DPOG2_MOUSE
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 03-AUG-2022, entry version 169.
DE RecName: Full=DNA polymerase subunit gamma-2, mitochondrial;
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: Mitochondrial polymerase processivity subunit. It regulates
CC the polymerase and exonuclease activities promoting processive DNA
CC synthesis. Binds to ss-DNA. {ECO:0000250|UniProtKB:Q9UHN1}.
CC -!- SUBUNIT: Heterotrimer composed of a catalytic subunit and a homodimer
CC of accessory subunits. {ECO:0000269|PubMed:11172710}.
CC -!- INTERACTION:
CC Q9QZM2; Q9QZM2: Polg2; NbExp=2; IntAct=EBI-853043, EBI-853043;
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
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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; Q9QZM2; -.
DR PRIDE; Q9QZM2; -.
DR ProteomicsDB; 277490; -.
DR Antibodypedia; 50586; 172 antibodies from 28 providers.
DR DNASU; 50776; -.
DR Ensembl; ENSMUST00000021060; ENSMUSP00000021060; ENSMUSG00000020718.
DR GeneID; 50776; -.
DR KEGG; mmu:50776; -.
DR UCSC; uc007lzm.2; mouse.
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; AFREHIF; -.
DR OrthoDB; 1183820at2759; -.
DR PhylomeDB; Q9QZM2; -.
DR TreeFam; TF103005; -.
DR BioGRID-ORCS; 50776; 31 hits in 107 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 220 other tissues.
DR ExpressionAtlas; Q9QZM2; baseline and differential.
DR Genevisible; Q9QZM2; MM.
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; ISO:MGI.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IMP:MGI.
DR GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; ISO:MGI.
DR GO; GO:0022904; P:respiratory electron transport chain; IMP:MGI.
DR CDD; cd00774; GlyRS-like_core; 1.
DR CDD; cd02426; Pol_gamma_b_Cterm; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 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; IPR027030; POLG2.
DR InterPro; IPR042064; POLG2_C.
DR PANTHER; PTHR10745; PTHR10745; 1.
DR PANTHER; PTHR10745:SF8; PTHR10745:SF8; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; DNA-binding; Mitochondrion;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..459
FT /note="DNA polymerase subunit gamma-2, mitochondrial"
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
