DPOG1_MOUSE
ID DPOG1_MOUSE Reviewed; 1218 AA.
AC P54099; Q9JI28;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=DNA polymerase subunit gamma-1;
DE EC=2.7.7.7;
DE AltName: Full=Mitochondrial DNA polymerase catalytic subunit;
DE AltName: Full=PolG-alpha;
GN Name=Polg; Synonyms=Polg1;
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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Muscle;
RA Chang S.W., Colvin S., Sarkos P., Denniger G., Zassenhaus H.P.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=11058962; DOI=10.1089/104454900750019353;
RA Mott J.L., Denniger G., Zullo S.J., Zassenhaus H.P.;
RT "Genomic structure of murine mitochondrial DNA polymerase-gamma.";
RL DNA Cell Biol. 19:601-605(2000).
CC -!- FUNCTION: Involved in the replication of mitochondrial DNA. Associates
CC with mitochondrial DNA (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Heterotrimer composed of a catalytic subunit and a homodimer
CC of accessory subunits (By similarity). Interacts with TTC3 (By
CC similarity). {ECO:0000250|UniProtKB:P54098,
CC ECO:0000250|UniProtKB:Q27607}.
CC -!- INTERACTION:
CC P54099; P09671: Sod2; NbExp=2; IntAct=EBI-863636, EBI-1635071;
CC P54099; P02340: Tp53; NbExp=2; IntAct=EBI-863636, EBI-474016;
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion matrix,
CC mitochondrion nucleoid {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA98977.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF82772.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U53584; AAA98977.1; ALT_FRAME; mRNA.
DR EMBL; AF268975; AAF82772.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF268970; AAF82772.1; JOINED; Genomic_DNA.
DR EMBL; AF268971; AAF82772.1; JOINED; Genomic_DNA.
DR EMBL; AF268972; AAF82772.1; JOINED; Genomic_DNA.
DR EMBL; AF268973; AAF82772.1; JOINED; Genomic_DNA.
DR EMBL; AF268974; AAF82772.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; P54099; -.
DR SMR; P54099; -.
DR ComplexPortal; CPX-2094; Mitochondrial DNA polymerase gamma complex.
DR IntAct; P54099; 2.
DR STRING; 10090.ENSMUSP00000073551; -.
DR iPTMnet; P54099; -.
DR PhosphoSitePlus; P54099; -.
DR SwissPalm; P54099; -.
DR EPD; P54099; -.
DR PaxDb; P54099; -.
DR PeptideAtlas; P54099; -.
DR PRIDE; P54099; -.
DR ProteomicsDB; 277389; -.
DR MGI; MGI:1196389; Polg.
DR eggNOG; KOG3657; Eukaryota.
DR InParanoid; P54099; -.
DR ChiTaRS; Polg; mouse.
DR PRO; PR:P54099; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P54099; protein.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005760; C:gamma DNA polymerase complex; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0008408; F:3'-5' exonuclease activity; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; ISO:MGI.
DR GO; GO:0004527; F:exonuclease activity; IDA:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0007568; P:aging; IMP:MGI.
DR GO; GO:0006261; P:DNA-templated DNA replication; ISO:MGI.
DR GO; GO:0006264; P:mitochondrial DNA replication; IMP:MGI.
DR InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR InterPro; IPR002297; DNA-dir_DNA_pol_A_mt.
DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR041336; DNApol_Exo.
DR InterPro; IPR012337; RNaseH-like_sf.
DR PANTHER; PTHR10267; PTHR10267; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR Pfam; PF18136; DNApol_Exo; 1.
DR PIRSF; PIRSF000797; DNA_pol_mt; 1.
