NEIL2_BOVIN
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 03-AUG-2022, entry version 110.
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; Q6IE77; -.
DR PRIDE; Q6IE77; -.
DR Ensembl; ENSBTAT00000006262; ENSBTAP00000006262; ENSBTAG00000004769.
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; YNCQMAW; -.
DR OrthoDB; 1467835at2759; -.
DR TreeFam; TF331502; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000004769; Expressed in oocyte and 104 other tissues.
DR ExpressionAtlas; Q6IE77; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:0008017; F:microtubule binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR InterPro; IPR012319; FPG_cat.
DR InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR Pfam; PF06831; H2TH; 1.
DR SMART; SM01232; H2TH; 1.
DR SUPFAM; SSF46946; SSF46946; 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
