DPOG2_DROME
ID DPOG2_DROME Reviewed; 361 AA.
AC Q9VJV8; O02005; Q9NKE7;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=DNA polymerase subunit gamma-2, mitochondrial {ECO:0000305};
DE AltName: Full=DNA polymerase beta subunit {ECO:0000303|PubMed:10930405, ECO:0000303|PubMed:9153213};
DE AltName: Full=DNA polymerase gamma 35kD subunit {ECO:0000303|PubMed:3095323};
DE AltName: Full=DNA polymerase gamma subunit 2 {ECO:0000312|FlyBase:FBgn0004407};
DE Flags: Precursor;
GN Name=PolG2 {ECO:0000312|FlyBase:FBgn0004407};
GN Synonyms=DNApol-gamma {ECO:0000312|FlyBase:FBgn0004407},
GN DNApol-gamma35 {ECO:0000303|PubMed:3095323}, DNApolG2 {ECO:0000305},
GN l(2)34De {ECO:0000312|FlyBase:FBgn0004407},
GN l(2)br16 {ECO:0000312|FlyBase:FBgn0004407},
GN MtPolB {ECO:0000312|FlyBase:FBgn0004407},
GN pol gamma-beta {ECO:0000303|PubMed:10930405};
GN ORFNames=CG33650 {ECO:0000312|FlyBase:FBgn0004407};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:AAC47536.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-37; 115-130; 158-196 AND
RP 342-360, IDENTIFICATION IN THE DNA POLYMERASE GAMMA COMPLEX, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Ovary {ECO:0000312|EMBL:AAC47536.1};
RX PubMed=9153213; DOI=10.1074/jbc.272.21.13640;
RA Wang Y., Farr C.L., Kaguni L.S.;
RT "Accessory subunit of mitochondrial DNA polymerase from Drosophila embryos.
RT Cloning, molecular analysis, and association in the native enzyme.";
RL J. Biol. Chem. 272:13640-13646(1997).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000312|EMBL:AAK92915.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAK92915.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAK92915.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE DNA POLYMERASE GAMMA COMPLEX, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=3095323; DOI=10.1016/s0021-9258(18)66938-8;
RA Wernette C.M., Kaguni L.S.;
RT "A mitochondrial DNA polymerase from embryos of Drosophila melanogaster.
RT Purification, subunit structure, and partial characterization.";
RL J. Biol. Chem. 261:14764-14770(1986).
RN [6] {ECO:0000305}
RP FUNCTION, AND IDENTIFICATION IN THE DNA POLYMERASE GAMMA COMPLEX.
RX PubMed=7499423; DOI=10.1074/jbc.270.48.28932;
RA Olson M.W., Wang Y., Elder R.H., Kaguni L.S.;
RT "Subunit structure of mitochondrial DNA polymerase from Drosophila embryos.
RT Physical and immunological studies.";
RL J. Biol. Chem. 270:28932-28937(1995).
RN [7] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=10930405; DOI=10.1074/jbc.m003024200;
RA Lefai E., Fernandez-Moreno M.A., Alahari A., Kaguni L.S., Garesse R.;
RT "Differential regulation of the catalytic and accessory subunit genes of
RT Drosophila mitochondrial DNA polymerase.";
RL J. Biol. Chem. 275:33123-33133(2000).
RN [8] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF GLY-31.
RX PubMed=11917141; DOI=10.1073/pnas.072664899;
RA Iyengar B., Luo N., Farr C.L., Kaguni L.S., Campos A.R.;
RT "The accessory subunit of DNA polymerase gamma is essential for
RT mitochondrial DNA maintenance and development in Drosophila melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4483-4488(2002).
RN [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=19924234; DOI=10.1371/journal.pone.0007874;
RA Baqri R.M., Turner B.A., Rheuben M.B., Hammond B.D., Kaguni L.S.,
RA Miller K.E.;
RT "Disruption of mitochondrial DNA replication in Drosophila increases
RT mitochondrial fast axonal transport in vivo.";
RL PLoS ONE 4:E7874-E7874(2009).
CC -!- FUNCTION: As accessory component of the DNA polymerase gamma complex is
CC involved in the replication of mitochondrial DNA (PubMed:3095323,
CC PubMed:7499423). Does not bind DNA (PubMed:7499423). Essential for
CC mitochondrial DNA maintenance and larval development (PubMed:11917141,
CC PubMed:19924234). {ECO:0000269|PubMed:11917141,
CC ECO:0000269|PubMed:19924234, ECO:0000269|PubMed:3095323,
CC ECO:0000269|PubMed:7499423}.
CC -!- SUBUNIT: Component of the DNA polymerase gamma complex consisting of
CC two subunits: the catalytic subunit DNApol-gamma/DNApolG1 and the
CC accessory subunit PolG2/DNApol-gamma35. {ECO:0000269|PubMed:3095323,
CC ECO:0000269|PubMed:7499423, ECO:0000269|PubMed:9153213}.
