NEIL3_MOUSE
ID NEIL3_MOUSE Reviewed; 606 AA.
AC Q8K203; Q4ADY6; Q8CD85; Q8R3P4;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Endonuclease 8-like 3;
DE EC=3.2.2.-;
DE EC=4.2.99.18 {ECO:0000269|PubMed:20185759, ECO:0000269|PubMed:22065741, ECO:0000269|PubMed:22569481, ECO:0000269|PubMed:23305905, ECO:0000269|PubMed:23313161};
DE AltName: Full=DNA glycosylase FPG2;
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 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] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RC TISSUE=Splenocyte;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS PRO-46;
RP HIS-90; GLY-114; GLU-150; ARG-220; GLY-256; ARG-287; ALA-325; LYS-556 AND
RP GLU-585.
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52.
RC STRAIN=129/SvJ;
RA Torisu K., Tsuchimoto D., Ohnishi Y., Nakabeppu Y.;
RT "Molecular cloning and characterization of mouse DNA glycosylase gene, nei
RT like 3 (Neil3); its regulated expression in lymphoid organs.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION AS A GLYCOSYLASE/LYASE, CATALYTIC ACTIVITY, CHARACTERIZATION OF
RP N-TERMINAL DOMAIN, AND PROBABLE CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22569481; DOI=10.1016/j.pep.2012.04.022;
RA Liu M., Bandaru V., Holmes A., Averill A.M., Cannan W., Wallace S.S.;
RT "Expression and purification of active mouse and human NEIL3 proteins.";
RL Protein Expr. Purif. 84:130-139(2012).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVE SITE.
RX PubMed=20185759; DOI=10.1073/pnas.0908307107;
RA Liu M., Bandaru V., Bond J.P., Jaruga P., Zhao X., Christov P.P.,
RA Burrows C.J., Rizzo C.J., Dizdaroglu M., Wallace S.S.;
RT "The mouse ortholog of NEIL3 is a functional DNA glycosylase in vitro and
RT in vivo.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:4925-4930(2010).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=19426544; DOI=10.1186/1471-2202-10-45;
RA Hildrestrand G.A., Neurauter C.G., Diep D.B., Castellanos C.G., Krauss S.,
RA Bjoras M., Luna L.;
RT "Expression patterns of Neil3 during embryonic brain development and
RT neoplasia.";
RL BMC Neurosci. 10:45-45(2009).
RN [8]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=19170771; DOI=10.1111/j.1365-2443.2008.01271.x;
RA Takao M., Oohata Y., Kitadokoro K., Kobayashi K., Iwai S., Yasui A.,
RA Yonei S., Zhang Q.M.;
RT "Human Nei-like protein NEIL3 has AP lyase activity specific for single-
RT stranded DNA and confers oxidative stress resistance in Escherichia coli
RT mutant.";
RL Genes Cells 14:261-270(2009).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22065741; DOI=10.1073/pnas.1106880108;
RA Sejersted Y., Hildrestrand G.A., Kunke D., Rolseth V., Krokeide S.Z.,
RA Neurauter C.G., Suganthan R., Atneosen-Asegg M., Fleming A.M.,
RA Saugstad O.D., Burrows C.J., Luna L., Bjoras M.;
RT "Endonuclease VIII-like 3 (Neil3) DNA glycosylase promotes neurogenesis
RT induced by hypoxia-ischemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:18802-18807(2011).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22959434; DOI=10.1016/j.celrep.2012.08.008;
RA Regnell C.E., Hildrestrand G.A., Sejersted Y., Medin T., Moldestad O.,
RA Rolseth V., Krokeide S.Z., Suganthan R., Luna L., Bjoras M.,
RA Bergersen L.H.;
RT "Hippocampal adult neurogenesis is maintained by Neil3-dependent repair of
RT oxidative DNA lesions in neural progenitor cells.";
RL Cell Rep. 2:503-510(2012).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23305905; DOI=10.1016/j.bbamcr.2012.12.024;
RA Rolseth V., Krokeide S.Z., Kunke D., Neurauter C.G., Suganthan R.,
RA Sejersted Y., Hildrestrand G.A., Bjoras M., Luna L.;
RT "Loss of Neil3, the major DNA glycosylase activity for removal of
RT hydantoins in single stranded DNA, reduces cellular proliferation and
RT sensitizes cells to genotoxic stress.";
RL Biochim. Biophys. Acta 1833:1157-1164(2013).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-282 IN COMPLEX WITH ZINC,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23313161; DOI=10.1016/j.str.2012.12.008;
RA Liu M., Imamura K., Averill A.M., Wallace S.S., Doublie S.;
RT "Structural characterization of a mouse ortholog of human NEIL3 with a
RT marked preference for single-stranded DNA.";
RL Structure 21:247-256(2013).
