ID NUDT3_HUMAN Reviewed; 172 AA. AC O95989; B2R8N4; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 11-NOV-2015, entry version 144. DE RecName: Full=Diphosphoinositol polyphosphate phosphohydrolase 1; DE Short=DIPP-1; DE EC=3.6.1.52; DE AltName: Full=Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 1; DE EC=3.6.1.-; DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 3; DE Short=Nudix motif 3; GN Name=NUDT3; Synonyms=DIPP, DIPP1; 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], FUNCTION, ENZYME ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND MUTAGENESIS OF RP GLU-70. RC TISSUE=Uterus; RX PubMed=9822604; DOI=10.1093/emboj/17.22.6599; RA Safrany S.T., Caffrey J.J., Yang X., Bembenek M.E., Moyer M.B., RA Burkhart W.A., Shears S.B.; RT "A novel context for the 'MutT' module, a guardian of cell integrity, RT in a diphosphoinositol polyphosphate phosphohydrolase."; RL EMBO J. 17:6599-6607(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 RT vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Amygdala; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Uterus; 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 [7] RP ENZYME ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=10419486; DOI=10.1074/jbc.274.31.21735; RA Safrany S.T., Ingram S.W., Cartwright J.L., Falck J.R., McLennan A.G., RA Barnes L.D., Shears S.B.; RT "The diadenosine hexaphosphate hydrolases from Schizosaccharomyces RT pombe and Saccharomyces cerevisiae are homologues of the human RT diphosphoinositol polyphosphate phosphohydrolase. Overlapping RT substrate specificities in a MutT-type protein."; RL J. Biol. Chem. 274:21735-21740(1999). RN [8] RP MUTAGENESIS OF GLY-50; GLY-51; GLY-52; GLU-66; GLY-72; GLY-75; GLY-78; RP GLY-82; PHE-84 AND HIS-91. RX PubMed=10585413; DOI=10.1074/jbc.274.50.35434; RA Yang X., Safrany S.T., Shears S.B.; RT "Site-directed mutagenesis of diphosphoinositol polyphosphate RT phosphohydrolase, a dual specificity NUDT enzyme that attacks RT diadenosine polyphosphates and diphosphoinositol polyphosphates."; RL J. Biol. Chem. 274:35434-35440(1999). RN [9] RP ENZYME ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. 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 RT ribose 1,5-bisphosphate."; RL J. Biol. Chem. 277:47313-47317(2002). RN [10] 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., RA Buerckstuemmer T., 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 [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS 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., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS; RP FLUORIDE AND INOSITOL HEXAKISPHOSPHATE, COFACTOR, AND ENZYME RP REGULATION. RX PubMed=19585659; DOI=10.1002/prot.22489; RA Thorsell A.G., Persson C., Graslund S., Hammarstrom M., Busam R.D., RA Hallberg B.M.; RT "Crystal structure of human diphosphoinositol phosphatase 1."; RL Proteins 77:242-246(2009). CC -!- FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in CC PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 CC (bisdiphosphoinositol tetrakisphosphate), suggesting that it may CC play a role in signal transduction. InsP6 (inositol CC hexakisphophate) is not a substrate. Acts as a negative regulator CC of the ERK1/2 pathway. Also able to catalyze the hydrolysis of CC dinucleoside oligophosphates, with Ap6A and Ap5A being the CC 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:9822604}. CC -!