ID   NEIL2_BOVIN             Reviewed;         329 AA.
AC   Q6IE77;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   24-JAN-2024, entry version 117.
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 homolog 2;
DE            Short=NEH2;
DE   AltName: Full=Nei-like protein 2;
GN   Name=NEIL2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19390049; DOI=10.1126/science.1169588;
RG   The bovine genome sequencing and analysis consortium;
RT   "The genome sequence of taurine cattle: a window to ruminant biology and
RT   evolution.";
RL   Science 324:522-528(2009).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=15025586; DOI=10.1111/j.1365-2052.2004.01101.x;
RA   Plis-Finarov A., Hudson H., Roe B., Ron M., Seroussi E.;
RT   "Mapping of the GATA4, NEIL2, FDFT1 genes and CTSB-associated
RT   microsatellites to the centromeric region of BTA8.";
RL   Anim. Genet. 35:154-155(2004).
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}.
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DR   EMBL; AC107065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BN000316; CAE48362.1; -; mRNA.
DR   RefSeq; NP_001013021.1; NM_001013003.1.
DR   RefSeq; XP_005209884.1; XM_005209827.3.
DR   RefSeq; XP_010806002.1; XM_010807700.2.
DR   AlphaFoldDB; Q6IE77; -.
DR   SMR; Q6IE77; -.
DR   STRING; 9913.ENSBTAP00000006262; -.
DR   PaxDb; 9913-ENSBTAP00000006262; -.
DR   Ensembl; ENSBTAT00000006262.3; ENSBTAP00000006262.2; ENSBTAG00000004769.3.
DR   GeneID; 444987; -.
DR   KEGG; bta:444987; -.
DR   CTD; 252969; -.
DR   VEuPathDB; HostDB:ENSBTAG00000004769; -.
DR   VGNC; VGNC:31989; NEIL2.
DR   eggNOG; ENOG502RIIB; Eukaryota.
DR   GeneTree; ENSGT00940000153230; -.
DR   HOGENOM; CLU_072818_0_0_1; -.
DR   InParanoid; Q6IE77; -.
DR   OMA; LTWWCPH; -.
DR   OrthoDB; 38342at2759; -.
DR   TreeFam; TF331502; -.
DR   Reactome; R-BTA-110329; Cleavage of the damaged pyrimidine.
DR   Reactome; R-BTA-5649702; APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
DR   Proteomes; UP000009136; Chromosome 8.
DR   Bgee; ENSBTAG00000004769; Expressed in oocyte and 104 other cell types or tissues.
DR   ExpressionAtlas; Q6IE77; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
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..329
FT                   /note="Endonuclease 8-like 2"
FT                   /id="PRO_0000170907"
FT   ZN_FING         280..316
FT                   /note="FPG-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00391"
FT   REGION          68..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..89
FT                   /note="Basic and acidic 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        306
FT                   /note="Proton donor; for delta-elimination activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00392"
FT   BINDING         227
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         149
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q969S2"
SQ   SEQUENCE   329 AA;  36392 MW;  0D48CC7BEDA526EA CRC64;
     MPEGPSVRKF HHLVSPFVGQ QVVKTGGSSK KLNPTSFQSL WLQDSQVHGK KLFLRFDPDE
     EAVSLGNSLL SEPLREGEQK DKARHHQEAS DPSSWSPGGD SAVPSGDDGL QCLGGDTPAG
     GAERWLQVSF GLFGSIRVNE FSRAKKANKR GDWRDPVPRL VLHFSGSGFL AFYNCQMTWR
     FSSPVVSPAS DILSEKFHRG QALEALGREQ PICYTLLDQR YFSGLGNIIK NEALFRAGIH
     PLSPGSLLGL PRLEALVDHV VAFSADWLQG KFQGTRQHTQ IYQKEQCPAG HQVVRESLGP
     PGGFQRLTWW CPQCQPRLSA DEPKQLQPS
//