Q9JKX6 (NUDT5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ADP-sugar pyrophosphatase
EC=3.6.1.-
EC=3.6.1.13

Alternative name(s):
Nucleoside diphosphate-linked moiety X motif 5
Short name=Nudix motif 5

Gene names

Name:

Nudt5

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	218 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes with similar activities ADP-ribose and ADP-mannose. Can also hydrolyzes ADP-glucose (40% of ADP-ribose activity) and other nucleotide sugars with low activity (10%).
Catalytic activity	ADP-ribose + H2O = AMP + D-ribose 5-phosphate. ADP-sugar + H2O = AMP + alpha-D-aldose 1-phosphate.
Cofactor	Binds 3 magnesium ions per subunit By similarity.
Tissue specificity	Widely expressed. Most abundant in liver.
Sequence similarities	Belongs to the Nudix hydrolase family. Contains 1 nudix hydrolase domain.

Ontologies

Keywords
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	ribonucleoside diphosphate catabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ADP-ribose diphosphatase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from sequence or structural similarity. Source: UniProtKB nucleoside-diphosphatase activity Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 218	218	ADP-sugar pyrophosphatase		PRO_0000057049
Regions
	Domain	56 – 196	141	Nudix hydrolase
	Region	45 – 46	2	Substrate binding; shared with dimeric partner
	Motif	96 – 117	22	Nudix box
Sites
	Metal binding	95	1	Magnesium 1; via carbonyl oxygen By similarity
	Metal binding	111	1	Magnesium 2 By similarity
	Metal binding	111	1	Magnesium 3 By similarity
	Metal binding	115	1	Magnesium 1 By similarity
	Metal binding	115	1	Magnesium 3 By similarity
	Metal binding	165	1	Magnesium 3 By similarity
	Binding site	27	1	Substrate By similarity
	Binding site	83	1	Substrate By similarity
	Binding site	97	1	Substrate; via amide nitrogen By similarity
	Binding site	132	1	Substrate By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	9	1	Phosphoserine Ref.6
	Modified residue	10	1	Phosphoserine Ref.7
	Modified residue	41	1	N6-acetyllysine By similarity
	Modified residue	209	1	N6-acetyllysine By similarity
	Modified residue	217	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	103	1	S → N in AAH04571. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9JKX6 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: E831852919F85DFE	FASTA	218	23,984
	10 20 30 40 50 60 METRESTESS PGKHLVTSEE LISEGKWVKF EKTTYMDPTG KTRTWETVKL TTRKGKSADA 70 80 90 100 110 120 VSVIPVLQRT LHHECVILVK QFRPPMGSYC LEFPAGFIED GESPEAAALR ELEEETGYKG 130 140 150 160 170 180 EVAECSPAVC MDPGLSNCTT HVVTVTINGD DAGNVRPKPK PGDGEFMEVI SLPKNDLLTR 190 200 210 LDALGAEQHL TVDAKVYAYG LALKHANSKP FEVPFLKF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a new member of the Nudix hydrolases from human and mouse." 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. J. Biol. Chem. 275:8844-8853(2000) [PubMed: 10722730] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[2]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: NOD. Tissue: Thymus.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." 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. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[5]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 175-180, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[6]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF222786 mRNA. Translation: AAF44630.1. AK088222 mRNA. Translation: BAC40220.1. AL928924 Genomic DNA. Translation: CAM20348.1. BC004571 mRNA. Translation: AAH04571.1. BC049595 mRNA. Translation: AAH49595.1.
IPI	IPI00123572.
RefSeq	NP_058614.1. NM_016918.3.
UniGene	Mm.251904.
3D structure databases
ProteinModelPortal	Q9JKX6.
SMR	Q9JKX6. Positions 12-207.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9JKX6.
PTM databases
PhosphoSite	Q9JKX6.
2D gel databases
REPRODUCTION-2DPAGE	Q9JKX6.
Proteomic databases
PRIDE	Q9JKX6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000026927; ENSMUSP00000026927; ENSMUSG00000025817.
GeneID	53893.
KEGG	mmu:53893.
UCSC	uc008ifv.1. mouse.
Organism-specific databases
CTD	11164.
MGI	MGI:1858232. Nudt5.
Phylogenomic databases
GeneTree	ENSGT00390000006280.
HOGENOM	HBG446368.
HOVERGEN	HBG052691.
InParanoid	Q9JKX6.
OMA	WISFKEI.
OrthoDB	EOG46Q6TG.
PhylomeDB	Q9JKX6.
Gene expression databases
ArrayExpress	Q9JKX6.
Bgee	Q9JKX6.
Genevestigator	Q9JKX6.
GermOnline	ENSMUSG00000025817. Mus musculus.
Family and domain databases
InterPro	IPR020476. Nudix_hydrolase. IPR020084. NUDIX_hydrolase_CS. IPR000086. NUDIX_hydrolase_dom. IPR015797. NUDIX_hydrolase_dom-like. [Graphical view]
Gene3D	G3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.
KO	K13987.
Pfam	PF00293. NUDIX. 1 hit. [Graphical view]
PRINTS	PR00502. NUDIXFAMILY.
SUPFAM	SSF55811. NUDIX_hydrolase. 1 hit.
PROSITE	PS51462. NUDIX. 1 hit. PS00893. NUDIX_BOX. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	310787.
PMAP-CutDB	Q9JKX6.
SOURCE	Search...

Entry information

Entry name

NUDT5_MOUSE

Accession

Primary (citable) accession number: Q9JKX6
Secondary accession number(s): A2ATT6, Q99KM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2004
Last sequence update:	October 1, 2000
Last modified:	November 16, 2011
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program