- CATALYTIC ACTIVITY: Diphospho-myo-inositol polyphosphate + H(2)O = CC myo-inositol polyphosphate + phosphate. CC {ECO:0000269|PubMed:10419486, ECO:0000269|PubMed:12370170, CC ECO:0000269|PubMed:9822604}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:19585659}; CC Note=Binds 3 Mg(2+) ions per subunit. CC {ECO:0000269|PubMed:19585659}; CC -!- ENZYME REGULATION: Inhibited by fluoride and InsP6. CC {ECO:0000269|PubMed:19585659}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=5.9 uM for Ap6A {ECO:0000269|PubMed:10419486, CC ECO:0000269|PubMed:12370170, ECO:0000269|PubMed:9822604}; CC KM=7.7 uM for Ap5A {ECO:0000269|PubMed:10419486, CC ECO:0000269|PubMed:12370170, ECO:0000269|PubMed:9822604}; CC KM=38 mM for 5-phosphoribose 1-diphosphate CC {ECO:0000269|PubMed:10419486, ECO:0000269|PubMed:12370170, CC ECO:0000269|PubMed:9822604}; CC KM=4.2 nM for PP-InsP5 {ECO:0000269|PubMed:10419486, CC ECO:0000269|PubMed:12370170, ECO:0000269|PubMed:9822604}; CC pH dependence: CC Optimum pH is 7-7.5. {ECO:0000269|PubMed:10419486, CC ECO:0000269|PubMed:12370170, ECO:0000269|PubMed:9822604}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in CC brain, heart, pancreas and liver. Also expressed in placenta, lung CC and kidney. {ECO:0000269|PubMed:9822604}. CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DIPP subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 nudix hydrolase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00794}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF062529; AAC83224.1; -; mRNA. DR EMBL; AF062530; AAC83225.1; -; mRNA. DR EMBL; BT019984; AAV38787.1; -; mRNA. DR EMBL; BT019985; AAV38788.1; -; mRNA. DR EMBL; AK313440; BAG36231.1; -; mRNA. DR EMBL; Z98036; CAI19715.1; -; Genomic_DNA. DR EMBL; AL355855; CAI19715.1; JOINED; Genomic_DNA. DR EMBL; AL355855; CAH72222.1; -; Genomic_DNA. DR EMBL; Z98036; CAH72222.1; JOINED; Genomic_DNA. DR EMBL; CH471081; EAX03781.1; -; Genomic_DNA. DR EMBL; BC007727; AAH07727.1; -; mRNA. DR CCDS; CCDS4791.1; -. DR RefSeq; NP_006694.1; NM_006703.3. DR UniGene; Hs.188882; -. DR PDB; 2FVV; X-ray; 1.25 A; A=1-172. DR PDB; 2Q9P; X-ray; 1.65 A; A=1-172. DR PDBsum; 2FVV; -. DR PDBsum; 2Q9P; -. DR ProteinModelPortal; O95989; -. DR SMR; O95989; 8-142. DR BioGrid; 116336; 40. DR IntAct; O95989; 38. DR MINT; MINT-1412881; -. DR STRING; 9606.ENSP00000351650; -. DR PhosphoSite; O95989; -. DR BioMuta; NUDT3; -. DR MaxQB; O95989; -. DR PaxDb; O95989; -. DR PeptideAtlas; O95989; -. DR PRIDE; O95989; -. DR DNASU; 11165; -. DR Ensembl; ENST00000607016; ENSP00000476119; ENSG00000272325. DR GeneID; 11165; -. DR KEGG; hsa:11165; -. DR UCSC; uc003ojl.3; human. DR CTD; 11165; -. DR GeneCards; NUDT3; -. DR HGNC; HGNC:8050; NUDT3. DR HPA; HPA047027; -. DR HPA; HPA055953; -. DR MIM; 609228; gene. DR neXtProt; NX_O95989; -. DR PharmGKB; PA31834; -. DR eggNOG; ENOG410ISY6; Eukaryota. DR eggNOG; ENOG4111I7R; LUCA. DR GeneTree; ENSGT00390000012928; -. DR HOGENOM; HOG000237336; -. DR HOVERGEN; HBG053341; -. DR InParanoid; O95989; -. DR KO; K07766; -. DR OMA; LQESCLT; -. DR OrthoDB; EOG7T7GVQ; -. DR PhylomeDB; O95989; -. DR TreeFam; TF106349; -. DR BioCyc; MetaCyc:HS03602-MONOMER; -. DR BRENDA; 3.6.1.60; 2681. DR Reactome; R-HSA-1855167; Synthesis of pyrophosphates in the cytosol. DR SABIO-RK; O95989; -. DR ChiTaRS; NUDT3; human. DR EvolutionaryTrace; O95989; -. DR GeneWiki; NUDT3; -. DR GenomeRNAi; 11165; -. DR NextBio; 42479; -. DR PRO; PR:O95989; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; O95989; -. DR CleanEx; HS_NUDT3; -. DR Genevisible; O95989; HS. