DPOLA_MOUSE
ID DPOLA_MOUSE Reviewed; 1465 AA.
AC P33609;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=DNA polymerase alpha catalytic subunit;
DE EC=2.7.7.7 {ECO:0000269|PubMed:8026492, ECO:0000269|PubMed:8253737};
DE AltName: Full=DNA polymerase alpha catalytic subunit p180;
GN Name=Pola1; Synonyms=Pola;
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], AND PROTEIN SEQUENCE OF 454-472 AND 1438-1455.
RX PubMed=8463324; DOI=10.1016/s0021-9258(18)53069-6;
RA Miyazawa H., Izumi M., Tada S., Takada R., Masutani M., Ui M., Hanaoka F.;
RT "Molecular cloning of the cDNAs for the four subunits of mouse DNA
RT polymerase alpha-primase complex and their gene expression during cell
RT proliferation and the cell cycle.";
RL J. Biol. Chem. 268:8111-8122(1993).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PRIM2, AND MUTAGENESIS OF
RP ASP-1008.
RX PubMed=8253737; DOI=10.1016/s0021-9258(19)74297-5;
RA Copeland W.C., Wang T.S.;
RT "Enzymatic characterization of the individual mammalian primase subunits
RT reveals a biphasic mechanism for initiation of DNA replication.";
RL J. Biol. Chem. 268:26179-26189(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8026492; DOI=10.1111/j.1432-1033.1994.tb18925.x;
RA Stadlbauer F., Brueckner A., Rehfuess C., Eckerskorn C., Lottspeich F.,
RA Foerster V., Tseng B.Y., Nasheuer H.-P.;
RT "DNA replication in vitro by recombinant DNA-polymerase-alpha-primase.";
RL Eur. J. Biochem. 222:781-793(1994).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-230, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-974, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP VARIANT PHE-1180.
RX PubMed=8125989; DOI=10.1016/s0021-9258(17)37335-0;
RA Izumi M., Miyazawa H., Harakawa S., Yatagai F., Hanaoka F.;
RT "Identification of a point mutation in the cDNA of the catalytic subunit of
RT DNA polymerase alpha from a temperature-sensitive mouse FM3A cell line.";
RL J. Biol. Chem. 269:7639-7644(1994).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=31006512; DOI=10.1016/j.ajhg.2019.03.006;
RA Van Esch H., Colnaghi R., Freson K., Starokadomskyy P., Zankl A., Backx L.,
RA Abramowicz I., Outwin E., Rohena L., Faulkner C., Leong G.M.,
RA Newbury-Ecob R.A., Challis R.C., Ounap K., Jaeken J., Seuntjens E.,
RA Devriendt K., Burstein E., Low K.J., O'Driscoll M.;
RT "Defective DNA Polymerase alpha-Primase Leads to X-Linked Intellectual
RT Disability Associated with Severe Growth Retardation, Microcephaly, and
RT Hypogonadism.";
RL Am. J. Hum. Genet. 104:957-967(2019).
CC -!- FUNCTION: Catalytic 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:8253737,
CC PubMed:8026492). During the S phase of the cell cycle, the DNA
CC polymerase alpha complex (composed of a catalytic subunit POLA1, a
CC regulatory subunit POLA2 and two primase subunits PRIM1 and PRIM2) is
CC recruited to DNA at the replicative forks via direct interactions with
CC MCM10 and WDHD1. The primase subunit of the polymerase alpha complex
CC initiates DNA synthesis by oligomerising short RNA primers on both
CC leading and lagging strands. These primers are initially extended by
CC the polymerase alpha catalytic subunit and subsequently transferred to
CC polymerase delta and polymerase epsilon for processive synthesis on the
CC lagging and leading strand, respectively. The reason this transfer
CC occurs is because the polymerase alpha has limited processivity and
CC lacks intrinsic 3' exonuclease activity for proofreading error, and
CC therefore is not well suited for replicating long complexes. In the
CC cytosol, responsible for a substantial proportion of the physiological
CC concentration of cytosolic RNA:DNA hybrids, which are necessary to
CC prevent spontaneous activation of type I interferon responses.
CC {ECO:0000250|UniProtKB:P09884, ECO:0000269|PubMed:8026492,
CC ECO:0000269|PubMed:8253737}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000269|PubMed:8026492,
CC ECO:0000269|PubMed:8253737};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22509;
CC Evidence={ECO:0000305|PubMed:8026492};
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:8253737,
CC PubMed:8026492). Within the complex, POLA1 directly interacts with
CC PRIM2 (PubMed:8253737). Interacts with PARP1; this interaction
CC functions as part of the control of replication fork progression.
CC Interacts with MCM10 and WDHD1; these interactions recruit the
CC polymerase alpha complex to the pre-replicative complex bound to DNA.
CC Interacts with RPA1; this interaction stabilizes the replicative
CC complex and reduces the misincorporation rate of DNA polymerase alpha
CC by acting as a fidelity clamp (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:8026492, ECO:0000269|PubMed:8253737}.
