NUD11_MOUSE
ID NUD11_MOUSE Reviewed; 164 AA.
AC P0C028; Q8BKF4; Q9JJD3;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Diphosphoinositol polyphosphate phosphohydrolase 3-beta {ECO:0000305};
DE Short=DIPP-3-beta;
DE Short=DIPP3-beta;
DE EC=3.6.1.52 {ECO:0000269|PubMed:12689335};
DE AltName: Full=Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-beta;
DE AltName: Full=Diadenosine hexaphosphate hydrolase (AMP-forming);
DE EC=3.6.1.60 {ECO:0000269|PubMed:12689335};
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 11;
DE Short=Nudix motif 11;
GN Name=Nudt11 {ECO:0000312|MGI:MGI:1930957}; Synonyms=Dipp3b;
GN ORFNames=MNCb-1696;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND
RP VARIANT THR-113.
RX PubMed=12689335; DOI=10.1042/bj20030142;
RA Hua L.V., Hidaka K., Pesesse X., Barnes L.D., Shears S.B.;
RT "Paralogous murine Nudt10 and Nudt11 genes have differential expression
RT patterns but encode identical proteins that are physiologically competent
RT diphosphoinositol polyphosphate phosphohydrolases.";
RL Biochem. J. 373:81-89(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-113.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; however, the relevance of such activity in
CC vivo remains unclear.
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:12689335};
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:12689335};
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:12689335};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q96G61};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q96G61};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. Mn(2+) may be the true
CC cofactor in vivo. {ECO:0000250|UniProtKB:Q96G61};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96G61}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain and is weakly or
CC not expressed in other tissues. {ECO:0000269|PubMed:12689335}.
CC -!- MISCELLANEOUS: Nudt10 and Nudt11 code for identical proteins, which
CC gives their indidual characterization difficult. Thus, most experiments
CC do not discriminate between the 2 proteins.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DIPP subfamily.
CC {ECO:0000305}.
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DR EMBL; AY152853; AAN41645.1; -; mRNA.
DR EMBL; AB041576; BAA95060.1; -; mRNA.
DR EMBL; AK053310; BAC35339.1; -; mRNA.
DR EMBL; BC071274; AAH71274.1; -; mRNA.
DR CCDS; CCDS29955.1; -.
DR RefSeq; NP_001026834.1; NM_001031664.1.
DR RefSeq; NP_067406.2; NM_021431.2.
DR RefSeq; XP_006527609.1; XM_006527546.2.
DR AlphaFoldDB; P0C028; -.
DR SMR; P0C028; -.
DR iPTMnet; P0C028; -.
DR PhosphoSitePlus; P0C028; -.
DR jPOST; P0C028; -.
DR MaxQB; P0C028; -.
DR PRIDE; P0C028; -.
DR DNASU; 102954; -.
DR DNASU; 58242; -.
DR Ensembl; ENSMUST00000103006; ENSMUSP00000100071; ENSMUSG00000073293.
DR Ensembl; ENSMUST00000103007; ENSMUSP00000100072; ENSMUSG00000073295.
DR GeneID; 102954; -.
DR GeneID; 58242; -.
DR KEGG; mmu:102954; -.
DR KEGG; mmu:58242; -.
DR CTD; 170685; -.
DR CTD; 55190; -.
DR MGI; MGI:1930957; Nudt11.
DR VEuPathDB; HostDB:ENSMUSG00000073293; -.
DR VEuPathDB; HostDB:ENSMUSG00000073295; -.
DR GeneTree; ENSGT00940000160559; -.
DR HOGENOM; CLU_037162_1_0_1; -.
DR OMA; VEKNECA; -.
DR OrthoDB; 1324716at2759; -.
DR PhylomeDB; P0C028; -.
DR TreeFam; TF106349; -.
DR BRENDA; 3.6.1.52; 3474.
DR Reactome; R-MMU-1855167; Synthesis of pyrophosphates in the cytosol.
DR BioGRID-ORCS; 102954; 2 hits in 40 CRISPR screens.
DR BioGRID-ORCS; 58242; 6 hits in 41 CRISPR screens.
DR PRO; PR:P0C028; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P0C028; protein.
DR Bgee; ENSMUSG00000073293; Expressed in cortical plate and 159 other tissues.
DR ExpressionAtlas; P0C028; baseline and differential.
DR Genevisible; P0C028; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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; IDA:MGI.
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; IPR020476; Nudix_hydrolase.
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 PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..164
FT /note="Diphosphoinositol polyphosphate phosphohydrolase 3-
FT beta"
FT /id="PRO_0000057066"
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 VARIANT 113
FT /note="I -> T"
FT /evidence="ECO:0000269|PubMed:12689335, ECO:0000269|Ref.2"
SQ SEQUENCE 164 AA; 18593 MW; 7141513979E4FBCD CRC64;
MKCKPNQTRT YDPEGFKKRA ACLCFRSERE DEVLLVSSSR YPDRWIVPGG GMEPEEEPDG
AAVREVYEEA GVKGKLGRLL GVFEQNQDRK HRTYVFVLTV TELLEDWEDS VSIGRKREWF
KIEDAIKVLQ CHKPVHAEYL EKLKLGGSPT NGNSAAPSPP ESEP
