NUDT5_MOUSE
ID NUDT5_MOUSE Reviewed; 218 AA.
AC Q9JKX6; A2ATT6; Q99KM4;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=ADP-sugar pyrophosphatase {ECO:0000250|UniProtKB:Q9UKK9};
DE EC=3.6.1.13 {ECO:0000250|UniProtKB:Q9UKK9};
DE AltName: Full=8-oxo-dGDP phosphatase {ECO:0000250|UniProtKB:Q9UKK9};
DE EC=3.6.1.58 {ECO:0000250|UniProtKB:Q9UKK9};
DE AltName: Full=Nuclear ATP-synthesis protein NUDIX5 {ECO:0000250|UniProtKB:Q9UKK9};
DE EC=2.7.7.96 {ECO:0000250|UniProtKB:Q9UKK9};
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 5 {ECO:0000305};
DE Short=Nudix motif 5 {ECO:0000305};
GN Name=Nudt5 {ECO:0000312|MGI:MGI:1858232};
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], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10722730; DOI=10.1074/jbc.275.12.8844;
RA Yang H., Slupska M.M., Wei Y.-F., Tai J.H., Luther W.M., Xia Y.-R.,
RA Shih D.M., Chiang J.-H., Baikalov C., Fitz-Gibbon S., Phan I.T., Conrad A.,
RA Miller J.H.;
RT "Cloning and characterization of a new member of the Nudix hydrolases from
RT human and mouse.";
RL J. Biol. Chem. 275:8844-8853(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [5]
RP PROTEIN SEQUENCE OF 175-180, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [8]
RP ABSENCE OF FUNCTION AS U8 SNORNA DECAPPING ENZYME, AND RNA-BINDING.
RX PubMed=21070968; DOI=10.1016/j.molcel.2010.10.010;
RA Song M.G., Li Y., Kiledjian M.;
RT "Multiple mRNA decapping enzymes in mammalian cells.";
RL Mol. Cell 40:423-432(2010).
CC -!- FUNCTION: Enzyme that can either act as an ADP-sugar pyrophosphatase in
CC absence of diphosphate or catalyze the synthesis of ATP in presence of
CC diphosphate (By similarity). In absence of diphosphate, hydrolyzes with
CC similar activities various modified nucleoside diphosphates such as
CC ADP-ribose, ADP-mannose, ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP
CC (PubMed:10722730). Can also hydrolyze other nucleotide sugars with low
CC activity (PubMed:10722730). In presence of diphosphate, mediates the
CC synthesis of ATP in the nucleus by catalyzing the conversion of ADP-
CC ribose to ATP and ribose 5-phosphate (By similarity). Nuclear ATP
CC synthesis takes place when dephosphorylated at Thr-44 (By similarity).
CC Nuclear ATP generation is required for extensive chromatin remodeling
CC events that are energy-consuming (By similarity). Does not play a role
CC in U8 snoRNA decapping activity (PubMed:21070968). Binds U8 snoRNA
CC (PubMed:21070968). {ECO:0000250|UniProtKB:Q9UKK9,
CC ECO:0000269|PubMed:10722730, ECO:0000269|PubMed:21070968}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribose 5-phosphate + H(+) = ADP-D-ribose +
CC diphosphate; Xref=Rhea:RHEA:50248, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57967,
CC ChEBI:CHEBI:78346; EC=2.7.7.96;
CC Evidence={ECO:0000250|UniProtKB:Q9UKK9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+);
CC Xref=Rhea:RHEA:10412, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57967, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215;
CC EC=3.6.1.13; Evidence={ECO:0000250|UniProtKB:Q9UKK9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8-oxo-dGDP + H2O = 8-oxo-dGMP + H(+) + phosphate;
CC Xref=Rhea:RHEA:32063, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:63224, ChEBI:CHEBI:63715; EC=3.6.1.58;
CC Evidence={ECO:0000250|UniProtKB:Q9UKK9};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9UKK9};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9UKK9};
CC -!- SUBUNIT: Homodimer. Interacts with PARG.
CC {ECO:0000250|UniProtKB:Q9UKK9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UKK9}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Most abundant in liver.
CC {ECO:0000269|PubMed:10722730}.
CC -!- PTM: Phosphorylation at Thr-44 is required for homodimer stability;
CC dephosphorylation results in destabilization of the homodimer.
CC Dephosphorylation at Thr-44 promotes the ATP-synthesis activity.
CC {ECO:0000250|UniProtKB:Q9UKK9}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; AF222786; AAF44630.1; -; mRNA.
DR EMBL; AK088222; BAC40220.1; -; mRNA.
DR EMBL; AL928924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004571; AAH04571.1; -; mRNA.
DR EMBL; BC049595; AAH49595.1; -; mRNA.
