKB/Swiss-Prot Q8CC86 (PNCB_MOUSE)

Last modified February 9, 2010. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Nicotinate phosphoribosyltransferase
      Short name=NAPRTase
    EC=2.4.2.11
Alternative name(s):
    Nicotinate phosphoribosyltransferase domain-containing protein 1
Gene names
Name: Naprt1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length538 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

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.

Catalytic activity

Nicotinate D-ribonucleotide + diphosphate = nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate.

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1.

Subcellular location

Cytoplasm › cytosol By similarity.

Tissue specificity

Abundantly expressed in the small intestine, liver and kidney. Ref.4

Sequence similarities

Belongs to the NAPRTase family.

Sequence caution

The sequence BAC33575.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAC33575.1 differs from that shown. Reason: Erroneous termination at position 517. Translated as Tyr.

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Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentCytoplasm
   Molecular functionGlycosyltransferase
Transferase
Gene Ontology (GO)
   Biological processresponse to oxidative stress

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentcytosol

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionnicotinate phosphoribosyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 538538Nicotinate phosphoribosyltransferase
PRO_0000315682

Experimental info

Sequence conflict5181P → T in BAC33575. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q8CC86-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: DFD3BC809E860A9E

FASTA53858,265
        10         20         30         40         50         60 
MEMELDSEGR MVVRPLLTDL YQATMALGYW RAGRACEAAE FELFFRHCPF GGSFALSAGL 

        70         80         90        100        110        120 
QDCMRFLRAF RLRDADVQFL ASVLPPDTDP AFFEHLRALD CSGVTVRALP EGSLAFPGVP 

       130        140        150        160        170        180 
LLQVSGPLLL VQLLETPLLC LVSYASLVAT NAARLRLIAG PDKKLLEMGL RRAQGPDGGF 

       190        200        210        220        230        240 
TASIYSYLGG FDSSSNTLAG QLRGVPVAGT LAHSFVTSFS GSEVPPDPML APASSEGPTV 

       250        260        270        280        290        300 
DLPARVNLWL KRVCLYLGLE EQEPHPGERA AFVAYALAFP RAFQGLLDSY SVRRSGLPNF 

       310        320        330        340        350        360 
LAVALALGEL GYRAVGVRLD SGDLLQQAKE IRGIFRTAGA QFQMPWLESV PIAVSNNIDE 

       370        380        390        400        410        420 
SELMRLAQKG SEVNVIGIGT SVVTCPKQPS MGCVYKLVSV GGQPRIKLTE DPEKQTLPGS 

       430        440        450        460        470        480 
KAAFRFLGPD GSLLLDLLQL AEEPPPKAGQ ELRVWPRGTQ EPCTVKPAQV EPLLRLYLQQ 

       490        500        510        520        530 
GQLCEPLPSL DESRRFAQQS LSLLRPAHKQ LQSPAVYPVA LSEKLRALVD SLSARGPL

« Hide

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References

« Hide 'large scale' references
[1]"Sequence analysis and molecular evolution of the eukaryotic nicotinate phosphoribosyltranferase 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. expand/collapse author list , 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: 16141072] [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: 15489334] [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: 17604275] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00228491.
RefSeqNP_766195.2.
UniGeneMm.288368

3D structure databases

HSSPHSSP built from PDB template 2F7F based on UniProtKB Q830Y8.
SMRQ8CC86. Positions 15-533.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8CC86.

PTM databases

PhosphoSiteQ8CC86.

Proteomic databases

PRIDEQ8CC86.

Genome annotation databases

EnsemblENSMUST00000023237; ENSMUSP00000023237; ENSMUSG00000022574; Mus musculus. [Genome view]
GeneID223646.
KEGGmmu:223646.
NMPDRfig|10090.3.peg.30095.
UCSCuc007whi.1. mouse.

Organism-specific databases

CTD223646.
MGIMGI:2442664. Naprt1.

Phylogenomic databases

eggNOGroNOG15279.
HOGENOMHBG292386.
HOVERGENQ8CC86.
InParanoidQ8CC86.
OMAFQTLVAT.
OrthoDBEOG9TTK3W.
PhylomeDBQ8CC86.

Enzyme and pathway databases

BRENDA2.4.2.11. 244.

Gene expression databases

ArrayExpressQ8CC86.
BgeeQ8CC86.
GenevestigatorQ8CC86.

Family and domain databases

InterProIPR015977. Nic_PRibTrfase-like.
IPR007229. Nic_PRibTrfase-rel.
IPR006405. Nic_PRibTrfase_put.
[Graphical view]
PANTHERPTHR11098:SF1. NAPRTase. 1 hit.
PfamPF04095. NAPRTase. 1 hit.
[Graphical view]
PIRSFPIRSF000484. NAPRT. 1 hit.
TIGRFAMsTIGR01513. NAPRTase_put. 1 hit.
ProtoNetSearch...

Other Resources

NextBio376772.
SOURCESearch...

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Entry information

Entry namePNCB_MOUSE
AccessionPrimary (citable) accession number: Q8CC86
Secondary accession number(s): Q8C7W2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 1, 2003
Last modified: February 9, 2010
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents