EXOG_MOUSE
ID EXOG_MOUSE Reviewed; 368 AA.
AC Q8C163; Q3UFL2;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Nuclease EXOG, mitochondrial;
DE EC=3.1.30.-;
DE AltName: Full=Endonuclease G-like 1;
DE Short=Endo G-like 1;
DE Flags: Precursor;
GN Name=Exog; Synonyms=Endogl1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Corpora quadrigemina, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Endo/exonuclease with nicking activity towards supercoiled
CC DNA, a preference for single-stranded DNA and 5'-3' exonuclease
CC activity. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}.
CC -!- MISCELLANEOUS: The active site contains 1 hydrated divalent metal
CC cation that has only 1 direct interaction with the protein; all other
CC interactions are via water molecules. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA/RNA non-specific endonuclease family.
CC {ECO:0000305}.
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DR EMBL; AK028887; BAC26174.1; -; mRNA.
DR EMBL; AK148426; BAE28548.1; -; mRNA.
DR EMBL; AK162566; BAE36970.1; -; mRNA.
DR EMBL; AK163555; BAE37396.1; -; mRNA.
DR EMBL; BC119024; AAI19025.1; -; mRNA.
DR CCDS; CCDS23616.1; -.
DR RefSeq; NP_766044.1; NM_172456.3.
DR AlphaFoldDB; Q8C163; -.
DR SMR; Q8C163; -.
DR BioGRID; 228962; 2.
DR IntAct; Q8C163; 1.
DR STRING; 10090.ENSMUSP00000129273; -.
DR iPTMnet; Q8C163; -.
DR PhosphoSitePlus; Q8C163; -.
DR SwissPalm; Q8C163; -.
DR EPD; Q8C163; -.
DR MaxQB; Q8C163; -.
DR PaxDb; Q8C163; -.
DR PeptideAtlas; Q8C163; -.
DR PRIDE; Q8C163; -.
DR ProteomicsDB; 275791; -.
DR Antibodypedia; 2527; 161 antibodies from 31 providers.
DR DNASU; 208194; -.
DR Ensembl; ENSMUST00000035094; ENSMUSP00000035094; ENSMUSG00000042787.
DR GeneID; 208194; -.
DR KEGG; mmu:208194; -.
DR UCSC; uc009saz.2; mouse.
DR CTD; 9941; -.
DR MGI; MGI:2143333; Exog.
DR VEuPathDB; HostDB:ENSMUSG00000042787; -.
DR eggNOG; KOG3721; Eukaryota.
DR GeneTree; ENSGT00940000160677; -.
DR HOGENOM; CLU_055174_3_0_1; -.
DR InParanoid; Q8C163; -.
DR OMA; CKFRPDP; -.
DR PhylomeDB; Q8C163; -.
DR BioGRID-ORCS; 208194; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Exog; mouse.
DR PRO; PR:Q8C163; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8C163; protein.
DR Bgee; ENSMUSG00000042787; Expressed in manus and 212 other tissues.
DR ExpressionAtlas; Q8C163; baseline and differential.
DR Genevisible; Q8C163; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0008409; F:5'-3' exonuclease activity; ISO:MGI.
DR GO; GO:0004519; F:endonuclease activity; ISO:MGI.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0006309; P:apoptotic DNA fragmentation; IBA:GO_Central.
DR Gene3D; 3.40.570.10; -; 1.
DR InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR InterPro; IPR041003; Exog_C.
DR InterPro; IPR020821; Extracellular_endonuc_su_A.
DR InterPro; IPR044925; His-Me_finger_sf.
DR InterPro; IPR040255; Non-specific_endonuclease.
DR PANTHER; PTHR13966; PTHR13966; 1.
DR Pfam; PF01223; Endonuclease_NS; 1.
DR Pfam; PF18026; Exog_C; 1.
DR SMART; SM00892; Endonuclease_NS; 1.
DR SMART; SM00477; NUC; 1.
DR SUPFAM; SSF54060; SSF54060; 1.
PE 1: Evidence at protein level;
KW Endonuclease; Hydrolase; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Nuclease; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 42..368
FT /note="Nuclease EXOG, mitochondrial"
FT /id="PRO_0000342610"
FT ACT_SITE 140
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 39
FT /note="F -> L (in Ref. 1; BAE28548)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="R -> C (in Ref. 1; BAE28548)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 368 AA; 41384 MW; EDAD3D41C82CC997 CRC64;
MAAKSFASRL RDSRRFLNGF LAGAVVGAAG AGLTALQFFR RPDAESAKLA RQPHESAEEA
VLEQFGFPLA GTETRRYTNH ALSYDQAKRV PRWVLEHISK DKIIGDADRK HCKFKPDPSV
PSAFSALNED YIGSGWSRGH MAPAGNNKFS SEAMAETFYL SNIVPQNFDN NSGYWNRIEM
YCRELTERFE DVWIVSGPLT LPHTRNDGTK TVSYQVIGED NVAVPSHLYK VILARRSPES
TEPLALGAFV VPNKAIGFQS QLSEFQVSLH DLEKMSGLVF FPRLDRSRDI RNICSVDTCK
LLGFQEFTLY LSTRKIDGAR SVARLEKVLE ALKSSGVEPD DYFLSRYEKK LEELKAKEQK
DAQLEKQS