CC -!- INTERACTION:
CC P33609; P33611: Pola2; NbExp=5; IntAct=EBI-688051, EBI-848759;
CC P33609; P20664: Prim1; NbExp=4; IntAct=EBI-688051, EBI-848742;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09884}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:P09884}. Note=In the cytosol,
CC colocalizes with RNA:DNA hybrids with a speckled pattern.
CC {ECO:0000250|UniProtKB:P09884}.
CC -!- TISSUE SPECIFICITY: Expressed in those zones containing proliferating
CC cells in the developing embryonic neocortex, as well as in the lateral
CC and medial ganglionic eminences. After birth, expressed in cells that
CC remain proliferating in the ventricular and subventricular zone of the
CC striatum. {ECO:0000269|PubMed:31006512}.
CC -!- MISCELLANEOUS: In eukaryotes there are five DNA polymerases: alpha,
CC beta, gamma, delta, and epsilon which are responsible for different
CC reactions of DNA synthesis.
CC -!- MISCELLANEOUS: Conserved regions II, IV, III and I are thought to be
CC involved in substrate recognition, binding or PP(i) hydrolysis.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR EMBL; D13543; BAA40003.1; -; mRNA.
DR EMBL; D17384; BAA04202.1; -; mRNA.
DR CCDS; CCDS30272.1; -.
DR PIR; S45628; S45628.
DR RefSeq; NP_032918.1; NM_008892.2.
DR AlphaFoldDB; P33609; -.
DR SMR; P33609; -.
DR BioGRID; 202287; 3.
DR ComplexPortal; CPX-2088; DNA polymerase alpha:primase complex.
DR CORUM; P33609; -.
DR IntAct; P33609; 4.
DR STRING; 10090.ENSMUSP00000006856; -.
DR ChEMBL; CHEMBL2797; -.
DR iPTMnet; P33609; -.
DR PhosphoSitePlus; P33609; -.
DR EPD; P33609; -.
DR jPOST; P33609; -.
DR MaxQB; P33609; -.
DR PaxDb; P33609; -.
DR PeptideAtlas; P33609; -.
DR PRIDE; P33609; -.
DR ProteomicsDB; 279570; -.
DR Antibodypedia; 498; 192 antibodies from 28 providers.
DR DNASU; 18968; -.
DR Ensembl; ENSMUST00000006856; ENSMUSP00000006856; ENSMUSG00000006678.
DR GeneID; 18968; -.
DR KEGG; mmu:18968; -.
DR UCSC; uc009tss.2; mouse.
DR CTD; 5422; -.
DR MGI; MGI:99660; Pola1.
DR VEuPathDB; HostDB:ENSMUSG00000006678; -.
DR eggNOG; KOG0970; Eukaryota.
DR GeneTree; ENSGT00550000074891; -.
DR HOGENOM; CLU_001718_0_0_1; -.
DR InParanoid; P33609; -.
DR OMA; WLKIEDA; -.
DR OrthoDB; 293315at2759; -.
DR PhylomeDB; P33609; -.
DR TreeFam; TF103001; -.
DR Reactome; R-MMU-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-MMU-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-MMU-174430; Telomere C-strand synthesis initiation.
DR Reactome; R-MMU-68952; DNA replication initiation.
DR Reactome; R-MMU-68962; Activation of the pre-replicative complex.
DR Reactome; R-MMU-69091; Polymerase switching.
DR Reactome; R-MMU-69166; Removal of the Flap Intermediate.
DR Reactome; R-MMU-69183; Processive synthesis on the lagging strand.
DR BioGRID-ORCS; 18968; 35 hits in 111 CRISPR screens.
DR ChiTaRS; Pola1; mouse.
DR PRO; PR:P33609; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P33609; protein.
DR Bgee; ENSMUSG00000006678; Expressed in morula and 198 other tissues.
DR Genevisible; P33609; MM.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; IDA:UniProtKB.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
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:0000166; F:nucleotide binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0017076; F:purine nucleotide binding; ISO:MGI.
DR GO; GO:0019103; F:pyrimidine nucleotide binding; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0071897; P:DNA biosynthetic process; ISO:MGI.
DR GO; GO:0006260; P:DNA replication; IDA:MGI.
DR GO; GO:0006270; P:DNA replication initiation; IDA:ComplexPortal.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IDA:UniProtKB.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; ISS:UniProtKB.
DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; ISO:MGI.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0006273; P:lagging strand elongation; ISS:UniProtKB.
DR GO; GO:0006272; P:leading strand elongation; ISS:UniProtKB.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IBA:GO_Central.
DR GO; GO:0032479; P:regulation of type I interferon production; ISS:UniProtKB.
DR CDD; cd05532; POLBc_alpha; 1.
DR Gene3D; 1.10.132.60; -; 1.
DR Gene3D; 1.10.3200.20; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.90.1600.10; -; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR024647; DNA_pol_a_cat_su_N.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR038256; Pol_alpha_znc_sf.
DR InterPro; IPR045846; POLBc_alpha.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR015088; Znf_DNA-dir_DNA_pol_B_alpha.
