Reviewed, UniProtKB/Swiss-Prot Q8BVU5 (NUDT9_MOUSE)

Names and origin

Protein names

Recommended name:
    ADP-ribose pyrophosphatase, mitochondrial
    EC=3.6.1.13
Alternative name(s):
    ADP-ribose diphosphatase
    Adenosine diphosphoribose pyrophosphatase
      Short name=ADPR-PPase
    ADP-ribose phosphohydrolase
    Nucleoside diphosphate-linked moiety X motif 9
      Short name=Nudix motif 9

Gene names

Name:

Nudt9

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

Protein attributes

Sequence length	350 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Hydrolyzes ADP-ribose (ADPR) to AMP and ribose 5'-phosphate.
Catalytic activity	ADP-ribose + H2O = AMP + D-ribose 5-phosphate.
Cofactor	Magnesium By similarity. Manganese By similarity.
Subunit structure	Monomer By similarity. Interacts with C17orf25 By similarity.
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the Nudix hydrolase family. NudF subfamily.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Magnesium Manganese
Molecular function	Hydrolase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	ADP catabolic process Inferred from direct assay. Source: MGI IDP catabolic process Inferred from direct assay. Source: MGI
Cellular component	mitochondrion Inferred from direct assay. Source: MGI
Molecular function	ADP-ribose diphosphatase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleoside-diphosphatase activity Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 46	46	Mitochondrion Potential
	Chain	47 – 350	304	ADP-ribose pyrophosphatase, mitochondrial		PRO_0000019951
Regions
	Motif	215 – 237	23	Nudix box
Amino acid modifications
	Modified residue	68	1	Phosphoserine By similarity
	Modified residue	121	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	343	1	H → R in AAH33921. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8BVU5-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: EDD9371307AB3373	FASTA	350	38,604
	10 20 30 40 50 60 MAGRSLGQAV ATVSLSVALA SVTVRSSACR AVPAPRNTFP TCGFHLNANI MSGSNGAKEN 70 80 90 100 110 120 SHNKARTSPY PGSKVERSQV PNEKVGWLVE WQDYNPVEYT AVSVLAGPQW ADPQISESNF 130 140 150 160 170 180 SPKFNEKDGH VERKSQNGLY EIENGRPRNP AGRTGLVGRG LLGRWGPNHA ADPIITRWKR 190 200 210 220 230 240 DESGNKITHP VSGKCILQFV AIKRKDCGEW AIPGGMVDPG EKISATLKRE FGEEALNSLQ 250 260 270 280 290 300 KSSAEKREIE EKLHALFSQE HLVIYKGYVD DPRNTDNAWM ETEAVNYHDE TGETMDNLTL 310 320 330 340 350 EAGDDAGKVK WVDISDQLKL YASHSQFIKL VAEKRDAHWS EDHAADSRGL

References

[1]

"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: C57BL/6J. Tissue: Head and Inner ear.

[2]

"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]. Strain: Czech II. Tissue: Mammary tumor.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK076500 mRNA. Translation: BAC36366.1. AK158058 mRNA. Translation: BAE34342.1. BC033921 mRNA. Translation: AAH33921.1.
IPI	IPI00405390.
RefSeq	NP_083070.2.
UniGene	Mm.241484
3D structure databases
HSSP	HSSP built from PDB template 1Q33 based on UniProtKB Q9BW91.
SMR	Q8BVU5. Positions 59-350.
ModBase	Search...
PTM databases
PhosphoSite	Q8BVU5.
Proteomic databases
PRIDE	Q8BVU5.
Genome annotation databases
Ensembl	ENSMUSG00000029310. Mus musculus. [Contig view]
GeneID	74167.
KEGG	mmu:74167.
NMPDR	fig|10090.3.peg.11998.
Organism-specific databases
MGI	MGI:1921417. Nudt9.
Phylogenomic databases
HOGENOM	Q8BVU5.
HOVERGEN	Q8BVU5.
OMA	Q8BVU5. QISESNF.
Enzyme and pathway databases
BRENDA	3.6.1.13. 244.
Gene expression databases
ArrayExpress	Q8BVU5.
Bgee	Q8BVU5.
GermOnline	ENSMUSG00000029310. Mus musculus.
Family and domain databases
InterPro	IPR000086. NUDIX_hydrolase_core. [Graphical view]
Gene3D	G3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.
Pfam	PF00293. NUDIX. 1 hit. [Graphical view]
PROSITE	PS00893. NUDIX. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	339972.
SOURCE	Search...

Entry information

Entry name

NUDT9_MOUSE

Accession

Primary (citable) accession number: Q8BVU5
Secondary accession number(s): Q3TZ68, Q8K1J4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	March 1, 2003
Last modified:	June 16, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)