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Protein

7,8-dihydro-8-oxoguanine triphosphatase

Gene

Nudt1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Antimutagenic. Acts as a sanitizing enzyme for oxidized nucleotide pools, thus suppressing cell dysfunction and death induced by oxidative stress. Hydrolyzes 8-oxo-dGTP, 8-oxo-dATP and 2-OH-dATP, thus preventing misincorporation of oxidized purine nucleoside triphosphates into DNA and subsequently preventing A:T to C:G and G:C to T:A transversions. Able to hydrolyze also the corresponding ribonucleotides, 2-OH-ATP, 8-oxo-GTP and 8-oxo-ATP. Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA.1 Publication

Catalytic activityi

8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate.1 Publication
2-hydroxy-dATP + H2O = 2-hydroxy-dAMP + diphosphate.1 Publication

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Enzyme regulationi

2-hydroxy-dATPase activity is inhibited by 2-OH-dADP, 8-OH-dGDP and 8-OH-dGTP. 8-OH-dGTPase activity is inhibited by 8-OH-dGDP, 2-OH-dADP and 2-OH-dATP (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei8 – 81Substrate; via carbonyl oxygenBy similarity
Binding sitei27 – 271SubstrateBy similarity
Sitei27 – 271Important for 2-OH-dATPase and 8-oxo-dGTPase activitiesBy similarity
Binding sitei33 – 331SubstrateBy similarity
Metal bindingi37 – 371Magnesium; via carbonyl oxygenBy similarity
Metal bindingi52 – 521MagnesiumBy similarity
Metal bindingi55 – 551MagnesiumBy similarity
Metal bindingi56 – 561MagnesiumBy similarity
Sitei117 – 1171Essential for 2-OH-dATPase and 8-oxo-dGTPase activitiesBy similarity
Sitei119 – 1191Essential for 2-OH-dATPase activity and important for 8-oxo-dGTPase activityBy similarity

GO - Molecular functioni

GO - Biological processi

  • aging Source: RGD
  • dATP catabolic process Source: UniProtKB
  • dGTP catabolic process Source: UniProtKB
  • DNA protection Source: UniProtKB
  • DNA repair Source: InterPro
  • male gonad development Source: RGD
  • purine nucleotide catabolic process Source: UniProtKB
  • response to cadmium ion Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding, RNA-binding

Enzyme and pathway databases

ReactomeiR-RNO-2393930. Phosphate bond hydrolysis by NUDT proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
7,8-dihydro-8-oxoguanine triphosphatase (EC:3.6.1.55)
Alternative name(s):
2-hydroxy-dATP diphosphatase (EC:3.6.1.56)
8-oxo-dGTPase
Nucleoside diphosphate-linked moiety X motif 1
Short name:
Nudix motif 1
Gene namesi
Name:Nudt1
Synonyms:Mth1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 12

Organism-specific databases

RGDi621080. Nudt1.

Subcellular locationi

GO - Cellular componenti

  • acrosomal vesicle Source: RGD
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: Ensembl
  • extracellular space Source: RGD
  • mitochondrial matrix Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • nuclear membrane Source: RGD
  • nucleus Source: UniProtKB
  • plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 1561367,8-dihydro-8-oxoguanine triphosphatasePRO_0000057101Add
BLAST

Proteomic databases

PaxDbiP53369.

Expressioni

Tissue specificityi

Expressed in liver in hepatocytes and weakly in Kupffer's cells. Expression detected in testes in primary and secondary spermatocytes and interstitial cells. High expression levels detected in the inner cortex of kidney, with lower levels detected in the tubules of the outer cortex, medulla, renal pelvis and glomeruli (at protein level). Expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis.2 Publications

Gene expression databases

GenevisibleiP53369. RN.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001700.