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) (PubMed:20185759, PubMed:22065741,
CC PubMed:22569481, PubMed:22959434, PubMed:23305905, PubMed:23313161).
CC Mediates interstrand cross-link repair in response to replication
CC stress: acts by mediating DNA glycosylase activity, cleaving one of the
CC two N-glycosyl bonds comprising the interstrand cross-link, which
CC avoids the formation of a double-strand break but generates an abasic
CC site that is bypassed by translesion synthesis polymerases (By
CC similarity). In vitro, displays strong glycosylase activity towards the
CC hydantoin lesions spiroiminodihydantoin (Sp) and guanidinohydantoin
CC (Gh) in both ssDNA and dsDNA; also recognizes FapyA, FapyG, 5-OHU, 5-
CC OHC, 5-OHMH, Tg and 8-oxoA lesions in ssDNA (PubMed:20185759,
CC PubMed:22065741, PubMed:22569481, PubMed:22959434, PubMed:23305905,
CC PubMed:23313161). No activity on 8-oxoG detected (PubMed:20185759,
CC PubMed:22065741, PubMed:22569481, PubMed:22959434, PubMed:23305905,
CC PubMed:23313161). Also shows weak DNA-(apurinic or apyrimidinic site)
CC lyase activity (PubMed:20185759, PubMed:22065741, PubMed:22569481,
CC PubMed:22959434, PubMed:23305905, PubMed:23313161). In vivo, appears to
CC be the primary enzyme involved in removing Sp and Gh from ssDNA in
CC neonatal tissues (PubMed:20185759, PubMed:22065741, PubMed:22569481,
CC PubMed:22959434, PubMed:23305905, PubMed:23313161).
CC {ECO:0000250|UniProtKB:A0A1L8HU22, ECO:0000269|PubMed:20185759,
CC ECO:0000269|PubMed:22065741, ECO:0000269|PubMed:22569481,
CC ECO:0000269|PubMed:22959434, ECO:0000269|PubMed:23305905,
CC ECO:0000269|PubMed:23313161}.
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, ECO:0000269|PubMed:20185759,
CC ECO:0000269|PubMed:22065741, ECO:0000269|PubMed:22569481,
CC ECO:0000269|PubMed:23305905, ECO:0000269|PubMed:23313161};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16428305}. Chromosome
CC {ECO:0000250|UniProtKB:A0A1L8HU22}. Note=Recruited to replication
CC stress sites via interaction with ubiquitinated CMG helicase.
CC {ECO:0000250|UniProtKB:A0A1L8HU22}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K203-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K203-2; Sequence=VSP_012210;
CC -!- TISSUE SPECIFICITY: Expressed in testis, thymus, spleen and bone
CC marrow. In young mice, expressed at higher levels in thymocytes than
CC splenocytes. At 12 dpc, abundant in the subventricular zone (SVZ) of
CC the lateral ventricles. At 17.5 dpc and P0, expression is limited to
CC distinct cells in the cortical SVZ, in cells of the secondary matrix,
CC the dentate gyrus migratory route and the dentate gyrus.
CC {ECO:0000269|PubMed:16428305, ECO:0000269|PubMed:19170771,
CC ECO:0000269|PubMed:19426544, ECO:0000269|PubMed:23305905}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in the developing brain at 12
CC dpc-13 dpc when neurogenesis starts. Expression decreases during later
CC development and is undetectable in adult brain.
