ID   APN1_SCHPO              Reviewed;         342 AA.
AC   P50525; Q9USI8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 3.
DT   27-MAR-2024, entry version 148.
DE   RecName: Full=Apurinic-apyrimidinic endonuclease 1;
DE            Short=AP endonuclease 1;
DE            EC=3.1.21.-;
GN   Name=apn1; ORFNames=SPCC622.17;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=14704348; DOI=10.1093/nar/gkh151;
RA   Ribar B., Izumi T., Mitra S.;
RT   "The major role of human AP-endonuclease homolog Apn2 in repair of abasic
RT   sites in Schizosaccharomyces pombe.";
RL   Nucleic Acids Res. 32:115-126(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   SEQUENCE REVISION.
RA   Seeger K., Harris D., Lyne M., Rajandream M.A., Barrell B.G.;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-319.
RX   PubMed=9524207; DOI=10.1016/s0167-4781(97)00160-7;
RA   Ramotar D., Vadnais J., Masson J.Y., Tremblay S.;
RT   "Schizosaccharomyces pombe apn1 encodes a homologue of the Escherichia coli
RT   endonuclease IV family of DNA repair proteins.";
RL   Biochim. Biophys. Acta 1396:15-20(1998).
RN   [5]
RP   LACK OF FUNCTION.
RX   PubMed=21193357; DOI=10.1016/j.dnarep.2010.11.014;
RA   Laerdahl J.K., Korvald H., Nilsen L., Dahl-Michelsen K., Rognes T.,
RA   Bjoras M., Alseth I.;
RT   "Schizosaccharomyces pombe encodes a mutated AP endonuclease 1.";
RL   DNA Repair 10:296-305(2011).
CC   -!- FUNCTION: DNA repair enzyme that cleaves apurinic/apyrimidinic (AP)
CC       sites and removes 3'-blocking groups present at single strand breaks of
CC       damaged DNA. Provides back-up AP endonuclease (APE) activity to apn2
CC       together with uve1. {ECO:0000269|PubMed:14704348}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the AP endonuclease 2 family. {ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene. This is a truncated
CC       version of AP endonuclease 1. In strain 972 and its derivative FY527,
CC       this gene has a stop codon in position 5, which disrupts the gene
CC       coding for this protein. PubMed:21193357 shows that the truncated
CC       protein is not functional. A full sequence for apn1 can be found in
CC       strains SPK19802 (S.pombe var. kambucha), NCYC 132, NCYC 683, NCYC 936
CC       and NCYC 2722 (PubMed:21193357). {ECO:0000305|PubMed:21193357}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC28163.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAC28163.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; AY483157; AAR83751.1; -; mRNA.
DR   EMBL; CU329672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U33625; AAC28163.1; ALT_SEQ; mRNA.
DR   PIR; T52563; T52563.
DR   AlphaFoldDB; P50525; -.
DR   SMR; P50525; -.
DR   STRING; 284812.P50525; -.
DR   PomBase; SPCC622.17; apn1.
DR   InParanoid; P50525; -.
DR   PhylomeDB; P50525; -.
DR   BRENDA; 4.2.99.18; 5613.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0140080; F:class III/IV DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:PomBase.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IBA:GO_Central.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR   CDD; cd00019; AP2Ec; 1.
DR   Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 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   NCBIfam; TIGR00587; nfo; 1.
DR   PANTHER; PTHR21445:SF0; APURINIC-APYRIMIDINIC ENDONUCLEASE; 1.
DR   PANTHER; PTHR21445; ENDONUCLEASE IV ENDODEOXYRIBONUCLEASE IV; 1.
DR   Pfam; PF01261; AP_endonuc_2; 1.
DR   SMART; SM00518; AP2Ec; 1.
DR   SUPFAM; SSF51658; Xylose isomerase-like; 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   5: Uncertain;
KW   DNA damage; DNA repair; Hydrolase; Metal-binding; Nucleus;
KW   Reference proteome; Zinc.
FT   CHAIN           1..342
FT                   /note="Apurinic-apyrimidinic endonuclease 1"
FT                   /id="PRO_0000190897"
FT   REGION          299..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         61
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         136
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         136
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         252
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   342 AA;  38657 MW;  C6711EC23691C51D CRC64;
     MCAINKAYLL TKFYISANSC AFFVKSQRKW TSPDLSEDVA QKFLETASEM KFDASKQVLV
     HGSYLINMAN ADEQKREQAF NCFVDDLKRC ERLGVGLYNF HPGSTASCTK EEGINNLAEC
     INRAHEETKS VIIVTENMAG QGNCLGGTFD DFAALKSKIK NLDRWRVCLD TCHTFAAGYD
     IRTEESYKKV IDEFDEKVGA KYVSGWHLND SKAPLGSNRD LHENIGLGFL GLEPFRLIMN
     DSRWDGIPLV LETPAKSPEQ WKKEVELLRF MVGKSSDDVE LMKESARLSN LGAASRKEHL
     NKFEKKEAKK DRKKKSKDGD QTTLLLRKKQ KLGNAEVKSL DE
//