NUD10_HUMAN
ID NUD10_HUMAN Reviewed; 164 AA.
AC Q8NFP7; A8K7D7; D3DX69; Q86VK1; Q86VR0;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Diphosphoinositol polyphosphate phosphohydrolase 3-alpha {ECO:0000303|PubMed:12105228};
DE Short=DIPP-3-alpha;
DE Short=DIPP3-alpha {ECO:0000303|PubMed:12105228};
DE Short=hDIPP3alpha {ECO:0000303|PubMed:12105228};
DE EC=3.6.1.52 {ECO:0000269|PubMed:12105228, ECO:0000269|PubMed:12121577, ECO:0000269|PubMed:12370170};
DE AltName: Full=Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-alpha;
DE AltName: Full=Diadenosine hexaphosphate hydrolase (AMP-forming);
DE EC=3.6.1.60 {ECO:0000269|PubMed:12105228, ECO:0000269|PubMed:12121577, ECO:0000269|PubMed:12370170};
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 10;
DE Short=Nudix motif 10;
DE AltName: Full=hAps2;
GN Name=NUDT10; Synonyms=APS2, DIPP3A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX 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 preferentially
RT expressed in testis and encode two new isoforms of diphosphoinositol
RT polyphosphate phosphohydrolase.";
RL J. Biol. Chem. 277:32730-32738(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
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., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., 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., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., 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., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., 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., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., 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., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=12121577; DOI=10.1186/1471-2091-3-20;
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 [7]
RP CATALYTIC ACTIVITY.
RX 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 ribose
RT 1,5-bisphosphate.";
RL J. Biol. Chem. 277:47313-47317(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 17-144 IN COMPLEX WITH CITRATE.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human diphosphoinositol polyphosphate
RT phosphohydrolase 3-alpha.";
RL Submitted (APR-2010) to the PDB data bank.
CC -!- FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-
CC InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may
CC play a role in signal transduction. Also able to catalyze the
CC hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being
CC the preferred substrates. The major reaction products are ADP and p4a
CC from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-
CC phosphoribose 1-diphosphate. {ECO:0000269|PubMed:12105228}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphospho-myo-inositol polyphosphate + H2O = myo-inositol
CC polyphosphate + phosphate.; EC=3.6.1.52;
CC Evidence={ECO:0000269|PubMed:12105228, ECO:0000269|PubMed:12121577,
CC ECO:0000269|PubMed:12370170};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + P(1),P(6)-bis(5'-adenosyl) hexaphosphate = adenosine 5'-
CC pentaphosphate + AMP + 2 H(+); Xref=Rhea:RHEA:32047,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:63740,
CC ChEBI:CHEBI:63813, ChEBI:CHEBI:456215; EC=3.6.1.60;
CC Evidence={ECO:0000269|PubMed:12105228, ECO:0000269|PubMed:12121577,
CC ECO:0000269|PubMed:12370170};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + P(1),P(5)-bis(5'-adenosyl) pentaphosphate = adenosine
CC 5'-tetraphosphate + AMP + 2 H(+); Xref=Rhea:RHEA:32051,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58450,
CC ChEBI:CHEBI:62041, ChEBI:CHEBI:456215; EC=3.6.1.60;
CC Evidence={ECO:0000269|PubMed:12105228, ECO:0000269|PubMed:12121577,
CC ECO:0000269|PubMed:12370170};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250, ECO:0000269|PubMed:12121577};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250, ECO:0000269|PubMed:12121577};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. Mn(2+) may be the true
CC cofactor in vivo. {ECO:0000250, ECO:0000269|PubMed:12121577};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.088 uM for PP-InsP5 {ECO:0000269|PubMed:12105228,
CC ECO:0000269|PubMed:12121577};
CC KM=19 uM for Ap6A {ECO:0000269|PubMed:12105228,
CC ECO:0000269|PubMed:12121577};
CC KM=50 uM for Ap5A {ECO:0000269|PubMed:12105228,
CC ECO:0000269|PubMed:12121577};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:12105228,
CC ECO:0000269|PubMed:12121577};
CC -!- INTERACTION:
CC Q8NFP7; O75031: HSF2BP; NbExp=3; IntAct=EBI-726826, EBI-7116203;
CC Q8NFP7; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-726826, EBI-742948;
CC Q8NFP7; Q9NR12: PDLIM7; NbExp=3; IntAct=EBI-726826, EBI-350517;
CC Q8NFP7; Q04864-2: REL; NbExp=3; IntAct=EBI-726826, EBI-10829018;
CC Q8NFP7; O75971: SNAPC5; NbExp=3; IntAct=EBI-726826, EBI-749483;
CC Q8NFP7; P15884: TCF4; NbExp=3; IntAct=EBI-726826, EBI-533224;
CC Q8NFP7; Q9BZR9: TRIM8; NbExp=3; IntAct=EBI-726826, EBI-2340370;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:12121577}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in testis and, at lower level in
CC brain. According to PubMed:12121577, it is widely expressed.
CC {ECO:0000269|PubMed:12105228, ECO:0000269|PubMed:12121577}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DIPP subfamily.
CC {ECO:0000305}.
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DR EMBL; AF469196; AAM64113.1; -; mRNA.
DR EMBL; AK291952; BAF84641.1; -; mRNA.
DR EMBL; AL158055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471180; EAW89910.1; -; Genomic_DNA.
DR EMBL; CH471180; EAW89911.1; -; Genomic_DNA.
DR EMBL; BC049383; AAH49383.1; -; mRNA.
DR EMBL; BC050700; AAH50700.1; -; mRNA.