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0008486; F:diphosphoinositol-polyphosphate diphosphatase activity; IDA:UniProtKB. DR GO; GO:0052840; F:inositol diphosphate tetrakisphosphate diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0052846; F:inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 1-diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0052847; F:inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0052843; F:inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0052848; F:inositol-3,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0052844; F:inositol-3-diphosphate-1,2,4,5,6-pentakisphosphate diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0052845; F:inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc. DR GO; GO:0015961; P:diadenosine polyphosphate catabolic process; TAS:ProtInc. DR GO; GO:0071544; P:diphosphoinositol polyphosphate catabolic process; IDA:UniProtKB. DR GO; GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. 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; Acetylation; Complete proteome; Cytoplasm; Hydrolase; KW Magnesium; Metal-binding; Reference proteome. FT CHAIN 1 172 Diphosphoinositol polyphosphate FT phosphohydrolase 1. FT /FTId=PRO_0000057055. FT DOMAIN 17 142 Nudix hydrolase. {ECO:0000255|PROSITE- FT ProRule:PRU00794}. FT REGION 18 20 Substrate binding. FT REGION 89 91 Substrate binding. FT MOTIF 51 72 Nudix box. FT ACT_SITE 69 69 Proton acceptor. {ECO:0000305}. FT METAL 50 50 Magnesium 1; via carbonyl oxygen. FT METAL 66 66 Magnesium 2. FT METAL 66 66 Magnesium 3. FT METAL 70 70 Magnesium 1. FT BINDING 10 10 Substrate. FT BINDING 41 41 Substrate. FT MOD_RES 1 1 N-acetylmethionine. FT {ECO:0000244|PubMed:22814378}. FT MUTAGEN 50 50 G->A,V: Loss of function. FT {ECO:0000269|PubMed:10585413}. FT MUTAGEN 51 51 G->A: Loss of function. FT {ECO:0000269|PubMed:10585413}. FT MUTAGEN 52 52 G->A,V: Loss of function. FT {ECO:0000269|PubMed:10585413}. FT MUTAGEN 66 66 E->Q: Loss of function. FT {ECO:0000269|PubMed:10585413}. FT MUTAGEN 70 70 E->Q: Loss of function. FT {ECO:0000269|PubMed:9822604}. FT MUTAGEN 72 72 G->A: Loss of function. FT {ECO:0000269|PubMed:10585413}. FT MUTAGEN 75 75 G->A: Loss of function. FT {ECO:0000269|PubMed:10585413}. FT MUTAGEN 78 78 G->A: No effect. FT {ECO:0000269|PubMed:10585413}. FT MUTAGEN 78 78 G->V: Loss of function. FT {ECO:0000269|PubMed:10585413}. FT MUTAGEN 82 82 G->A: Loss of function. FT {ECO:0000269|PubMed:10585413}. FT MUTAGEN 84 84 F->Y: Induces a strong decrease in Ap6A FT and [PP]-InsP4 hydrolysis, while it only FT weakly affects PP-InsP5 hydrolysis. FT {ECO:0000269|PubMed:10585413}. FT MUTAGEN 91 91 H->L: Induces a strong decrease in Ap6A FT and [PP]-InsP4 hydrolysis, while it only FT weakly affects PP-InsP5 hydrolysis. FT {ECO:0000269|PubMed:10585413}. FT STRAND 18 28 {ECO:0000244|PDB:2FVV}. FT STRAND 33 38 {ECO:0000244|PDB:2FVV}. FT STRAND 45 47 {ECO:0000244|PDB:2FVV}. FT STRAND 49 52 {ECO:0000244|PDB:2FVV}. FT HELIX 59 71 {ECO:0000244|PDB:2FVV}. FT STRAND 73 86 {ECO:0000244|PDB:2FVV}. FT TURN 87 90 {ECO:0000244|PDB:2FVV}. FT STRAND 91 103 {ECO:0000244|PDB:2FVV}. FT HELIX 108 113 {ECO:0000244|PDB:2FVV}. FT STRAND 117 121 {ECO:0000244|PDB:2FVV}. FT HELIX 122 129 {ECO:0000244|PDB:2FVV}. FT TURN 130 132 {ECO:0000244|PDB:2FVV}. FT HELIX 134 139 {ECO:0000244|PDB:2FVV}. SQ SEQUENCE 172 AA; 19471 MW; DE823FECF5C6438A CRC64; MMKLKSNQTR TYDGDGYKKR AACLCFRSES EEEVLLVSSS RHPDRWIVPG GGMEPEEEPS VAAVREVCEE AGVKGTLGRL VGIFENQERK HRTYVYVLIV TEVLEDWEDS VNIGRKREWF KIEDAIKVLQ YHKPVQASYF ETLRQGYSAN NGTPVVATTY SVSAQSSMSG IR //