ID   NUD10_HUMAN             Reviewed;         164 AA.
AC   Q8NFP7; Q86VK1; Q86VR0;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   07-JUL-2009, entry version 56.
DE   RecName: Full=Diphosphoinositol polyphosphate phosphohydrolase 3-alpha;
DE            Short=DIPP-3-alpha;
DE            Short=DIPP3-alpha;
DE            Short=hDIPP3alpha;
DE            EC=3.6.1.52;
DE   AltName: Full=Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-alpha;
DE            EC=3.6.1.-;
DE   AltName: Full=Nucleoside diphosphate-linked moiety X motif 10;
DE            Short=Nudix motif 10;
DE            Short=hAps2;
GN   Name=NUDT10; Synonyms=APS2, DIPP3A;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND TISSUE SPECIFICITY.
RX   MEDLINE=22194402; PubMed=12105228; DOI=10.1074/jbc.M205476200;
RA   Hidaka K., Caffrey J.J., Hua L., Zhang T., Falck J.R., Nickel G.C.,
RA   Carrel L., Barnes L.D., Shears S.B.;
RT   "An adjacent pair of human NUDT genes on chromosome X are
RT   preferentially expressed in testis and encode two new isoforms of
RT   diphosphoinositol polyphosphate phosphohydrolase.";
RL   J. Biol. Chem. 277:32730-32738(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA   Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA   Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA   Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA   Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA   Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA   Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA   Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA   Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA   Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA   Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA   Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA   Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA   Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA   Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA   Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA   Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA   Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA   Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA   Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA   Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA   Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA   Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA   Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA   de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA   Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA   Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA   Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA   Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA   Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA   Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA   Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA   Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA   Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA   Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA   Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA   Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA   Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA   Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA   Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA   Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA   Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA   Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA   Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   ENZYME ACTIVITY, SUBCELLULAR LOCATION, COFACTOR, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND TISSUE SPECIFICITY.
RX   MEDLINE=22325330; PubMed=12121577; DOI=10.1186/1472-2091-3-20;
RA   Leslie N.R., McLennan A.G., Safrany S.T.;
RT   "Cloning and characterisation of hAps1 and hAps2, human diadenosine
RT   polyphosphate-metabolising Nudix hydrolases.";
RL   BMC Biochem. 3:20-20(2002).
RN   [5]
RP   ENZYME ACTIVITY.
RX   MEDLINE=22344714; PubMed=12370170; DOI=10.1074/jbc.M209795200;
RA   Fisher D.I., Safrany S.T., Strike P., McLennan A.G., Cartwright J.L.;
RT   "Nudix hydrolases that degrade dinucleoside and diphosphoinositol
RT   polyphosphates also have 5-phosphoribosyl 1-pyrophosphate (PRPP)
RT   pyrophosphatase activity that generates the glycolytic activator
RT   ribose 1,5-bisphosphate.";
RL   J. Biol. Chem. 277:47313-47317(2002).
RN   [6]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
CC   -!- FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in
CC       PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it
CC       may play a role in signal transduction. Also able to catalyzes the
CC       hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A
CC       being the preferred substrates. The major reaction products are
CC       ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to
CC       hydrolyze 5-phosphoribose 1-diphosphate.
CC   -!- CATALYTIC ACTIVITY: Diphospho-myo-inositol polyphosphate + H(2)O =
CC       myo-inositol polyphosphate + phosphate.
CC   -!- COFACTOR: Magnesium or manganese. Manganese may be the true
CC       cofactor in vivo.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.088 uM for PP-InsP5;
CC         KM=19 uM for Ap6A;
CC         KM=50 uM for Ap5A;
CC       pH dependence:
CC         Optimum pH is 8.5;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- TISSUE SPECIFICITY: Mainly expressed in testis and, at lower level
CC       in brain. According to PubMed:12121577, it is widely expressed.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. DIPP subfamily.
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DR   EMBL; AF469196; AAM64113.1; -; mRNA.
DR   EMBL; AL158055; CAI40295.1; -; Genomic_DNA.
DR   EMBL; BC049383; AAH49383.1; -; mRNA.
DR   EMBL; BC050700; AAH50700.1; -; mRNA.
DR   IPI; IPI00549204; -.
DR   RefSeq; NP_694853.1; -.
DR   UniGene; Hs.375178; -.
DR   SMR; Q8NFP7; 8-146.
DR   IntAct; Q8NFP7; 1.
DR   PRIDE; Q8NFP7; -.
DR   Ensembl; ENSG00000122824; Homo sapiens.
DR   GeneID; 170685; -.
DR   KEGG; hsa:170685; -.
DR   UCSC; uc004dph.1; human.
DR   GeneCards; GC0XP051091; -.
DR   H-InvDB; HIX0028345; -.
DR   HGNC; HGNC:17621; NUDT10.
DR   MIM; 300527; gene.
DR   PharmGKB; PA31831; -.
DR   HOGENOM; Q8NFP7; -.
DR   HOVERGEN; Q8NFP7; -.
DR   OMA; Q8NFP7; DEWEDSK.
DR   BRENDA; 3.6.1.52; 247.
DR   NextBio; 89092; -.
DR   ArrayExpress; Q8NFP7; -.
DR   Bgee; Q8NFP7; -.
DR   CleanEx; HS_NUDT10; -.
DR   GermOnline; ENSG00000122824; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008486; F:diphosphoinositol-polyphosphate diphosphata...; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR000086; NUDIX_hydrolase_core.
DR   Gene3D; G3DSA:3.90.79.10; NUDIX_hydrolase; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Hydrolase; Magnesium; Manganese;
KW   Metal-binding.
FT   CHAIN         1    164       Diphosphoinositol polyphosphate
FT                                phosphohydrolase 3-alpha.
FT                                /FTId=PRO_0000057062.
FT   MOTIF        50     71       Nudix box.
FT   METAL        65     65       Magnesium or manganese (By similarity).
FT   METAL        69     69       Magnesium or manganese (By similarity).
FT   CONFLICT     90     90       K -> E (in Ref. 3; AAH50700).
FT   CONFLICT    135    135       V -> M (in Ref. 3; AAH49383).
SQ   SEQUENCE   164 AA;  18500 MW;  589F342E02B285A7 CRC64;
     MKCKPNQTRT YDPEGFKKRA ACLCFRSERE DEVLLVSSSR YPDRWIVPGG GMEPEEEPGG
     AAVREVYEEA GVKGKLGRLL GVFEQNQDPK HRTYVYVLTV TELLEDWEDS VSIGRKREWF
     KVEDAIKVLQ CHKPVHAEYL EKLKLGGSPT NGNSMAPSSP DSDP
//