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DNA-(apurinic or apyrimidinic site) lyase (EC 4.2.99.18) (Fragment)

 D3Z124_MOUSE            Unreviewed;       177 AA.
D3Z124;
20-APR-2010, integrated into UniProtKB/TrEMBL.
20-APR-2010, sequence version 1.
12-SEP-2018, entry version 68.
RecName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|RuleBase:RU362131};
EC=4.2.99.18 {ECO:0000256|RuleBase:RU362131};
Flags: Fragment;
Name=Apex1 {ECO:0000313|Ensembl:ENSMUSP00000123148,
ECO:0000313|MGI:MGI:88042};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000123148, ECO:0000313|Proteomes:UP000000589};
[1] {ECO:0000313|Ensembl:ENSMUSP00000123148, ECO:0000313|Proteomes:UP000000589}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000123148,
ECO:0000313|Proteomes:UP000000589};
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2] {ECO:0000213|PubMed:21183079}
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[3] {ECO:0000313|Ensembl:ENSMUSP00000123148}
IDENTIFICATION.
STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000123148};
Ensembl;
Submitted (MAY-2011) to UniProtKB.
-!- FUNCTION: Initiates repair of AP sites in DNA by catalyzing
hydrolytic incision of the phosphodiester backbone immediately
adjacent to the damage, generating a single-strand break with 5'-
deoxyribose phosphate and 3'-hydroxyl ends.
{ECO:0000256|RuleBase:RU362131}.
-!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
apyrimidinic site in DNA is broken by a beta-elimination reaction,
leaving a 3'-terminal unsaturated sugar and a product with a
terminal 5'-phosphate. {ECO:0000256|RuleBase:RU362131}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|RuleBase:RU362131};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|RuleBase:RU362131};
Note=Probably binds two magnesium or manganese ions per subunit.
{ECO:0000256|RuleBase:RU362131};
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU362131}.
Cytoplasm {ECO:0000256|RuleBase:RU362131}. Mitochondrion
{ECO:0000256|RuleBase:RU362131}.
-!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family.
{ECO:0000256|RuleBase:RU362131}.
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EMBL; AC027184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
SMR; D3Z124; -.
MaxQB; D3Z124; -.
PeptideAtlas; D3Z124; -.
PRIDE; D3Z124; -.
Ensembl; ENSMUST00000136753; ENSMUSP00000123148; ENSMUSG00000035960.
MGI; MGI:88042; Apex1.
eggNOG; KOG1294; Eukaryota.
eggNOG; COG0708; LUCA.
GeneTree; ENSGT00530000063540; -.
HOGENOM; HOG000034586; -.
ChiTaRS; Apex1; mouse.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000035960; Expressed in 319 organ(s), highest expression level in optic fissure.
ExpressionAtlas; D3Z124; baseline and differential.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0045454; P:cell redox homeostasis; IEA:Ensembl.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
Gene3D; 3.60.10.10; -; 1.
InterPro; IPR004808; AP_endonuc_1.
InterPro; IPR020847; AP_endonuclease_F1_BS.
InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
InterPro; IPR005135; Endo/exonuclease/phosphatase.
PANTHER; PTHR22748; PTHR22748; 1.
Pfam; PF03372; Exo_endo_phos; 1.
SUPFAM; SSF56219; SSF56219; 1.
TIGRFAMs; TIGR00633; xth; 1.
PROSITE; PS00726; AP_NUCLEASE_F1_1; 1.
PROSITE; PS51435; AP_NUCLEASE_F1_4; 1.
1: Evidence at protein level;
Complete proteome {ECO:0000313|Proteomes:UP000000589};
Cytoplasm {ECO:0000256|RuleBase:RU362131};
DNA damage {ECO:0000256|RuleBase:RU362131};
DNA repair {ECO:0000256|RuleBase:RU362131};
DNA-binding {ECO:0000256|RuleBase:RU362131};
Endonuclease {ECO:0000256|RuleBase:RU362131};
Hydrolase {ECO:0000256|RuleBase:RU362131};
Lyase {ECO:0000256|RuleBase:RU362131};
Magnesium {ECO:0000256|RuleBase:RU362131};
Metal-binding {ECO:0000256|RuleBase:RU362131};
Mitochondrion {ECO:0000256|RuleBase:RU362131};
Nuclease {ECO:0000256|RuleBase:RU362131};
Nucleus {ECO:0000256|RuleBase:RU362131};
Proteomics identification {ECO:0000213|EPD:D3Z124,
ECO:0000213|MaxQB:D3Z124, ECO:0000213|PeptideAtlas:D3Z124};
Reference proteome {ECO:0000313|Proteomes:UP000000589}.
DOMAIN 65 154 Endo/exonuclease/phosphatase.
{ECO:0000259|Pfam:PF03372}.
NON_TER 177 177 {ECO:0000313|Ensembl:ENSMUSP00000123148}.
SEQUENCE 177 AA; 19302 MW; B5900D1A3389FA67 CRC64;
MPKRGKKAAA DDGEEPKSEP ETKKSKGAAK KTEKEAAGEG PVLYEDPPDQ KTSPSGKSAT
LKICSWNVDG LRAWIKKKGL DWVKEEAPDI LCLQETKCSE NKLPAELQEL PGLTHQYWSA
PSDKEGYSGV GLLSRQCPLK VSYGIGEEEH DQEGRVIVAE FESFVLVTAY VPNAGRG


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