NEIL2_MOUSE
ID NEIL2_MOUSE Reviewed; 329 AA.
AC Q6R2P8; G3X969;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 4.
DT 03-AUG-2022, entry version 125.
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; Synonyms=Gm1212;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/Ola;
RA Ang C.C., Ng P.W.P., Wei C.L., Ruan Y.;
RT "Gene identification signature analysis: a novel method for genome
RT annotation.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) 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}.
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DR EMBL; AY518221; AAR98807.1; -; mRNA.
DR EMBL; AC090654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466535; EDL36068.1; -; Genomic_DNA.
DR CCDS; CCDS36949.1; -.
DR RefSeq; NP_963904.2; NM_201610.2.
DR RefSeq; XP_006519262.1; XM_006519199.3.
DR AlphaFoldDB; Q6R2P8; -.
DR SMR; Q6R2P8; -.
DR BioGRID; 238543; 1.
DR STRING; 10090.ENSMUSP00000045200; -.
DR PhosphoSitePlus; Q6R2P8; -.
DR MaxQB; Q6R2P8; -.
DR PaxDb; Q6R2P8; -.
DR PRIDE; Q6R2P8; -.
DR ProteomicsDB; 252803; -.
DR Antibodypedia; 22115; 144 antibodies from 24 providers.
DR DNASU; 382913; -.
DR Ensembl; ENSMUST00000038229; ENSMUSP00000045200; ENSMUSG00000035121.
DR GeneID; 382913; -.
DR KEGG; mmu:382913; -.
DR UCSC; uc007uhk.1; mouse.
DR CTD; 252969; -.
DR MGI; MGI:2686058; Neil2.
DR VEuPathDB; HostDB:ENSMUSG00000035121; -.
DR eggNOG; ENOG502RIIB; Eukaryota.
DR GeneTree; ENSGT00940000153230; -.
DR HOGENOM; CLU_072818_0_0_1; -.
DR InParanoid; Q6R2P8; -.
DR OMA; YNCQMAW; -.
DR OrthoDB; 1467835at2759; -.
DR PhylomeDB; Q6R2P8; -.
DR TreeFam; TF331502; -.
DR Reactome; R-MMU-110329; Cleavage of the damaged pyrimidine.
DR Reactome; R-MMU-5649702; APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
DR BioGRID-ORCS; 382913; 1 hit in 107 CRISPR screens.
DR PRO; PR:Q6R2P8; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q6R2P8; protein.
DR Bgee; ENSMUSG00000035121; Expressed in primary oocyte and 57 other tissues.
DR ExpressionAtlas; Q6R2P8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0072686; C:mitotic spindle; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; IDA:MGI.
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_0000170909"
FT ZN_FING 280..316
FT /note="FPG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00391"
FT REGION 88..112
FT /note="Disordered"
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 150
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q969S2"
FT CONFLICT 220
FT /note="R -> K (in Ref. 1; AAR98807)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="L -> F (in Ref. 1; AAR98807)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="L -> P (in Ref. 1; AAR98807)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 329 AA; 36834 MW; 221781934B9EB5A5 CRC64;
MPEGPSVRKF HHLVSPFVGQ KVVKTGGSSK KLHPAAFQSL WLQDAQVHGK KLFLRFDPDE
EMEPLNSSPQ PIQGMWQKEA VDRELALGPS AQEPSAGPSG SGEPVPSRSA ETYNLGKIPS
ADAQRWLEVR FGLFGSIWVN DFSRAKKANK KGDWRDPVPR LVLHFSGGGF LVFYNCQMSW
SPPPVIEPTC DILSEKFHRG QALEALSQAQ PVCYTLLDQR YFSGLGNIIK NEALYRARIH
PLSLGSCLSS SSREALVDHV VEFSKDWLRD KFQGKERHTQ IYQKEQCPSG HQVMKETFGP
PDGLQRLTWW CPQCQPQLSS KGPQNLPSS
