ID   NUDT4_HUMAN             Reviewed;         180 AA.
AC   Q9NZJ9; B7Z916; Q4AEJ6; Q53EZ2; Q68DD7; Q9NPC5; Q9NS30; Q9NZK0; Q9NZK1;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 2.
DT   27-MAR-2024, entry version 189.
DE   RecName: Full=Diphosphoinositol polyphosphate phosphohydrolase 2 {ECO:0000305};
DE            Short=DIPP-2;
DE            EC=3.6.1.52 {ECO:0000269|PubMed:10777568, ECO:0000269|PubMed:12370170};
DE   AltName: Full=Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 2;
DE   AltName: Full=Nucleoside diphosphate-linked moiety X motif 4;
DE            Short=Nudix motif 4;
GN   Name=NUDT4 {ECO:0000312|HGNC:HGNC:8051}; Synonyms=DIPP2, KIAA0487;
GN   ORFNames=HDCMB47P;
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] (ISOFORMS 1 AND 2), FUNCTION, ENZYME ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC   TISSUE=Cerebellum;
RX   PubMed=10777568; DOI=10.1074/jbc.275.17.12730;
RA   Caffrey J.J., Safrany S.T., Yang X., Shears S.B.;
RT   "Discovery of molecular and catalytic diversity among human
RT   diphosphoinositol-polyphosphate phosphohydrolases. The expanding NUDT
RT   family.";
RL   J. Biol. Chem. 275:12730-12736(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA   Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA   Nomura N., Ohara O.;
RT   "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT   human brain.";
RL   DNA Res. 4:345-349(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA   Zhao Z., Huang X., Li N., Zhu X., Cao X.;
RT   "Novel gene identified from dendritic cells.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Retina;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Trachea;
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Lymph, and Placenta;
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   [9]
RP   SUBCELLULAR LOCATION.
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   [10]
RP   FUNCTION, AND ENZYME 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   [11]
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   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [13] {ECO:0007744|PDB:5LTU}
RP   X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS).
RA   Srikannathasan V., Huber K.;
RT   "Crystal Structure of Human NUDT4A- Diphosphoinositol polyphosphate
RT   phosphohydrolase 2.";
RL   Submitted (SEP-2016) to the PDB data bank.
CC   -!- FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-
CC       InsP5 (diphosphoinositol pentakisphosphate), PP-InsP4 and [PP]2-InsP4
CC       (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a
CC       role in signal transduction (PubMed:10777568, PubMed:12370170). Can
CC       also catalyze the hydrolysis of diadenosine 5',5'''-P1,P6-hexaphosphate
CC       (Ap6A) but not diadenosine 5',5'''-P1,P5-pentaphosphate (Ap5A) and the
CC       major reaction products are ADP and p4a from Ap6A (PubMed:12370170).
CC       Also able to hydrolyze 5-phosphoribose 1-diphosphate (PubMed:12370170).
CC       Does not play a role in U8 snoRNA decapping activity (By similarity).
CC       Binds U8 snoRNA (By similarity). {ECO:0000250|UniProtKB:Q8R2U6,
CC       ECO:0000269|PubMed:10777568, ECO:0000269|PubMed:12370170}.
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:10777568, ECO:0000269|PubMed:12370170};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + H2O
CC         = 1D-myo-inositol hexakisphosphate + H(+) + phosphate;
CC         Xref=Rhea:RHEA:22384, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58130, ChEBI:CHEBI:58628; EC=3.6.1.52;
CC         Evidence={ECO:0000269|PubMed:10777568, ECO:0000269|PubMed:12370170};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3,5-bis(diphospho)-1D-myo-inositol 1,2,4,6-tetrakisphosphate +
CC         H2O = 3-diphospho-1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 2
CC         H(+) + phosphate; Xref=Rhea:RHEA:56312, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:140372,
CC         ChEBI:CHEBI:140374; EC=3.6.1.52;
CC         Evidence={ECO:0000269|PubMed:10777568, ECO:0000269|PubMed:12370170};
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.
