APN1_SCHPO
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 03-AUG-2022, entry version 143.
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 PRIDE; 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; ISO:PomBase.
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 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 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