DR CCDS; CCDS15667.1; -.
DR RefSeq; NP_058614.1; NM_016918.3.
DR RefSeq; XP_006497575.1; XM_006497512.3.
DR RefSeq; XP_006497576.1; XM_006497513.3.
DR AlphaFoldDB; Q9JKX6; -.
DR SMR; Q9JKX6; -.
DR BioGRID; 207516; 5.
DR IntAct; Q9JKX6; 1.
DR STRING; 10090.ENSMUSP00000026927; -.
DR iPTMnet; Q9JKX6; -.
DR PhosphoSitePlus; Q9JKX6; -.
DR SwissPalm; Q9JKX6; -.
DR REPRODUCTION-2DPAGE; Q9JKX6; -.
DR EPD; Q9JKX6; -.
DR jPOST; Q9JKX6; -.
DR MaxQB; Q9JKX6; -.
DR PaxDb; Q9JKX6; -.
DR PeptideAtlas; Q9JKX6; -.
DR PRIDE; Q9JKX6; -.
DR ProteomicsDB; 289950; -.
DR Antibodypedia; 11248; 115 antibodies from 25 providers.
DR DNASU; 53893; -.
DR Ensembl; ENSMUST00000026927; ENSMUSP00000026927; ENSMUSG00000025817.
DR Ensembl; ENSMUST00000179748; ENSMUSP00000136233; ENSMUSG00000025817.
DR GeneID; 53893; -.
DR KEGG; mmu:53893; -.
DR UCSC; uc033hlj.1; mouse.
DR CTD; 11164; -.
DR MGI; MGI:1858232; Nudt5.
DR VEuPathDB; HostDB:ENSMUSG00000025817; -.
DR eggNOG; KOG3041; Eukaryota.
DR GeneTree; ENSGT00940000154045; -.
DR InParanoid; Q9JKX6; -.
DR OMA; CNTNLHM; -.
DR OrthoDB; 1466354at2759; -.
DR PhylomeDB; Q9JKX6; -.
DR TreeFam; TF106347; -.
DR Reactome; R-MMU-2393930; Phosphate bond hydrolysis by NUDT proteins.
DR SABIO-RK; Q9JKX6; -.
DR BioGRID-ORCS; 53893; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Nudt5; mouse.
DR PRO; PR:Q9JKX6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9JKX6; protein.
DR Bgee; ENSMUSG00000025817; Expressed in metanephric loop of Henle and 261 other tissues.
DR ExpressionAtlas; Q9JKX6; baseline and differential.
DR Genevisible; Q9JKX6; MM.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0044715; F:8-oxo-dGDP phosphatase activity; ISS:UniProtKB.
DR GO; GO:0044716; F:8-oxo-GDP phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; ISS:UniProtKB.
DR GO; GO:0019144; F:ADP-sugar diphosphatase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0017110; F:nucleoside-diphosphatase activity; IDA:MGI.
DR GO; GO:0016779; F:nucleotidyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0030515; F:snoRNA binding; IDA:UniProtKB.
DR GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0019303; P:D-ribose catabolic process; ISS:UniProtKB.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IDA:MGI.
DR GO; GO:0006753; P:nucleoside phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0009191; P:ribonucleoside diphosphate catabolic process; ISS:UniProtKB.
DR GO; GO:0019693; P:ribose phosphate metabolic process; IBA:GO_Central.
DR InterPro; IPR020476; Nudix_hydrolase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Hydrolase; Isopeptide bond;
KW Magnesium; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Transferase; Ubl conjugation.
FT CHAIN 1..218
FT /note="ADP-sugar pyrophosphatase"
FT /id="PRO_0000057049"
FT DOMAIN 56..196
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 96..117
FT /note="Nudix box"
FT BINDING 27
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT BINDING 45..46
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT BINDING 83
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT BINDING 95
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT BINDING 97
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT BINDING 111
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT BINDING 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT BINDING 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT BINDING 132
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 44
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT MOD_RES 209
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT MOD_RES 217
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT CROSSLNK 41
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT CONFLICT 103
FT /note="S -> N (in Ref. 4; AAH04571)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 218 AA; 23984 MW; E831852919F85DFE CRC64;
METRESTESS PGKHLVTSEE LISEGKWVKF EKTTYMDPTG KTRTWETVKL TTRKGKSADA
VSVIPVLQRT LHHECVILVK QFRPPMGSYC LEFPAGFIED GESPEAAALR ELEEETGYKG
EVAECSPAVC MDPGLSNCTT HVVTVTINGD DAGNVRPKPK PGDGEFMEVI SLPKNDLLTR
LDALGAEQHL TVDAKVYAYG LALKHANSKP FEVPFLKF