CC -!- INTERACTION:
CC Q9VJV8; Q27607: tam; NbExp=2; IntAct=EBI-852898, EBI-122256;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9153213}.
CC -!- TISSUE SPECIFICITY: Expressed in ovaries (at protein level).
CC {ECO:0000269|PubMed:9153213}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos (at protein level)
CC (PubMed:9153213, PubMed:3095323). Expressed at low level in eggs
CC (PubMed:10930405). Levels increase in early embryonic stages followed
CC by a decrease in late embryos and a moderate increase in first-instar
CC larvae (PubMed:10930405). {ECO:0000269|PubMed:10930405,
CC ECO:0000269|PubMed:3095323, ECO:0000269|PubMed:9153213}.
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DR EMBL; U94702; AAC47536.1; -; mRNA.
DR EMBL; AE014134; AAF53341.2; -; Genomic_DNA.
DR EMBL; AY051491; AAK92915.1; -; mRNA.
DR RefSeq; NP_001027262.1; NM_001032091.3.
DR AlphaFoldDB; Q9VJV8; -.
DR SMR; Q9VJV8; -.
DR ComplexPortal; CPX-2096; Mitochondrial DNA polymerase gamma complex.
DR IntAct; Q9VJV8; 2.
DR STRING; 7227.FBpp0099758; -.
DR PaxDb; Q9VJV8; -.
DR PRIDE; Q9VJV8; -.
DR EnsemblMetazoa; FBtr0091627; FBpp0099758; FBgn0004407.
DR GeneID; 3772064; -.
DR KEGG; dme:Dmel_CG33650; -.
DR UCSC; CG33650-RA; d. melanogaster.
DR CTD; 3772064; -.
DR FlyBase; FBgn0004407; PolG2.
DR VEuPathDB; VectorBase:FBgn0004407; -.
DR eggNOG; KOG4247; Eukaryota.
DR GeneTree; ENSGT00940000153759; -.
DR HOGENOM; CLU_834911_0_0_1; -.
DR InParanoid; Q9VJV8; -.
DR OMA; KIWWMRL; -.
DR PhylomeDB; Q9VJV8; -.
DR BioGRID-ORCS; 3772064; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 3772064; -.
DR PRO; PR:Q9VJV8; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0004407; Expressed in brain and 10 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005760; C:gamma DNA polymerase complex; IDA:FlyBase.
DR GO; GO:0005759; C:mitochondrial matrix; IC:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0030337; F:DNA polymerase processivity factor activity; ISS:FlyBase.
DR GO; GO:0071667; F:DNA/RNA hybrid binding; IDA:FlyBase.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:FlyBase.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006261; P:DNA-templated DNA replication; IDA:FlyBase.
DR GO; GO:0006264; P:mitochondrial DNA replication; IMP:FlyBase.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IMP:FlyBase.
DR GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; ISS:FlyBase.
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; 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.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA replication; Mitochondrion;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..18
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:9153213"
FT CHAIN 19..361
FT /note="DNA polymerase subunit gamma-2, mitochondrial"
FT /id="PRO_0000448561"
FT MUTAGEN 31
FT /note="G->E: Loss of mitochondrial DNA which disrupts
FT mitochondrial morphology; larval brains are smaller due to
FT defective cell proliferation leading to death at the pupal
FT stage."
FT /evidence="ECO:0000269|PubMed:11917141"
FT CONFLICT 56
FT /note="K -> R (in Ref. 1; AAC47536)"
FT /evidence="ECO:0000305"
FT CONFLICT 108..112
FT /note="NSLFG -> HSLFA (in Ref. 1; AAC47536)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="T -> A (in Ref. 1; AAC47536)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="I -> T (in Ref. 1; AAC47536)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 41027 MW; 0762099440E5931C CRC64;
MSRIQRCFKS LASAGFFRTV EDNKLELLSH GREYAKLLQQ HWTRLRPLAA HLGATKEPIN
PVNIQRFSFP QSQQFRNNFQ KLVKDHPRKA KCPTLLKHQS TCSGPTSNSL FGIKGPTLHL
TTDFLVEPHR ALEHFYNMQR ESKIWWMRLS SNPSRYRIVP CDLAEDLNPN DYQAIDIRTS
YGDAGEVTVE QLSLVRIVDD KDFRLPDART GEIVQPTVIR SVIELETTTC ALLLDGCDHG
RDSQSLLLHR VLAPYQCGIA CVESDSELSA DLSDLCQHLK HVLNHAGLRL SEGDGIRTTK
NASHLAEHLL ETDMLGIPYT LVINEQTLRN GLMQLRSRDT RLAETIHISD VPDYLLNIFK
N
