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   27-MAR-2024, entry version 152.
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; 10090-ENSMUSP00000023237; -.
DR   PeptideAtlas; Q8CC86; -.
DR   ProteomicsDB; 289703; -.
DR   Pumba; Q8CC86; -.
DR   Antibodypedia; 14617; 218 antibodies from 27 providers.
DR   DNASU; 223646; -.
DR   Ensembl; ENSMUST00000023237.8; ENSMUSP00000023237.7; ENSMUSG00000022574.8.
DR   GeneID; 223646; -.
DR   KEGG; mmu:223646; -.
DR   UCSC; uc007whi.1; mouse.
DR   AGR; MGI:2442664; -.
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; NPHIYKV; -.
DR   OrthoDB; 1333333at2759; -.
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 76 CRISPR screens.
DR   PRO; PR:Q8CC86; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q8CC86; Protein.
DR   Bgee; ENSMUSG00000022574; Expressed in duodenum and 133 other cell types or tissues.
DR   ExpressionAtlas; Q8CC86; baseline and differential.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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   CDD; cd01570; NAPRTase_A; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 2.
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   NCBIfam; TIGR01513; NAPRTase_put; 1.
DR   PANTHER; PTHR11098; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11098:SF1; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF17956; NAPRTase_C; 1.
DR   Pfam; PF17767; NAPRTase_N; 1.
DR   PIRSF; PIRSF000484; NAPRT; 1.
DR   SUPFAM; SSF51690; Nicotinate/Quinolinate PRTase C-terminal domain-like; 1.
DR   SUPFAM; SSF54675; Nicotinate/Quinolinate PRTase N-terminal domain-like; 1.
DR   Genevisible; Q8CC86; MM.
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
//