ID APN2_YEAST Reviewed; 520 AA.
AC P38207; D6VPY1; E9P926;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 01-MAY-2013, entry version 102.
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; Synonyms=ETH1; OrderedLocusNames=YBL019W; ORFNames=YBL0443;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
RA Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
RA Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
RA Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
RA Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
RA Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
RA Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
RA Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
RA Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
RA Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
RA Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
RA van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
RA Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
RA Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RG Saccharomyces Genome Database;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
RA Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA Kolodner R.D., LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-
RT encoding clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP CHARACTERIZATION.
RX PubMed=9765213;
RA Johnson R.E., Torres-Ramos C.A., Izumi T., Mitra S., Prakash S.,
RA Prakash L.;
RT "Identification of APN2, the Saccharomyces cerevisiae homolog of the
RT major human AP endonuclease HAP1, and its role in the repair of abasic
RT sites.";
RL Genes Dev. 12:3137-3143(1998).
RN [5]
RP CHARACTERIZATION.
RX PubMed=10806210; DOI=10.1074/jbc.M002845200;
RA Unk I., Haracska L., Johnson R.E., Prakash S., Prakash L.;
RT "Apurinic endonuclease activity of yeast Apn2 protein.";
RL J. Biol. Chem. 275:22427-22434(2000).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA Dephoure N., O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(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.
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.
CC -!- MISCELLANEOUS: Present with 414 molecules/cell in log phase SD
CC medium.
CC -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family.
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DR EMBL; Z35780; CAA84838.1; -; Genomic_DNA.
DR EMBL; AY693183; AAT93202.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07101.1; -; Genomic_DNA.
DR PIR; S45753; S45753.
DR RefSeq; NP_009534.1; NM_001178259.1.
DR ProteinModelPortal; P38207; -.
DR SMR; P38207; 17-365.
DR DIP; DIP-3930N; -.
DR IntAct; P38207; 2.
DR MINT; MINT-515848; -.
DR STRING; 4932.YBL019W; -.
DR PaxDb; P38207; -.
DR EnsemblFungi; YBL019W; YBL019W; YBL019W.
DR GeneID; 852262; -.
DR KEGG; sce:YBL019W; -.
DR CYGD; YBL019w; -.
DR SGD; S000000115; APN2.
DR eggNOG; COG0708; -.
DR GeneTree; ENSGT00530000063540; -.
DR HOGENOM; HOG000246560; -.
DR KO; K10772; -.
DR OMA; MYTVWNT; -.
DR OrthoDB; EOG4GQTDH; -.
DR NextBio; 970856; -.
DR Genevestigator; P38207; -.
DR GermOnline; YBL019W; Saccharomyces cerevisiae.
DR GO; GO:0005634; C:nucleus; IC:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IDA:SGD.
DR GO; GO:0008311; F:double-stranded DNA specific 3'-5' exodeoxyribonuclease activity; IDA:SGD.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IGI:SGD.
DR InterPro; IPR020848; AP_endonuclease_F1_CS.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR004808; ExoDNase_III.
DR InterPro; IPR010666; Znf_GRF.
DR PANTHER; PTHR22748; PTHR22748; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF06839; zf-GRF; 1.
DR SUPFAM; SSF56219; Exo_endo_phos; 1.
DR PROSITE; PS00726; AP_NUCLEASE_F1_1; FALSE_NEG.
DR PROSITE; PS00727; AP_NUCLEASE_F1_2; FALSE_NEG.
DR PROSITE; PS00728; AP_NUCLEASE_F1_3; 1.
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 1 520 DNA-(apurinic or apyrimidinic site) lyase
FT 2.
FT /FTId=PRO_0000200020.
FT ACT_SITE 181 181 By similarity.
FT ACT_SITE 222 222 Proton donor/acceptor (By similarity).
FT METAL 59 59 Magnesium 1 (By similarity).
FT METAL 222 222 Magnesium 2 (By similarity).
FT METAL 224 224 Magnesium 2 (By similarity).
FT METAL 353 353 Magnesium 1 (By similarity).
FT SITE 224 224 Transition state stabilizer (By
FT similarity).
FT SITE 328 328 Important for catalytic activity (By
FT similarity).
FT SITE 354 354 Interaction with DNA substrate (By
FT similarity).
FT CONFLICT 15 15 N -> D (in Ref. 3; AAT93202).
SQ SEQUENCE 520 AA; 59445 MW; E3947C4D904C53FB CRC64;
MSSSENTLLD GKSENTIRFL TFNVNGIRTF FHYQPFSQMN QSLRSVFDFF RADIITFQEL
KTEKLSISKW GRVDGFYSFI SIPQTRKGYS GVGCWIRIPE KNHPLYHALQ VVKAEEGITG
YLTIKNGKHS AISYRNDVNQ GIGGYDSLDP DLDEKSALEL DSEGRCVMVE LACGIVIISV
YCPANSNSSE EGEMFRLRFL KVLLRRVRNL DKIGKKIVLM GDVNVCRDLI DSADTLEQFS
IPITDPMGGT KLEAQYRDKA IQFIINPDTP HRRIFNQILA DSLLPDASKR GILIDTTRLI
QTRNRLKMYT VWNMLKNLRP SNYGSRIDFI LVSLKLERCI KAADILPDIL GSDHCPVYSD
LDILDDRIEP GTTQVPIPKF EARYKYNLRN HNVLEMFAKK DTNKESNKQK YCVSKVMNTK
KNSNIKNKSL DSFFQKVNGE KDDRIKESSE IPQQAKKRIS TPKLNFKDVF GKPPLCRHGE
ESMLKTSKTS ANPGRKFWIC KRSRGDSNNT ESSCGFFQWV
//
