ID   F1RT18_PIG              Unreviewed;       596 AA.
AC   F1RT18; A0A4X1VS65;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   04-NOV-2026, entry version 89.
DE   RecName: Full=Endonuclease 8-like 3 {ECO:0000256|ARBA:ARBA00073168};
DE            EC=4.2.99.18 {ECO:0000256|ARBA:ARBA00012720};
DE   AltName: Full=DNA glycosylase/AP lyase Neil3 {ECO:0000256|ARBA:ARBA00081871};
DE   AltName: Full=Endonuclease VIII-like 3 {ECO:0000256|ARBA:ARBA00083341};
DE   AltName: Full=Nei-like protein 3 {ECO:0000256|ARBA:ARBA00082922};
GN   Name=NEIL3 {ECO:0000313|Ensembl:ENSSSCP00000016711.1,
GN   ECO:0000313|VGNC:VGNC:96046};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000016711.1, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000016711.1, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000016711.1,
RC   ECO:0000313|Proteomes:UP000008227};
RX   PubMed=32543654;
RA   Warr A., Affara N., Aken B., Beiki H., Bickhart D.M., Billis K., Chow W.,
RA   Eory L., Finlayson H.A., Flicek P., Giron C.G., Griffin D.K., Hall R.,
RA   Hannum G., Hourlier T., Howe K., Hume D.A., Izuogu O., Kim K., Koren S.,
RA   Liu H., Manchanda N., Martin F.J., Nonneman D.J., O'Connor R.E.,
RA   Phillippy A.M., Rohrer G.A., Rosen B.D., Rund L.A., Sargent C.A.,
RA   Schook L.B., Schroeder S.G., Schwartz A.S., Skinner B.M., Talbot R.,
RA   Tseng E., Tuggle C.K., Watson M., Smith T.P.L., Archibald A.L.;
RT   "An improved pig reference genome sequence to enable pig genetics and
RT   genomics research.";
RL   Gigascience 9:giaa051-giaa051(2020).
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000016711.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2026) to UniProtKB.
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). Mediates interstrand cross-link repair in
CC       response to replication stress: acts by mediating DNA glycosylase
CC       activity, cleaving one of the two N-glycosyl bonds comprising the
CC       interstrand cross-link, which avoids the formation of a double-strand
CC       break but generates an abasic site that is bypassed by translesion
CC       synthesis polymerases. In vitro, displays strong glycosylase activity
CC       towards the hydantoin lesions spiroiminodihydantoin (Sp) and
CC       guanidinohydantoin (Gh) in both ssDNA and dsDNA; also recognizes FapyA,
CC       FapyG, 5-OHU, 5-OHC, 5-OHMH, Tg and 8-oxoA lesions in ssDNA. No
CC       activity on 8-oxoG detected. Also shows weak DNA-(apurinic or
CC       apyrimidinic site) lyase activity. In vivo, appears to be the primary
CC       enzyme involved in removing Sp and Gh from ssDNA in neonatal tissues.
CC       {ECO:0000256|ARBA:ARBA00059921}.
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'-phospho-2'-
CC         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;
CC         Evidence={ECO:0000256|ARBA:ARBA00044632};
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the FPG family. {ECO:0000256|ARBA:ARBA00009409}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00392}.
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DR   RefSeq; XP_001926185.3; XM_001926150.6.
DR   AlphaFoldDB; F1RT18; -.
DR   SMR; F1RT18; -.
DR   STRING; 9823.ENSSSCP00000016711; -.
DR   PaxDb; 9823-ENSSSCP00000016711; -.
DR   Ensembl; ENSSSCT00000017172.3; ENSSSCP00000016711.1; ENSSSCG00000015771.4.
DR   GeneID; 100156631; -.
DR   KEGG; ssc:100156631; -.
DR   CTD; 55247; -.
DR   VGNC; VGNC:96046; NEIL3.
DR   eggNOG; ENOG502QWRN; Eukaryota.
DR   GeneTree; ENSGT00940000153230; -.
DR   HOGENOM; CLU_482283_0_0_1; -.
DR   OrthoDB; 498125at2759; -.
DR   Reactome; R-SSC-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR   Reactome; R-SSC-110331; Cleavage of the damaged purine.
DR   Proteomes; UP000008227; Chromosome 15.
