NUDT4_RAT
ID NUDT4_RAT Reviewed; 179 AA.
AC Q99MY2;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Diphosphoinositol polyphosphate phosphohydrolase 2 {ECO:0000305};
DE Short=DIPP-2;
DE Short=rDIPP2;
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:0000312|RGD:621355}; Synonyms=Dipp2;
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 [MRNA], AND INDUCTION.
RC STRAIN=Sprague-Dawley;
RX PubMed=11331144; DOI=10.1016/s0893-133x(00)00233-5;
RA Hua L.V., Green M., Warsh J.J., Li P.P.;
RT "Molecular cloning of a novel isoform of diphosphoinositol polyphosphate
RT phosphohydrolase: a potential target of lithium therapy.";
RL Neuropsychopharmacology 24:640-651(2001).
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.
CC {ECO:0000250|UniProtKB:Q96G61};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NZJ9}.
CC -!- INDUCTION: Overexpressed in frontal cortex upon chronic lithium
CC treatment. {ECO:0000269|PubMed:11331144}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DIPP subfamily.
CC {ECO:0000305}.
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DR EMBL; AF253473; AAK29279.1; -; mRNA.
DR RefSeq; NP_446050.1; NM_053598.1.
DR AlphaFoldDB; Q99MY2; -.
DR SMR; Q99MY2; -.
DR IntAct; Q99MY2; 1.
DR STRING; 10116.ENSRNOP00000012363; -.
DR iPTMnet; Q99MY2; -.
DR PhosphoSitePlus; Q99MY2; -.
DR jPOST; Q99MY2; -.
DR PaxDb; Q99MY2; -.
DR GeneID; 94267; -.
DR KEGG; rno:94267; -.
DR UCSC; RGD:621355; rat.
DR CTD; 11163; -.
DR RGD; 621355; Nudt4.
DR VEuPathDB; HostDB:ENSRNOG00000009094; -.
DR eggNOG; KOG2839; Eukaryota.
DR HOGENOM; CLU_037162_1_0_1; -.
DR InParanoid; Q99MY2; -.
DR OMA; PEEDPCG; -.
DR OrthoDB; 1324716at2759; -.
DR PhylomeDB; Q99MY2; -.
DR TreeFam; TF106349; -.
DR Reactome; R-RNO-1855167; Synthesis of pyrophosphates in the cytosol.
DR PRO; PR:Q99MY2; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000009094; Expressed in kidney and 20 other tissues.
DR Genevisible; Q99MY2; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IEA:UniProtKB-EC.
DR GO; GO:0052840; F:inositol diphosphate tetrakisphosphate diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0050072; F:m7G(5')pppN diphosphatase activity; IBA:GO_Central.
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: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:0046488; P:phosphatidylinositol metabolic process; NAS:RGD.
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 Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Reference proteome; RNA-binding.
FT CHAIN 1..179
FT /note="Diphosphoinositol polyphosphate phosphohydrolase 2"
FT /id="PRO_0000057061"
FT DOMAIN 17..143
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 50..71
FT /note="Nudix box"
FT ACT_SITE 68
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 17..19
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 38..40
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 49
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 65
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 65
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 88..90
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
SQ SEQUENCE 179 AA; 20138 MW; DE59B9CCA615A6A9 CRC64;
MKFKPNQTRT YDREGFKKRA ACLCFRSEQE DEVLLVSSSR YPDQWIVPGG GVEPEEEPGG
AAAREVYEEA GVKGKLGRLL GIFENQDRKH RTYVYVLTVT EILEDWEDSV NIGRKREWFK
VEDAIKVLQC HKPVHAEYLE RLKLGCSPTN GNSTVPSLPD NNALFVTAAP PSGVPSSIR
