NUD18_MOUSE
ID NUD18_MOUSE Reviewed; 323 AA.
AC Q3U2V3; Q8C223; Q8K1Y7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Inner ear, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3U2V3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U2V3-2; Sequence=VSP_032279;
CC Name=3;
CC IsoId=Q3U2V3-3; Sequence=VSP_032278;
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; AK089446; BAC40887.1; -; mRNA.
DR EMBL; AK145997; BAE26818.1; -; mRNA.
DR EMBL; AK155086; BAE33037.1; -; mRNA.
DR EMBL; AK157937; BAE34271.1; -; mRNA.
DR EMBL; BC036718; AAH36718.1; -; mRNA.
DR CCDS; CCDS27258.1; -. [Q3U2V3-1]
DR RefSeq; NP_694776.2; NM_153136.4. [Q3U2V3-1]
DR RefSeq; XP_006518856.1; XM_006518793.2.
DR AlphaFoldDB; Q3U2V3; -.
DR SMR; Q3U2V3; -.
DR BioGRID; 229442; 1.
DR STRING; 10090.ENSMUSP00000086450; -.
DR PhosphoSitePlus; Q3U2V3; -.
DR SwissPalm; Q3U2V3; -.
DR EPD; Q3U2V3; -.
DR MaxQB; Q3U2V3; -.
DR PaxDb; Q3U2V3; -.
DR PRIDE; Q3U2V3; -.
DR ProteomicsDB; 293809; -. [Q3U2V3-1]
DR ProteomicsDB; 293810; -. [Q3U2V3-2]
DR ProteomicsDB; 293811; -. [Q3U2V3-3]
DR Antibodypedia; 74437; 182 antibodies from 21 providers.
DR DNASU; 213484; -.
DR Ensembl; ENSMUST00000089049; ENSMUSP00000086450; ENSMUSG00000045211. [Q3U2V3-1]
DR GeneID; 213484; -.
DR KEGG; mmu:213484; -.
DR UCSC; uc007uok.1; mouse. [Q3U2V3-1]
DR CTD; 79873; -.
DR MGI; MGI:2385853; Nudt18.
DR VEuPathDB; HostDB:ENSMUSG00000045211; -.
DR eggNOG; KOG0648; Eukaryota.
DR GeneTree; ENSGT00390000002931; -.
DR HOGENOM; CLU_061042_2_0_1; -.
DR InParanoid; Q3U2V3; -.
DR OMA; DHADGIC; -.
DR OrthoDB; 1327589at2759; -.
DR PhylomeDB; Q3U2V3; -.
DR TreeFam; TF106355; -.
DR Reactome; R-MMU-2393930; Phosphate bond hydrolysis by NUDT proteins.
DR BioGRID-ORCS; 213484; 4 hits in 72 CRISPR screens.
DR PRO; PR:Q3U2V3; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q3U2V3; protein.
DR Bgee; ENSMUSG00000045211; Expressed in seminiferous tubule of testis and 214 other tissues.
DR ExpressionAtlas; Q3U2V3; baseline and differential.
DR Genevisible; Q3U2V3; MM.
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 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nucleotide metabolism; Reference proteome.
FT CHAIN 1..323
FT /note="8-oxo-dGDP phosphatase NUDT18"
FT /id="PRO_0000324568"
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"
FT VAR_SEQ 1..173
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032278"
FT VAR_SEQ 1..77
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032279"
SQ SEQUENCE 323 AA; 35694 MW; 6056DF1DB350CF9F CRC64;
MATEGLAGAL ATVLGGKGLL VQSCDSEPAG KPLFPVRLRK NVCYVVLAVF LNEQDEVLMI
QEAKRECRGT WYLPAGRMEP GETIVEAMQR EVKEEAGLLC EPVTLLSVEE RGASWIRFVF
LARPTGGVLK TSKDADSESL QAGWYPRVSL PTPLRAHDVL HLVELGAKFC QQAMHPLILP
QELPCSVVCQ RLVTTFTTVQ SVWVLVGTVG TPHLPITACG FTPMEQRGGI KVAILRLLQE
CLTLHSLAVE TKGLLGLQHL GRDHVDGVCL NVLVTVAFRN PGIQDEPPKI RGENYFWWKV
LEEDLQKLLL YRLQESSVIP LSR
