ID   NUD18_HUMAN             Reviewed;         323 AA.
AC   Q6ZVK8; Q8IZ75; Q9H687;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2013, sequence version 3.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=8-oxo-dGDP phosphatase NUDT18 {ECO:0000305|PubMed:22556419};
DE            EC=3.6.1.58 {ECO:0000269|PubMed:22556419};
DE   AltName: Full=2-hydroxy-dADP phosphatase;
DE   AltName: Full=7,8-dihydro-8-oxoguanine phosphatase;
DE   AltName: Full=MutT homolog 3 {ECO:0000303|PubMed:22556419};
DE   AltName: Full=Nucleoside diphosphate-linked moiety X motif 18;
DE            Short=Nudix motif 18;
GN   Name=NUDT18 {ECO:0000312|HGNC:HGNC:26194};
GN   Synonyms=MTH3 {ECO:0000303|PubMed:22556419};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Cerebellum;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Uterus;
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   [4]
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND FUNCTION.
RX   PubMed=22556419; DOI=10.1074/jbc.m112.363010;
RA   Takagi Y., Setoyama D., Ito R., Kamiya H., Yamagata Y., Sekiguchi M.;
RT   "Human MTH3 (NUDT18) protein hydrolyzes oxidized forms of guanosine and
RT   deoxyguanosine diphosphates: comparison with MTH1 and MTH2.";
RL   J. Biol. Chem. 287:21541-21549(2012).
RN   [5] {ECO:0007744|PDB:3GG6}
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 26-179.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of the nudix domain of human nudt18.";
RL   Submitted (MAR-2009) to the PDB data bank.
RN   [6] {ECO:0007744|PDB:4HVY}
RP   X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 26-179 IN COMPLEX WITH MG(2+).
RX   PubMed=24352381; DOI=10.1038/ncomms3901;
RA   Asial I., Cheng Y.X., Engman H., Dollhopf M., Wu B., Nordlund P.,
RA   Cornvik T.;
RT   "Engineering protein thermostability using a generic activity-independent
RT   biophysical screen inside the cell.";
RL   Nat. Commun. 4:2901-2901(2013).
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. {ECO:0000269|PubMed:22556419}.
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         Evidence={ECO:0000269|PubMed:22556419};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32064;
CC         Evidence={ECO:0000305|PubMed:22556419};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=8-oxo-dADP + H2O = 8-oxo-dAMP + H(+) + phosphate;
CC         Xref=Rhea:RHEA:35219, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:71361, ChEBI:CHEBI:71362;
CC         Evidence={ECO:0000269|PubMed:22556419};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35220;
CC         Evidence={ECO:0000305|PubMed:22556419};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxo-dADP + H2O = 2-oxo-dAMP + H(+) + phosphate;
CC         Xref=Rhea:RHEA:35223, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:63212, ChEBI:CHEBI:71363;
CC         Evidence={ECO:0000269|PubMed:22556419};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35224;
CC         Evidence={ECO:0000305|PubMed:22556419};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=8-oxo-GDP + H2O = 8-oxo-GMP + H(+) + phosphate;
CC         Xref=Rhea:RHEA:62356, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:143554, ChEBI:CHEBI:145694;
CC         EC=3.6.1.58; Evidence={ECO:0000305|PubMed:22556419};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62357;
CC         Evidence={ECO:0000305|PubMed:22556419};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:22556419};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:22556419};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=10.7 uM for 8-Oxo-dGDP {ECO:0000269|PubMed:22556419};
CC         KM=11.7 uM for 8-Oxo-GDP {ECO:0000269|PubMed:22556419};
CC         Vmax=212 pmol/min/ug enzyme toward 8-Oxo-dGDP (at 30 degrees Celsius)
CC         {ECO:0000269|PubMed:22556419};
CC         Vmax=246 pmol/min/ug enzyme toward 8-Oxo-GDP (at 30 degrees Celsius)
CC         {ECO:0000269|PubMed:22556419};
CC       pH dependence:
CC         Optimum pH is 8.5. {ECO:0000269|PubMed:22556419};
CC   -!- INTERACTION:
CC       Q6ZVK8; Q96GX9: APIP; NbExp=4; IntAct=EBI-740486, EBI-359248;
CC       Q6ZVK8; P49366: DHPS; NbExp=3; IntAct=EBI-740486, EBI-741925;
CC       Q6ZVK8; P33316: DUT; NbExp=3; IntAct=EBI-740486, EBI-353224;
CC       Q6ZVK8; Q96CN4: EVI5L; NbExp=3; IntAct=EBI-740486, EBI-749523;
CC       Q6ZVK8; Q9BPX1: HSD17B14; NbExp=3; IntAct=EBI-740486, EBI-742664;
CC       Q6ZVK8; P49902: NT5C2; NbExp=3; IntAct=EBI-740486, EBI-742084;
CC       Q6ZVK8; P22234: PAICS; NbExp=3; IntAct=EBI-740486, EBI-712261;
CC       Q6ZVK8; Q8TBN0: RAB3IL1; NbExp=3; IntAct=EBI-740486, EBI-743796;
CC       Q6ZVK8; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-740486, EBI-712367;
CC       Q6ZVK8; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-740486, EBI-750109;
CC       Q6ZVK8; P03410: tax; Xeno; NbExp=4; IntAct=EBI-740486, EBI-9676218;
CC       Q6ZVK8; P14079: tax; Xeno; NbExp=5; IntAct=EBI-740486, EBI-9675698;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6ZVK8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZVK8-2; Sequence=VSP_032276, VSP_032277;
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC85853.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK026147; BAB15376.1; -; mRNA.
