Primary Information |
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BoMiProt ID | Bomi5485 |
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Protein Name | Endonuclease 8-like 3/DNA glycosylase/AP lyase Neil3/Endonuclease VIII-like 3/Nei-like protein 3 |
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Organism | Bos taurus |
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Uniprot ID | Q3MHN7 |
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Milk Fraction | Whey |
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Ref Sequence ID | NP_001029662.1 |
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Aminoacid Length | 606 |
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Molecular Weight | 67384 |
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FASTA Sequence |
Download |
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Gene Name | NEIL3 |
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Gene ID | 515343 |
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Protein Existence Status | reviewed |
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Secondary Information |
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Protein Function | DNA glycosylase which prefers single-stranded DNA (ssDNA) and dsDNA.Initiate the first step in base excision repair by cleaving bases damaged by reactive oxygen species and introducing a DNA strand break via the associated lyase reaction. |
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Biochemical Properties | Contain helix-two turns-helix (H2TH) motif and the zinc finger motif for DNA binding. In the conserved N-terminus, a valine replaces the catalytic proline found in most of the Fpg/Nei family members. The C-terminal extension of the Neil3 proteins contains additional zinc finger motifs, a RanBP-like zinc finger and two GRF zinc finger motifs. |
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PTMs | Phosphorylation on Ser |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q3MHN7|NEIL3_BOVIN Endonuclease 8-like 3 OS=Bos taurus OX=9913 GN=NEIL3 PE=2 SV=2
MVEGPGCTLNGEKIRARVRPGQAVTDVRGRALQGLGGPGSPPAAPGPMGTSQAAALNNNK
NSSQDFLRLFNGHGYSGVETLGKELFMYFGPKALRIHFGMKGSLVINPLESKNKNGVSPV
FEVQLTKDLICFFDSSVEIRNSTESQQRIRVMEELDVCSPRFSFSRAESEVKKQKGRMLC
DVLMDQKVLPGVGNIIKNEALFDSGFHPSVKVCQLTDEQIHHLVKMIRNFSILFYRCCKV
GSALSKHYKVYKRPNCGQCCCKITVCRLGENNRMTYFCPHCQKENPQHVDIRMLPVRNTT
VNWPSSRERHLMDCVAQKSEEQWTCEVCTLINKLSSKTCDACLTSRPADSVLRNEGNPIV
FNNLMKYPCNSFGKSKAKVKINRKTAFGTTTLVLTDFSNKHSALEREESHSHIPDGEFPS
PPPNVCGSDTLNTSKERTNCRSQPSDKVNIS*451PVVCSQYKLFSPAHKKLKTTHYSSPDLKS
CNPGFSNSELQSSMTDGPCLLNAGSPRCSKHGRPCALRVVRKSGENKGRHFYACPLAREA
QCGFFEWADLSFPFCNHGKRSIMRTVLKIGPNNGKNFFVCPLGKEKQCNFFQWAQNGPGI
NIIPGC |
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Predicted Disorder Regions | 402-445, 463-476 |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Bibliography | 1.Liu M, Doublié S, Wallace SS. Neil3, the final frontier for the DNA glycosylases that recognize oxidative damage. Mutat Res. 2013 Mar-Apr;743-744:4-11. doi: 10.1016/j.mrfmmm.2012.12.003. Epub 2012 Dec 26. PMID: 23274422; PMCID: PMC3657305. |