Structurei

3D structure databases

ProteinModelPortaliP53369.
SMRiP53369. Positions 1-154.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 132112Nudix hydrolasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni35 – 384Substrate bindingBy similarity
Regioni117 – 1204Substrate bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi37 – 5822Nudix boxAdd
BLAST

Sequence similaritiesi

Belongs to the Nudix hydrolase family.Curated
Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IXIA. Eukaryota.
COG0494. LUCA.
GeneTreeiENSGT00390000000341.
HOGENOMiHOG000261970.
HOVERGENiHBG000032.
InParanoidiP53369.
KOiK17816.
OMAiGAGKWNG.
OrthoDBiEOG7BS4BT.
PhylomeDBiP53369.
TreeFamiTF106348.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR020476. Nudix_hydrolase.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
IPR003563. OxG-triPHTase.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
PRINTSiPR01403. 8OXTPHPHTASE.
PR00502. NUDIXFAMILY.
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P53369-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTSRLYTLV LVLQPQRVLL GMKKRGFGAG RWNGFGGKVQ EGETIEDGAK
60 70 80 90 100
RELLEESGLR VDTLHKVGHI SFEFVGSPEL MDVHIFSTDH VHGTPTESEE
110 120 130 140 150
MRPQWFQLDQ IPFADMWPDD SYWFPLLLQK KKFCGHFKFH GQDTILSYSL

REVDEF
Length:156
Mass (Da):18,018
Last modified:October 1, 1996 - v1
Checksum:i60AFB6522CB03E18
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49977 mRNA. Translation: BAA08726.1.
D49980 Genomic DNA. Translation: BAA08727.1.
RefSeqiNP_476461.1. NM_057120.1.
XP_006248973.1. XM_006248911.2.
UniGeneiRn.10669.

Genome annotation databases

EnsembliENSRNOT00000001700; ENSRNOP00000001700; ENSRNOG00000001260.
GeneIDi117260.
KEGGirno:117260.
UCSCiRGD:621080. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49977 mRNA. Translation: BAA08726.1.
D49980 Genomic DNA. Translation: BAA08727.1.
RefSeqiNP_476461.1. NM_057120.1.
XP_006248973.1. XM_006248911.2.
UniGeneiRn.10669.

3D structure databases

ProteinModelPortaliP53369.
SMRiP53369. Positions 1-154.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001700.

Proteomic databases

PaxDbiP53369.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000001700; ENSRNOP00000001700; ENSRNOG00000001260.
GeneIDi117260.
KEGGirno:117260.
UCSCiRGD:621080. rat.

Organism-specific databases

CTDi4521.
RGDi621080. Nudt1.

Phylogenomic databases

eggNOGiENOG410IXIA. Eukaryota.
COG0494. LUCA.
GeneTreeiENSGT00390000000341.
HOGENOMiHOG000261970.
HOVERGENiHBG000032.
InParanoidiP53369.
KOiK17816.
OMAiGAGKWNG.
OrthoDBiEOG7BS4BT.
PhylomeDBiP53369.
TreeFamiTF106348.

Enzyme and pathway databases

ReactomeiR-RNO-2393930. Phosphate bond hydrolysis by NUDT proteins.

Miscellaneous databases

NextBioi620134.
PROiP53369.

Gene expression databases

GenevisibleiP53369. RN.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR020476. Nudix_hydrolase.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
IPR003563. OxG-triPHTase.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
PRINTSiPR01403. 8OXTPHPHTASE.
PR00502. NUDIXFAMILY.
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "cDNA and genomic sequences for rat 8-oxo-dGTPase that prevents occurrence of spontaneous mutations due to oxidation of guanine nucleotides."
    Cai J.P., Kakuma T., Tsuzuki T., Sekiguchi M.
    Carcinogenesis 16:2343-2350(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    Strain: Donryu.
    Tissue: Spleen.
  2. "Intracellular distribution of the antimutagenic enzyme MTH1 in the liver, kidney and testis of F344 rats and its modulation by cadmium."
    Kasprzak K.S., Nakabeppu Y., Kakuma T., Sakai Y., Tsuruya K., Sekiguchi M., Ward J.M., Diwan B.A., Nagashima K., Kasprzak B.H.
    Exp. Toxicol. Pathol. 53:325-335(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry namei8ODP_RAT
AccessioniPrimary (citable) accession number: P53369
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: March 16, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.