DR   EMBL; AK124446; BAC85853.1; ALT_INIT; mRNA.
DR   EMBL; BC016902; AAH16902.1; -; mRNA.
DR   CCDS; CCDS75706.1; -. [Q6ZVK8-1]
DR   RefSeq; NP_079091.3; NM_024815.3. [Q6ZVK8-1]
DR   PDB; 3GG6; X-ray; 2.10 A; A=26-179.
DR   PDB; 4HVY; X-ray; 1.46 A; A=26-179.
DR   PDBsum; 3GG6; -.
DR   PDBsum; 4HVY; -.
DR   AlphaFoldDB; Q6ZVK8; -.
DR   SMR; Q6ZVK8; -.
DR   BioGRID; 122961; 53.
DR   IntAct; Q6ZVK8; 43.
DR   MINT; Q6ZVK8; -.
DR   STRING; 9606.ENSP00000480722; -.
DR   iPTMnet; Q6ZVK8; -.
DR   PhosphoSitePlus; Q6ZVK8; -.
DR   BioMuta; NUDT18; -.
DR   DMDM; 460018323; -.
DR   EPD; Q6ZVK8; -.
DR   jPOST; Q6ZVK8; -.
DR   MassIVE; Q6ZVK8; -.
DR   MaxQB; Q6ZVK8; -.
DR   PaxDb; 9606-ENSP00000480722; -.
DR   PeptideAtlas; Q6ZVK8; -.
DR   ProteomicsDB; 68421; -. [Q6ZVK8-1]
DR   ProteomicsDB; 68422; -. [Q6ZVK8-2]
DR   Pumba; Q6ZVK8; -.
DR   Antibodypedia; 74437; 220 antibodies from 21 providers.
DR   DNASU; 79873; -.
DR   Ensembl; ENST00000611621.2; ENSP00000480722.1; ENSG00000275074.2. [Q6ZVK8-1]
DR   GeneID; 79873; -.
DR   KEGG; hsa:79873; -.
DR   MANE-Select; ENST00000611621.2; ENSP00000480722.1; NM_024815.4; NP_079091.3.
DR   UCSC; uc033beu.2; human. [Q6ZVK8-1]
DR   AGR; HGNC:26194; -.
DR   CTD; 79873; -.
DR   DisGeNET; 79873; -.
DR   GeneCards; NUDT18; -.
DR   HGNC; HGNC:26194; NUDT18.
DR   HPA; ENSG00000275074; Low tissue specificity.
DR   MIM; 615791; gene.
DR   neXtProt; NX_Q6ZVK8; -.
DR   OpenTargets; ENSG00000275074; -.
DR   PharmGKB; PA142671238; -.
DR   VEuPathDB; HostDB:ENSG00000275074; -.
DR   eggNOG; KOG0648; Eukaryota.
DR   GeneTree; ENSGT00390000002931; -.
DR   HOGENOM; CLU_061042_2_0_1; -.
DR   InParanoid; Q6ZVK8; -.
DR   OMA; PSCAGKW; -.
DR   OrthoDB; 2899128at2759; -.
DR   PhylomeDB; Q6ZVK8; -.
DR   TreeFam; TF106355; -.
DR   BioCyc; MetaCyc:ENSG00000173566-MONOMER; -.
