ID   DPOG2_MOUSE             Reviewed;         459 AA.
AC   Q9QZM2; B1ARB5; O35614;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 178.
DE   RecName: Full=DNA polymerase subunit gamma-2;
DE   AltName: Full=DNA polymerase gamma accessory 55 kDa subunit;
DE            Short=p55;
DE   AltName: Full=Mitochondrial DNA polymerase accessory subunit;
DE   AltName: Full=MtPolB;
DE   AltName: Full=PolG-beta;
DE   Flags: Precursor;
GN   Name=Polg2; Synonyms=Mtpolb;
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=Swiss Webster / NIH;
RX   PubMed=10666468; DOI=10.1093/nar/28.5.1237;
RA   Carrodeguas J.A., Bogenhagen D.F.;
RT   "Protein sequences conserved in prokaryotic aminoacyl-tRNA synthetases are
RT   important for the activity of the processivity factor of human
RT   mitochondrial DNA polymerase.";
RL   Nucleic Acids Res. 28:1237-1244(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 164-459.
RA   Kaguni L.S.;
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-459, AND SUBUNIT.
RX   PubMed=11172710; DOI=10.1016/s1097-2765(01)00153-8;
RA   Carrodeguas J.A., Theis K., Bogenhagen D.F., Kisker C.;
RT   "Crystal structure and deletion analysis show that the accessory subunit of
RT   mammalian DNA polymerase gamma, Pol gamma B, functions as a homodimer.";
RL   Mol. Cell 7:43-54(2001).
CC   -!- FUNCTION: Accessory subunit of DNA polymerase gamma solely responsible
CC       for replication of mitochondrial DNA (mtDNA). Acts as an allosteric
CC       regulator of the holoenzyme activities. Enhances the polymerase
CC       activity and the processivity of POLG by increasing its interactions
CC       with the DNA template. Suppresses POLG exonucleolytic proofreading
CC       especially toward homopolymeric templates bearing mismatched termini.
CC       Binds to single-stranded DNA. {ECO:0000250|UniProtKB:Q9UHN1}.
CC   -!- SUBUNIT: Heterotrimer composed of a catalytic subunit and a homodimer
CC       of accessory subunits (POLG:POLG2). {ECO:0000250|UniProtKB:Q9UHN1,
CC       ECO:0000269|PubMed:11172710}.
CC   -!- INTERACTION:
CC       Q9QZM2; Q9QZM2: Polg2; NbExp=2; IntAct=EBI-853043, EBI-853043;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P54098}.
CC       Mitochondrion matrix, mitochondrion nucleoid
CC       {ECO:0000250|UniProtKB:P54098}.
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DR   EMBL; AF177202; AAD56641.1; -; mRNA.
DR   EMBL; AL603664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF006072; AAB62894.1; -; mRNA.
DR   CCDS; CCDS25561.1; -.
DR   RefSeq; NP_056625.2; NM_015810.2.
DR   PDB; 1G5H; X-ray; 1.95 A; A/B/C/D=17-459.
DR   PDB; 1G5I; X-ray; 2.30 A; A/B/C/D=17-459.
DR   PDBsum; 1G5H; -.
DR   PDBsum; 1G5I; -.
DR   AlphaFoldDB; Q9QZM2; -.
DR   SMR; Q9QZM2; -.
DR   ComplexPortal; CPX-2094; Mitochondrial DNA polymerase gamma complex.
DR   STRING; 10090.ENSMUSP00000021060; -.
DR   iPTMnet; Q9QZM2; -.
DR   PhosphoSitePlus; Q9QZM2; -.
DR   MaxQB; Q9QZM2; -.
DR   PaxDb; 10090-ENSMUSP00000021060; -.
DR   ProteomicsDB; 277490; -.
DR   Antibodypedia; 50586; 190 antibodies from 28 providers.
DR   DNASU; 50776; -.
DR   Ensembl; ENSMUST00000021060.6; ENSMUSP00000021060.6; ENSMUSG00000020718.13.
DR   GeneID; 50776; -.
DR   KEGG; mmu:50776; -.
DR   UCSC; uc007lzm.2; mouse.
DR   AGR; MGI:1354947; -.
DR   CTD; 11232; -.
DR   MGI; MGI:1354947; Polg2.
DR   VEuPathDB; HostDB:ENSMUSG00000020718; -.
DR   eggNOG; KOG2298; Eukaryota.
DR   GeneTree; ENSGT00940000153759; -.
DR   HOGENOM; CLU_055833_0_0_1; -.
DR   InParanoid; Q9QZM2; -.
DR   OMA; WGQEVLE; -.
DR   OrthoDB; 2901447at2759; -.
DR   PhylomeDB; Q9QZM2; -.
DR   TreeFam; TF103005; -.
