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UniProtKB/Swiss-Prot entry Q8NFP7


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NUD10_HUMAN
Primary accession number Q8NFP7
Secondary accession numbers Q86VK1 Q86VR0
Integrated into Swiss-Prot on July 5, 2005
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 47)
Name and origin of the protein
Protein name Diphosphoinositol polyphosphate phosphohydrolase 3-alpha
Synonyms DIPP-3-alpha
DIPP3-alpha
hDIPP3alpha
EC 3.6.1.52
Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-alpha
EC 3.6.1.-
Nucleoside diphosphate-linked moiety X motif 10
Nudix motif 10
hAps2
Gene name
Name: NUDT10
Synonyms: APS2, DIPP3A
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
DOI=10.1074/jbc.M205476200; PubMed=12105228 [NCBI, ExPASy, EBI, Israel, Japan]
Hidaka K., Caffrey J.J., Hua L., Zhang T., Falck J.R., Nickel G.C., Carrel L., Barnes L.D., Shears S.B.;
"An adjacent pair of human NUDT genes on chromosome X are preferentially expressed in testis and encode two new isoforms of diphosphoinositol polyphosphate phosphohydrolase.";
J. Biol. Chem. 277:32730-32738(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03440; PubMed=15772651 [NCBI, ExPASy, EBI, Israel, Japan]
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
ENZYME ACTIVITY, SUBCELLULAR LOCATION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
DOI=10.1186/1472-2091-3-20; PubMed=12121577 [NCBI, ExPASy, EBI, Israel, Japan]
Leslie N.R., McLennan A.G., Safrany S.T.;
"Cloning and characterisation of hAps1 and hAps2, human diadenosine polyphosphate-metabolising Nudix hydrolases.";
BMC Biochem. 3:20-20(2002).
[5]
ENZYME ACTIVITY.
DOI=10.1074/jbc.M209795200; PubMed=12370170 [NCBI, ExPASy, EBI, Israel, Japan]
Fisher D.I., Safrany S.T., Strike P., McLennan A.G., Cartwright J.L.;
"Nudix hydrolases that degrade dinucleoside and diphosphoinositol polyphosphates also have 5-phosphoribosyl 1-pyrophosphate (PRPP) pyrophosphatase activity that generates the glycolytic activator ribose 1,5-bisphosphate.";
J. Biol. Chem. 277:47313-47317(2002).
Comments
  • FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyzes the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-phosphoribose 1-diphosphate.
  • CATALYTIC ACTIVITY: Diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.
  • COFACTOR: Magnesium or manganese. Manganese may be the true cofactor in vivo.
  • BIOPHYSICOCHEMICAL PROPERTIES:
    Kinetic parameters:   KM=0.088 µM for PP-InsP5;
    KM=19 µM for Ap6A;
    KM=50 µM for Ap5A;
    pH dependence:   Optimum pH is 8.5;
  • SUBCELLULAR LOCATION: Cytoplasm (Probable).
  • TISSUE SPECIFICITY: Mainly expressed in testis and, at lower level in brain. According to Ref.4, it is widely expressed.
  • SIMILARITY: Belongs to the Nudix hydrolase family. DIPP subfamily.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF469196; AAM64113.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL158055; CAI40295.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC049383; AAH49383.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC050700; AAH50700.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_694853.1; -.
UniGene Hs.375178
3D structure databases
SMR Q8NFP7; 8-146.
ModBase Q8NFP7.
Protein-protein interaction databases
IntAct Q8NFP7; -.
Organism-specific databases
H-InvDB HIX0028345; -.
HGNC HGNC:17621; NUDT10.
GenAtlas NUDT10.
MIM 300527; gene. [NCBI / EBI]
PharmGKB PA31831; -.
GeneCards Q8NFP7.
Gene expression databases
ArrayExpress Q8NFP7; -.
CleanEx HS_NUDT10; -.
GermOnline ENSG00000122824; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0008486; Molecular function: diphosphoinositol-polyphosphate diphosphatase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145; Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000086; NUDIX_hydrolase_core.
Graphical view of domain structure.
Gene3D G3DSA:3.90.79.10; NUDIX_hydrolase; 1.
Pfam PF00293; NUDIX; 1.
Pfam graphical view of domain structure.
PRINTS PR00502; NUDIXFAMILY.
PROSITE PS00893; NUDIX; 1.
ProtoNet Q8NFP7.
Genome annotation databases
Ensembl ENSG00000122824; Homo sapiens. [Contig view]
GeneID 170685; -.
KEGG hsa:170685; -.
Phylogenomic databases
HOGENOM Q8NFP7; -.
HOVERGEN Q8NFP7; -.
Other
NextBio 89092; -.
SOURCE NUDT10; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   164  164     Diphosphoinositol polyphosphate phosphohydrolase 3-alpha. PRO_0000057062
MOTIF   50    71  22     Nudix box. 
METAL   65    65        Magnesium or manganese (By similarity). 
METAL   69    69        Magnesium or manganese (By similarity). 
CONFLICT   90    90        K -> E (in Ref. 3; AAH50700). 
CONFLICT   135   135        V -> M (in Ref. 3; AAH49383). 
Sequence information
Length: 164 AA [This is the length of the unprocessed precursor] Molecular weight: 18500 Da [This is the MW of the unprocessed precursor] CRC64: 589F342E02B285A7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKCKPNQTRT YDPEGFKKRA ACLCFRSERE DEVLLVSSSR YPDRWIVPGG GMEPEEEPGG 

        70         80         90        100        110        120 
AAVREVYEEA GVKGKLGRLL GVFEQNQDPK HRTYVYVLTV TELLEDWEDS VSIGRKREWF 

       130        140        150        160 
KVEDAIKVLQ CHKPVHAEYL EKLKLGGSPT NGNSMAPSSP DSDP 

Q8NFP7 in FASTA format

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