CC       {ECO:0000250|UniProtKB:Q96G61};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.2 nM for PP-InsP5 {ECO:0000269|PubMed:10777568};
CC   -!- INTERACTION:
CC       Q9NZJ9; P04792: HSPB1; NbExp=3; IntAct=EBI-4280066, EBI-352682;
CC       Q9NZJ9; P42858: HTT; NbExp=6; IntAct=EBI-4280066, EBI-466029;
CC       Q9NZJ9; Q14145: KEAP1; NbExp=3; IntAct=EBI-4280066, EBI-751001;
CC       Q9NZJ9; O76024: WFS1; NbExp=3; IntAct=EBI-4280066, EBI-720609;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12121577}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Alpha, DIPP2alpha;
CC         IsoId=Q9NZJ9-1; Sequence=Displayed;
CC       Name=2; Synonyms=Beta, DIPP2beta;
CC         IsoId=Q9NZJ9-2; Sequence=VSP_014270;
CC       Name=3;
CC         IsoId=Q9NZJ9-3; Sequence=VSP_014269, VSP_014270;
CC   -!- TISSUE SPECIFICITY: Expressed in heart and, at lower level in skeletal
CC       muscle, pancreas and kidney. {ECO:0000269|PubMed:10777568}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. DIPP subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF75563.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAE16985.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF191649; AAF68855.1; -; mRNA.
DR   EMBL; AF191650; AAF68856.1; -; mRNA.
DR   EMBL; AF191651; AAF68857.1; -; mRNA.
DR   EMBL; AF191652; AAF68858.2; -; mRNA.
DR   EMBL; AF191653; AAF68859.1; -; mRNA.
DR   EMBL; AB007956; BAE16985.1; ALT_INIT; mRNA.
DR   EMBL; AF067803; AAF75563.1; ALT_SEQ; mRNA.
DR   EMBL; CR749445; CAH18283.1; -; mRNA.
DR   EMBL; BT020109; AAV38912.1; -; mRNA.
DR   EMBL; BT020110; AAV38913.1; -; mRNA.
DR   EMBL; AK304296; BAH14152.1; -; mRNA.
DR   EMBL; AK223497; BAD97217.1; -; mRNA.
DR   EMBL; BC012069; AAH12069.1; -; mRNA.
DR   EMBL; BC051310; AAH51310.1; -; mRNA.
DR   CCDS; CCDS44952.1; -. [Q9NZJ9-1]
DR   CCDS; CCDS73504.1; -. [Q9NZJ9-3]
DR   CCDS; CCDS9044.1; -. [Q9NZJ9-2]
DR   RefSeq; NP_001287951.1; NM_001301022.1. [Q9NZJ9-3]
DR   RefSeq; NP_001287952.1; NM_001301023.1.
DR   RefSeq; NP_001287953.1; NM_001301024.1.
DR   RefSeq; NP_061967.3; NM_019094.5. [Q9NZJ9-1]
DR   RefSeq; NP_950241.1; NM_199040.3. [Q9NZJ9-2]
DR   RefSeq; XP_011536096.1; XM_011537794.2.
DR   RefSeq; XP_011536097.1; XM_011537795.2.
DR   RefSeq; XP_011536098.1; XM_011537796.2.
DR   PDB; 5LTU; X-ray; 2.23 A; A/B=1-180.
DR   PDB; 7NNJ; X-ray; 1.75 A; A/B=9-146.
DR   PDBsum; 5LTU; -.
DR   PDBsum; 7NNJ; -.
DR   AlphaFoldDB; Q9NZJ9; -.
DR   SMR; Q9NZJ9; -.
DR   BioGRID; 116334; 14.
DR   IntAct; Q9NZJ9; 7.
DR   MINT; Q9NZJ9; -.
