NUD13_MOUSE
ID NUD13_MOUSE Reviewed; 352 AA.
AC Q8JZU0; Q9CXN4;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=NAD(P)H pyrophosphatase NUDT13, mitochondrial {ECO:0000305};
DE EC=3.6.1.22 {ECO:0000269|PubMed:28755312, ECO:0000269|PubMed:31101919};
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 13 {ECO:0000303|PubMed:28755312};
DE Short=Nudix motif 13 {ECO:0000303|PubMed:28755312};
DE Flags: Precursor;
GN Name=Nudt13 {ECO:0000303|PubMed:28755312, ECO:0000312|MGI:MGI:1914975};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Heart;
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).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=28755312; DOI=10.1007/s10930-017-9734-x;
RA Abdelraheim S.R., Spiller D.G., McLennan A.G.;
RT "Mouse Nudt13 is a Mitochondrial Nudix Hydrolase with NAD(P)H
RT Pyrophosphohydrolase Activity.";
RL Protein J. 36:425-432(2017).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31101919; DOI=10.1038/s41589-019-0293-7;
RA Grudzien-Nogalska E., Wu Y., Jiao X., Cui H., Mateyak M.K., Hart R.P.,
RA Tong L., Kiledjian M.;
RT "Structural and mechanistic basis of mammalian Nudt12 RNA deNADding.";
RL Nat. Chem. Biol. 15:575-582(2019).
CC -!- FUNCTION: NAD(P)H pyrophosphatase that hydrolyzes NADH into NMNH and
CC AMP, and NADPH into NMNH and 2',5'-ADP (PubMed:28755312). Has a marked
CC preference for the reduced pyridine nucleotides (PubMed:28755312). Does
CC not show activity toward NAD-capped RNAs; the NAD-cap is an atypical
CC cap present at the 5'-end of some RNAs (PubMed:31101919).
CC {ECO:0000269|PubMed:28755312, ECO:0000269|PubMed:31101919}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADH = AMP + 2 H(+) + reduced beta-nicotinamide D-
CC ribonucleotide; Xref=Rhea:RHEA:48868, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57945, ChEBI:CHEBI:90832,
CC ChEBI:CHEBI:456215; EC=3.6.1.22;
CC Evidence={ECO:0000269|PubMed:28755312};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48869;
CC Evidence={ECO:0000269|PubMed:28755312};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = AMP + beta-nicotinamide D-ribonucleotide + 2
CC H(+); Xref=Rhea:RHEA:11800, ChEBI:CHEBI:14649, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:456215;
CC EC=3.6.1.22; Evidence={ECO:0000269|PubMed:31101919};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11801;
CC Evidence={ECO:0000269|PubMed:31101919};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADPH = adenosine 3',5'-bisphosphate + 2 H(+) + reduced
CC beta-nicotinamide D-ribonucleotide; Xref=Rhea:RHEA:60820,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:90832;
CC Evidence={ECO:0000269|PubMed:31101919};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60821;
CC Evidence={ECO:0000269|PubMed:31101919};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:28755312};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:28755312};
CC Note=Divalent metal cations. Mg(2+) or Mn(2+).
CC {ECO:0000269|PubMed:28755312};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.34 mM for NADH {ECO:0000269|PubMed:28755312};
CC Note=kcat is 7 sec(-1) for NADH. {ECO:0000269|PubMed:28755312};
CC pH dependence:
CC Optimum pH is 7.8-8.2. {ECO:0000269|PubMed:28755312};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:28755312}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH37091.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB29203.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK014204; BAB29203.1; ALT_INIT; mRNA.
DR EMBL; BC037091; AAH37091.1; ALT_INIT; mRNA.
DR CCDS; CCDS36815.1; -.
DR RefSeq; NP_080617.2; NM_026341.2.
DR RefSeq; XP_006519526.1; XM_006519463.2.
DR AlphaFoldDB; Q8JZU0; -.
DR SMR; Q8JZU0; -.
DR STRING; 10090.ENSMUSP00000022343; -.
DR iPTMnet; Q8JZU0; -.
DR PhosphoSitePlus; Q8JZU0; -.
DR EPD; Q8JZU0; -.
DR MaxQB; Q8JZU0; -.
DR PaxDb; Q8JZU0; -.
DR PRIDE; Q8JZU0; -.
DR ProteomicsDB; 293808; -.
DR Antibodypedia; 29309; 73 antibodies from 20 providers.
DR DNASU; 67725; -.
DR Ensembl; ENSMUST00000022343; ENSMUSP00000022343; ENSMUSG00000021809.
DR Ensembl; ENSMUST00000223663; ENSMUSP00000153558; ENSMUSG00000021809.
DR GeneID; 67725; -.
DR KEGG; mmu:67725; -.
DR UCSC; uc007sjb.1; mouse.
DR CTD; 25961; -.
DR MGI; MGI:1914975; Nudt13.
DR VEuPathDB; HostDB:ENSMUSG00000021809; -.
DR eggNOG; KOG3084; Eukaryota.
DR GeneTree; ENSGT00940000158879; -.
DR HOGENOM; CLU_037162_0_0_1; -.
DR InParanoid; Q8JZU0; -.
DR OMA; CDMGENV; -.
DR OrthoDB; 1436400at2759; -.
DR PhylomeDB; Q8JZU0; -.
DR TreeFam; TF106352; -.
DR Reactome; R-MMU-499943; Interconversion of nucleotide di- and triphosphates.
DR BioGRID-ORCS; 67725; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Nudt13; mouse.
DR PRO; PR:Q8JZU0; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8JZU0; protein.
DR Bgee; ENSMUSG00000021809; Expressed in ascending aorta and 248 other tissues.
DR ExpressionAtlas; Q8JZU0; baseline and differential.
DR Genevisible; Q8JZU0; MM.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000210; F:NAD+ diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0035529; F:NADH pyrophosphatase activity; IDA:UniProtKB.
DR GO; GO:0006734; P:NADH metabolic process; IDA:UniProtKB.
DR GO; GO:0006742; P:NADP catabolic process; IDA:UniProtKB.
DR InterPro; IPR015375; NADH_PPase-like_N.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR015376; Znr_NADH_PPase.
DR Pfam; PF00293; NUDIX; 1.
DR Pfam; PF09296; NUDIX-like; 1.
DR Pfam; PF09297; zf-NADH-PPase; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Mitochondrion; NAD; NADP;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 21..352
FT /note="NAD(P)H pyrophosphatase NUDT13, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000057112"
FT DOMAIN 196..323
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 216..240
FT /note="Nudix box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
SQ SEQUENCE 352 AA; 39137 MW; 0FEE29EFEE3FD6C4 CRC64;
MSLYCRTFFR RKSFGCYRLL STYVTKARYL FELKEDEEAC RKAQKTGVFY LFHDLDPLLQ
ASGHRYLVPR LSRAELEGLL GKFGQDSQRI EDSVLVGCSE QQEAWFALDL GLKSASSSRA
SLPKSEMEAE LGGSFIKLRQ ALFQLNSVDS SLLFTAQALL RWHDGHQFCS KSGQPTQKNV
AGSKRVCPSS KIIYYPQMAP VVITLVSDGA RCLLARQSSF PKGLYSALAG FCDIGESVEE
TVHREVAEEV GLEVENIQYS ASQHWPFPNS SLMIACHATV KPGHTEIQVN LKELEAAAWF
SLDEVTTALR RKGSLALQPS EASPLLLPPK LAIAHHLIKK WVETRSCSSL AA
