NUDT4_PONAB
ID NUDT4_PONAB Reviewed; 180 AA.
AC Q5RAF0;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Diphosphoinositol polyphosphate phosphohydrolase 2 {ECO:0000250|UniProtKB:Q9NZJ9};
DE Short=DIPP-2;
DE EC=3.6.1.52 {ECO:0000250|UniProtKB:Q9NZJ9};
DE AltName: Full=Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 2;
DE EC=3.6.1.-;
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 4;
DE Short=Nudix motif 4;
GN Name=NUDT4 {ECO:0000250|UniProtKB:Q9NZJ9}; Synonyms=DIPP2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Can also catalyze the
CC hydrolysis of diadenosine 5',5'''-P1,P6-hexaphosphate (Ap6A) but not
CC diadenosine 5',5'''-P1,P5-pentaphosphate (Ap5A) and the major reaction
CC products are ADP and p4a from Ap6A (By similarity). Also able to
CC hydrolyze 5-phosphoribose 1-diphosphate (By similarity). Does not play
CC a role in U8 snoRNA decapping activity (By similarity). Binds U8 snoRNA
CC (By similarity). {ECO:0000250|UniProtKB:Q8R2U6,
CC ECO:0000250|UniProtKB:Q9NZJ9}.
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:Q9NZJ9};
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:Q9NZJ9};
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:Q9NZJ9};
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. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q96G61};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NZJ9}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DIPP subfamily.
CC {ECO:0000305}.
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DR EMBL; CR859067; CAH91260.1; -; mRNA.
DR RefSeq; NP_001125746.1; NM_001132274.1.
DR AlphaFoldDB; Q5RAF0; -.
DR SMR; Q5RAF0; -.
DR STRING; 9601.ENSPPYP00000005509; -.
DR GeneID; 100172671; -.
DR KEGG; pon:100172671; -.
DR CTD; 11163; -.
DR eggNOG; KOG2839; Eukaryota.
DR HOGENOM; CLU_037162_1_0_1; -.
DR InParanoid; Q5RAF0; -.
DR OMA; NTNPRHN; -.
DR TreeFam; TF106349; -.
DR Proteomes; UP000001595; Chromosome 12.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008486; F:diphosphoinositol-polyphosphate diphosphatase activity; IEA:UniProtKB-EC.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030515; F:snoRNA binding; 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; Manganese; Metal-binding;
KW Reference proteome; RNA-binding.
FT CHAIN 1..180
FT /note="Diphosphoinositol polyphosphate phosphohydrolase 2"
FT /id="PRO_0000057060"
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:0000250|UniProtKB:Q9NZJ9"
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
