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Database: UniProt
Entry: F7GIK6_MACMU
LinkDB: F7GIK6_MACMU
Original site: F7GIK6_MACMU 
ID   F7GIK6_MACMU            Unreviewed;       318 AA.
AC   F7GIK6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   05-JUN-2019, entry version 67.
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|EMBL:AFH32205.1,
GN   ECO:0000313|Ensembl:ENSMMUP00000044871};
GN   ORFNames=EGK_17940 {ECO:0000313|EMBL:EHH27677.1};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000044871, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Ensembl:ENSMMUP00000044871, ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000044871,
RC   ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C.,
RA   Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W.,
RA   Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E.,
RA   Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y.,
RA   Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T.,
RA   Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J.,
RA   Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A.,
RA   Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M.,
RA   Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D.,
RA   Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J.,
RA   Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E.,
RA   Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S.,
RA   Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X.,
RA   Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E.,
RA   Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M.,
RA   Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M.,
RA   Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y.,
RA   Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J.,
RA   Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A.,
RA   Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B.,
RA   Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S.,
RA   Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V.,
RA   Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A.,
RA   Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C.,
RA   Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P.,
RA   Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E.,
RA   Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque
RT   genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|EMBL:EHH27677.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CR-5 {ECO:0000313|EMBL:EHH27677.1};
RX   PubMed=22002653; DOI=10.1038/nbt.1992;
RA   Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N.,
RA   Li Q., Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P.,
RA   Huang Z., Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T.,
RA   Huang Y., Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D.,
RA   Li B., Liu X., Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X.,
RA   Li Y., Wang W., Katze M.G., Su B., Nielsen R., Yang H., Wang J.,
RA   Wang X., Wang J.;
RT   "Genome sequencing and comparison of two nonhuman primate animal
RT   models, the cynomolgus and Chinese rhesus macaques.";
RL   Nat. Biotechnol. 29:1019-1023(2011).
RN   [3] {ECO:0000313|EMBL:AFH32205.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Testis {ECO:0000313|EMBL:AFI36995.1}, and Thymus
RC   {ECO:0000313|EMBL:AFH32205.1};
RX   PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA   Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X.,
RA   Pandey S., Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P.,
RA   Tharp G.K., Marcais G., Roberts M., Ferguson B., Fox H.S.,
RA   Treangen T., Salzberg S.L., Yorke J.A., Norgren R.B.Jr.;
RT   "A new rhesus macaque assembly and annotation for next-generation
RT   sequencing analyses.";
RL   Biol. Direct 9:20-20(2014).
RN   [4] {ECO:0000313|Ensembl:ENSMMUP00000044871}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000044871};
RG   Ensembl;
RL   Submitted (OCT-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   EMBL; JSUE03039242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; JU475401; AFH32205.1; -; mRNA.
DR   EMBL; JV046924; AFI36995.1; -; mRNA.
DR   EMBL; JV046925; AFI36996.1; -; mRNA.
DR   EMBL; JV046926; AFI36997.1; -; mRNA.
DR   EMBL; CM001259; EHH27677.1; -; Genomic_DNA.
DR   RefSeq; NP_001245038.1; NM_001258109.1.
DR   RefSeq; XP_014998571.1; XM_015143085.1.
DR   RefSeq; XP_014998573.1; XM_015143087.1.
DR   RefSeq; XP_014998574.1; XM_015143088.1.
DR   RefSeq; XP_014998575.1; XM_015143089.1.
DR   RefSeq; XP_014998576.1; XM_015143090.1.
DR   RefSeq; XP_014998577.1; XM_015143091.1.
DR   RefSeq; XP_014998578.1; XM_015143092.1.
DR   STRING; 9544.ENSMMUP00000025143; -.
DR   Ensembl; ENSMMUT00000055046; ENSMMUP00000044871; ENSMMUG00000048039.
DR   GeneID; 702757; -.
DR   KEGG; mcc:702757; -.
DR   CTD; 328; -.
DR   eggNOG; KOG1294; Eukaryota.
DR   eggNOG; COG0708; LUCA.
DR   GeneTree; ENSGT00530000063540; -.
DR   KO; K10771; -.
DR   OMA; GTAVFTK; -.
DR   OrthoDB; 1105625at2759; -.
DR   TreeFam; TF315048; -.
DR   Proteomes; UP000006718; Chromosome 7.
DR   Bgee; ENSMMUG00000019123; Expressed in 14 organ(s), highest expression level in CD4-positive helper T cell.
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   2: Evidence at transcript level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006718};
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, ECO:0000313|EMBL:AFH32205.1};
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:UP000006718}.
FT   DOMAIN       66    309       Endo/exonuclease/phosphatase.
FT                                {ECO:0000259|Pfam:PF03372}.
FT   REGION        1     60       Disordered. {ECO:0000256|MobiDB-lite:
FT                                F7GIK6}.
FT   COMPBIAS      1     41       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                F7GIK6}.
SQ   SEQUENCE   318 AA;  35632 MW;  5CABCC7FBC0D4B49 CRC64;
     MPKRGKKGAV AEDGDELKTE PEPKKSKTPA KKNDKEAAGE GPALYEDPPD QKTSPSGKPA
     TLKICSWNVD GLRAWIKKKG LDWVKEEAPD ILCLQETKCS ENKLPAELQE LPGLSHQYWS
     APSDKEGYSG VGLLSRHCPL KVSYGIGEEE HDQEGRVIVA EFDSFVLVTT YVPNAGRGLV
     RLEYRQRWDE AFRKFLKGLA SRKPLVLCGD LNVAHEEIDL RNPKGNKKNA GFTPQERQGF
     GELLQAVPLA DSFRHLYPNT PYAYTFWTYM MNARSKNVGW RLDYFLLSHS LLPALCDSKI
     RSKALGSDHC PITLYLAL
//
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