DR Pfam; PF12254; DNA_pol_alpha_N; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF08996; zf-DNA_Pol; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; DNA replication;
KW DNA-binding; DNA-directed DNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1465
FT /note="DNA polymerase alpha catalytic subunit"
FT /id="PRO_0000046429"
FT ZN_FING 1287..1317
FT /note="CysA-type"
FT REGION 20..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..719
FT /note="DNA-binding"
FT /evidence="ECO:0000255"
FT REGION 1249..1380
FT /note="DNA-binding"
FT /evidence="ECO:0000255"
FT MOTIF 1352..1378
FT /note="CysB motif"
FT COMPBIAS 110..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09884"
FT BINDING 1290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09884"
FT BINDING 1314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09884"
FT BINDING 1319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09884"
FT BINDING 1352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P09884"
FT BINDING 1357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P09884"
FT BINDING 1375
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P09884"
FT BINDING 1378
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P09884"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P09884"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09884"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 230
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 974
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VARIANT 1180
FT /note="S -> F (in temperature-sensitive FT20 cell line;
FT defective activity)"
FT /evidence="ECO:0000269|PubMed:8125989"
FT MUTAGEN 1008
FT /note="D->N: Results in loss of primer extension catalytic
FT activity but retains ability to bind to the primase
FT complex."
FT /evidence="ECO:0000269|PubMed:8253737"
SQ SEQUENCE 1465 AA; 167340 MW; 46D1A9818A7944A3 CRC64;
MAPMHEEDCK LEASAVSDSG SFAASRARRE KKSKKGRQEA LERLKKAKAG EKYKYEVEDL
TSVYEEVDEE QYSKLVQARQ DDDWIVDDDG IGYVEDGREI FDDDLEDDAL DTCGKGSDGK
AHRKDRKDVK KPSVTKPNNI KAMFIASAGK KTTDKAVDLS KDDLLGDILQ DLNTETAQIT
PPPVLIPKKK RSTGALLNPF SVHTPKAIPS GKPASPVLRN EPLLTPIPLK RAELAGELAQ
PECPEDEQEL GVMEFEDGDF DESMDTEKVD EKPVTAKTWD QETEPVERVE HEADPERGTT
SYLENFLPDV SCWDIDQDDE SIPQEVQVDS SNLPLVKGAD DEQVFQFYWL DAYEDPYNQP
GVVFLFGKVW IESVKTHVSC CVMVKNIERT LYFLPREMKF DLNTGKETAI PVTMKDVYEE
FDSKISAKYK IMKFKSKIVE KNYAFEIPDV PEKSEYLEVR YSAEVPQLPQ NLKGETFSHV
FGTNTSSLEL FLMNRKIKGP CWLEVKNPQL LNQPISWCKF EVMALKPDLV NVIKDVSPPP
LVVMSFSMKT MQNVQNHQHE IIAMAALVHH SFALDKAPPE PPFQTHFCVV SKPKDCIFPC
DFKEVISKKN MKVEIAATER TLIGFFLAKV HKIDPDILVG HNICSFELEV LLQRINECKV
PYWSKIGRLR RSNMPKLGSR SGFGERNATC GRMICDVEIS AKELIHCKSY HLSELVQQIL
KTERIVIPTE NIRNMYSESS YLLYLLEHIW KDARFILQIM CELNVLPLAL QITNIAGNIM
SRTLMGGRSE RNEFLLLHAF YENNYIVPDK QIFRKPQQKL GDEDEEIDGD TNKYKKGRKK
ATYAGGLVLD PKVGFYDKFI LLLDFNSLYP SIIQEFNICF TTVQRVTSEV QKATEDEEQE
QIPELPDPNL EMGILPREIR KLVERRKQVK QLMKQQDLNP DLVLQYDIRQ KALKLTANSM
YGCLGFSYSR FYAKPLAALV TYKGREILMH TKDMVQKMNL EVIYGDTDSI MINTNSTNLE
EVFKLGNKVK SEVNKLYKLL EIDIDAVFKS LLLLKKKKYA ALVVEPTSDG NYITKQELKG
LDIVRRDWCD LAKDTGNFVI GQILSDQSRD TIVENIQKRL IEIGENVLNG SVPVSQFEIN
KALTKDPQDY PDRKSLPHVH VALWINSQGG RKVKAGDTVS YVICQDGSNL TATQRAYAPE
QLQKLDNLAI DTQYYLAQQI HPVVARICEP IDGIDAVLIA LWLGLDSTQF RVHQYHKDEE
NDALLGGPAQ LTDEEKYKDC EKFKCLCPSC GTENIYDNVF EGSGLDMEPS LYRCSNVDCK
VSPLTFMVQL SNKLIMDIRR CIKKYYDGWL ICEEPTCCSR LRRLPLHFSR NGPLCPVCMK
AVLRPEYSDK SLYTQLCFYR YIFDADCALE KLTEHEKDKL KKQFFPLRVL QDYRKVKNIA
EQFLSWSGYS EVNLSKLFAN YAGKS
