APN1_CAEEL
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 03-AUG-2022, entry version 151.
DE RecName: Full=Apurinic-apyrimidinic endonuclease;
DE Short=AP endonuclease;
DE EC=3.1.21.-;
GN Name=apn-1; ORFNames=T05H10.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX 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 investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 104-396.
RX 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 Escherichia
RT coli and yeast apurinic/apyrimidinic endonuclease.";
RL Gene 179:291-293(1996).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 3 Zn(2+) ions. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AP endonuclease 2 family. {ECO:0000305}.
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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; NM_063286.5.
DR AlphaFoldDB; Q10002; -.
DR SMR; Q10002; -.
DR BioGRID; 39623; 1.
DR IntAct; Q10002; 1.
DR STRING; 6239.T05H10.2; -.
DR EPD; Q10002; -.
DR PaxDb; Q10002; -.
DR PeptideAtlas; Q10002; -.
DR EnsemblMetazoa; T05H10.2.1; T05H10.2.1; WBGene00000151.
DR GeneID; 174291; -.
DR KEGG; cel:CELE_T05H10.2; -.
DR UCSC; T05H10.2; c. elegans.
DR CTD; 174291; -.
DR WormBase; T05H10.2; CE28953; WBGene00000151; apn-1.
DR eggNOG; KOG3997; Eukaryota.
DR GeneTree; ENSGT00390000013698; -.
DR HOGENOM; CLU_025885_0_0_1; -.
DR InParanoid; Q10002; -.
DR OMA; ACKPMEE; -.
DR OrthoDB; 1247820at2759; -.
DR PhylomeDB; Q10002; -.
DR PRO; PR:Q10002; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00000151; Expressed in germ line (C elegans) and 7 other tissues.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0017005; F:3'-tyrosyl-DNA phosphodiesterase activity; IDA:CACAO.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:WormBase.
DR GO; GO:0008311; F:double-stranded DNA 3'-5' exodeoxyribonuclease activity; IDA:CACAO.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IDA:WormBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IDA:WormBase.
DR CDD; cd00019; AP2Ec; 1.
DR HAMAP; MF_00152; Nfo; 1.
DR InterPro; IPR001719; AP_endonuc_2.
DR InterPro; IPR018246; AP_endonuc_F2_Zn_BS.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR PANTHER; PTHR21445; PTHR21445; 1.
DR Pfam; PF01261; AP_endonuc_2; 1.
DR SMART; SM00518; AP2Ec; 1.
DR SUPFAM; SSF51658; SSF51658; 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 DNA damage; DNA repair; Hydrolase; Metal-binding; Nucleus;
KW Reference proteome; Zinc.
FT CHAIN 1..396
FT /note="Apurinic-apyrimidinic endonuclease"
FT /id="PRO_0000190899"
FT REGION 31..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
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
