Functions as a weak apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents (PubMed:16687656). Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5′-deoxyribose phosphate and 3′-hydroxyl ends. Also displays double-stranded DNA 3′-5′ exonuclease, 3′-phosphodiesterase activities (PubMed:16687656, PubMed:19443450, PubMed:32516598). Shows robust 3′-5′ exonuclease activity on 3′-recessed heteroduplex DNA and is able to remove mismatched nucleotides preferentially (PubMed:16687656, PubMed:19443450). Also exhibits 3′-5′ exonuclease activity on a single nucleotide gap containing heteroduplex DNA and on blunt-ended substrates (PubMed:16687656). Shows fairly strong 3′-phosphodiesterase activity involved in the removal of 3′-damaged termini formed in DNA by oxidative agents (PubMed:16687656, PubMed:19443450). In the nucleus functions in the PCNA-dependent BER pathway (PubMed:11376153). Plays a role in reversing blocked 3′ DNA ends, problematic lesions that preclude DNA synthesis (PubMed:32516598). Required for somatic hypermutation (SHM) and DNA cleavage step of class switch recombination (CSR) of immunoglobulin genes (By similarity). Required for proper cell cycle progression during proliferation of peripheral lymphocytes (By similarity).
