Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P54137

- NTH_CAEEL

UniProt

P54137 - NTH_CAEEL

Protein

Endonuclease III homolog

Gene

nth-1

Organism
Caenorhabditis elegans
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.1 PublicationUniRule annotation

    Catalytic activityi

    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.UniRule annotation

    Cofactori

    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.UniRule annotation

    Temperature dependencei

    Optimum temperature is 26 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei158 – 1581Nucleophile; for N-glycosylase activityUniRule annotation
    Sitei177 – 1771Important for catalytic activityUniRule annotation
    Metal bindingi226 – 2261Iron-sulfur (4Fe-4S)UniRule annotation
    Metal bindingi233 – 2331Iron-sulfur (4Fe-4S)UniRule annotation
    Metal bindingi236 – 2361Iron-sulfur (4Fe-4S)UniRule annotation
    Metal bindingi242 – 2421Iron-sulfur (4Fe-4S)UniRule annotation

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    2. 5-formyluracil DNA N-glycosylase activity Source: WormBase
    3. 5-hydroxymethyluracil DNA N-glycosylase activity Source: WormBase
    4. DNA binding Source: InterPro
    5. metal ion binding Source: UniProtKB-KW
    6. oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity Source: WormBase

    GO - Biological processi

    1. cellular response to hydrogen peroxide Source: WormBase
    2. depyrimidination Source: WormBase
    3. DNA catabolic process, endonucleolytic Source: GOC
    4. DNA repair Source: WormBase

    Keywords - Molecular functioni

    Glycosidase, Hydrolase, Lyase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    4Fe-4S, Iron, Iron-sulfur, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endonuclease III homologUniRule annotation (EC:3.2.2.-UniRule annotation, EC:4.2.99.18UniRule annotation)
    Short name:
    CeNTH
    Alternative name(s):
    Bifunctional DNA N-glycoslyase/DNA-(apurinic or apyrimidinic site) lyaseUniRule annotation
    Short name:
    DNA glycoslyase/AP lyaseUniRule annotation
    Gene namesi
    Name:nth-1UniRule annotation
    ORF Names:R10E4.5
    OrganismiCaenorhabditis elegans
    Taxonomic identifieri6239 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
    ProteomesiUP000001940: Chromosome III

    Organism-specific databases

    WormBaseiR10E4.5a; CE44645; WBGene00011201; nth-1.
    R10E4.5b; CE44659; WBGene00011201; nth-1.
    R10E4.5c; CE44689; WBGene00011201; nth-1.
    R10E4.5d; CE44095; WBGene00011201; nth-1.

    Subcellular locationi

    Nucleus UniRule annotation. Mitochondrion UniRule annotation

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell
    2. nucleus Source: WormBase

    Keywords - Cellular componenti

    Mitochondrion, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    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.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 298298Endonuclease III homologPRO_0000102229Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi6239.R10E4.5.

    Structurei

    3D structure databases

    ProteinModelPortaliP54137.
    SMRiP54137. Positions 65-239.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini138 – 16528HhHUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the Nth/MutY family.UniRule annotation
    Contains 1 HhH domain.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0177.
    GeneTreeiENSGT00510000047513.
    HOGENOMiHOG000252209.
    InParanoidiP54137.
    OMAiWRNKVKY.
    OrthoDBiEOG76MK8Z.

    Family and domain databases

    Gene3Di1.10.1670.10. 1 hit.
    1.10.340.30. 1 hit.
    HAMAPiMF_03183. Endonuclease_III_Nth.
    InterProiIPR011257. 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]
    PfamiPF00633. HHH. 1 hit.
    PF00730. HhH-GPD. 1 hit.
    [Graphical view]
    SMARTiSM00478. ENDO3c. 1 hit.
    SM00525. FES. 1 hit.
    [Graphical view]
    SUPFAMiSSF48150. SSF48150. 1 hit.
    PROSITEiPS00764. ENDONUCLEASE_III_1. 1 hit.
    PS01155. ENDONUCLEASE_III_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing and alternative initiation. Align

    Isoform d (identifier: P54137-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MHSFSMKRVV ASSSVAAVAT CDVEGTVVAW RRDVELIRKM RKDMIAPVDT    50
    MGCHKLADPL AAPPVHRFQV LVALMLSSQT RDEVNAAAMK RLKDHGLSIG 100
    KILEFKVPDL ETILCPVGFY KRKAVYLQKT AKILKDDFSG DIPDSLDGLC 150
    ALPGVGPKMA NLVMQIAWGE CVGIAVDTHV HRISNRLGWI KTSTPEKTQK 200
    ALEILLPKSE WQPINHLLVG FGQMQCQPVR PKCGTCLCRF TCPSSTAKNV 250
    KSETEETSTS IEVKQEVEDE FEDEKPAKKI KKTRKTRTKI EVKTESET 298
    Length:298
    Mass (Da):33,117
    Last modified:July 27, 2011 - v2
    Checksum:iACD504175243F42A
    GO
    Isoform a (identifier: P54137-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-5: Missing.