DR   BioGRID-ORCS; 50776; 33 hits in 114 CRISPR screens.
DR   ChiTaRS; Polg2; mouse.
DR   EvolutionaryTrace; Q9QZM2; -.
DR   PRO; PR:Q9QZM2; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q9QZM2; Protein.
DR   Bgee; ENSMUSG00000020718; Expressed in pigmented layer of retina and 224 other cell types or tissues.
DR   ExpressionAtlas; Q9QZM2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005760; C:gamma DNA polymerase complex; ISO:MGI.
DR   GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0070182; F:DNA polymerase binding; ISO:MGI.
DR   GO; GO:0030337; F:DNA polymerase processivity factor activity; ISO:MGI.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:MGI.
DR   GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0006281; P:DNA repair; TAS:MGI.
DR   GO; GO:0006260; P:DNA replication; IC:MGI.
DR   GO; GO:0006261; P:DNA-templated DNA replication; ISO:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0032042; P:mitochondrial DNA metabolic process; IMP:MGI.
DR   GO; GO:0006264; P:mitochondrial DNA replication; IMP:MGI.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR   CDD; cd00774; GlyRS-like_core; 1.
DR   CDD; cd02426; Pol_gamma_b_Cterm; 1.
DR   Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR027031; Gly-tRNA_synthase/POLG2.
DR   InterPro; IPR033731; GlyRS-like_core.
DR   InterPro; IPR042064; POLG2_C.
DR   PANTHER; PTHR10745:SF8; DNA POLYMERASE SUBUNIT GAMMA-2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10745; GLYCYL-TRNA SYNTHETASE/DNA POLYMERASE SUBUNIT GAMMA-2; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   Genevisible; Q9QZM2; MM.
PE   1: Evidence at protein level;
KW   3D-structure; DNA replication; DNA-binding; Mitochondrion;
KW   Mitochondrion nucleoid; Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..459
FT                   /note="DNA polymerase subunit gamma-2"
FT                   /id="PRO_0000007315"
FT   CONFLICT        53
FT                   /note="F -> L (in Ref. 1; AAD56641)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        226
FT                   /note="L -> S (in Ref. 3; AAB62894)"
FT                   /evidence="ECO:0000305"
FT   HELIX           42..49
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   HELIX           57..60
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   HELIX           62..67
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   HELIX           75..92
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   TURN            93..95
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   STRAND          99..101
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   STRAND          106..108
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   STRAND          120..122
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   HELIX           124..131
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   HELIX           138..151
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   STRAND          152..155
FT                   /evidence="ECO:0007829|PDB:1G5I"
FT   HELIX           160..165
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   HELIX           167..173
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   TURN            174..176
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   STRAND          180..192
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   STRAND          204..217
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   HELIX           219..238
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   HELIX           244..246
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   STRAND          247..253
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   STRAND          259..267
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   STRAND          270..282
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   HELIX           283..288
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   HELIX           293..295
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   STRAND          298..300
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   STRAND          303..305
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   STRAND          308..315
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   HELIX           316..327
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   STRAND          337..339
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   TURN            350..352
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   STRAND          357..361
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   HELIX           366..382
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   STRAND          387..389
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   HELIX           390..392
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   HELIX           399..408
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   STRAND          412..417
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   HELIX           419..424
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   STRAND          426..431
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   TURN            432..434
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   STRAND          437..441
FT                   /evidence="ECO:0007829|PDB:1G5H"
FT   TURN            442..444
FT                   /evidence="ECO:0007829|PDB:1G5I"
FT   HELIX           445..459
FT                   /evidence="ECO:0007829|PDB:1G5H"
SQ   SEQUENCE   459 AA;  51467 MW;  052C790C2AF9A249 CRC64;
     MRCGGGARAC RRACRCWLSG YAGPADGTQQ PDAPEHAVAR EALVDLCRRR HFFSGTPQQL
     STAALLSGCH ARFGPLGVEL RKNLASQWWS SMVVFREQVF AVDSLHQEPG SSQPRDSAFR
     LVSPESIREI LQDREPSKEQ LVAFLENLLK TSGKLRATLL HGALEHYVNC LDLVNRKLPF
     GLAQIGVCFH PVSNSNQTPS SVTRVGEKTE ASLVWFTPTR TSSQWLDFWL RHRLLWWRKF
     AMSPSNFSSA DCQDELGRKG SKLYYSFPWG KEPIETLWNL GDQELLHTYP GNVSTIQGRD
     GRKNVVPCVL SVSGDVDLGT LAYLYDSFQL AENSFARKKS LQRKVLKLHP CLAPIKVALD
     VGKGPTVELR QVCQGLLNEL LENGISVWPG YSETVHSSLE QLHSKYDEMS VLFSVLVTET
     TLENGLIQLR SRDTTMKEMM HISKLRDFLV KYLASASNV
//