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Database: UniProt
Entry: P38207
LinkDB: P38207
Original site: P38207 
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   29-OCT-2014, entry version 112.
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;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
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; DOI=10.1101/gad.12.19.3137;
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. {ECO:0000255|PROSITE-ProRule:PRU00764}.
CC   -!- COFACTOR: Magnesium. Can also utilize manganese. Probably binds
CC       two magnesium or manganese ions per subunit (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- MISCELLANEOUS: Present with 414 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family.
CC       {ECO:0000305}.
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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   BioGrid; 32679; 39.
DR   DIP; DIP-3930N; -.
DR   IntAct; P38207; 2.
DR   MINT; MINT-515848; -.
DR   STRING; 4932.YBL019W; -.
DR   MaxQB; P38207; -.
DR   PaxDb; P38207; -.
DR   PRIDE; 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   InParanoid; P38207; -.
DR   KO; K10772; -.
DR   OMA; GRKFWIC; -.
DR   OrthoDB; EOG7TTQJT; -.
DR   BioCyc; YEAST:G3O-28922-MONOMER; -.
DR   NextBio; 970856; -.
DR   PRO; PR:P38207; -.
DR   Genevestigator; P38207; -.
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 3'-5' exodeoxyribonuclease activity; IDA:SGD.
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   GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IDA:GOC.
DR   GO; GO:0000738; P:DNA catabolic process, exonucleolytic; IDA:GOC.
DR   Gene3D; 3.60.10.10; -; 2.
DR   InterPro; IPR004808; AP_endonuc_1.
DR   InterPro; IPR020848; AP_endonuclease_F1_CS.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
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; SSF56219; 2.
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       {ECO:0000250}.
FT   ACT_SITE    222    222       Proton donor/acceptor. {ECO:0000250}.
FT   METAL        59     59       Magnesium 1. {ECO:0000250}.
FT   METAL       222    222       Magnesium 2. {ECO:0000250}.
FT   METAL       224    224       Magnesium 2. {ECO:0000250}.
FT   METAL       353    353       Magnesium 1. {ECO:0000250}.
FT   SITE        224    224       Transition state stabilizer.
FT                                {ECO:0000250}.
FT   SITE        328    328       Important for catalytic activity.
FT                                {ECO:0000250}.
FT   SITE        354    354       Interaction with DNA substrate.
FT                                {ECO:0000250}.
FT   CONFLICT     15     15       N -> D (in Ref. 3; AAT93202).
FT                                {ECO:0000305}.
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
//
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