NUDT3_RAT
ID NUDT3_RAT Reviewed; 168 AA.
AC Q566C7;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Diphosphoinositol polyphosphate phosphohydrolase 1 {ECO:0000305};
DE Short=DIPP-1;
DE EC=3.6.1.52 {ECO:0000269|PubMed:9822604};
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 {ECO:0000312|RGD:1310183}; Synonyms=Dipp, Dipp1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [2]
RP PROTEIN SEQUENCE OF 3-17; 20-115 AND 117-121, FUNCTION, ENZYME ACTIVITY,
RP COFACTOR, ACTIVITY REGULATION, AND SUBUNIT.
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, in a
RT diphosphoinositol polyphosphate phosphohydrolase.";
RL EMBO J. 17:6599-6607(1998).
CC -!- FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-
CC InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4
CC (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a
CC role in signal transduction (PubMed:9822604). InsP6 (inositol
CC hexakisphosphate) is not a substrate (By similarity). Acts as a
CC negative regulator of the ERK1/2 pathway (By similarity). Also able to
CC catalyze the hydrolysis of dinucleoside oligophosphates, with
CC diadenosine 5',5'''-P1,P6-hexaphosphate (Ap6A) and diadenosine
CC 5',5'''- P1,P5-pentaphosphate (Ap5A) being the preferred substrates (By
CC similarity). The major reaction products are ADP and p4a from Ap6A and
CC ADP and ATP from Ap5A (By similarity). Also able to hydrolyze
CC 5- phosphoribose 1-diphosphate (By similarity). Acts as a decapping
CC enzyme that modulates the stability of a subset of mRNAs implicated in
CC cell motility (By similarity). {ECO:0000250|UniProtKB:O95989,
CC ECO:0000250|UniProtKB:Q9JI46, ECO:0000269|PubMed:9822604}.
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:9822604};
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:9822604};
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:9822604};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O95989};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:O95989};
CC -!- ACTIVITY REGULATION: Inhibited by fluoride and InsP6.
CC {ECO:0000269|PubMed:9822604}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=340 nM for PP-InsP5 {ECO:0000269|PubMed:9822604};
CC KM=34 nM for [PP]2-InsP4 {ECO:0000269|PubMed:9822604};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9822604}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DIPP subfamily.
CC {ECO:0000305}.
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DR EMBL; BC093618; AAH93618.1; -; mRNA.
DR RefSeq; NP_001019414.1; NM_001024243.1.
DR AlphaFoldDB; Q566C7; -.
DR SMR; Q566C7; -.
DR STRING; 10116.ENSRNOP00000000581; -.
DR jPOST; Q566C7; -.
DR PaxDb; Q566C7; -.
DR PRIDE; Q566C7; -.
DR Ensembl; ENSRNOT00000083169; ENSRNOP00000074608; ENSRNOG00000061176.
DR GeneID; 294292; -.
DR KEGG; rno:294292; -.
DR UCSC; RGD:1310183; rat.
DR CTD; 11165; -.
DR RGD; 1310183; Nudt3.
DR eggNOG; KOG2839; Eukaryota.
DR GeneTree; ENSGT00940000157882; -.
DR HOGENOM; CLU_037162_1_0_1; -.
DR InParanoid; Q566C7; -.
DR OMA; VKVLQYH; -.
DR OrthoDB; 1324716at2759; -.
DR PhylomeDB; Q566C7; -.
DR TreeFam; TF106349; -.
DR Reactome; R-RNO-1855167; Synthesis of pyrophosphates in the cytosol.
DR PRO; PR:Q566C7; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000061176; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; Q566C7; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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; ISS:UniProtKB.
DR GO; GO:0052840; F:inositol diphosphate tetrakisphosphate diphosphatase activity; ISS:UniProtKB.
DR GO; GO:0050072; F:m7G(5')pppN diphosphatase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
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:0071544; P:diphosphoinositol polyphosphate catabolic process; ISS:UniProtKB.
DR GO; GO:0071543; P:diphosphoinositol polyphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0110154; P:RNA decapping; ISS:UniProtKB.
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 Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase; Magnesium;
KW Metal-binding; Reference proteome.
FT CHAIN 1..168
FT /note="Diphosphoinositol polyphosphate phosphohydrolase 1"
FT /id="PRO_0000057057"
FT DOMAIN 17..142
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:0000250|UniProtKB:O95989"
SQ SEQUENCE 168 AA; 19096 MW; 6743B325524B634E CRC64;
MMKLKSNQTR TYDGDGYKKR AACLCFRSES EEEVLLVSSS RHPDRWIVPG GGMEPEEEPS
VAAVREVCEE AGVKGTLGRL VGIFENQERK HRTYVYVLIV TEVLEDWEDS VNIGRKREWF
KIEEAVKVLQ YHKPVQASYF EALRQGYSAN NGTPVLPTTY SSSMSGIR
