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 01-MAY-2013, entry version 88.
DE RecName: Full=DNA-(apurinic or apyrimidinic site) lyase 2;
DE EC=4.2.99.18;
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;
OC Schizosaccharomycetaceae; Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP MUTAGENESIS 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
RT abasic 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.,
RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
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
RT repair pathways in vivo.";
RL DNA Repair 2:1253-1267(2003).
CC -!- FUNCTION: DNA repair enzyme that cleaves apurinic/apyrimidinic
CC (AP) sites and removes 3'-blocking groups present at single strand
CC breaks of damaged DNA. Provides the majority of the AP-
CC endonuclease (APE) activity. Repairs phleomycin D1-induced DNA
CC damage. Plays a role in oxidative damage repair.
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: Magnesium. Can also utilize manganese. Probably binds
CC two magnesium or manganese ions per subunit (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family.
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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 ProteinModelPortal; P87175; -.
DR STRING; 4896.SPBC3D6.10-1; -.
DR EnsemblFungi; SPBC3D6.10.1; SPBC3D6.10.1:pep; SPBC3D6.10.
DR GeneID; 2540679; -.
DR KEGG; spo:SPBC3D6.10; -.
DR PomBase; SPBC3D6.10; -.
DR eggNOG; COG0708; -.
DR KO; K10772; -.
DR OMA; FIDSYRC; -.
DR OrthoDB; EOG4GQTDH; -.
DR NextBio; 20801803; -.
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) lyase activity; IEA:EC.
DR GO; GO:0008311; F:double-stranded DNA specific 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; ISO:PomBase.
DR GO; GO:0006284; P:base-excision repair; IC:PomBase.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:PomBase.
DR InterPro; IPR020847; AP_endonuclease_F1_BS.
DR InterPro; IPR020848; AP_endonuclease_F1_CS.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR004808; ExoDNase_III.
DR PANTHER; PTHR22748; PTHR22748; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SUPFAM; SSF56219; Exo_endo_phos; 1.
DR TIGRFAMs; TIGR00633; xth; 1.
DR PROSITE; PS00726; AP_NUCLEASE_F1_1; 1.
DR PROSITE; PS00727; AP_NUCLEASE_F1_2; 1.
DR PROSITE; PS00728; AP_NUCLEASE_F1_3; FALSE_NEG.
DR PROSITE; PS51435; AP_NUCLEASE_F1_4; 1.
PE 1: Evidence at protein level;
KW Complete proteome; DNA damage; DNA repair; Lyase; Magnesium;
KW Metal-binding; Nucleus; Reference proteome.
FT CHAIN 1 523 DNA-(apurinic or apyrimidinic site) lyase
FT 2.
FT /FTId=PRO_0000200019.
FT ACT_SITE 151 151 By similarity.
FT ACT_SITE 191 191 Proton donor/acceptor (By similarity).
FT METAL 42 42 Magnesium 1 (By similarity).
FT METAL 191 191 Magnesium 2 (By similarity).
FT METAL 193 193 Magnesium 2 (By similarity).
FT METAL 294 294 Magnesium 1 (By similarity).
FT SITE 193 193 Transition state stabilizer (By
FT similarity).
FT SITE 269 269 Important for catalytic activity (By
FT similarity).
FT SITE 295 295 Interaction with DNA substrate (By
FT similarity).
FT MUTAGEN 402 402 F->A: No change in activity; when
FT associated with A-403.
FT MUTAGEN 403 403 F->A: No change in activity; when
FT associated with A-402.
FT MUTAGEN 456 456 P->A: No change in activity; when
FT associated with A-457 and A-458.
FT MUTAGEN 457 457 L->A: No change in activity; when
FT associated with A-456 and A-458.
FT MUTAGEN 458 458 C->A: No change in activity; when
FT associated with A-456 and A-457.
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
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