ID   APN1_CAEEL              Reviewed;         396 AA.
AC   Q10002;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   19-DEC-2001, sequence version 2.
DT   16-JUN-2009, entry version 71.
DE   RecName: Full=DNA-(apurinic or apyrimidinic site) lyase;
DE            EC=4.2.99.18;
DE   AltName: Full=Apurinic-apyrimidinic endonuclease;
DE            Short=AP endonuclease;
GN   Name=apn-1; ORFNames=T05H10.2;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 104-396.
RX   MEDLINE=97128321; PubMed=8972914; DOI=10.1016/S0378-1119(96)00375-7;
RA   Masson J.Y., Tremblay S., Ramotar D.;
RT   "The Caenorhabditis elegans gene CeAPN1 encodes a homolog of
RT   Escherichia coli and yeast apurinic/apyrimidinic endonuclease.";
RL   Gene 179:291-293(1996).
CC   -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
CC       apyrimidinic site in DNA is broken by a beta-elimination reaction,
CC       leaving a 3'-terminal unsaturated sugar and a product with a
CC       terminal 5'-phosphate.
CC   -!- COFACTOR: Binds 3 zinc ions (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- SIMILARITY: Belongs to the AP endonuclease 2 family.
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DR   EMBL; Z47812; CAA87789.2; -; Genomic_DNA.
DR   EMBL; U40707; AAB39924.1; -; mRNA.
DR   PIR; JC5235; JC5235.
DR   RefSeq; NP_495687.1; -.
DR   UniGene; Cel.32771; -.
DR   HSSP; P12638; 1QTW.
DR   Ensembl; T05H10.2; Caenorhabditis elegans.
DR   GeneID; 174291; -.
DR   KEGG; cel:T05H10.2; -.
DR   NMPDR; fig|6239.3.peg.6447; -.
DR   WormBase; WBGene00000151; apn-1.
DR   WormPep; T05H10.2; CE28953.
DR   OMA; Q10002; FAMFLKS.
DR   BRENDA; 4.2.99.18; 672.
DR   NextBio; 883392; -.
DR   ArrayExpress; Q10002; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase a...; IEA:EC.
DR   GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0009792; P:embryonic development ending in birth or eg...; IMP:WormBase.
DR   InterPro; IPR001719; AP_endonuc_F2.
DR   InterPro; IPR018246; AP_endonuc_F2_Zn_BS.
DR   InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR   InterPro; IPR012307; Xyl_isomerase-typ_TIM-brl.
DR   Gene3D; G3DSA:3.20.20.150; Xyl_isomerase-like_TIM-brl; 1.
DR   PANTHER; PTHR21445; AP_endnuclease2; 1.
DR   Pfam; PF01261; AP_endonuc_2; 1.
DR   SMART; SM00518; AP2Ec; 1.
DR   TIGRFAMs; TIGR00587; nfo; 1.
DR   PROSITE; PS00729; AP_NUCLEASE_F2_1; 1.
DR   PROSITE; PS00730; AP_NUCLEASE_F2_2; 1.
DR   PROSITE; PS00731; AP_NUCLEASE_F2_3; 1.
DR   PROSITE; PS51432; AP_NUCLEASE_F2_4; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; DNA damage; DNA repair; Lyase; Metal-binding;
KW   Nucleus; Zinc.
FT   CHAIN         1    396       DNA-(apurinic or apyrimidinic site)
FT                                lyase.
FT                                /FTId=PRO_0000190899.
FT   METAL       185    185       Zinc 1 (By similarity).
FT   METAL       225    225       Zinc 1 (By similarity).
FT   METAL       261    261       Zinc 1 (By similarity).
FT   METAL       261    261       Zinc 2 (By similarity).
FT   METAL       295    295       Zinc 2 (By similarity).
FT   METAL       298    298       Zinc 3 (By similarity).
FT   METAL       332    332       Zinc 2 (By similarity).
FT   METAL       345    345       Zinc 3 (By similarity).
FT   METAL       347    347       Zinc 3 (By similarity).
FT   METAL       377    377       Zinc 2 (By similarity).
SQ   SEQUENCE   396 AA;  44747 MW;  0C1D1B26AB35BA15 CRC64;
     MANKKVTFRE DVKSPAIRKL KQKLTPLKIK KGRGKIQKHI QKTLQKMKEE EESENQSPGT
     TVEETLTEEN ISTDKEETSK LENKPKKTRK TSGETIAQKK SRETVGVEVL KTSEGSSKML
     GFHVSAAGGL EQAIYNARAE GCRSFAMFVR NQRTWNHKPM SEEVVENWWK AVRETNFPLD
     QIVPHGSYLM NAGSPEAEKL EKSRLAMLDE CQRAEKLGIT MYNFHPGSTV GKCEKEECMT
     TIAETIDFVV EKTENIILVL ETMAGQGNSI GGTFEELKFI IDKVKVKSRV GVCIDTCHIF
     AGGYDIRTQK AYEEVMKNFG EVVGWNYLKA IHINDSKGDV GSKLDRHEHI GQGKIGKAAF
     ELLMNDNRLD GIPMILETPE GKYPEEMMIM YNMDKR
//