DPOA2_DROME
ID DPOA2_DROME Reviewed; 609 AA.
AC Q9VB62; Q95S59; Q9TXB0;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=DNA polymerase alpha subunit B {ECO:0000303|PubMed:6773966};
DE AltName: Full=DNA polymerase alpha 73 kDa subunit;
GN Name=PolA2 {ECO:0000312|FlyBase:FBgn0005696};
GN Synonyms=DNApol-alpha73 {ECO:0000312|FlyBase:FBgn0005696};
GN ORFNames=CG5923 {ECO:0000312|FlyBase:FBgn0005696};
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;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=1508723; DOI=10.1093/nar/20.16.4325;
RA Cotterill S., Lehman I.R., McLachlan P.;
RT "Cloning of the gene for the 73 kD subunit of the DNA polymerase alpha
RT primase of Drosophila melanogaster.";
RL Nucleic Acids Res. 20:4325-4330(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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:0000305}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
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:0000305, ECO:0000312|EMBL:AAL28491.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Ovary {ECO:0000269|PubMed:12537569};
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]
RP FUNCTION, IDENTIFICATION IN THE DNA POLYMERASE ALPHA COMPLEX, AND TISSUE
RP SPECIFICITY.
RX PubMed=6773966; DOI=10.1016/s0021-9258(19)70587-0;
RA Villani G., Sauer B., Lehman I.R.;
RT "DNA polymerase alpha from Drosophila melanogaster embryos. Subunit
RT structure.";
RL J. Biol. Chem. 255:9479-9483(1980).
RN [6]
RP FUNCTION, IDENTIFICATION IN THE DNA POLYMERASE ALPHA COMPLEX, AND TISSUE
RP SPECIFICITY.
RX PubMed=6403945; DOI=10.1073/pnas.80.8.2221;
RA Kaguni L.S., Rossignol J.M., Conaway R.C., Lehman I.R.;
RT "Isolation of an intact DNA polymerase-primase from embryos of Drosophila
RT melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:2221-2225(1983).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE DNA POLYMERASE ALPHA COMPLEX, AND TISSUE
RP SPECIFICITY.
RX PubMed=6409898; DOI=10.1016/s0021-9258(17)44626-6;
RA Kaguni L.S., Rossignol J.M., Conaway R.C., Banks G.R., Lehman I.R.;
RT "Association of DNA primase with the beta/gamma subunits of DNA polymerase
RT alpha from Drosophila melanogaster embryos.";
RL J. Biol. Chem. 258:9037-9039(1983).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=7592543; DOI=10.1093/oxfordjournals.jbchem.a124780;
RA Kuroda K., Ueda R.;
RT "A 130 kDa polypeptide immunologically related to the 180 kDa catalytic
RT subunit of DNA polymerase alpha-primase complex is detected in early
RT embryos of Drosophila.";
RL J. Biochem. 117:809-818(1995).
RN [9]
RP TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RX PubMed=9918845; DOI=10.1006/bbrc.1998.9944;
RA Kuroda K., Ueda R.;
RT "Phosphorylation and dephosphorylation of the B subunit of DNA polymerase
RT alpha-primase complex in the early embryogenesis of Drosophila.";
RL Biochem. Biophys. Res. Commun. 254:372-377(1999).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; THR-164; SER-166 AND
RP SER-168, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Accessory subunit of the DNA polymerase alpha complex (also
CC known as the alpha DNA polymerase-primase complex) which plays an
CC essential role in the initiation of DNA synthesis (PubMed:6773966,
CC PubMed:6403945, PubMed:6409898, PubMed:7592543). During the S phase of
CC the cell cycle, the DNA polymerase alpha complex (composed of a
CC catalytic subunit PolA1, an accessory subunit PolA2 and two primase
CC subunits, the catalytic subunit Prim1 and the regulatory subunit Prim2)
CC is recruited to DNA at the replicative forks (By similarity). The
CC primase subunit of the polymerase alpha complex initiates DNA synthesis
CC by oligomerising short RNA primers on both leading and lagging strands.
CC These primers are initially extended by the polymerase alpha catalytic
CC subunit and subsequently transferred to polymerase delta and polymerase
CC epsilon for processive synthesis on the lagging and leading strand,
CC respectively (By similarity). {ECO:0000250|UniProtKB:P09884,
CC ECO:0000250|UniProtKB:P20664, ECO:0000269|PubMed:6403945,
CC ECO:0000269|PubMed:6409898, ECO:0000269|PubMed:6773966,
CC ECO:0000269|PubMed:7592543}.
CC -!- SUBUNIT: Component of the alpha DNA polymerase complex (also known as
CC the alpha DNA polymerase-primase complex) consisting of four subunits:
CC the catalytic subunit PolA1, the regulatory subunit PolA2, and the
CC primase complex subunits Prim1 and Prim2 respectively (PubMed:6773966,
CC PubMed:6403945, PubMed:6409898). PolA1 associates with the DNA primase
CC complex before association with PolA2 (PubMed:6409898).
CC {ECO:0000269|PubMed:6403945, ECO:0000269|PubMed:6409898,
CC ECO:0000269|PubMed:6773966}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7592543}.
CC -!- TISSUE SPECIFICITY: Expressed in embryos (at protein level).
CC {ECO:0000269|PubMed:6403945, ECO:0000269|PubMed:6409898,
CC ECO:0000269|PubMed:6773966, ECO:0000269|PubMed:7592543,
CC ECO:0000269|PubMed:9918845}.
