Reviewed, UniProtKB/Swiss-Prot Q8R2U6 (NUDT4_MOUSE)

Names and origin

Protein names

Recommended 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

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	179 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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	Magnesium or manganese By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the Nudix hydrolase family. DIPP subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Magnesium Manganese Metal-binding
Molecular function	Hydrolase
Technical term	3D-structure
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	diphosphoinositol-polyphosphate diphosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 179	179	Diphosphoinositol polyphosphate phosphohydrolase 2		PRO_0000057059
Regions
	Motif	50 – 71	22	Nudix box
Sites
	Metal binding	65	1	Magnesium or manganese By similarity
	Metal binding	69	1	Magnesium or manganese By similarity
Experimental info
	Sequence conflict	69	1	E → Q in BAC33229. Ref.1
	Sequence conflict	168	1	A → C in BAB30582. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8R2U6-1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 05A78EBBA8256B89	FASTA	179	20,156
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AK017075 mRNA. Translation: BAB30582.1.
AK048062 mRNA. Translation: BAC33229.1.
BC027209 mRNA. Translation: AAH27209.1.

IPI

IPI00854941.

RefSeq

NP_081998.3.

UniGene

Mm.24397

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DUK	X-ray	2.62	A/B	8-145	[»]

SMR

Q8R2U6. Positions 8-145.

ModBase

Search...

Genome annotation databases

Ensembl

ENSMUSG00000020029. Mus musculus. [Contig view]

GeneID

71207.

KEGG

mmu:71207.

Organism-specific databases

MGI

MGI:1918457. Nudt4.

Phylogenomic databases

HOGENOM

Q8R2U6.

HOVERGEN

Q8R2U6.

OMA

Q8R2U6. LYVTSAQ.

Enzyme and pathway databases

BRENDA

3.6.1.52. 244.

Gene expression databases

ArrayExpress

Q8R2U6.

Bgee

Q8R2U6.

GermOnline

ENSMUSG00000020029. 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. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

333289.

SOURCE

Search...

Entry information

Entry name

NUDT4_MOUSE

Accession

Primary (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:	June 16, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)