DR   Bgee; ENSSSCG00000015771; Expressed in oocyte and 32 other cell types or tissues.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000405; F:bubble DNA binding; 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:0003690; F:double-stranded DNA binding; IEA:Ensembl.
DR   GO; GO:0003697; F:single-stranded DNA 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   GO; GO:0000012; P:single strand break repair; IEA:Ensembl.
DR   CDD; cd08969; MeNeil3_N; 1.
DR   FunFam; 2.30.30.380:FF:000017; Nei like DNA glycosylase 3; 1.
DR   FunFam; 3.20.190.10:FF:000005; Nei like DNA glycosylase 3; 1.
DR   FunFam; 1.10.8.50:FF:000008; Nei-like DNA glycosylase 3; 1.
DR   Gene3D; 1.10.8.50; -; 1.
DR   Gene3D; 3.20.190.10; MutM-like, N-terminal; 1.
DR   Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR   InterPro; IPR015887; DNA_glyclase_Znf_dom_DNA_BS.
DR   InterPro; IPR012319; FPG_cat.
DR   InterPro; IPR035937; FPG_N.
DR   InterPro; IPR015886; H2TH_FPG.
DR   InterPro; IPR010979; Ribosomal_uS13-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   PANTHER; PTHR22993:SF10; ENDONUCLEASE 8-LIKE 3; 1.
DR   PANTHER; PTHR22993; FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE; 1.
DR   Pfam; PF06831; H2TH; 1.
DR   Pfam; PF06839; Zn_ribbon_GRF; 2.
DR   Pfam; PF00641; Zn_ribbon_RanBP; 1.
DR   SMART; SM01232; H2TH; 1.
DR   SMART; SM00547; ZnF_RBZ; 1.
DR   SUPFAM; SSF81624; N-terminal domain of MutM-like DNA repair proteins; 1.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR   SUPFAM; SSF46946; S13-like H2TH domain; 1.
DR   PROSITE; PS51068; FPG_CAT; 1.
DR   PROSITE; PS01242; ZF_FPG_1; 1.
DR   PROSITE; PS51066; ZF_FPG_2; 1.
DR   PROSITE; PS51999; ZF_GRF; 2.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
DR   PROSITE; PS50199; ZF_RANBP2_2; 1.
PE   3: Inferred from homology;
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00322}.
FT   DOMAIN          2..139
FT                   /note="Formamidopyrimidine-DNA glycosylase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51068"
FT   DOMAIN          249..283
FT                   /note="FPG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51066"
FT   DOMAIN          319..348
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          498..541
FT                   /note="GRF-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51999"
FT   DOMAIN          545..587
FT                   /note="GRF-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51999"
SQ   SEQUENCE   596 AA;  66365 MW;  01577D2D3A0E6F27 CRC64;
     MVEGPGCTLN GEKIRARVRP GQAVTDVRGS ALQNAGGPGL PLSASETVVP SQAIALNNNK
     LCSQNSLRLL NGHVYSGVET LGKELFMYFG PKALRIHFGM KGSLAINPLE SKSKNGVSPV
     FEVQLTKDLI CFFDSSVEIR NTAESQQRIR MMEELDVCSP KFSFSRAERE VKKQGGRMLC
     DVLMDQKVLP GVGNIIKNEA LFDSGLHPAV KVCQLTDEQT HHLVKMIHDF SILFYRCCKA
     GSAVSKHYKV YKRPNCGQCF CKITVCRLGE NNRMTYFCPH CQKENPQHVD ICLLPARNTF
     VPWPSSRENH FTDCVARKSE EQWTCEVCTL INKPSSQACD ACLSSRPVDS VLENKENPTA
     LNNLVKYPCN SFGKPRTEVK INRKTAFGTT TLVLTDFSNK SSALKREESQ KQILDGEFPN
     PLSSPERANY ITQLSNKVNV LPMICTQSKI FSPAYTNLKT THYSSPDHKT CNPGFSNSEL
     QINTTDGPHT LNAGSPRCSK HGRPCILRVV RKDGENKGRQ FYACPLPREA QCGFFEWADL
     SFPFCNHGKR SIMRTVLKIG PNNGKNFFVC PLGKEKQCNF FQWAENGPGI NIIPGC
//