CC {ECO:0000269|PubMed:19170771, ECO:0000269|PubMed:19426544}.
CC -!- INDUCTION: By mitogen stimulation in splenocytes, and by hypoxic-
CC ischemic injury in the striatum and hippocampus.
CC {ECO:0000269|PubMed:16428305, ECO:0000269|PubMed:22065741}.
CC -!- DOMAIN: The N-terminal region (2-282) contains the glycosylase and
CC lyase activities.
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 -!- DISRUPTION PHENOTYPE: Perinatal mice show reduced regeneration of
CC neural tissue following ischemic brain damage (stroke), associated with
CC fewer activated microglia and impaired neural stem cell proliferation.
CC Aged mice show deficits in learning and memory, decreased anxiety-like
CC behavior, and changes in hippocampal synapse composition. Otherwise
CC viable and fertile. {ECO:0000269|PubMed:16428305,
CC ECO:0000269|PubMed:22065741, ECO:0000269|PubMed:22959434,
CC ECO:0000269|PubMed:23305905}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000255|PROSITE-
CC ProRule:PRU00392}.
CC -!- CAUTION: Was originally thought to be inactive as a glycosylase, but
CC recent reports demonstrate that cleavage of the initiator methionine is
CC essential for catalytic activity. {ECO:0000269|PubMed:20185759,
CC ECO:0000269|PubMed:22569481}.
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DR EMBL; AB072931; BAC22661.1; -; mRNA.
DR EMBL; AK031027; BAC27219.1; -; mRNA.
DR EMBL; BC024921; AAH24921.1; -; mRNA.
DR EMBL; BC034753; AAH34753.1; -; mRNA.
DR EMBL; AB202125; BAE16548.1; -; Genomic_DNA.
DR CCDS; CCDS22305.1; -. [Q8K203-1]
DR RefSeq; NP_666320.1; NM_146208.2. [Q8K203-1]
DR PDB; 3W0F; X-ray; 2.00 A; A=2-282.
DR PDBsum; 3W0F; -.
DR AlphaFoldDB; Q8K203; -.
DR SMR; Q8K203; -.
DR BioGRID; 231506; 2.
DR STRING; 10090.ENSMUSP00000041909; -.
DR iPTMnet; Q8K203; -.
DR PhosphoSitePlus; Q8K203; -.
DR EPD; Q8K203; -.
DR MaxQB; Q8K203; -.
DR PaxDb; Q8K203; -.
DR PeptideAtlas; Q8K203; -.
DR PRIDE; Q8K203; -.
DR ProteomicsDB; 287359; -. [Q8K203-1]
DR ProteomicsDB; 287360; -. [Q8K203-2]
DR Antibodypedia; 17262; 188 antibodies from 29 providers.
DR DNASU; 234258; -.
DR Ensembl; ENSMUST00000047768; ENSMUSP00000041909; ENSMUSG00000039396. [Q8K203-1]
DR GeneID; 234258; -.
DR KEGG; mmu:234258; -.
DR UCSC; uc009lsa.2; mouse. [Q8K203-1]
DR UCSC; uc009lsb.2; mouse. [Q8K203-2]
DR CTD; 55247; -.
DR MGI; MGI:2384588; Neil3.
DR VEuPathDB; HostDB:ENSMUSG00000039396; -.
DR eggNOG; ENOG502QWRN; Eukaryota.
DR GeneTree; ENSGT00940000153230; -.
DR HOGENOM; CLU_482283_0_0_1; -.
DR InParanoid; Q8K203; -.
DR OMA; CSPEFSF; -.
DR OrthoDB; 1467835at2759; -.
DR PhylomeDB; Q8K203; -.
DR TreeFam; TF331502; -.
DR BRENDA; 3.2.2.23; 3474.
DR Reactome; R-MMU-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-MMU-110331; Cleavage of the damaged purine.
DR BioGRID-ORCS; 234258; 2 hits in 111 CRISPR screens.
DR ChiTaRS; Neil3; mouse.
DR PRO; PR:Q8K203; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8K203; protein.
