PNCB_MOUSE
ID PNCB_MOUSE Reviewed; 538 AA.
AC Q8CC86; Q8C7W2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Nicotinate phosphoribosyltransferase;
DE Short=NAPRTase;
DE EC=6.3.4.21 {ECO:0000250|UniProtKB:Q6XQN6};
DE AltName: Full=Nicotinate phosphoribosyltransferase domain-containing protein 1;
GN Name=Naprt; Synonyms=Naprt1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Huang C.-H., Peng J., Chen Y.;
RT "Sequence analysis and molecular evolution of the eukaryotic nicotinate
RT phosphoribosyltransferase family.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cecum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=17604275; DOI=10.1074/jbc.m610357200;
RA Hara N., Yamada K., Shibata T., Osago H., Hashimoto T., Tsuchiya M.;
RT "Elevation of cellular NAD levels by nicotinic acid and involvement of
RT nicotinic acid phosphoribosyltransferase in human cells.";
RL J. Biol. Chem. 282:24574-24582(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
RC Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the first step in the biosynthesis of NAD from
CC nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-
CC ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate.
CC Helps prevent cellular oxidative stress via its role in NAD
CC biosynthesis. {ECO:0000250|UniProtKB:Q6XQN6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O +
CC nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide +
CC phosphate; Xref=Rhea:RHEA:36163, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32544, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57502, ChEBI:CHEBI:58017,
CC ChEBI:CHEBI:456216; EC=6.3.4.21;
CC Evidence={ECO:0000250|UniProtKB:Q6XQN6};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q6XQN6};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q6XQN6};
CC Note=Activity is highest with Mn(2+). {ECO:0000250|UniProtKB:Q6XQN6};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from nicotinate: step 1/1.
CC {ECO:0000250|UniProtKB:Q6XQN6}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q6XQN6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q6XQN6}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in the small intestine, liver
CC and kidney. {ECO:0000269|PubMed:17604275}.
CC -!- PTM: Transiently phosphorylated on a His residue during the reaction
CC cycle. Phosphorylation strongly increases the affinity for substrates
CC and increases the rate of nicotinate D-ribonucleotide production.
CC Dephosphorylation regenerates the low-affinity form of the enzyme,
CC leading to product release. {ECO:0000250|UniProtKB:P22253}.
CC -!- SIMILARITY: Belongs to the NAPRTase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC33575.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC33575.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY214331; AAP69609.1; -; mRNA.
DR EMBL; AK033661; BAC28414.1; -; mRNA.
DR EMBL; AK049157; BAC33575.1; ALT_SEQ; mRNA.
DR EMBL; AK159127; BAE34841.1; -; mRNA.
DR EMBL; AK170518; BAE41854.1; -; mRNA.
DR EMBL; BC058800; AAH58800.1; -; mRNA.
DR CCDS; CCDS27552.1; -.
DR RefSeq; NP_766195.2; NM_172607.3.
DR AlphaFoldDB; Q8CC86; -.
DR SMR; Q8CC86; -.
DR BioGRID; 230165; 3.
DR STRING; 10090.ENSMUSP00000023237; -.
DR iPTMnet; Q8CC86; -.
DR PhosphoSitePlus; Q8CC86; -.
DR SwissPalm; Q8CC86; -.
DR EPD; Q8CC86; -.
DR jPOST; Q8CC86; -.
DR MaxQB; Q8CC86; -.
DR PaxDb; Q8CC86; -.
DR PeptideAtlas; Q8CC86; -.
DR PRIDE; Q8CC86; -.
DR ProteomicsDB; 289703; -.
DR Antibodypedia; 14617; 195 antibodies from 27 providers.
DR DNASU; 223646; -.
DR Ensembl; ENSMUST00000023237; ENSMUSP00000023237; ENSMUSG00000022574.
DR GeneID; 223646; -.
DR KEGG; mmu:223646; -.
DR UCSC; uc007whi.1; mouse.
DR CTD; 93100; -.
DR MGI; MGI:2442664; Naprt.
