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Q8BVU5 (NUDT9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ADP-ribose pyrophosphatase, mitochondrial
EC=3.6.1.13
Alternative name(s):
ADP-ribose diphosphatase
ADP-ribose phosphohydrolase
Adenosine diphosphoribose pyrophosphatase
Short name=ADPR-PPase
Nucleoside diphosphate-linked moiety X motif 9
Short name=Nudix motif 9
Gene names
Name:Nudt9
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Contains 1 nudix hydrolase domain.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandMagnesium
Manganese
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processADP catabolic process

Inferred from direct assay. Source: MGI

IDP catabolic process

Inferred from direct assay. Source: MGI

   Cellular componentmitochondrion

Inferred from direct assay. Source: MGI

   Molecular functionADP-ribose diphosphatase activity

Inferred from electronic annotation. Source: EC

adenosine-diphosphatase activity

Inferred from direct assay. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4646Mitochondrion Potential
Chain47 – 350304ADP-ribose pyrophosphatase, mitochondrial
PRO_0000019951

Regions

Domain178 – 334157Nudix hydrolase
Motif215 – 23723Nudix box

Amino acid modifications

Modified residue681Phosphoserine By similarity
Modified residue1211Phosphoserine By similarity

Experimental info

Sequence conflict3431H → R in AAH33921. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8BVU5 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: EDD9371307AB3373

FASTA35038,604
        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

« Hide

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. expand/collapse author list , 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]"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. expand/collapse author list , 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.
[3]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK076500 mRNA. Translation: BAC36366.1.
AK158058 mRNA. Translation: BAE34342.1.
AL714024 Genomic DNA. Translation: CAM13353.1.
BC033921 mRNA. Translation: AAH33921.1.
IPIIPI00405390.
RefSeqNP_083070.2. NM_028794.3.
UniGeneMm.241484.

3D structure databases

ProteinModelPortalQ8BVU5.
SMRQ8BVU5. Positions 59-350.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8BVU5.

PTM databases

PhosphoSiteQ8BVU5.

Proteomic databases

PRIDEQ8BVU5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031250; ENSMUSP00000031250; ENSMUSG00000029310.
GeneID74167.
KEGGmmu:74167.
NMPDRfig|10090.3.peg.11998.
UCSCuc008yka.1. mouse.

Organism-specific databases

CTD53343.
MGIMGI:1921417. Nudt9.

Phylogenomic databases

GeneTreeENSGT00390000017405.
HOGENOMHBG379993.
HOVERGENHBG052693.
InParanoidQ8BVU5.
OMAQISESNF.
OrthoDBEOG4VHK76.
PhylomeDBQ8BVU5.

Gene expression databases

ArrayExpressQ8BVU5.
BgeeQ8BVU5.
GenevestigatorQ8BVU5.
GermOnlineENSMUSG00000029310. Mus musculus.

Family and domain databases

InterProIPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
Gene3DG3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.
KOK13988.
PfamPF00293. NUDIX. 1 hit.
[Graphical view]
SUPFAMSSF55811. NUDIX_hydrolase. 1 hit.
PROSITEPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio339972.
SOURCESearch...

Entry information

Entry nameNUDT9_MOUSE
AccessionPrimary (citable) accession number: Q8BVU5
Secondary accession number(s): A2AH31, Q3TZ68, Q8K1J4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: March 1, 2003
Last modified: November 16, 2011
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents