APN2_SCHPO
ID APN2_SCHPO Reviewed; 523 AA.
AC P87175;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=DNA-(apurinic or apyrimidinic site) endonuclease 2;
DE EC=3.1.11.2 {ECO:0000269|PubMed:14704348};
DE AltName: Full=AP endonuclease 2;
DE AltName: Full=Apurinic-apyrimidinic endonuclease 2;
GN Name=apn2; ORFNames=SPBC3D6.10;
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS
RP OF PHE-402; PHE-403; PRO-456; LEU-457 AND CYS-458.
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] {ECO:0000305}
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] {ECO:0000305}
RP FUNCTION.
RX PubMed=14599746; DOI=10.1016/j.dnarep.2003.08.005;
RA Fraser J.L.A., Neill E., Davey S.;
RT "Fission yeast Uve1 and Apn2 function in distinct oxidative damage repair
RT pathways in vivo.";
RL DNA Repair 2:1253-1267(2003).
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 the majority of the AP-endonuclease (APE)
CC activity. Repairs phleomycin D1-induced DNA damage. Plays a role in
CC oxidative damage repair. {ECO:0000269|PubMed:14599746,
CC ECO:0000269|PubMed:14704348}.
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:0000269|PubMed:14704348};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Probably binds two magnesium or manganese ions per subunit.
CC {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00764}.
CC -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family.
CC {ECO:0000305}.
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DR EMBL; AY483158; AAR83752.1; -; mRNA.
DR EMBL; CU329671; CAB09119.1; -; Genomic_DNA.
DR PIR; T40370; T40370.
DR RefSeq; NP_595522.1; NM_001021431.2.
DR AlphaFoldDB; P87175; -.
DR SMR; P87175; -.
DR BioGRID; 277204; 28.
DR STRING; 4896.SPBC3D6.10.1; -.
DR iPTMnet; P87175; -.
DR MaxQB; P87175; -.
DR PaxDb; P87175; -.
DR PRIDE; P87175; -.
DR EnsemblFungi; SPBC3D6.10.1; SPBC3D6.10.1:pep; SPBC3D6.10.
DR GeneID; 2540679; -.
DR KEGG; spo:SPBC3D6.10; -.
DR PomBase; SPBC3D6.10; apn2.
DR VEuPathDB; FungiDB:SPBC3D6.10; -.
DR eggNOG; KOG1294; Eukaryota.
DR HOGENOM; CLU_010374_2_0_1; -.
DR InParanoid; P87175; -.
DR OMA; FIWSSDW; -.
DR PhylomeDB; P87175; -.
DR PRO; PR:P87175; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:PomBase.
DR GO; GO:0008311; F:double-stranded DNA 3'-5' exodeoxyribonuclease activity; IMP:PomBase.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004528; F:phosphodiesterase I activity; IDA:PomBase.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IBA:GO_Central.
DR GO; GO:0006284; P:base-excision repair; EXP:PomBase.
DR GO; GO:0006281; P:DNA repair; IMP:PomBase.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR004808; AP_endonuc_1.
DR InterPro; IPR020847; AP_endonuclease_F1_BS.
DR InterPro; IPR020848; AP_endonuclease_F1_CS.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR PANTHER; PTHR22748; PTHR22748; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
DR TIGRFAMs; TIGR00633; xth; 1.
DR PROSITE; PS00726; AP_NUCLEASE_F1_1; 1.
DR PROSITE; PS00727; AP_NUCLEASE_F1_2; 1.
DR PROSITE; PS51435; AP_NUCLEASE_F1_4; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Hydrolase; Magnesium; Metal-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..523
FT /note="DNA-(apurinic or apyrimidinic site) endonuclease 2"
FT /id="PRO_0000200019"
FT REGION 348..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /evidence="ECO:0000250"
FT ACT_SITE 191
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT SITE 193
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 269
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 295
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 402
FT /note="F->A: No change in activity; when associated with A-
FT 403."
FT /evidence="ECO:0000269|PubMed:14704348"
FT MUTAGEN 403
FT /note="F->A: No change in activity; when associated with A-
FT 402."
FT /evidence="ECO:0000269|PubMed:14704348"
FT MUTAGEN 456
FT /note="P->A: No change in activity; when associated with A-
FT 457 and A-458."
FT /evidence="ECO:0000269|PubMed:14704348"
FT MUTAGEN 457
FT /note="L->A: No change in activity; when associated with A-
FT 456 and A-458."
FT /evidence="ECO:0000269|PubMed:14704348"
FT MUTAGEN 458
FT /note="C->A: No change in activity; when associated with A-
FT 456 and A-457."
FT /evidence="ECO:0000269|PubMed:14704348"
SQ SEQUENCE 523 AA; 60313 MW; B2A79AE61579FA1C CRC64;
MRILSWNVNG IQNPFNYFPW NKKNSYKEIF QELQADVICV QELKMQKDSF PQQYAVVEGF
DSYFTFPKIR KGYSGVGFYV KKDVAIPVKA EEGITGILPV RGQKYSYSEA PEHEKIGFFP
KDIDRKTANW IDSEGRCILL DFQMFILIGV YCPVNSGENR LEYRRAFYKA LRERIERLIK
EGNRKIILVG DVNILCNPID TADQKDIIRE SLIPSIMESR QWIRDLLLPS RLGLLLDIGR
IQHPTRKGMF TCWNTRLNTR PTNYGTRIDY TLATPDLLPW VQDADIMAEV MGSDHCPVYL
DLKEEYEGKK LSNFLSHSKE PPLLSTAHHS AYRPSKNIHS MFQHFNSMKK NKNNSPTQSE
NVSASASSGS SPTVSRANSV IDVDAYPPEK RRRKEQSKLL SFFAKQKEEK EETNKTEDVS
IEVLDNNNES DIGLTVKKKV ENGNAWKQIF SERAPPLCEG HKEPCKYLTV RKPGINYGRK
FWICARPVGE LIKNSNAVSE EDTQPFQCRF FIWDSDWRAN SKD
