NEIL3_BOVIN
ID NEIL3_BOVIN Reviewed; 606 AA.
AC Q3MHN7; F1N383;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Endonuclease 8-like 3;
DE EC=3.2.2.-;
DE EC=4.2.99.18;
DE AltName: Full=DNA glycosylase/AP lyase Neil3;
DE AltName: Full=Endonuclease VIII-like 3;
DE AltName: Full=Nei-like protein 3;
GN Name=NEIL3;
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=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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) (By similarity). Mediates interstrand
CC cross-link repair in response to replication stress: acts by mediating
CC DNA glycosylase activity, cleaving one of the two N-glycosyl bonds
CC comprising the interstrand cross-link, which avoids the formation of a
CC double-strand break but generates an abasic site that is bypassed by
CC translesion synthesis polymerases (By similarity). In vitro, displays
CC strong glycosylase activity towards the hydantoin lesions
CC spiroiminodihydantoin (Sp) and guanidinohydantoin (Gh) in both ssDNA
CC and dsDNA; also recognizes FapyA, FapyG, 5-OHU, 5-OHC, 5-OHMH, Tg and
CC 8-oxoA lesions in ssDNA. No activity on 8-oxoG detected. Also shows
CC weak DNA-(apurinic or apyrimidinic site) lyase activity. In vivo,
CC appears to be the primary enzyme involved in removing Sp and Gh from
CC ssDNA in neonatal tissues (By similarity).
CC {ECO:0000250|UniProtKB:A0A1L8HU22, ECO:0000250|UniProtKB:Q8K203}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TAT5}.
CC Chromosome {ECO:0000250|UniProtKB:A0A1L8HU22}. Note=Recruited to
CC replication stress sites via interaction with ubiquitinated CMG
CC helicase. {ECO:0000250|UniProtKB:A0A1L8HU22}.
CC -!- DOMAIN: The N-terminal region (2-283) contains the glycosylase and
CC lyase activities. {ECO:0000250}.
CC -!- DOMAIN: The RanBP2-type zinc-finger, also named NZF zinc finger,
CC recognizes and binds ubiquitinated CMG helicase complex. The GRF-type
CC zinc-fingers recognize single-stranded DNA (ssDNA), possibly on the
CC lagging strand template. {ECO:0000250|UniProtKB:A0A1L8HU22}.
CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000255|PROSITE-
CC ProRule:PRU00392}.
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DR EMBL; DAAA02060028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC105168; AAI05169.1; -; mRNA.
DR RefSeq; NP_001029662.1; NM_001034490.2.
DR AlphaFoldDB; Q3MHN7; -.
DR SMR; Q3MHN7; -.
DR STRING; 9913.ENSBTAP00000007661; -.
DR PaxDb; Q3MHN7; -.
DR PRIDE; Q3MHN7; -.
DR GeneID; 515343; -.
DR KEGG; bta:515343; -.
DR CTD; 55247; -.
DR eggNOG; ENOG502QWRN; Eukaryota.
DR HOGENOM; CLU_482283_0_0_1; -.
DR InParanoid; Q3MHN7; -.
DR OrthoDB; 1467835at2759; -.
DR TreeFam; TF331502; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000405; F:bubble DNA binding; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0019104; F:DNA N-glycosylase activity; ISS:UniProtKB.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:1904931; F:MCM complex binding; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; ISS:UniProtKB.
DR GO; GO:0036297; P:interstrand cross-link repair; ISS:UniProtKB.
DR Gene3D; 3.20.190.10; -; 1.
DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR InterPro; IPR015887; DNA_glyclase_Znf_dom_DNA_BS.
DR InterPro; IPR012319; FPG_cat.
DR InterPro; IPR035937; MutM-like_N-ter.
DR InterPro; IPR010979; Ribosomal_S13-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 Pfam; PF06831; H2TH; 1.
DR Pfam; PF06839; zf-GRF; 2.
DR Pfam; PF00641; zf-RanBP; 1.
DR SMART; SM01232; H2TH; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF46946; SSF46946; 1.
DR SUPFAM; SSF81624; SSF81624; 1.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS51068; FPG_CAT; 1.
DR PROSITE; PS01242; ZF_FPG_1; 1.
DR PROSITE; PS51066; ZF_FPG_2; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 2: Evidence at transcript level;
KW Chromosome; DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase;
KW Lyase; Metal-binding; Multifunctional enzyme; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..606
FT /note="Endonuclease 8-like 3"
FT /id="PRO_0000248634"
FT ZN_FING 249..283
FT /note="FPG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00391"
FT ZN_FING 319..348
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 507..550
FT /note="GRF-type 1"
FT ZN_FING 553..596
FT /note="GRF-type 2"
FT REGION 31..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2
FT /note="Schiff-base intermediate with DNA; via amino
FT nitrogen"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00392"
FT BINDING 194
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT SITE 2
FT /note="Important for monofunctional glycosylase activity"
FT /evidence="ECO:0000250"
FT SITE 83
FT /note="Required for glycosylase activity"
FT /evidence="ECO:0000250"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TAT5"
FT CONFLICT 64
FT /note="Q -> H (in Ref. 2; AAI05169)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 606 AA; 67384 MW; 30EE4917DC869250 CRC64;
MVEGPGCTLN GEKIRARVRP GQAVTDVRGR ALQGLGGPGS PPAAPGPMGT SQAAALNNNK
NSSQDFLRLF NGHGYSGVET LGKELFMYFG PKALRIHFGM KGSLVINPLE SKNKNGVSPV
FEVQLTKDLI CFFDSSVEIR NSTESQQRIR VMEELDVCSP RFSFSRAESE VKKQKGRMLC
DVLMDQKVLP GVGNIIKNEA LFDSGFHPSV KVCQLTDEQI HHLVKMIRNF SILFYRCCKV
GSALSKHYKV YKRPNCGQCC CKITVCRLGE NNRMTYFCPH CQKENPQHVD IRMLPVRNTT
VNWPSSRERH LMDCVAQKSE EQWTCEVCTL INKLSSKTCD ACLTSRPADS VLRNEGNPIV
FNNLMKYPCN SFGKSKAKVK INRKTAFGTT TLVLTDFSNK HSALEREESH SHIPDGEFPS
PPPNVCGSDT LNTSKERTNC RSQPSDKVNI SPVVCSQYKL FSPAHKKLKT THYSSPDLKS
CNPGFSNSEL QSSMTDGPCL LNAGSPRCSK HGRPCALRVV RKSGENKGRH FYACPLAREA
QCGFFEWADL SFPFCNHGKR SIMRTVLKIG PNNGKNFFVC PLGKEKQCNF FQWAQNGPGI
NIIPGC