DR VEuPathDB; HostDB:ENSMUSG00000022574; -.
DR eggNOG; KOG2511; Eukaryota.
DR GeneTree; ENSGT00940000153456; -.
DR HOGENOM; CLU_025154_1_0_1; -.
DR InParanoid; Q8CC86; -.
DR OMA; VYFPGSP; -.
DR OrthoDB; 577034at2759; -.
DR PhylomeDB; Q8CC86; -.
DR TreeFam; TF314732; -.
DR BRENDA; 6.3.4.21; 3474.
DR Reactome; R-MMU-197264; Nicotinamide salvaging.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR UniPathway; UPA00253; UER00457.
DR BioGRID-ORCS; 223646; 4 hits in 71 CRISPR screens.
DR PRO; PR:Q8CC86; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8CC86; protein.
DR Bgee; ENSMUSG00000022574; Expressed in duodenum and 131 other tissues.
DR ExpressionAtlas; Q8CC86; baseline and differential.
DR Genevisible; Q8CC86; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR GO; GO:0009435; P:NAD biosynthetic process; ISO:MGI.
DR GO; GO:0034355; P:NAD salvage; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR041619; NAPRTase_C.
DR InterPro; IPR040727; NAPRTase_N.
DR InterPro; IPR007229; Nic_PRibTrfase-Fam.
DR InterPro; IPR006405; Nic_PRibTrfase_pncB.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR PANTHER; PTHR11098; PTHR11098; 1.
DR Pfam; PF17956; NAPRTase_C; 1.
DR Pfam; PF17767; NAPRTase_N; 1.
DR PIRSF; PIRSF000484; NAPRT; 1.
DR SUPFAM; SSF51690; SSF51690; 1.
DR TIGRFAMs; TIGR01513; NAPRTase_put; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Ligase; Magnesium; Manganese; Metal-binding; Phosphoprotein;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..538
FT /note="Nicotinate phosphoribosyltransferase"
FT /id="PRO_0000315682"
FT BINDING 21
FT /ligand="nicotinate"
FT /ligand_id="ChEBI:CHEBI:32544"
FT /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT BINDING 210
FT /ligand="nicotinate"
FT /ligand_id="ChEBI:CHEBI:32544"
FT /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT BINDING 318
FT /ligand="nicotinate"
FT /ligand_id="ChEBI:CHEBI:32544"
FT /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT BINDING 380
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT MOD_RES 213
FT /note="Phosphohistidine"
FT /evidence="ECO:0000250|UniProtKB:P22253"
FT CONFLICT 518
FT /note="P -> T (in Ref. 2; BAC33575)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 538 AA; 58265 MW; DFD3BC809E860A9E CRC64;
MEMELDSEGR MVVRPLLTDL YQATMALGYW RAGRACEAAE FELFFRHCPF GGSFALSAGL
QDCMRFLRAF RLRDADVQFL ASVLPPDTDP AFFEHLRALD CSGVTVRALP EGSLAFPGVP
LLQVSGPLLL VQLLETPLLC LVSYASLVAT NAARLRLIAG PDKKLLEMGL RRAQGPDGGF
TASIYSYLGG FDSSSNTLAG QLRGVPVAGT LAHSFVTSFS GSEVPPDPML APASSEGPTV
DLPARVNLWL KRVCLYLGLE EQEPHPGERA AFVAYALAFP RAFQGLLDSY SVRRSGLPNF
LAVALALGEL GYRAVGVRLD SGDLLQQAKE IRGIFRTAGA QFQMPWLESV PIAVSNNIDE
SELMRLAQKG SEVNVIGIGT SVVTCPKQPS MGCVYKLVSV GGQPRIKLTE DPEKQTLPGS
KAAFRFLGPD GSLLLDLLQL AEEPPPKAGQ ELRVWPRGTQ EPCTVKPAQV EPLLRLYLQQ
GQLCEPLPSL DESRRFAQQS LSLLRPAHKQ LQSPAVYPVA LSEKLRALVD SLSARGPL