    Note: Produced by alternative initiation.

    Show »
    Length:293
    Mass (Da):32,527
    Checksum:i1FF1D1B8626B6B8E
    GO
    Isoform b (identifier: P54137-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-74: Missing.

    Note: Produced by alternative splicing.

    Show »
    Length:224
    Mass (Da):25,017
    Checksum:i25407C4744713639
    GO
    Isoform c (identifier: P54137-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-158: Missing.

    Note: Produced by alternative splicing.

    Show »
    Length:140
    Mass (Da):15,858
    Checksum:iBB4A45A3DC81D3CD
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 158158Missing in isoform c. CuratedVSP_041643Add
    BLAST
    Alternative sequencei1 – 7474Missing in isoform b. CuratedVSP_041642Add
    BLAST
    Alternative sequencei1 – 55Missing in isoform a. CuratedVSP_041641

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiT24131.
    RefSeqiNP_001254906.1. NM_001267977.1. [P54137-1]
    NP_001254907.1. NM_001267978.1. [P54137-2]
    NP_001254908.1. NM_001267979.1. [P54137-3]
    NP_001254909.1. NM_001267980.1. [P54137-4]
    UniGeneiCel.10201.
    Cel.40199.

    Genome annotation databases

    EnsemblMetazoaiR10E4.5d; R10E4.5d; WBGene00011201. [P54137-1]
    GeneIDi187770.
    KEGGicel:CELE_R10E4.5.

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi T24131.
    RefSeqi NP_001254906.1. NM_001267977.1. [P54137-1 ]
    NP_001254907.1. NM_001267978.1. [P54137-2 ]
    NP_001254908.1. NM_001267979.1. [P54137-3 ]
    NP_001254909.1. NM_001267980.1. [P54137-4 ]
    UniGenei Cel.10201.
    Cel.40199.

    3D structure databases

    ProteinModelPortali P54137.
    SMRi P54137. Positions 65-239.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 6239.R10E4.5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai R10E4.5d ; R10E4.5d ; WBGene00011201 . [P54137-1 ]
    GeneIDi 187770.
    KEGGi cel:CELE_R10E4.5.

    Organism-specific databases

    CTDi 187770.
    WormBasei R10E4.5a ; CE44645 ; WBGene00011201 ; nth-1.
    R10E4.5b ; CE44659 ; WBGene00011201 ; nth-1.
    R10E4.5c ; CE44689 ; WBGene00011201 ; nth-1.
    R10E4.5d ; CE44095 ; WBGene00011201 ; nth-1.

    Phylogenomic databases

    eggNOGi COG0177.
    GeneTreei ENSGT00510000047513.
    HOGENOMi HOG000252209.
    InParanoidi P54137.
    OMAi WRNKVKY.
    OrthoDBi EOG76MK8Z.

    Miscellaneous databases

    NextBioi 936446.
    PROi P54137.

    Family and domain databases

    Gene3Di 1.10.1670.10. 1 hit.
    1.10.340.30. 1 hit.
    HAMAPi MF_03183. Endonuclease_III_Nth.
    InterProi IPR011257. 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 ]
    Pfami PF00633. HHH. 1 hit.
    PF00730. HhH-GPD. 1 hit.
    [Graphical view ]
    SMARTi SM00478. ENDO3c. 1 hit.
    SM00525. FES. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48150. SSF48150. 1 hit.
    PROSITEi PS00764. ENDONUCLEASE_III_1. 1 hit.
    PS01155. ENDONUCLEASE_III_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiNTH_CAEEL
    AccessioniPrimary (citable) accession number: P54137
    Secondary accession number(s): C7G4V3
    , D5MCR0, D5MCR1, D5MCR2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 106 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programCaenorhabditis annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Caenorhabditis elegans
      Caenorhabditis elegans: entries, gene names and cross-references to WormBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3