Search by BoMiProt ID - Bomi5485


Primary Information

BoMiProt ID Bomi5485
Protein Name Endonuclease 8-like 3/DNA glycosylase/AP lyase Neil3/Endonuclease VIII-like 3/Nei-like protein 3
Organism Bos taurus
Uniprot IdQ3MHN7
Milk FractionWhey
Ref Sequence Id NP_001029662.1
Aminoacid Length 606
Molecular Weight 67384
Fasta Sequence https://www.uniprot.org/uniprot/Q3MHN7.fasta
Gene Name NEIL3
Gene Id 515343
Protein Existence Status reviewed

Secondary Information

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.
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.
PTMs Phosphorylation on Ser
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
Predicted Disorder Regions 402-445, 463-476
DisProt Annotation
TM Helix Prediction No TM helices
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.