NUDT3_BOVIN
ID NUDT3_BOVIN Reviewed; 172 AA.
AC A2VE79;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Diphosphoinositol polyphosphate phosphohydrolase 1 {ECO:0000250|UniProtKB:O95989};
DE Short=DIPP-1;
DE EC=3.6.1.52 {ECO:0000250|UniProtKB:O95989};
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:0000250|UniProtKB:O95989}; Synonyms=DIPP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal lung;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). InsP6 (inositol
CC hexakisphosphate) is not a substrate (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:Q566C7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphospho-myo-inositol polyphosphate + H2O = myo-inositol
CC polyphosphate + phosphate.; EC=3.6.1.52;
CC Evidence={ECO:0000250|UniProtKB:O95989};
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:0000250|UniProtKB:O95989};
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:0000250|UniProtKB:O95989};
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:0000250|UniProtKB:O95989}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q566C7}.
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; BC133614; AAI33615.1; -; mRNA.
DR RefSeq; NP_001075935.1; NM_001082466.2.
DR AlphaFoldDB; A2VE79; -.
DR SMR; A2VE79; -.
DR STRING; 9913.ENSBTAP00000026239; -.
DR PaxDb; A2VE79; -.
DR PRIDE; A2VE79; -.
DR Ensembl; ENSBTAT00000026239; ENSBTAP00000026239; ENSBTAG00000019684.
DR GeneID; 618855; -.
DR KEGG; bta:618855; -.
DR CTD; 11165; -.
DR VEuPathDB; HostDB:ENSBTAG00000019684; -.
DR VGNC; VGNC:32338; NUDT3.
DR eggNOG; KOG2839; Eukaryota.
DR GeneTree; ENSGT00940000157882; -.
DR HOGENOM; CLU_037162_1_0_1; -.
DR InParanoid; A2VE79; -.
DR OMA; VKVLQYH; -.
DR OrthoDB; 1324716at2759; -.
DR TreeFam; TF106349; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000019684; Expressed in temporal cortex and 102 other tissues.
DR ExpressionAtlas; A2VE79; baseline.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..172
FT /note="Diphosphoinositol polyphosphate phosphohydrolase 1"
FT /id="PRO_0000297487"
FT DOMAIN 17..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:0000250|UniProtKB:O95989"
SQ SEQUENCE 172 AA; 19362 MW; E399197DEADCC786 CRC64;
MMKLKSNQTR TYDGDGYKKR AACLCFRSES EEEVLLVSSS RHPDRWIVPG GGMEPEEEPG
TAAVREVCEE AGVKGTLGRL VGIFENQERK HRTYVYVLIV TEVLEDWEDS VSIGRKREWF
KIEDAINVLQ CHKPVQASYF ETLRQGYSAN NGTPLVAPTY SVSAQSSMPG IR