CC -!- PTM: Phosphorylated in embryos until cycle 13.
CC {ECO:0000269|PubMed:9918845}.
CC -!- SIMILARITY: Belongs to the DNA polymerase alpha subunit B family.
CC {ECO:0000255}.
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DR EMBL; AE014297; AAF56680.4; -; Genomic_DNA.
DR EMBL; AY060943; AAL28491.1; -; mRNA.
DR PIR; S40962; S40962.
DR RefSeq; NP_733206.3; NM_170327.4.
DR AlphaFoldDB; Q9VB62; -.
DR SMR; Q9VB62; -.
DR BioGRID; 68166; 19.
DR ComplexPortal; CPX-2090; DNA polymerase alpha:primase complex.
DR IntAct; Q9VB62; 3.
DR STRING; 7227.FBpp0113035; -.
DR iPTMnet; Q9VB62; -.
DR PaxDb; Q9VB62; -.
DR PRIDE; Q9VB62; -.
DR EnsemblMetazoa; FBtr0114543; FBpp0113035; FBgn0005696.
DR GeneID; 43278; -.
DR KEGG; dme:Dmel_CG5923; -.
DR CTD; 43278; -.
DR FlyBase; FBgn0005696; PolA2.
DR VEuPathDB; VectorBase:FBgn0005696; -.
DR eggNOG; KOG1625; Eukaryota.
DR HOGENOM; CLU_014923_3_0_1; -.
DR InParanoid; Q9VB62; -.
DR OMA; QQFDEMG; -.
DR OrthoDB; 513979at2759; -.
DR PhylomeDB; Q9VB62; -.
DR Reactome; R-DME-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-DME-68952; DNA replication initiation.
DR Reactome; R-DME-68962; Activation of the pre-replicative complex.
DR Reactome; R-DME-69091; Polymerase switching.
DR Reactome; R-DME-69166; Removal of the Flap Intermediate.
DR Reactome; R-DME-69183; Processive synthesis on the lagging strand.
DR BioGRID-ORCS; 43278; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43278; -.
DR PRO; PR:Q9VB62; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0005696; Expressed in secondary oocyte and 13 other tissues.
DR ExpressionAtlas; Q9VB62; baseline and differential.
DR Genevisible; Q9VB62; DM.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; IDA:FlyBase.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006270; P:DNA replication initiation; IDA:ComplexPortal.
DR GO; GO:0006261; P:DNA-templated DNA replication; IDA:FlyBase.
DR Gene3D; 1.10.8.530; -; 1.
DR InterPro; IPR007185; DNA_pol_a/d/e_bsu.
DR InterPro; IPR043034; DNA_pol_alpha_B_N_sf.
DR InterPro; IPR016722; DNA_pol_alpha_bsu.
DR PANTHER; PTHR23061; PTHR23061; 1.
DR Pfam; PF04042; DNA_pol_E_B; 1.
DR PIRSF; PIRSF018300; DNA_pol_alph_2; 1.
PE 1: Evidence at protein level;
KW DNA replication; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..609
FT /note="DNA polymerase alpha subunit B"
FT /id="PRO_0000194039"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 164
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 73..89
FT /note="KDKAGYKATGQKAKSYG -> RTRRDTRQLARRRNHMS (in Ref. 1;
FT no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 366..408
FT /note="SGPFTDSTDLFYEPLHDLLKYLKDHRPDVLVLTGPFLDADHKM -> PDPLR
FT TVRISSTNRCTTCSSTSRITDLTCWCSRDHSWMPITRL (in Ref. 1; no
FT nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="A -> S (in Ref. 4; AAL28491)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="F -> L (in Ref. 4; AAL28491)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="A -> V (in Ref. 4; AAL28491)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="I -> T (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 609 AA; 66971 MW; 45AFE71682C98B85 CRC64;
MEEELKQQFD EMGVEPADAV LGRCAELAIT YNIHDATEFV EQWMAFSLSH LQGEDPAIEN
LGDFERKVLQ LRKDKAGYKA TGQKAKSYGS PSVQDTSSLA TYGVMEDDPM LDDYVSESAV
DSSALHTPKA KKQSDRTANL KGAALFSPAS YTPQSAKRKA GLETPSNSVA GKPGDIVDTF
GHPKLLAGSS WQSQMEHTVP VTQKLLHNDA PLTIANLGYM NDLLTDRCHN LRVRFNQTGP
ALVDKKLGQA GAAECIWYPQ DRQVLQSAGG LHAVGMIHSE DDGPLDAHSA FMAVLDDDVE
DEMDPTLTLN FSRVKSASIF PGQVVLAKGF IPRGKTFMVE EIHTERKLTP ATPLQIDREL
QFVVASGPFT DSTDLFYEPL HDLLKYLKDH RPDVLVLTGP FLDADHKMVG ELAETFDTFF
EKMIGGIMES IGSHTAVLVV TSQKDAMALS VYPTPPPALR RTYPNLYMLP DPSLVDLDGF
TLGVTSTDVV DHLLSHEFAV NAGERMHRAI NHLFHQGSFY PLYPPADEDM AYDSQLALKY
AQLKQLPNVL ILPSDQRHFI RLVNDCLVIN PGRVADKKGG TFARFLVAPS VPGKAANMFN
SVACQVQRI
