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Database: UniProt
Entry: A0A140T846_BOVIN
LinkDB: A0A140T846_BOVIN
Original site: A0A140T846_BOVIN 
ID   A0A140T846_BOVIN        Unreviewed;       318 AA.
AC   A0A140T846;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   05-JUN-2019, entry version 25.
DE   RecName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|RuleBase:RU362131};
DE            EC=4.2.99.18 {ECO:0000256|RuleBase:RU362131};
GN   Name=APEX1 {ECO:0000313|Ensembl:ENSBTAP00000003559,
GN   ECO:0000313|VGNC:VGNC:26011};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000003559, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000003559, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000003559,
RC   ECO:0000313|Proteomes:UP000009136};
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C.,
RA   Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S.,
RA   Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000003559}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000003559};
RG   Ensembl;
RL   Submitted (MAR-2016) to UniProtKB.
CC   -!- FUNCTION: Initiates repair of AP sites in DNA by catalyzing
CC       hydrolytic incision of the phosphodiester backbone immediately
CC       adjacent to the damage, generating a single-strand break with 5'-
CC       deoxyribose phosphate and 3'-hydroxyl ends.
CC       {ECO:0000256|RuleBase:RU362131}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=The C-O-P bond 3' to the apurinic or apyrimidinic site in
CC         DNA is broken by a beta-elimination reaction, leaving a 3'-
CC         terminal unsaturated sugar and a product with a terminal 5'-
CC         phosphate.; EC=4.2.99.18;
CC         Evidence={ECO:0000256|RuleBase:RU362131};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU362131};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU362131};
CC       Note=Probably binds two magnesium or manganese ions per subunit.
CC       {ECO:0000256|RuleBase:RU362131};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU362131}.
CC       Cytoplasm {ECO:0000256|RuleBase:RU362131}. Mitochondrion
CC       {ECO:0000256|RuleBase:RU362131}.
CC   -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family.
CC       {ECO:0000256|RuleBase:RU362131}.
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DR   RefSeq; NP_788782.2; NM_176609.3.
DR   SMR; A0A140T846; -.
DR   Ensembl; ENSBTAT00000003559; ENSBTAP00000003559; ENSBTAG00000002745.
DR   GeneID; 281630; -.
DR   KEGG; bta:281630; -.
DR   CTD; 328; -.
DR   VGNC; VGNC:26011; APEX1.
DR   GeneTree; ENSGT00530000063540; -.
DR   KO; K10771; -.
DR   OMA; GTAVFTK; -.
DR   OrthoDB; 1105625at2759; -.
DR   Proteomes; UP000009136; Chromosome 10.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
DR   GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:Ensembl.
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:0003691; F:double-stranded telomeric DNA binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:Ensembl.
DR   GO; GO:0004528; F:phosphodiesterase I activity; IBA:GO_Central.
DR   GO; GO:0016890; F:site-specific endodeoxyribonuclease activity, specific for altered base; IEA:Ensembl.
DR   GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR   GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:Ensembl.
DR   GO; GO:0080111; P:DNA demethylation; IEA:Ensembl.
DR   GO; GO:0042981; P:regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0043488; P:regulation of mRNA stability; IEA:Ensembl.
DR   GO; GO:0097698; P:telomere maintenance via base-excision repair; IEA:Ensembl.
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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000009136};
KW   Cytoplasm {ECO:0000256|RuleBase:RU362131};
KW   DNA damage {ECO:0000256|RuleBase:RU362131};
KW   DNA repair {ECO:0000256|RuleBase:RU362131};
KW   DNA-binding {ECO:0000256|RuleBase:RU362131};
KW   Endonuclease {ECO:0000256|RuleBase:RU362131};
KW   Hydrolase {ECO:0000256|RuleBase:RU362131};
KW   Lyase {ECO:0000256|RuleBase:RU362131};
KW   Magnesium {ECO:0000256|RuleBase:RU362131};
KW   Metal-binding {ECO:0000256|RuleBase:RU362131};
KW   Mitochondrion {ECO:0000256|RuleBase:RU362131};
KW   Nuclease {ECO:0000256|RuleBase:RU362131};
KW   Nucleus {ECO:0000256|RuleBase:RU362131};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136}.
FT   DOMAIN       66    309       Endo/exonuclease/phosphatase.
FT                                {ECO:0000259|Pfam:PF03372}.
FT   REGION        1     59       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A140T846}.
FT   COMPBIAS      1     41       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A140T846}.
SQ   SEQUENCE   318 AA;  35584 MW;  40C733E00350738D CRC64;
     MPKRGKKGAV VEDAEEPKTE PEAKKSKAGA KKNEKEAVGE GAVLYEDPPD QKTSPSGKSA
     TLKICSWNVD GLRAWIKKKG LDWVKEEAPD ILCLQETKCS ENKLPVELQE LSGLSHQYWS
     APSDKEGYSG VGLLSRQCPL KVSYGIGEEE HDQEGRVIVA EYDAFVLVTA YVPNAGRGLV
     RLEYRQRWDE AFRKFLKGLA SRKPLVLCGD LNVAHEEIDL RNPKGNKKNA GFTPQERQGF
     GELLQAVPLT DSFRHLYPNT AYAYTFWTYM MNARSKNVGW RLDYFLLSQS LLPALCDSKI
     RSKALGSDHC PITLYLAL
//
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