DR   ChEMBL; CHEMBL4295967; -.
DR   iPTMnet; Q9NZJ9; -.
DR   MetOSite; Q9NZJ9; -.
DR   PhosphoSitePlus; Q9NZJ9; -.
DR   BioMuta; NUDT4; -.
DR   DMDM; 68565946; -.
DR   EPD; Q9NZJ9; -.
DR   jPOST; Q9NZJ9; -.
DR   MassIVE; Q9NZJ9; -.
DR   MaxQB; Q9NZJ9; -.
DR   PeptideAtlas; Q9NZJ9; -.
DR   ProteomicsDB; 83421; -. [Q9NZJ9-1]
DR   ProteomicsDB; 83422; -. [Q9NZJ9-2]
DR   ProteomicsDB; 83423; -. [Q9NZJ9-3]
DR   Pumba; Q9NZJ9; -.
DR   TopDownProteomics; Q9NZJ9-2; -. [Q9NZJ9-2]
DR   Antibodypedia; 17488; 99 antibodies from 20 providers.
DR   DNASU; 11163; -.
DR   Ensembl; ENST00000337179.9; ENSP00000338352.5; ENSG00000173598.14. [Q9NZJ9-2]
DR   Ensembl; ENST00000415493.7; ENSP00000406612.2; ENSG00000173598.14. [Q9NZJ9-1]
DR   Ensembl; ENST00000547014.5; ENSP00000448032.1; ENSG00000173598.14. [Q9NZJ9-3]
DR   GeneID; 11163; -.
DR   KEGG; hsa:11163; -.
DR   MANE-Select; ENST00000415493.7; ENSP00000406612.2; NM_019094.6; NP_061967.3.
DR   UCSC; uc001tcm.4; human. [Q9NZJ9-1]
DR   AGR; HGNC:8051; -.
DR   CTD; 11163; -.
DR   GeneCards; NUDT4; -.
DR   HGNC; HGNC:8051; NUDT4.
DR   HPA; ENSG00000173598; Low tissue specificity.
DR   MIM; 609229; gene.
DR   neXtProt; NX_Q9NZJ9; -.
DR   OpenTargets; ENSG00000173598; -.
DR   PharmGKB; PA31835; -.
DR   VEuPathDB; HostDB:ENSG00000173598; -.
DR   eggNOG; KOG2839; Eukaryota.
DR   GeneTree; ENSGT00940000155210; -.
DR   HOGENOM; CLU_037162_1_0_1; -.
DR   InParanoid; Q9NZJ9; -.
DR   OMA; NTNPRHN; -.
DR   OrthoDB; 5389130at2759; -.
DR   PhylomeDB; Q9NZJ9; -.
DR   TreeFam; TF106349; -.
DR   BioCyc; MetaCyc:HS10696-MONOMER; -.
DR   PathwayCommons; Q9NZJ9; -.
DR   Reactome; R-HSA-1855167; Synthesis of pyrophosphates in the cytosol.
DR   SABIO-RK; Q9NZJ9; -.
DR   SignaLink; Q9NZJ9; -.
DR   BioGRID-ORCS; 11163; 574 hits in 1156 CRISPR screens.
DR   ChiTaRS; NUDT4; human.
DR   GeneWiki; NUDT4; -.
DR   GenomeRNAi; 11163; -.
DR   Pharos; Q9NZJ9; Tbio.
DR   PRO; PR:Q9NZJ9; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q9NZJ9; Protein.
DR   Bgee; ENSG00000173598; Expressed in heart right ventricle and 212 other cell types or tissues.
DR   ExpressionAtlas; Q9NZJ9; baseline and differential.
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; IDA:UniProtKB.
DR   GO; GO:0000298; F:endopolyphosphatase activity; IBA:GO_Central.
DR   GO; GO:0052848; F:inositol-3,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity; IEA:RHEA.
