ID B4DWI9_HUMAN Unreviewed; 347 AA. AC B4DWI9; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 29-MAY-2024, entry version 71. DE RecName: Full=DNA-(apurinic or apyrimidinic site) endonuclease 2 {ECO:0000256|ARBA:ARBA00013541}; DE EC=3.1.11.2 {ECO:0000256|ARBA:ARBA00012115}; 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR604808-2}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR604808-2}; CC Note=Probably binds two magnesium or manganese ions per subunit. CC {ECO:0000256|PIRSR:PIRSR604808-2}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; 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 DisGeNET; 27301; -. DR OrthoDB; 169291at2759; -. DR BioGRID-ORCS; 27301; 59 hits in 782 CRISPR screens. DR GenomeRNAi; 27301; -. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW. DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:TreeGrafter. DR GO; GO:0008311; F:double-stranded DNA 3'-5' DNA exonuclease activity; IEA:TreeGrafter. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:TreeGrafter. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006284; P:base-excision repair; IEA:TreeGrafter. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 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 PANTHER; PTHR22748:SF4; DNA-(APURINIC OR APYRIMIDINIC SITE) ENDONUCLEASE 2; 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. DR PROSITE; PS51999; ZF_GRF; 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 Magnesium {ECO:0000256|PIRSR:PIRSR604808-2}; KW Manganese {ECO:0000256|PIRSR:PIRSR604808-2}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR604808-2}; Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE- KW ProRule:PRU01343}. FT DOMAIN 298..347 FT /note="GRF-type" FT /evidence="ECO:0000259|PROSITE:PS51999" FT REGION 184..236 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 26 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 28 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 132 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 133 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT SITE 28 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" FT SITE 106 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" FT SITE 133 FT /note="Interaction with DNA substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" 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 //