ID Q5U3G8_DANRE Unreviewed; 550 AA. AC Q5U3G8; DT 07-DEC-2004, integrated into UniProtKB/TrEMBL. DT 07-DEC-2004, sequence version 1. DT 27-MAR-2024, entry version 130. DE RecName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|ARBA:ARBA00012720}; DE EC=4.2.99.18 {ECO:0000256|ARBA:ARBA00012720}; GN Name=neil3 {ECO:0000313|EMBL:AAH85550.1, GN ECO:0000313|ZFIN:ZDB-GENE-041114-18}; GN Synonyms=zgc:103553 {ECO:0000313|RefSeq:NP_001007336.1}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAH85550.1}; RN [1] {ECO:0000313|EMBL:AAH85550.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ovary {ECO:0000313|EMBL:AAH85550.1}, and PCR rescue RC {ECO:0000313|EMBL:AAI64271.1}; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|RefSeq:NP_001007336.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16428305; DOI=10.1093/jb/mvi168; RA Torisu K., Tsuchimoto D., Ohnishi Y., Nakabeppu Y.; RT "Hematopoietic tissue-specific expression of mouse Neil3 for endonuclease RT VIII-like protein."; RL J. Biochem. 138:763-772(2005). RN [3] {ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23594743; DOI=10.1038/nature12111; RG Genome Reference Consortium Zebrafish; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D., RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B., RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J., RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D., RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B., RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P., RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., RA Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). RN [4] {ECO:0000313|RefSeq:NP_001007336.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=27189481; RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I., RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y., RA Bobe J.; RT "Gene evolution and gene expression after whole genome duplication in fish: RT the PhyloFish database."; RL BMC Genomics 17:368-368(2016). RN [5] {ECO:0000313|RefSeq:NP_001007336.1} RP IDENTIFICATION. RG RefSeq; RL Submitted (NOV-2023) to UniProtKB. 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; CC Evidence={ECO:0000256|ARBA:ARBA00024490}; CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000256|ARBA:ARBA00009409}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC085550; AAH85550.1; -; mRNA. DR EMBL; BC164271; AAI64271.1; -; mRNA. DR RefSeq; NP_001007336.1; NM_001007335.1. DR GeneID; 492463; -. DR KEGG; dre:492463; -. DR AGR; ZFIN:ZDB-GENE-041114-18; -. DR CTD; 55247; -. DR ZFIN; ZDB-GENE-041114-18; neil3. DR OrthoDB; 38342at2759; -. DR Proteomes; UP000000437; Alternate scaffold 14. DR Proteomes; UP000000437; Chromosome 14. 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:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central. DR CDD; cd08969; MeNeil3_N; 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; 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_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; zf-GRF; 2. DR Pfam; PF00641; zf-RanBP; 1. DR SMART; SM00898; Fapy_DNA_glyco; 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 2: Evidence at transcript level; KW DNA damage {ECO:0000256|ARBA:ARBA00022763}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125}; KW Endonuclease {ECO:0000313|EMBL:AAH85550.1, KW ECO:0000313|RefSeq:NP_001007336.1}; 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 Nuclease {ECO:0000313|EMBL:AAH85550.1, ECO:0000313|RefSeq:NP_001007336.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE- KW ProRule:PRU00322}. FT DOMAIN 2..115 FT /note="Formamidopyrimidine-DNA glycosylase catalytic" FT /evidence="ECO:0000259|PROSITE:PS51068" FT DOMAIN 225..259 FT /note="FPG-type" FT /evidence="ECO:0000259|PROSITE:PS51066" FT DOMAIN 295..324 FT /note="RanBP2-type" FT /evidence="ECO:0000259|PROSITE:PS50199" FT DOMAIN 453..495 FT /note="GRF-type" FT /evidence="ECO:0000259|PROSITE:PS51999" FT DOMAIN 499..541 FT /note="GRF-type" FT /evidence="ECO:0000259|PROSITE:PS51999" FT REGION 372..457 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 372..412 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 432..457 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 550 AA; 61684 MW; 92663E81FAF35D9B CRC64; MVEGPGCTLN GEKIRARVQK RQKVLHIQGN ETKTTSDDGS RSSFQSFTGG EFTGVETLGK ELFMYFGVRA LRLHFGMNGS MRINPLKKDL HGKPPVLVIQ LTNDAICFFD TTVEIRLSED CEQKVRAMEA LDICSPKFSF SRAVEAVKTE RARMLCDVLL DQTVLPGVGN IIKNEALFDS GLNPAVKVSQ LTDEQVHHLV KMTRDFTLLF YKCRKNGSPL YKHYKVYKRP NCGQCSGTVT VCRLGDNGRM TYYCQRCQTG DPSEVNISKL LTRNSLIGWV YQGGMSSSEH VAKQEEEEWA CSLCTLINRP FNKHCDACMS PRPDEPQKLE HSPLSPDLIR YPCNSFSKPL QEIKMNRRAA FGTTTLVLTS LSAKPDSPSS PAISQAHTPE TMRGLSTHGN WQRKSPCNGV SGMQFKGNEP CKRESPTDHS QPNKRMKTTN GTFSGGNIKH ISSSHHRPCT QRVVTKEGEN KGRQFYTCSL PRETQCNFFE WADLHFPMCH HGKRTVMKTV LKLGPNNGRN FYTCPVKMGK QCNFFQWAEN GPGISILPGC //