ID NEIL2_PONAB Reviewed; 332 AA. AC Q5RAJ7; DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 08-NOV-2023, entry version 79. DE RecName: Full=Endonuclease 8-like 2; DE EC=3.2.2.-; DE EC=4.2.99.18; DE AltName: Full=DNA glycosylase/AP lyase Neil2; DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase Neil2; DE AltName: Full=Endonuclease VIII-like 2; DE AltName: Full=Nei-like protein 2; GN Name=NEIL2; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pongo. OX NCBI_TaxID=9601; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in base excision repair of DNA damaged by oxidation CC or by mutagenic agents. Has DNA glycosylase activity towards 5- CC hydroxyuracil and other oxidized derivatives of cytosine with a CC preference for mismatched double-stranded DNA (DNA bubbles). Has low or CC no DNA glycosylase activity towards thymine glycol, 2-hydroxyadenine, CC hypoxanthine and 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase CC activity and introduces nicks in the DNA strand. Cleaves the DNA CC backbone by beta-delta elimination to generate a single-strand break at CC the site of the removed base with both 3'- and 5'-phosphates (By CC similarity). {ECO:0000250}. 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}; CC -!- ACTIVITY REGULATION: Acetylation of Lys-50 leads to loss of DNA nicking CC activity. {ECO:0000250}. CC -!- SUBUNIT: Binds EP300. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- DOMAIN: The zinc-finger domain is important for DNA binding. CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000255|PROSITE- CC ProRule:PRU00392}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CR859018; CAH91213.1; -; mRNA. DR RefSeq; NP_001125714.1; NM_001132242.1. DR AlphaFoldDB; Q5RAJ7; -. DR SMR; Q5RAJ7; -. DR STRING; 9601.ENSPPYP00000020561; -. DR GeneID; 100172638; -. DR KEGG; pon:100172638; -. DR CTD; 252969; -. DR eggNOG; ENOG502RIIB; Eukaryota. DR InParanoid; Q5RAJ7; -. DR OrthoDB; 38342at2759; -. DR Proteomes; UP000001595; Unplaced. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 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; IEA:InterPro. DR GO; GO:0019104; F:DNA N-glycosylase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006284; P:base-excision repair; IEA:InterPro. DR CDD; cd08968; MeNeil2_N; 1. DR Gene3D; 1.10.8.50; -; 1. DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd. DR InterPro; IPR012319; FPG_cat. DR InterPro; IPR010979; Ribosomal_uS13-like_H2TH. DR InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase. DR PANTHER; PTHR22993:SF29; ENDONUCLEASE 8-LIKE 2; 1. DR PANTHER; PTHR22993; FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE; 1. DR Pfam; PF06831; H2TH; 1. DR SMART; SM01232; H2TH; 1. DR SUPFAM; SSF46946; S13-like H2TH domain; 1. DR PROSITE; PS51068; FPG_CAT; 1. DR PROSITE; PS51066; ZF_FPG_2; 1. PE 2: Evidence at transcript level; KW Acetylation; DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase; KW Lyase; Metal-binding; Multifunctional enzyme; Nucleus; Phosphoprotein; KW Reference proteome; Zinc; Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..332 FT /note="Endonuclease 8-like 2" FT /id="PRO_0000248635" FT ZN_FING 284..320 FT /note="FPG-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00391" FT REGION 56..121 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 94..109 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 2 FT /note="Schiff-base intermediate with DNA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00392" FT ACT_SITE 3 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00392" FT ACT_SITE 50 FT /note="Proton donor; for beta-elimination activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00392" FT ACT_SITE 310 FT /note="Proton donor; for delta-elimination activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00392" FT BINDING 231 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000250" FT MOD_RES 50 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q969S2" FT MOD_RES 68 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q969S2" FT MOD_RES 154 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q969S2" SQ SEQUENCE 332 AA; 36814 MW; 607670A7EFE6E6C5 CRC64; MPEGPLVRKF HHLVSPFVGQ QVVKTGGSSK KLQPASLQCL WLQDTQVNGK KLFLRFDPDE EMGPPGSSPP PEPPQKEAQK EGAADPKQVG EPSGQKTPDG SSQSAELVPQ GEDDSEYLER DAPAGDAGRW LRVSFGLFGS VWVNEFSRAK QANKRGDWRD PSPRLVLHCG GGGFLAFYNC QMSWSSSPVV TPTCDILSEK FHRGQALEAL GQAQPVCYTL LDQRYFSGLG NIIKNEALYR AGIHPLSLGS VLSASRREVL VDHVVEFSTA WLQGKFQGRP QRTQVYQREQ CPAGHQVMKE AFGPQDGLQR LTWWCPQCQP QLSEEPEQRQ FS //