DR   PathwayCommons; Q6ZVK8; -.
DR   Reactome; R-HSA-2393930; Phosphate bond hydrolysis by NUDT proteins. [Q6ZVK8-1]
DR   SABIO-RK; Q6ZVK8; -.
DR   SignaLink; Q6ZVK8; -.
DR   BioGRID-ORCS; 79873; 12 hits in 361 CRISPR screens.
DR   EvolutionaryTrace; Q6ZVK8; -.
DR   GenomeRNAi; 79873; -.
DR   Pharos; Q6ZVK8; Tbio.
DR   PRO; PR:Q6ZVK8; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q6ZVK8; Protein.
DR   Bgee; ENSG00000275074; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 119 other cell types or tissues.
DR   ExpressionAtlas; Q6ZVK8; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0044717; F:8-hydroxy-dADP phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0044715; F:8-oxo-dGDP phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0044716; F:8-oxo-GDP phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR   GO; GO:0046057; P:dADP catabolic process; IDA:UniProtKB.
DR   GO; GO:0046067; P:dGDP catabolic process; IDA:UniProtKB.
DR   GO; GO:0046712; P:GDP catabolic process; IDA:UniProtKB.
DR   GO; GO:0055086; P:nucleobase-containing small molecule metabolic process; TAS:Reactome.
DR   CDD; cd04671; Nudix_Hydrolase_13; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 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   PANTHER; PTHR22769:SF56; 8-OXO-DGDP PHOSPHATASE NUDT18; 1.
DR   PANTHER; PTHR22769; MUTT/NUDIX HYDROLASE; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
DR   Genevisible; Q6ZVK8; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Hydrolase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide metabolism; Reference proteome.
FT   CHAIN           1..323
FT                   /note="8-oxo-dGDP phosphatase NUDT18"
FT                   /id="PRO_0000324567"
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         58
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007744|PDB:4HVY"
FT   VAR_SEQ         1..100
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_032276"
FT   VAR_SEQ         101..125
FT                   /note="EPETLLSVEERGPSWVRFVFLARPT -> MSVDSARAALLSTQTLPAPSPTS
FT                   PP (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_032277"
FT   CONFLICT        177
FT                   /note="L -> P (in Ref. 1; BAB15376)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        224
FT                   /note="M -> V (in Ref. 1; BAB15376/BAC85853)"
FT                   /evidence="ECO:0000305"
FT   STRAND          43..49
FT                   /evidence="ECO:0007829|PDB:4HVY"
FT   STRAND          55..61
FT                   /evidence="ECO:0007829|PDB:4HVY"
FT   HELIX           65..67
FT                   /evidence="ECO:0007829|PDB:4HVY"
FT   STRAND          74..77
FT                   /evidence="ECO:0007829|PDB:4HVY"
FT   HELIX           84..96
FT                   /evidence="ECO:0007829|PDB:4HVY"
FT   STRAND          98..112
FT                   /evidence="ECO:0007829|PDB:4HVY"
FT   STRAND          115..127
FT                   /evidence="ECO:0007829|PDB:4HVY"
FT   HELIX           132..134
FT                   /evidence="ECO:0007829|PDB:4HVY"
FT   STRAND          136..138
FT                   /evidence="ECO:0007829|PDB:3GG6"
FT   STRAND          140..146
FT                   /evidence="ECO:0007829|PDB:4HVY"
FT   STRAND          152..155
FT                   /evidence="ECO:0007829|PDB:4HVY"
FT   HELIX           158..172
FT                   /evidence="ECO:0007829|PDB:4HVY"
SQ   SEQUENCE   323 AA;  35501 MW;  8162BA4BDEC4374D CRC64;
     MASEGLAGAL ASVLAGQGSS VHSCDSAPAG EPPAPVRLRK NVCYVVLAVF LSEQDEVLLI
     QEAKRECRGS WYLPAGRMEP GETIVEALQR EVKEEAGLHC EPETLLSVEE RGPSWVRFVF
     LARPTGGILK TSKEADAESL QAAWYPRTSL PTPLRAHDIL HLVELAAQYR QQARHPLILP
     QELPCDLVCQ RLVATFTSAQ TVWVLVGTVG MPHLPVTACG LDPMEQRGGM KMAVLRLLQE
     CLTLHHLVVE IKGLLGLQHL GRDHSDGICL NVLVTVAFRS PGIQDEPPKV RGENFSWWKV
     MEEDLQSQLL QRLQGSSVVP VNR
//