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Database: UniProt
Entry: W5QEQ3_SHEEP
LinkDB: W5QEQ3_SHEEP
Original site: W5QEQ3_SHEEP 
ID   W5QEQ3_SHEEP            Unreviewed;       318 AA.
AC   W5QEQ3;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   05-JUN-2019, entry version 27.
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:ENSOARP00000021201};
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Caprinae; Ovis.
OX   NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000021201, ECO:0000313|Proteomes:UP000002356};
RN   [1] {ECO:0000313|Ensembl:ENSOARP00000021201, ECO:0000313|Proteomes:UP000002356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000021201};
RX   PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA   Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA   Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C.,
RA   Wang J., Wang W., Xun X.;
RT   "The sheep genome reference sequence: a work in progress.";
RL   Anim. Genet. 41:449-453(2010).
RN   [2] {ECO:0000313|Ensembl:ENSOARP00000021201}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (FEB-2014) 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   EMBL; AMGL01102304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004010439.1; XM_004010390.2.
DR   RefSeq; XP_012036475.1; XM_012181085.1.
DR   RefSeq; XP_012036476.1; XM_012181086.1.
DR   RefSeq; XP_012036477.1; XM_012181087.2.
DR   STRING; 9940.ENSOARP00000021201; -.
DR   Ensembl; ENSOART00000021496; ENSOARP00000021201; ENSOARG00000019740.
DR   GeneID; 101115462; -.
DR   KEGG; oas:101115462; -.
DR   CTD; 328; -.
DR   GeneTree; ENSGT00530000063540; -.
DR   KO; K10771; -.
DR   OMA; GTAVFTK; -.
DR   OrthoDB; 1105625at2759; -.
DR   Proteomes; UP000002356; Chromosome 7.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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:UP000002356};
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:UP000002356}.
FT   DOMAIN       66    309       Endo/exonuclease/phosphatase.
FT                                {ECO:0000259|Pfam:PF03372}.
FT   REGION        1     59       Disordered. {ECO:0000256|MobiDB-lite:
FT                                W5QEQ3}.
FT   COMPBIAS      1     41       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                W5QEQ3}.
SQ   SEQUENCE   318 AA;  35582 MW;  A34CCB9B5466EC0B CRC64;
     MPKRGKKGAV VEDAEEPKTE PEAKKSKAGA KKNEKEAVGE GAVLYEDPPD QKTSPSGKSA
     TLKICSWNVD GLRAWIKKKG LDWIKEEAPD ILCLQETKCS ENKLPVELQE LSGLPHQYWS
     APSDKEGYSG VGLLSRQCPL KVSYGIGEEE HDQEGRVIVA EYDAFVLVTA YVPNAGRGLV
     RLEYRQCWDE AFRKFLKGLA SRKPLVLCGD LNVAHEEIDL RNPKGNKKNA GFTPQERQGF
     GELLQAAPLT DSFRHLYPNR AYAYTFWTYM MNARSKNVGW RLDYFLLSQS LLPALCDSKI
     RSKALGSDHC PITLYLAL
//
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