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Q8R2U6 (NUDT4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Diphosphoinositol polyphosphate phosphohydrolase 2
Short name=DIPP-2
EC=3.6.1.52
Alternative name(s):
Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 2
EC=3.6.1.-
Nucleoside diphosphate-linked moiety X motif 4
Short name=Nudix motif 4
Gene names
Name:Nudt4
Synonyms:Dipp2
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 length179 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), PP-InsP4 and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphate Ap6A, but not Ap5A. The major reaction products are ADP and p4a from Ap6A. Also able to hydrolyze 5-phosphoribose 1-diphosphate By similarity.

Catalytic activity

Diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.

Cofactor

Binds 3 magnesium or manganese ions per subunit By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the Nudix hydrolase family. DIPP subfamily.

Contains 1 nudix hydrolase domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMagnesium
Manganese
Metal-binding
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondiphosphoinositol-polyphosphate diphosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 179179Diphosphoinositol polyphosphate phosphohydrolase 2
PRO_0000057059

Regions

Domain17 – 143127Nudix hydrolase
Region17 – 193Substrate binding By similarity
Region88 – 903Substrate binding By similarity
Motif50 – 7122Nudix box

Sites

Active site681Proton acceptor By similarity
Metal binding491Magnesium 1; via carbonyl oxygen By similarity
Metal binding651Magnesium 2 By similarity
Metal binding651Magnesium 3 By similarity
Metal binding691Magnesium 1 By similarity
Binding site91Substrate By similarity
Binding site401Substrate By similarity

Experimental info

Sequence conflict691E → Q in BAC33229. Ref.1
Sequence conflict1681A → C in BAB30582. Ref.1

Secondary structure

1 ..................... 179
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8R2U6 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 05A78EBBA8256B89

FASTA17920,156
        10         20         30         40         50         60 
MKFKPNQTRT YDREGFKKRA ACLCFRSEQE DEVLLVSSSR YPDQWIVPGG GMEPEEEPGG 

        70         80         90        100        110        120 
AAVREVYEEA GVKGKLGRLL GIFENQDRKH RTYVYVLTVT EILEDWEDSV NIGRKREWFK 

       130        140        150        160        170 
VEDAIKVLQC HKPVHAEYLE KLKLGCSPTN GNSSVPSLPD NNALFVTAAP PSGVPSSIR

« Hide

References

« Hide 'large scale' 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 Testis.
[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.
[3]"Crystal structure of MS0616."
RIKEN structural genomics initiative (RSGI)
Submitted (JAN-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 8-145.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK017075 mRNA. Translation: BAB30582.1.
AK048062 mRNA. Translation: BAC33229.1.
BC027209 mRNA. Translation: AAH27209.1.
IPIIPI00854941.
RefSeqNP_081998.3. NM_027722.4.
UniGeneMm.24397.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DUKX-ray2.62A/B8-145[»]
ProteinModelPortalQ8R2U6.
SMRQ8R2U6. Positions 8-145.
ModBaseSearch...

Proteomic databases

PRIDEQ8R2U6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020217; ENSMUSP00000020217; ENSMUSG00000020029.
GeneID71207.
KEGGmmu:71207.

Organism-specific databases

CTD11163.
MGIMGI:1918457. Nudt4.

Phylogenomic databases

GeneTreeENSGT00390000012928.
HOGENOMHBG713158.
HOVERGENHBG053341.
InParanoidQ8R2U6.
OMAEWEDSRS.
OrthoDBEOG479F89.
PhylomeDBQ8R2U6.

Gene expression databases

ArrayExpressQ8R2U6.
BgeeQ8R2U6.
GenevestigatorQ8R2U6.
GermOnlineENSMUSG00000020029. Mus musculus.

Family and domain databases

InterProIPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
Gene3DG3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.
KOK07766.
PfamPF00293. NUDIX. 1 hit.
[Graphical view]
SUPFAMSSF55811. NUDIX_hydrolase. 1 hit.
PROSITEPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio333289.
SOURCESearch...

Entry information

Entry nameNUDT4_MOUSE
AccessionPrimary (citable) accession number: Q8R2U6
Secondary accession number(s): Q8BXB9, Q9D3T6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2002
Last modified: November 16, 2011
This is version 83 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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