DR CCDS; CCDS35278.1; -.
DR RefSeq; NP_001291892.1; NM_001304963.1.
DR RefSeq; NP_694853.1; NM_153183.3.
DR PDB; 3MCF; X-ray; 2.00 A; A/B=17-144.
DR PDBsum; 3MCF; -.
DR AlphaFoldDB; Q8NFP7; -.
DR SMR; Q8NFP7; -.
DR BioGRID; 128079; 18.
DR IntAct; Q8NFP7; 9.
DR STRING; 9606.ENSP00000365174; -.
DR ChEMBL; CHEMBL4295904; -.
DR iPTMnet; Q8NFP7; -.
DR PhosphoSitePlus; Q8NFP7; -.
DR BioMuta; NUDT10; -.
DR DMDM; 68565913; -.
DR EPD; Q8NFP7; -.
DR jPOST; Q8NFP7; -.
DR MassIVE; Q8NFP7; -.
DR MaxQB; Q8NFP7; -.
DR PaxDb; Q8NFP7; -.
DR PeptideAtlas; Q8NFP7; -.
DR PRIDE; Q8NFP7; -.
DR ProteomicsDB; 73332; -.
DR Antibodypedia; 26316; 199 antibodies from 22 providers.
DR DNASU; 170685; -.
DR Ensembl; ENST00000356450.3; ENSP00000348831.2; ENSG00000122824.11.
DR Ensembl; ENST00000376006.7; ENSP00000365174.3; ENSG00000122824.11.
DR GeneID; 170685; -.
DR KEGG; hsa:170685; -.
DR MANE-Select; ENST00000356450.3; ENSP00000348831.2; NM_001304963.2; NP_001291892.1.
DR UCSC; uc004dph.3; human.
DR CTD; 170685; -.
DR DisGeNET; 170685; -.
DR GeneCards; NUDT10; -.
DR HGNC; HGNC:17621; NUDT10.
DR HPA; ENSG00000122824; Tissue enhanced (testis).
DR MIM; 300527; gene.
DR neXtProt; NX_Q8NFP7; -.
DR OpenTargets; ENSG00000122824; -.
DR PharmGKB; PA31831; -.
DR VEuPathDB; HostDB:ENSG00000122824; -.
DR eggNOG; KOG2839; Eukaryota.
DR GeneTree; ENSGT01040000240679; -.
DR HOGENOM; CLU_037162_1_0_1; -.
DR InParanoid; Q8NFP7; -.
DR OMA; VEKNECA; -.
DR OrthoDB; 1324716at2759; -.
DR PhylomeDB; Q8NFP7; -.
DR TreeFam; TF106349; -.
DR BioCyc; MetaCyc:HS04604-MON; -.
DR BRENDA; 3.6.1.60; 2681.
DR PathwayCommons; Q8NFP7; -.
DR Reactome; R-HSA-1855167; Synthesis of pyrophosphates in the cytosol.
DR SignaLink; Q8NFP7; -.
DR BioGRID-ORCS; 170685; 17 hits in 611 CRISPR screens.
DR ChiTaRS; NUDT10; human.
DR EvolutionaryTrace; Q8NFP7; -.
DR GenomeRNAi; 170685; -.
DR Pharos; Q8NFP7; Tbio.
DR PRO; PR:Q8NFP7; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8NFP7; protein.
DR Bgee; ENSG00000122824; Expressed in cortical plate and 121 other tissues.
DR Genevisible; Q8NFP7; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0034431; F:bis(5'-adenosyl)-hexaphosphatase activity; IBA:GO_Central.
DR GO; GO:0034432; F:bis(5'-adenosyl)-pentaphosphatase activity; IBA:GO_Central.
DR GO; GO:0008486; F:diphosphoinositol-polyphosphate diphosphatase activity; ISS:UniProtKB.
DR GO; GO:0000298; F:endopolyphosphatase activity; IBA:GO_Central.
DR GO; GO:0052842; F:inositol diphosphate pentakisphosphate diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052840; F:inositol diphosphate tetrakisphosphate diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0050072; F:m7G(5')pppN diphosphatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901911; P:adenosine 5'-(hexahydrogen pentaphosphate) catabolic process; IBA:GO_Central.
DR GO; GO:1901909; P:diadenosine hexaphosphate catabolic process; IBA:GO_Central.
DR GO; GO:1901907; P:diadenosine pentaphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0071543; P:diphosphoinositol polyphosphate metabolic process; IBA:GO_Central.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..164
FT /note="Diphosphoinositol polyphosphate phosphohydrolase 3-
FT alpha"
FT /id="PRO_0000057062"
FT DOMAIN 17..144
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 144..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 50..71
FT /note="Nudix box"
FT COMPBIAS 147..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 68
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 17..19
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 38..40
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 49
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 65
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 65
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 89..91
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT CONFLICT 90
FT /note="K -> E (in Ref. 5; AAH50700)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="V -> M (in Ref. 5; AAH49383)"
FT /evidence="ECO:0000305"
FT STRAND 18..27
FT /evidence="ECO:0007829|PDB:3MCF"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:3MCF"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:3MCF"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:3MCF"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:3MCF"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:3MCF"
FT STRAND 72..83
FT /evidence="ECO:0007829|PDB:3MCF"
FT STRAND 92..103
FT /evidence="ECO:0007829|PDB:3MCF"
FT HELIX 108..113
FT /evidence="ECO:0007829|PDB:3MCF"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:3MCF"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:3MCF"
FT HELIX 134..144
FT /evidence="ECO:0007829|PDB:3MCF"
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
