APN2_YEAST
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 03-AUG-2022, entry version 159.
DE RecName: Full=DNA-(apurinic or apyrimidinic site) endonuclease 2;
DE EC=3.1.11.2 {ECO:0000269|PubMed:10806210, ECO:0000269|PubMed:9765213};
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; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
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., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA 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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and 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., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 major
RT human AP endonuclease HAP1, and its role in the repair of abasic sites.";
RL Genes Dev. 12:3137-3143(1998).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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., Dephoure N.,
RA 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 (AP)
CC sites and removes 3'-blocking groups present at single strand breaks of
CC damaged DNA. {ECO:0000269|PubMed:10806210, ECO:0000269|PubMed:9765213}.
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:10806210, ECO:0000269|PubMed:9765213};
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.
CC -!- MISCELLANEOUS: Present with 414 molecules/cell in log phase SD medium.
CC {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 AlphaFoldDB; P38207; -.
DR SMR; P38207; -.
DR BioGRID; 32679; 78.
DR DIP; DIP-3930N; -.
DR IntAct; P38207; 4.
DR MINT; P38207; -.
DR STRING; 4932.YBL019W; -.
DR MaxQB; P38207; -.
DR PaxDb; P38207; -.
DR PRIDE; P38207; -.
DR EnsemblFungi; YBL019W_mRNA; YBL019W; YBL019W.
DR GeneID; 852262; -.
DR KEGG; sce:YBL019W; -.
DR SGD; S000000115; APN2.
DR VEuPathDB; FungiDB:YBL019W; -.
DR eggNOG; KOG1294; Eukaryota.
DR GeneTree; ENSGT00530000063540; -.
DR HOGENOM; CLU_010374_0_0_1; -.
DR InParanoid; P38207; -.
DR OMA; YTVWNTL; -.
DR BioCyc; YEAST:G3O-28922-MON; -.
DR PRO; PR:P38207; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38207; protein.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:SGD.
DR GO; GO:0008311; F:double-stranded DNA 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 Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR004808; AP_endonuc_1.
DR InterPro; IPR020848; AP_endonuclease_F1_CS.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
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; 1.
DR PROSITE; PS00728; AP_NUCLEASE_F1_3; 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; Zinc; Zinc-finger.
FT CHAIN 1..520
FT /note="DNA-(apurinic or apyrimidinic site) endonuclease 2"
FT /id="PRO_0000200020"
FT ZN_FING 474..520
FT /note="GRF-type"
FT ACT_SITE 181
FT /evidence="ECO:0000250"
FT ACT_SITE 222
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT SITE 224
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 328
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 354
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 15
FT /note="N -> D (in Ref. 3; AAT93202)"
FT /evidence="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