DR PRINTS; PR00867; DNAPOLG.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE 1: Evidence at protein level;
KW DNA replication; DNA-binding; DNA-directed DNA polymerase; Magnesium;
KW Mitochondrion; Mitochondrion nucleoid; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..1218
FT /note="DNA polymerase subunit gamma-1"
FT /id="PRO_0000101271"
FT REGION 31..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 23..24
FT /note="AR -> EG (in Ref. 1; AAA98977)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="A -> S (in Ref. 1; AAA98977)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="D -> A (in Ref. 1; AAA98977)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="T -> N (in Ref. 1; AAA98977)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="I -> T (in Ref. 1; AAA98977)"
FT /evidence="ECO:0000305"
FT CONFLICT 303..308
FT /note="HKNPAA -> QQDPAV (in Ref. 1; AAA98977)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="E -> D (in Ref. 1; AAA98977)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="Missing (in Ref. 1; AAA98977)"
FT /evidence="ECO:0000305"
FT CONFLICT 557
FT /note="Q -> K (in Ref. 1; AAA98977)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="N -> S (in Ref. 1; AAA98977)"
FT /evidence="ECO:0000305"
FT CONFLICT 861
FT /note="P -> T (in Ref. 1; AAA98977)"
FT /evidence="ECO:0000305"
FT CONFLICT 886
FT /note="F -> L (in Ref. 1; AAA98977)"
FT /evidence="ECO:0000305"
FT CONFLICT 919..921
FT /note="GIS -> RIH (in Ref. 1; AAA98977)"
FT /evidence="ECO:0000305"
FT CONFLICT 1024
FT /note="A -> S (in Ref. 1; AAA98977)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1218 AA; 136758 MW; 55BC904A7318DA26 CRC64;
MSRLLWKKVA GAKVASGPVP ATARWVASSV LDPVPSDGRP PSQMPSSENG QLRLNPLLIQ
MLSRGLHEQI FGCGGEMPDE AAVQRSVEHL QKHGLWGQPA TPLPDVELRL PRLFGGNLDQ
HFRLLAQKQS LPYLEAAASL LEAQLPPEPK SWAWAEGWTR YGPEGEAEPV AIPEERALVF
DVEVCLAEGT CPTLAVAISP SAWYSWCSRR LVEERYSWTS QLSPADLIPL GGSTSASSST
KQDGQEQLVV GHNVSFDRAH IREQYLIQDS RMRFLDTMSM HMAISGLSSF QRSLWMGAKQ
GKHKNPAAHK ARAEVPEESQ WSSESSSWDW MDISSANNLA DVHNLYVGGP PLEKEPRELF
VKGSMRDIRE NFQDLMQYCA RDVWATFEVF QQQLPLFLER CPHPVTLAGM LEMGVSYLPV
NQNWERYLTE AQNTYEELQR EMKKSLMDLA NDACQLLSGE RYKEDPWLWD LEWDLQEFKQ
KKAKKVKKPA SASKLPIEGA GPFGDPMDQE DPGPPSEEEE LQRSVTAHNR LQQLRSTTDL
LPKRPQHLPG HPGWYRQLCP RLDDPAWAPG PSLLSLQMRV TPKLMALTWD GFPLHYSDSH
GWGYLVPGRR DNLTEPPVSP TVESAAVTCP YRAIESLYRK HCLEQGKQQL EPQEVDLAEE
FLLTDNSAMW QTVEELGCLD VEAEAKMENS GLSQPLVLPA ACAPKSSQPT YHHGNGPYND
VNIPGCWFFK LPHKDGNNYN VGSPFAKDFL PKMEDGTLQA GPGGASGPRA LEINKMISFW
RNAHKRISSQ MVVWLPRSAL PRVVTRHPAF DEEGHYGAIL PQVVTAGTIT RRAVEPTWLT
ASNARPDRVG SELKAMVQAP PGYVLVGADV DSQELWIAAV LGDAHFAGMH GCTAFGWMTL
QGRKSRGTDL HSKTAATVGI SREHAKIFNY GRIYGAGQSF AERLLMQFNH RLTRQEAAEK
AQQMYAVTKG LRRYRLSADG EWLVKQLNLP VDRTEDGWVS LQDLRMIRRE ASRKSRWKKW
EVAAERAWTG GTESEMFNKL ESIAMSDTPR TPVLGCCISR ALEPSVVQGE FITSRVNWVV
QSSAVDYLHL MLVAMKWLFE EFAIDGRFCI SIHDEVRYLV REEDRYRAAL ALQITNLLTR
CMFAYKLGLN DLPQSVAFFS AVDIDQCLRK EVTMDCKTPS NPTGMERRYG IPQGEALDIY
QIIELTKGSL EKRSQPGP
