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ADP-sugar pyrophosphatase (EC 3.6.1.13) (8-oxo-dGDP phosphatase) (EC 3.6.1.58) (Nuclear ATP-synthesis protein NUDIX5) (EC 2.7.7.96) (Nucleoside diphosphate-linked moiety X motif 5) (Nudix motif 5)

 NUDT5_MOUSE             Reviewed;         218 AA.
Q9JKX6; A2ATT6; Q99KM4;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
28-FEB-2018, entry version 130.
RecName: Full=ADP-sugar pyrophosphatase {ECO:0000250|UniProtKB:Q9UKK9};
EC=3.6.1.13 {ECO:0000250|UniProtKB:Q9UKK9};
AltName: Full=8-oxo-dGDP phosphatase {ECO:0000250|UniProtKB:Q9UKK9};
EC=3.6.1.58 {ECO:0000250|UniProtKB:Q9UKK9};
AltName: Full=Nuclear ATP-synthesis protein NUDIX5 {ECO:0000250|UniProtKB:Q9UKK9};
EC=2.7.7.96 {ECO:0000250|UniProtKB:Q9UKK9};
AltName: Full=Nucleoside diphosphate-linked moiety X motif 5 {ECO:0000305};
Short=Nudix motif 5 {ECO:0000305};
Name=Nudt5 {ECO:0000312|MGI:MGI:1858232};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
PubMed=10722730; DOI=10.1074/jbc.275.12.8844;
Yang H., Slupska M.M., Wei Y.-F., Tai J.H., Luther W.M., Xia Y.-R.,
Shih D.M., Chiang J.-H., Baikalov C., Fitz-Gibbon S., Phan I.T.,
Conrad A., Miller J.H.;
"Cloning and characterization of a new member of the Nudix hydrolases
from human and mouse.";
J. Biol. Chem. 275:8844-8853(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NOD; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
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., 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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 175-180, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
FUNCTION, AND RNA-BINDING.
PubMed=21070968; DOI=10.1016/j.molcel.2010.10.010;
Song M.G., Li Y., Kiledjian M.;
"Multiple mRNA decapping enzymes in mammalian cells.";
Mol. Cell 40:423-432(2010).
-!- FUNCTION: Enzyme that can either act as an ADP-sugar
pyrophosphatase in absence of diphosphate or catalyze the
synthesis of ATP in presence of diphosphate (By similarity). In
absence of diphosphate, hydrolyzes with similar activities various
modified nucleoside diphosphates such as ADP-ribose, ADP-mannose,
ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP (PubMed:10722730). Can also
hydrolyze other nucleotide sugars with low activity
(PubMed:10722730). In presence of diphosphate, mediates the
synthesis of ATP in the nucleus by catalyzing the conversion of
ADP-ribose to ATP and ribose 5-phosphate (By similarity). Nuclear
ATP synthesis takes place when dephosphorylated at Thr-44 (By
similarity). Nuclear ATP generation is required for extensive
chromatin remodeling events that are energy-consuming (By
similarity). Does not play a role in U8 snoRNA decapping activity
(PubMed:21070968). Binds U8 snoRNA (PubMed:21070968).
{ECO:0000250|UniProtKB:Q9UKK9, ECO:0000269|PubMed:10722730,
ECO:0000269|PubMed:21070968}.
-!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = diphosphate +
ADP-D-ribose. {ECO:0000250|UniProtKB:Q9UKK9}.
-!- CATALYTIC ACTIVITY: ADP-D-ribose + H(2)O = AMP + D-ribose 5-
phosphate. {ECO:0000250|UniProtKB:Q9UKK9}.
-!- CATALYTIC ACTIVITY: 8-oxo-dGDP + H(2)O = 8-oxo-dGMP + phosphate.
{ECO:0000250|UniProtKB:Q9UKK9}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q9UKK9};
Note=Binds 3 Mg(2+) ions per subunit.
{ECO:0000250|UniProtKB:Q9UKK9};
-!- SUBUNIT: Homodimer. Interacts with PARG.
{ECO:0000250|UniProtKB:Q9UKK9}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UKK9}.
-!- TISSUE SPECIFICITY: Widely expressed. Most abundant in liver.
{ECO:0000269|PubMed:10722730}.
-!- PTM: Phosphorylation at Thr-44 is required for homodimer
stability; dephosphorylation results in destabilization of the
homodimer. Dephosphorylation at Thr-44 promotes the ATP-synthesis
activity. {ECO:0000250|UniProtKB:Q9UKK9}.
-!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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EMBL; AF222786; AAF44630.1; -; mRNA.
EMBL; AK088222; BAC40220.1; -; mRNA.
EMBL; AL928924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC004571; AAH04571.1; -; mRNA.
EMBL; BC049595; AAH49595.1; -; mRNA.
CCDS; CCDS15667.1; -.
RefSeq; NP_058614.1; NM_016918.3.
RefSeq; XP_006497575.1; XM_006497512.3.
RefSeq; XP_006497576.1; XM_006497513.3.
UniGene; Mm.251904; -.
ProteinModelPortal; Q9JKX6; -.