DR   GO; GO:0052845; F:inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity; IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030515; F:snoRNA binding; ISS:UniProtKB.
DR   GO; GO:1901911; P:adenosine 5'-(hexahydrogen pentaphosphate) catabolic process; IBA:GO_Central.
DR   GO; GO:0019722; P:calcium-mediated signaling; TAS:UniProtKB.
DR   GO; GO:0019935; P:cyclic-nucleotide-mediated signaling; TAS:UniProtKB.
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   GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
DR   CDD; cd04666; Nudix_Hydrolase_9; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR047198; DDP-like_NUDIX.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   PANTHER; PTHR12629; DIPHOSPHOINOSITOL POLYPHOSPHATE PHOSPHOHYDROLASE; 1.
DR   PANTHER; PTHR12629:SF6; DIPHOSPHOINOSITOL POLYPHOSPHATE PHOSPHOHYDROLASE 2-RELATED; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
DR   Genevisible; Q9NZJ9; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm; Hydrolase;
KW   Magnesium; Manganese; Metal-binding; Reference proteome; RNA-binding.
FT   CHAIN           1..180
FT                   /note="Diphosphoinositol polyphosphate phosphohydrolase 2"
FT                   /id="PRO_0000057058"
FT   DOMAIN          18..144
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           51..72
FT                   /note="Nudix box"
FT   ACT_SITE        69
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O95989"
FT   BINDING         18..20
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O95989"
FT   BINDING         39..41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O95989"
FT   BINDING         50
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:O95989"
FT   BINDING         66
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O95989"
FT   BINDING         66
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:O95989"
FT   BINDING         70
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   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   VAR_SEQ         1..52
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:17974005, ECO:0000303|Ref.3"
FT                   /id="VSP_014269"
FT   VAR_SEQ         85
FT                   /note="E -> EQ (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:10777568,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:17974005, ECO:0000303|Ref.3,
FT                   ECO:0000303|Ref.5"
FT                   /id="VSP_014270"
FT   CONFLICT        16
FT                   /note="G -> D (in Ref. 1; AAF68857)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        41
FT                   /note="R -> Q (in Ref. 7; BAD97217)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        73
FT                   /note="V -> D (in Ref. 3; AAF75563)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        164
FT                   /note="A -> V (in Ref. 1; AAF68857)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        177
FT                   /note="S -> P (in Ref. 1; AAF68858)"
FT                   /evidence="ECO:0000305"
FT   STRAND          18..28
FT                   /evidence="ECO:0007829|PDB:7NNJ"
FT   STRAND          33..38
FT                   /evidence="ECO:0007829|PDB:7NNJ"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:7NNJ"
FT   HELIX           59..71
FT                   /evidence="ECO:0007829|PDB:7NNJ"
FT   STRAND          73..86
FT                   /evidence="ECO:0007829|PDB:7NNJ"
FT   TURN            87..90
FT                   /evidence="ECO:0007829|PDB:7NNJ"
FT   STRAND          91..103
FT                   /evidence="ECO:0007829|PDB:7NNJ"
FT   STRAND          116..121
FT                   /evidence="ECO:0007829|PDB:7NNJ"
FT   HELIX           122..132
FT                   /evidence="ECO:0007829|PDB:7NNJ"
FT   HELIX           134..145
FT                   /evidence="ECO:0007829|PDB:7NNJ"
SQ   SEQUENCE   180 AA;  20306 MW;  86D766F8F5B22D13 CRC64;
     MMKFKPNQTR TYDREGFKKR AACLCFRSEQ EDEVLLVSSS RYPDQWIVPG GGMEPEEEPG
     GAAVREVYEE AGVKGKLGRL LGIFENQDRK HRTYVYVLTV TEILEDWEDS VNIGRKREWF
     KVEDAIKVLQ CHKPVHAEYL EKLKLGCSPA NGNSTVPSLP DNNALFVTAA QTSGLPSSVR
//