DPOA2_RAT
ID DPOA2_RAT Reviewed; 600 AA.
AC O89043; Q9QYV6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=DNA polymerase alpha subunit B;
DE AltName: Full=DNA polymerase alpha 70 kDa subunit;
DE AltName: Full=DNA polymerase subunit II;
GN Name=Pola2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=11536367; DOI=10.1002/mc.1052;
RA Popanda O., Flohr C., Dai J.C., Hunzicker A., Thielmann H.W.;
RT "A mutation in subunit B of the DNA polymerase alpha-primase complex from
RT Novikoff hepatoma cells concomitant with a conformational change and
RT abnormal catalytic properties of the DNA polymerase alpha-primase
RT complex.";
RL Mol. Carcinog. 31:171-183(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 106-600.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=10541966; DOI=10.1007/s004320050322;
RA Popanda O., Flohr T., Fox G., Thielmann H.W.;
RT "A mutation detected in DNA polymerase delta cDNA from Novikoff hepatoma
RT cells correlates with abnormal catalytic properties of the enzyme.";
RL J. Cancer Res. Clin. Oncol. 125:598-608(1999).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130; SER-141 AND SER-152, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity).
CC During the S phase of the cell cycle, the DNA polymerase alpha complex
CC (composed of a catalytic subunit POLA1, an accessory subunit POLA2 and
CC two primase subunits, the catalytic subunit PRIM1 and the regulatory
CC subunit PRIM2) is recruited to DNA at the replicative forks via direct
CC interactions with MCM10 and WDHD1 (By similarity). The primase subunit
CC of the polymerase alpha complex initiates DNA synthesis by
CC 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:0000250|UniProtKB:Q14181}.
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 (By similarity).
CC Within the complex, POLA1 directly interacts with PRIM2 (By
CC similarity). {ECO:0000250|UniProtKB:P20664,
CC ECO:0000250|UniProtKB:Q14181}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Phosphorylated in a cell cycle-dependent manner, in G2/M phase.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase alpha subunit B family.
CC {ECO:0000305}.
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DR EMBL; AJ245648; CAB56208.1; -; mRNA.
DR EMBL; AJ011606; CAA09721.1; -; mRNA.
DR AlphaFoldDB; O89043; -.
DR SMR; O89043; -.
DR ComplexPortal; CPX-2089; DNA polymerase alpha:primase complex.
DR STRING; 10116.ENSRNOP00000028406; -.
DR iPTMnet; O89043; -.
DR jPOST; O89043; -.
DR PaxDb; O89043; -.
DR PRIDE; O89043; -.
DR UCSC; RGD:621817; rat.
DR RGD; 621817; Pola2.
DR eggNOG; KOG1625; Eukaryota.
DR InParanoid; O89043; -.
DR PhylomeDB; O89043; -.
DR Reactome; R-RNO-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-RNO-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-RNO-174430; Telomere C-strand synthesis initiation.
DR Reactome; R-RNO-68952; DNA replication initiation.
DR Reactome; R-RNO-68962; Activation of the pre-replicative complex.
DR Reactome; R-RNO-69091; Polymerase switching.
DR Reactome; R-RNO-69166; Removal of the Flap Intermediate.
DR Reactome; R-RNO-69183; Processive synthesis on the lagging strand.
DR PRO; PR:O89043; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IMP:RGD.
DR GO; GO:0006260; P:DNA replication; IMP:RGD.
DR GO; GO:0006270; P:DNA replication initiation; ISO:RGD.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; ISO:RGD.
DR GO; GO:0006606; P:protein import into nucleus; ISO:RGD.
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 InterPro; IPR013627; Pol_alpha_B_N.
DR PANTHER; PTHR23061; PTHR23061; 1.
DR Pfam; PF04042; DNA_pol_E_B; 1.
DR Pfam; PF08418; Pol_alpha_B_N; 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..600
FT /note="DNA polymerase alpha subunit B"
FT /id="PRO_0000194037"
FT REGION 112..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14181"
FT MOD_RES 127
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14181"
FT MOD_RES 130
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14181"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14181"
FT CONFLICT 112
FT /note="A -> S (in Ref. 2; CAA09721)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="R -> K (in Ref. 2; CAA09721)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="N -> S (in Ref. 2; CAA09721)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 600 AA; 66636 MW; 1C6E1C08DD14DED4 CRC64;
MAVSTQQLAE ELQIFGLDCE DSLLEKLAEL CTLYRQTEER MVSELIAFCT SAGKSCLTGE
ILSSFEHEVL NKKLSKACHS ASKDNRHAGA RDIVSIQELI EAEEEEETLL SAYTTPSKGP
HKRVSSTPET PLTKRSISTR SPHQLLSPSS FSPSATPSQK YSSRTNRGEV VTTFGSAQGV
SWSGRGGSGS ISLKVMGYPE PLTSSYKTMF QQLPDIREVL TCKIEELGSE LKEHYKIEAF
TPLLVPAQEP VILLGQIGCD SNGRLNSKSV ILEGDREHSS GAQIPVDVSE LKDYSLFPGQ
VVIMEGFNTT GRRLTATKLY EGVPLPFYQP TEEEGDFEQT MVLVACGPYT TSDSITYDPL
LDLISTINHD RPDVCILFGP FLDAKHEQVE NCKLTSPFED IFKQCLRTVI EGTRSSGSHL
VFVPSLRDVH HEPVYPQPPF TFSELPREDK KRVQFVSEPC NLSINGVMFG LTSTDLLFHI
GAEEICSSSG TSDRFSRILK HILTQRSYYP LYPPHEDMAI DYENFYTYAQ LPVTPDVFIV
PSELRYFVKD IFGCVCMNPG RLTKGQVGGT FGRLYLRRQP KGTDSEGRQG LSVAAQVVRI
