ID B4DWI9_HUMAN Unreviewed; 347 AA. AC B4DWI9; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 14-DEC-2022, entry version 64. DE RecName: Full=DNA-(apurinic or apyrimidinic site) endonuclease 2 {ECO:0000256|ARBA:ARBA00013541}; DE EC=3.1.11.2 {ECO:0000256|ARBA:ARBA00012115}; DE AltName: Full=Apurinic-apyrimidinic endonuclease 2 {ECO:0000256|ARBA:ARBA00030064}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG63051.1}; RN [1] {ECO:0000313|EMBL:BAG63051.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Breast {ECO:0000313|EMBL:BAG63051.1}; RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A., RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y., RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T., RA Sugano S., Nomura N., Isogai T.; RT "NEDO human cDNA sequencing project focused on splicing variants."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield CC nucleoside 5'-phosphates.; EC=3.1.11.2; CC Evidence={ECO:0000256|ARBA:ARBA00000493}; CC -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family. CC {ECO:0000256|ARBA:ARBA00007092}. 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; AK301555; BAG63051.1; -; mRNA. DR RefSeq; NP_001258677.1; NM_001271748.1. DR AlphaFoldDB; B4DWI9; -. DR PeptideAtlas; B4DWI9; -. DR DNASU; 27301; -. DR GeneID; 27301; -. DR CTD; 27301; -. DR BioGRID-ORCS; 27301; 56 hits in 707 CRISPR screens. DR GenomeRNAi; 27301; -. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0004518; F:nuclease activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR Gene3D; 3.60.10.10; -; 1. DR InterPro; IPR004808; AP_endonuc_1. DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf. DR InterPro; IPR005135; Endo/exonuclease/phosphatase. DR InterPro; IPR010666; Znf_GRF. DR PANTHER; PTHR22748; AP ENDONUCLEASE; 1. DR Pfam; PF03372; Exo_endo_phos; 1. DR Pfam; PF06839; zf-GRF; 1. DR SUPFAM; SSF56219; DNase I-like; 1. DR PROSITE; PS51435; AP_NUCLEASE_F1_4; 1. PE 2: Evidence at transcript level; KW DNA damage {ECO:0000256|ARBA:ARBA00022763}; KW DNA recombination {ECO:0000256|ARBA:ARBA00023172}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204}; KW Lyase {ECO:0000313|EMBL:BAG63051.1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}. FT DOMAIN 2..133 FT /note="Endo/exonuclease/phosphatase" FT /evidence="ECO:0000259|Pfam:PF03372" FT DOMAIN 296..344 FT /note="zf-GRF" FT /evidence="ECO:0000259|Pfam:PF06839" FT REGION 184..236 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 347 AA; 38578 MW; C79E7A5774C5E84D CRC64; MRFYRLLQIR TEALLAAGSH VIILGDLNTA HRPIDHWDAV NLECFEEDPG RKWMDSLLSN LGCQSASHVG PFIDSYRCFQ PKQEGAFTCW SAVTGARHLN YGSRLDYVLG DRTLVIDTFQ ASFLLPEVMG SDHCPVGAVL SVSSVPAKQC PPLCTRFLPE FAGTQLKILR FLVPLEQSPV LEQSTLQHNN QTRVQTCQNK AQVRSTRPQP SQVGSSRGQK NLKSYFQPSP SCPQASPDIE LPSLPLMSAL MTPKTPEEKA VAKVVKGQAK TSEAKDEKEL RTSFWKSVLA GPLRTPLCGG HREPCVMRTV KKPGPNLGRR FYMCARPRGP PTDPSSRCNF FLWSRPS //