SMR; Q9JKX6; -.
BioGrid; 207516; 2.
IntAct; Q9JKX6; 2.
MINT; Q9JKX6; -.
STRING; 10090.ENSMUSP00000026927; -.
iPTMnet; Q9JKX6; -.
PhosphoSitePlus; Q9JKX6; -.
SwissPalm; Q9JKX6; -.
REPRODUCTION-2DPAGE; Q9JKX6; -.
EPD; Q9JKX6; -.
MaxQB; Q9JKX6; -.
PaxDb; Q9JKX6; -.
PeptideAtlas; Q9JKX6; -.
PRIDE; Q9JKX6; -.
DNASU; 53893; -.
Ensembl; ENSMUST00000026927; ENSMUSP00000026927; ENSMUSG00000025817.
Ensembl; ENSMUST00000179748; ENSMUSP00000136233; ENSMUSG00000025817.
GeneID; 53893; -.
KEGG; mmu:53893; -.
UCSC; uc033hlj.1; mouse.
CTD; 11164; -.
MGI; MGI:1858232; Nudt5.
eggNOG; KOG3041; Eukaryota.
eggNOG; COG0494; LUCA.
GeneTree; ENSGT00390000006280; -.
HOGENOM; HOG000174302; -.
HOVERGEN; HBG052691; -.
InParanoid; Q9JKX6; -.
KO; K13987; -.
OMA; RTLHYDC; -.
OrthoDB; EOG091G0LL6; -.
PhylomeDB; Q9JKX6; -.
TreeFam; TF106347; -.
Reactome; R-MMU-2393930; Phosphate bond hydrolysis by NUDT proteins.
SABIO-RK; Q9JKX6; -.
PMAP-CutDB; Q9JKX6; -.
PRO; PR:Q9JKX6; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000025817; -.
ExpressionAtlas; Q9JKX6; baseline and differential.
Genevisible; Q9JKX6; MM.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0044715; F:8-oxo-dGDP phosphatase activity; ISS:UniProtKB.
GO; GO:0047631; F:ADP-ribose diphosphatase activity; ISS:UniProtKB.
GO; GO:0019144; F:ADP-sugar diphosphatase activity; ISS:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
GO; GO:0017110; F:nucleoside-diphosphatase activity; IDA:MGI.
GO; GO:0016779; F:nucleotidyltransferase activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0030515; F:snoRNA binding; IDA:UniProtKB.
GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; ISO:MGI.
GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
GO; GO:0019303; P:D-ribose catabolic process; ISS:UniProtKB.
GO; GO:0006139; P:nucleobase-containing compound metabolic process; IDA:MGI.
GO; GO:0009191; P:ribonucleoside diphosphate catabolic process; ISS:UniProtKB.
InterPro; IPR020476; Nudix_hydrolase.
InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
InterPro; IPR020084; NUDIX_hydrolase_CS.
InterPro; IPR000086; NUDIX_hydrolase_dom.
Pfam; PF00293; NUDIX; 1.
PRINTS; PR00502; NUDIXFAMILY.
SUPFAM; SSF55811; SSF55811; 1.
PROSITE; PS51462; NUDIX; 1.
PROSITE; PS00893; NUDIX_BOX; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Direct protein sequencing; Hydrolase;
Isopeptide bond; Magnesium; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; RNA-binding; Transferase; Ubl conjugation.
CHAIN 1 218 ADP-sugar pyrophosphatase.
/FTId=PRO_0000057049.
DOMAIN 56 196 Nudix hydrolase. {ECO:0000255|PROSITE-
ProRule:PRU00794}.
REGION 45 46 Substrate binding; shared with dimeric
partner.
MOTIF 96 117 Nudix box.
METAL 95 95 Magnesium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q9UKK9}.
METAL 111 111 Magnesium 2.
{ECO:0000250|UniProtKB:Q9UKK9}.
METAL 111 111 Magnesium 3.
{ECO:0000250|UniProtKB:Q9UKK9}.
METAL 115 115 Magnesium 1.
{ECO:0000250|UniProtKB:Q9UKK9}.
METAL 115 115 Magnesium 3.
{ECO:0000250|UniProtKB:Q9UKK9}.
METAL 165 165 Magnesium 3.
{ECO:0000250|UniProtKB:Q9UKK9}.
BINDING 27 27 Substrate.
{ECO:0000250|UniProtKB:Q9UKK9}.
BINDING 83 83 Substrate.
{ECO:0000250|UniProtKB:Q9UKK9}.
BINDING 97 97 Substrate; via amide nitrogen.
{ECO:0000250}.
BINDING 132 132 Substrate.
{ECO:0000250|UniProtKB:Q9UKK9}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q9UKK9}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000244|PubMed:19131326}.
MOD_RES 44 44 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9UKK9}.
MOD_RES 209 209 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9UKK9}.
MOD_RES 217 217 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9UKK9}.
CROSSLNK 41 41 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9UKK9}.
CONFLICT 103 103 S -> N (in Ref. 4; AAH04571).
{ECO:0000305}.
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


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