NEIL3_XENLA
ID NEIL3_XENLA Reviewed; 616 AA.
AC A0A1L8HU22;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Endonuclease 8-like 3;
DE EC=3.2.2.- {ECO:0000250|UniProtKB:Q8TAT5};
DE EC=4.2.99.18 {ECO:0000269|PubMed:30842657};
DE AltName: Full=DNA glycosylase/AP lyase Neil3;
DE AltName: Full=Endonuclease VIII-like 3;
DE AltName: Full=Nei-like protein 3;
GN Name=neil3 {ECO:0000312|Xenbase:XB-GENE-1001617};
GN ORFNames=XELAEV_18005394mg {ECO:0000312|EMBL:OCT99612.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|Proteomes:UP000186698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J;
RX PubMed=27762356; DOI=10.1038/nature19840;
RA Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I.,
RA Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J.,
RA Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL Nature 538:336-343(2016).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS
RP OF 351-THR-LEU-352.
RX PubMed=30842657; DOI=10.1038/s41586-019-1002-0;
RA Wu R.A., Semlow D.R., Kamimae-Lanning A.N., Kochenova O.V., Chistol G.,
RA Hodskinson M.R., Amunugama R., Sparks J.L., Wang M., Deng L., Mimoso C.A.,
RA Low E., Patel K.J., Walter J.C.;
RT "TRAIP is a master regulator of DNA interstrand crosslink repair.";
RL Nature 567:267-272(2019).
CC -!- FUNCTION: DNA glycosylase which prefers single-stranded DNA (ssDNA), or
CC partially ssDNA structures such as bubble and fork structures, to
CC double-stranded DNA (dsDNA) (PubMed:30842657). Mediates interstrand
CC cross-link repair in response to replication stress: recruited to
CC replication stress sites via interaction with ubiquitinated CMG
CC helicase and acts by mediating DNA glycosylase activity
CC (PubMed:30842657). Cleaves one of the two N-glycosyl bonds comprising
CC the interstrand cross-link, which avoids the formation of a double-
CC strand break but generates an abasic site that is bypassed by
CC translesion synthesis polymerases (PubMed:30842657).
CC {ECO:0000269|PubMed:30842657}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC 2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00392, ECO:0000269|PubMed:30842657};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TAT5}.
CC Chromosome {ECO:0000269|PubMed:30842657}. Note=Recruited to replication
CC stress sites via interaction with ubiquitinated CMG helicase.
CC {ECO:0000269|PubMed:30842657}.
CC -!- DOMAIN: The RanBP2-type zinc-finger, also named NZF zinc finger,
CC recognizes and binds ubiquitinated CMG helicase complex
CC (PubMed:30842657). The GRF-type zinc-fingers recognize single-stranded
CC DNA (ssDNA), possibly on the lagging strand template (PubMed:30842657).
CC {ECO:0000269|PubMed:30842657}.
CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000255|PROSITE-
CC ProRule:PRU00392}.
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DR EMBL; CM004466; OCT99612.1; -; Genomic_DNA.
DR RefSeq; XP_018086201.1; XM_018230712.1.
DR AlphaFoldDB; A0A1L8HU22; -.
DR SMR; A0A1L8HU22; -.
DR STRING; 8355.A0A1L8HU22; -.
DR GeneID; 100380996; -.
DR KEGG; xla:100380996; -.
DR CTD; 100380996; -.
DR Xenbase; XB-GENE-1001617; neil3.L.
DR OMA; CSPEFSF; -.
DR OrthoDB; 1467835at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 100380996; Expressed in egg cell and 15 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
DR GO; GO:0019104; F:DNA N-glycosylase activity; TAS:Reactome.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:UniProtKB.
DR GO; GO:1904931; F:MCM complex binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR GO; GO:0036297; P:interstrand cross-link repair; IDA:UniProtKB.
DR Gene3D; 3.20.190.10; -; 1.
DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR InterPro; IPR015887; DNA_glyclase_Znf_dom_DNA_BS.
DR InterPro; IPR035937; MutM-like_N-ter.
DR InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR InterPro; IPR010666; Znf_GRF.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR Pfam; PF06831; H2TH; 1.
DR Pfam; PF06839; zf-GRF; 2.
DR SMART; SM01232; H2TH; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF46946; SSF46946; 1.
DR SUPFAM; SSF81624; SSF81624; 1.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS01242; ZF_FPG_1; 1.
DR PROSITE; PS51066; ZF_FPG_2; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase;
KW Lyase; Metal-binding; Multifunctional enzyme; Nucleus; Reference proteome;
KW Repeat; Zinc; Zinc-finger.
FT CHAIN 1..616
FT /note="Endonuclease 8-like 3"
FT /id="PRO_0000451422"
FT ZN_FING 271..305
FT /note="FPG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00391"
FT ZN_FING 341..370
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 525..568
FT /note="GRF-type"
FT /evidence="ECO:0000255"
FT ZN_FING 572..615
FT /note="GRF-type"
FT /evidence="ECO:0000255"
FT REGION 491..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 101
FT /note="Required for glycosylase and lyase activities"
FT /evidence="ECO:0000250|UniProtKB:Q8TAT5"
FT MUTAGEN 351..352
FT /note="TL->LV: Decreased binding to interstrand cross-
FT links."
FT /evidence="ECO:0000269|PubMed:30842657"
SQ SEQUENCE 616 AA; 69092 MW; 5D347D8E8F543E0D CRC64;
MEALPPQVLK PLDCMSIYSR HREPENRHNE LSTGRCGRGH VIFSSMKALQ PQVLKPTGSH
ANLQQVLYAP AATIITAPAS SHNDLSSLTG CSYAGVETLG KELFIYFGLK AMRVHFGMNG
SMRINQPMKK GQENGRPIPI AVLEVQLTKD LICFYESTVD VRNASECQEK IRFFEELDVC
SSKFSFPRAE CEIKKQRTRM LCDILLDQMI LPGVGNIIKN EALFDSGLHP GVQAGLLTDE
QVSHLVKMTR DFTLLFYKCR KSGSALYKHY KVYKRPNCGQ CGTKITVCRL GEHNRMTYFC
PKCQKDKPQH VDVSKLPTRN SLIGWVQRTA SNANEHVATS KEEHWACAVC TLINKPSDKQ
CDACLTLRPE VSSLAVSDEA AELNTDLVKY PCNNFAKVLP ELKLNRRTAF GNTTLVLTDF
GAKEGLADKN SQQNILNRST FDVPLNNKYY HTKTPSNKRS NENEHWTNTL NAVNGHSAAS
NNVFNHPQKK LKTGHTTSNT IHLSSTISSP QSKMTGDAAA KTGNPQCSAH NVPCALQVVR
KEGENKGRSF YTCSLPRERR CQYFEWADLH FPFCNHGKRC IVRTVLKIGP NNGKNFYVCP
MGKDKQCNFF EWAKTE