DR Bgee; ENSMUSG00000039396; Expressed in animal zygote and 138 other tissues.
DR ExpressionAtlas; Q8K203; baseline and differential.
DR Genevisible; Q8K203; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000405; F:bubble DNA binding; IDA: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; IDA:UniProtKB.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:1904931; F:MCM complex binding; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IDA: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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome; DNA damage; DNA repair;
KW DNA-binding; Glycosidase; Hydrolase; Lyase; Metal-binding;
KW Multifunctional enzyme; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..606
FT /note="Endonuclease 8-like 3"
FT /id="PRO_0000170911"
FT ZN_FING 248..282
FT /note="FPG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00391"
FT ZN_FING 318..347
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 506..550
FT /note="GRF-type 1"
FT ZN_FING 553..596
FT /note="GRF-type 2"
FT REGION 479..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..493
FT /note="Polar residues"
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:0000305|PubMed:20185759"
FT BINDING 193
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 272
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 82
FT /note="Required for glycosylase activity"
FT /evidence="ECO:0000250"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TAT5"
FT VAR_SEQ 212..606
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012210"
FT VARIANT 46
FT /note="L -> P (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 90
FT /note="P -> H (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 114
FT /note="A -> G (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 150
FT /note="V -> E (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 220
FT /note="C -> R (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 256
FT /note="D -> G (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 287
FT /note="C -> R (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 325
FT /note="V -> A (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 556
FT /note="R -> K (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 585
FT /note="K -> E (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT HELIX 4..17
FT /evidence="ECO:0007829|PDB:3W0F"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:3W0F"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:3W0F"
FT HELIX 64..68
FT /evidence="ECO:0007829|PDB:3W0F"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:3W0F"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:3W0F"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:3W0F"
FT STRAND 91..106
FT /evidence="ECO:0007829|PDB:3W0F"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:3W0F"
FT STRAND 128..140
FT /evidence="ECO:0007829|PDB:3W0F"
FT HELIX 141..151
FT /evidence="ECO:0007829|PDB:3W0F"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:3W0F"
FT HELIX 163..171
FT /evidence="ECO:0007829|PDB:3W0F"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:3W0F"
FT HELIX 178..183
FT /evidence="ECO:0007829|PDB:3W0F"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:3W0F"
FT HELIX 193..203
FT /evidence="ECO:0007829|PDB:3W0F"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:3W0F"
FT HELIX 216..239
FT /evidence="ECO:0007829|PDB:3W0F"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:3W0F"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:3W0F"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:3W0F"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:3W0F"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:3W0F"
SQ SEQUENCE 606 AA; 67416 MW; 941C38FA8538BAA8 CRC64;
MVEGPGCTLN GEKIRARVLP GQAVTGVRGT ALQSLLGPAM SPAASLADVA TSAAPMNAKD
SGWKLLRLFN GYVYSGVETL GKELFMYFGP RALRIHFGMK GSILINPREG ENRAGASPAL
AVQLTRDLIC FYDSSVELRN SVESQQRVRV MEELDICSPK FSFSRAESEV KKQGDRMLCD
VLLDQRVLPG VGNIIKNEAL FDSGLHPAVK VCQLSDKQAC HLVKMTRDFS ILFYRCCKAG
SAISKHCKVY KRPNCDQCHS KITVCRFGEN SRMTYFCPHC QKENPQCVQV CQLPTRNTEI
SWTPRGEDCF TDSVARKSEE QWSCVVCTLI NRPSAKACDA CLTTRPLDSV LKNRENSIAF
NNLVKYPCNN FENTHTEVKI NRKTAFGNTT LVLTDLSNKS SALARKKRAN HTIDGESQMF
LPTDIGFSDS QHPSKEGINY ITQPSNKVNI SPTVCAQSKL FSSAHKKFKP AHTSATELKS
YNSGLSNSEL QTNRTRGHHS KSDGSPLCKM HHRRCVLRVV RKDGENKGRQ FYACSLPRGA
QCGFFEWADL SFPFCRHGKR SIMKTVLKIG PNNGKNFFVC PLEKKKQCNF FQWAENGPGM
EIVPGC
