APEA_DICDI
ID APEA_DICDI Reviewed; 361 AA.
AC P51173; Q54Z97; Q75K06;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=DNA-(apurinic or apyrimidinic site) endonuclease;
DE EC=3.1.-.-;
DE AltName: Full=Class II apurinic/apyrimidinic(AP)-endonuclease;
GN Name=apeA; ORFNames=DDB_G0277701;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8657579; DOI=10.1093/nar/24.10.1950;
RA Freeland T.M., Guyer R.B., Ling A.Z., Deering R.A.;
RT "Apurinic/apyrimidinic (AP) endonuclease from Dictyostelium discoideum:
RT cloning, nucleotide sequence and induction by sublethal levels of DNA
RT damaging agents.";
RL Nucleic Acids Res. 24:1950-1953(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 -!- INDUCTION: By DNA-damaging agents including UV, MNNG, gamma rays,
CC bleomycin and streptozotocin.
CC -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family.
CC {ECO:0000305}.
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DR EMBL; U31631; AAC47024.1; -; Genomic_DNA.
DR EMBL; AAFI02000021; EAL68586.1; -; Genomic_DNA.
DR PIR; S68268; S68268.
DR RefSeq; XP_642518.1; XM_637426.1.
DR AlphaFoldDB; P51173; -.
DR SMR; P51173; -.
DR STRING; 44689.DDB0185018; -.
DR PaxDb; P51173; -.
DR EnsemblProtists; EAL68586; EAL68586; DDB_G0277701.
DR GeneID; 8621167; -.
DR KEGG; ddi:DDB_G0277701; -.
DR dictyBase; DDB_G0277701; apeA.
DR eggNOG; KOG1294; Eukaryota.
DR HOGENOM; CLU_027539_1_3_1; -.
DR InParanoid; P51173; -.
DR OMA; WWSYRGR; -.
DR PhylomeDB; P51173; -.
DR Reactome; R-DDI-110357; Displacement of DNA glycosylase by APEX1.
DR Reactome; R-DDI-110362; POLB-Dependent Long Patch Base Excision Repair.
DR Reactome; R-DDI-110373; Resolution of AP sites via the multiple-nucleotide patch replacement pathway.
DR Reactome; R-DDI-73930; Abasic sugar-phosphate removal via the single-nucleotide replacement pathway.
DR Reactome; R-DDI-73933; Resolution of Abasic Sites (AP sites).
DR PRO; PR:P51173; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IBA:GO_Central.
DR GO; GO:0008311; F:double-stranded DNA 3'-5' exodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0016889; F:endodeoxyribonuclease activity, producing 3'-phosphomonoesters; TAS:dictyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IBA:GO_Central.
DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
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; PS00728; AP_NUCLEASE_F1_3; 1.
DR PROSITE; PS51435; AP_NUCLEASE_F1_4; 1.
PE 2: Evidence at transcript level;
KW DNA damage; DNA repair; Hydrolase; Magnesium; Metal-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..361
FT /note="DNA-(apurinic or apyrimidinic site) endonuclease"
FT /id="PRO_0000200016"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 41..44
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 211
FT /evidence="ECO:0000250"
FT ACT_SITE 252
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT SITE 254
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 324
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 351
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 126
FT /note="Y -> C (in Ref. 1; AAC47024)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="D -> V (in Ref. 1; AAC47024)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 41327 MW; BBD46E1CE3B5135A CRC64;
MTSRTKKLKM DEEEILKKED GSETTSEEEK EEVEEEEEED KKRKLVKKTP AKKAPAKKAA
AKKKSKDEDE DEEEKEEEEE TNKTTASVSI AIDNLDEPKV EENQMKIISW NVAGFKSVLS
KGFTEYVEKE NPDVLCLQET KINPSNIKKD QMPKGYEYHF IEADQKGHHG TGVLTKKKPN
AITFGIGIAK HDNEGRVITL EYDQFYIVNT YIPNAGTRGL QRLDYRIKEW DVDFQAYLEK
LNATKPIIWC GDLNVAHTEI DLKNPKTNKK SAGFTIEERT SFSNFLEKGY VDSYRHFNPG
KEGSYTFWSY LGGGRSKNVG WRLDYFVVSK RLMDSIKISP FHRTSVMGSD HCPIGVVVDL
N
