NUD18_RAT
ID NUD18_RAT Reviewed; 323 AA.
AC Q641Y7; Q4KM80;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=8-oxo-dGDP phosphatase NUDT18;
DE EC=3.6.1.58;
DE AltName: Full=2-hydroxy-dADP phosphatase;
DE AltName: Full=7,8-dihydro-8-oxoguanine phosphatase;
DE AltName: Full=MutT homolog 3;
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 18;
DE Short=Nudix motif 18;
GN Name=Nudt18; Synonyms=Mth3;
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, and Testis;
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).
CC -!- FUNCTION: Mediates the hydrolysis of oxidized nucleoside diphosphate
CC derivatives. Hydrolyzes 8-oxo-7,8-dihydroguanine (8-oxo-Gua)-containing
CC deoxyribo- and ribonucleoside diphosphates to the monophosphates.
CC Hydrolyzes 8-oxo-dGDP and 8-oxo-GDP with the same efficiencies.
CC Hydrolyzes also 8-OH-dADP and 2-OH-dADP. Exhibited no or minimal
CC hydrolysis activity against 8-oxo-dGTP, 8-oxo-GTP, dGTP, GTP, dGDP and
CC GDP. Probably removes oxidized guanine nucleotides from both the DNA
CC and RNA precursor pools (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8-oxo-dGDP + H2O = 8-oxo-dGMP + H(+) + phosphate;
CC Xref=Rhea:RHEA:32063, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:63224, ChEBI:CHEBI:63715; EC=3.6.1.58;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH82050.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH98710.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC082050; AAH82050.1; ALT_INIT; mRNA.
DR EMBL; BC098710; AAH98710.1; ALT_INIT; mRNA.
DR RefSeq; NP_001094202.1; NM_001100732.1.
DR AlphaFoldDB; Q641Y7; -.
DR SMR; Q641Y7; -.
DR STRING; 10116.ENSRNOP00000015969; -.
DR PaxDb; Q641Y7; -.
DR Ensembl; ENSRNOT00000015969; ENSRNOP00000015969; ENSRNOG00000011831.
DR GeneID; 361068; -.
DR KEGG; rno:361068; -.
DR UCSC; RGD:1311802; rat.
DR CTD; 79873; -.
DR RGD; 1311802; Nudt18.
DR eggNOG; KOG0648; Eukaryota.
DR GeneTree; ENSGT00390000002931; -.
DR HOGENOM; CLU_061042_2_0_1; -.
DR InParanoid; Q641Y7; -.
DR OMA; DHADGIC; -.
DR OrthoDB; 1327589at2759; -.
DR PhylomeDB; Q641Y7; -.
DR TreeFam; TF106355; -.
DR Reactome; R-RNO-2393930; Phosphate bond hydrolysis by NUDT proteins.
DR PRO; PR:Q641Y7; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000011831; Expressed in testis and 19 other tissues.
DR ExpressionAtlas; Q641Y7; baseline and differential.
DR Genevisible; Q641Y7; RN.
DR GO; GO:0044717; F:8-hydroxy-dADP phosphatase activity; ISS:UniProtKB.
DR GO; GO:0044715; F:8-oxo-dGDP phosphatase activity; ISS:UniProtKB.
DR GO; GO:0044716; F:8-oxo-GDP phosphatase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0046057; P:dADP catabolic process; ISS:UniProtKB.
DR GO; GO:0046067; P:dGDP catabolic process; ISS:UniProtKB.
DR GO; GO:0046712; P:GDP catabolic process; ISS:UniProtKB.
DR CDD; cd04671; Nudix_Hydrolase_13; 1.
DR InterPro; IPR020476; Nudix_hydrolase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR042970; NUDT18_NUDIX.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Nucleotide metabolism;
KW Reference proteome.
FT CHAIN 1..323
FT /note="8-oxo-dGDP phosphatase NUDT18"
FT /id="PRO_0000324569"
FT DOMAIN 37..167
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 76..97
FT /note="Nudix box"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 323 AA; 35647 MW; 82B49A0C7878B545 CRC64;
MATEGLAGAL ATVLGGKGLL VQSCDSEPAG KPLLPVRLRK NVCYVVLAVF LNEQDEVLMI
QEAKRECRGT WYLPAGRMEP GETIVEAMQR EVKEEAGLLC EPVTLLSVEE RGASWIRFVF
LARPTGGVLK TSKNADSESL QAGWYPRVSL PTPLRAHDVV HLVELGAKFC QQATHPLILP
QELPCNMVCQ RLVATFTTVQ SVWVLVGTVG TPHLPITACG FTPMEQRGGI KVAILRLLQE
CLTLHSLAVE TKGLLGLQHL GRDHVDGICL NVLVTVAFRN PGIQDEPPKI RGENYFWWKV
LEEDLQKQLL HRLQESSVVP LTR
