Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P54137 (NTH_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endonuclease III homolog

Short name=CeNTH
EC=3.2.2.-
EC=4.2.99.18
Alternative name(s):
Bifunctional DNA N-glycoslyase/DNA-(apurinic or apyrimidinic site) lyase
Short name=DNA glycoslyase/AP lyase
Gene names
Name:nth-1
ORF Names:R10E4.5
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines. Ref.1

Catalytic activity

The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. HAMAP-Rule MF_03183

Cofactor

Binds 1 4Fe-4S cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand By similarity.

Subcellular location

Nucleus By similarity. Mitochondrion By similarity HAMAP-Rule MF_03183.

Disruption phenotype

Increases the total average mutation rate 17-fold. No significant abnormality in lifespan or sensitivity to oxidizing agents such as hydrogen peroxide and methyl viologen (MV); due to the redundancy with other DNA glycosylases. Ref.1 Ref.3

Sequence similarities

Belongs to the Nth/MutY family.

Contains 1 HhH domain.

Biophysicochemical properties

Temperature dependence:

Optimum temperature is 26 degrees Celsius. Ref.1

Alternative products

This entry describes 4 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform d (identifier: P54137-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform a (identifier: P54137-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: Missing.
Note: Produced by alternative initiation.
Isoform b (identifier: P54137-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-74: Missing.
Note: Produced by alternative splicing.
Isoform c (identifier: P54137-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-158: Missing.
Note: Produced by alternative splicing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 298298Endonuclease III homolog HAMAP-Rule MF_03183
PRO_0000102229

Regions

Domain138 – 16528HhH

Sites

Active site1581Nucleophile; for N-glycosylase activity By similarity
Metal binding2261Iron-sulfur (4Fe-4S) By similarity
Metal binding2331Iron-sulfur (4Fe-4S) By similarity
Metal binding2361Iron-sulfur (4Fe-4S) By similarity
Metal binding2421Iron-sulfur (4Fe-4S) By similarity
Site1771Important for catalytic activity By similarity

Natural variations

Alternative sequence1 – 158158Missing in isoform c.
VSP_041643
Alternative sequence1 – 7474Missing in isoform b.
VSP_041642
Alternative sequence1 – 55Missing in isoform a.
VSP_041641

Sequences

Sequence LengthMass (Da)Tools
Isoform d [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: ACD504175243F42A

FASTA29833,117
        10         20         30         40         50         60 
MHSFSMKRVV ASSSVAAVAT CDVEGTVVAW RRDVELIRKM RKDMIAPVDT MGCHKLADPL 

        70         80         90        100        110        120 
AAPPVHRFQV LVALMLSSQT RDEVNAAAMK RLKDHGLSIG KILEFKVPDL ETILCPVGFY 

       130        140        150        160        170        180 
KRKAVYLQKT AKILKDDFSG DIPDSLDGLC ALPGVGPKMA NLVMQIAWGE CVGIAVDTHV 

       190        200        210        220        230        240 
HRISNRLGWI KTSTPEKTQK ALEILLPKSE WQPINHLLVG FGQMQCQPVR PKCGTCLCRF 

       250        260        270        280        290 
TCPSSTAKNV KSETEETSTS IEVKQEVEDE FEDEKPAKKI KKTRKTRTKI EVKTESET 

« Hide

Isoform a [UniParc].

Checksum: 1FF1D1B8626B6B8E
Show »

FASTA29332,527
Isoform b [UniParc].

Checksum: 25407C4744713639
Show »

FASTA22425,017
Isoform c [UniParc].

Checksum: BB4A45A3DC81D3CD
Show »

FASTA14015,858

References

« Hide 'large scale' references
[1]"Purification and characterization of Caenorhabditis elegans NTH, a homolog of human endonuclease III: essential role of N-terminal region."
Morinaga H., Yonekura S., Nakamura N., Sugiyama H., Yonei S., Zhang-Akiyama Q.M.
DNA Repair 8:844-851(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
[2]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE INITIATION, ALTERNATIVE SPLICING.
Strain: Bristol N2.
[3]"The relative roles of three DNA repair pathways in preventing Caenorhabditis elegans mutation accumulation."
Denver D.R., Feinberg S., Steding C., Durbin M., Lynch M.
Genetics 174:57-65(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB518695 mRNA. Translation: BAI22676.1.
Z50874 Genomic DNA. Translation: CAA90766.2.
Z50874 Genomic DNA. Translation: CBK55598.1.
Z50874 Genomic DNA. Translation: CBK55599.1.
Z50874 Genomic DNA. Translation: CBK55600.1.
PIRT24131.
RefSeqNP_001254906.1. NM_001267977.1.
NP_001254907.1. NM_001267978.1.
NP_001254908.1. NM_001267979.1.
NP_001254909.1. NM_001267980.1.
UniGeneCel.10201.
Cel.40199.

3D structure databases

ProteinModelPortalP54137.
SMRP54137. Positions 65-239.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING6239.R10E4.5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaR10E4.5d; R10E4.5d; R10E4.5. [P54137-1]
GeneID187770.
KEGGcel:CELE_R10E4.5.

Organism-specific databases

CTD187770.
WormBaseR10E4.5a; CE44645; WBGene00011201; nth-1.
R10E4.5b; CE44659; WBGene00011201; nth-1.
R10E4.5c; CE44689; WBGene00011201; nth-1.
R10E4.5d; CE44095; WBGene00011201; nth-1.

Phylogenomic databases

eggNOGCOG0177.
HOGENOMHOG000252209.
InParanoidP54137.
OMAWRNKVKY.
OrthoDBEOG76MK8Z.

Family and domain databases

Gene3D1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
HAMAPMF_03183. Endonuclease_III_Nth.
InterProIPR011257. DNA_glycosylase.
IPR004036. Endonuclease-III-like_CS2.
IPR004035. Endouclease-III_FeS-bd_BS.
IPR003651. Endouclease3_FeS-loop_motif.
IPR003265. HhH-GPD_domain.
IPR000445. HhH_motif.
IPR023170. HTH_base_excis_C.
[Graphical view]
PfamPF00633. HHH. 1 hit.
PF00730. HhH-GPD. 1 hit.
[Graphical view]
SMARTSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
[Graphical view]
SUPFAMSSF48150. SSF48150. 1 hit.
PROSITEPS00764. ENDONUCLEASE_III_1. 1 hit.
PS01155. ENDONUCLEASE_III_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio936446.
PROP54137.

Entry information

Entry nameNTH_CAEEL
AccessionPrimary (citable) accession number: P54137
Secondary accession number(s): C7G4V3 expand/collapse secondary AC list , D5MCR0, D5MCR1, D5MCR2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase