DPOLQ_HUMAN
ID DPOLQ_HUMAN Reviewed; 2590 AA.
AC O75417; O95160; Q6VMB5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=DNA polymerase theta {ECO:0000303|PubMed:10395804, ECO:0000303|PubMed:14576298, ECO:0000312|HGNC:HGNC:9186};
DE EC=2.7.7.7 {ECO:0000269|PubMed:14576298, ECO:0000269|PubMed:22135286};
DE AltName: Full=DNA polymerase eta {ECO:0000303|Ref.4};
GN Name=POLQ {ECO:0000303|PubMed:10395804, ECO:0000303|PubMed:14576298,
GN ECO:0000312|HGNC:HGNC:9186}; Synonyms=POLH {ECO:0000303|Ref.4};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
RX PubMed=10395804; DOI=10.1006/geno.1999.5843;
RA Sharief F.S., Vojta P.J., Ropp P.A., Copeland W.C.;
RT "Cloning and chromosomal mapping of the human DNA polymerase theta (POLQ),
RT the eighth human DNA polymerase.";
RL Genomics 59:90-96(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP CATALYTIC ACTIVITY.
RX PubMed=14576298; DOI=10.1093/nar/gkg814;
RA Seki M., Marini F., Wood R.D.;
RT "POLQ (Pol theta), a DNA polymerase and DNA-dependent ATPase in human
RT cells.";
RL Nucleic Acids Res. 31:6117-6126(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1435-2590.
RA Harris P.V., Kaelin C.B., Burtis K.C.;
RT "Catalytic activity of Pol eta, a new human DNA polymerase related to the
RT bacterial DNA polymerase I family and Drosophila Mus308.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=18503084; DOI=10.1093/nar/gkn310;
RA Arana M.E., Seki M., Wood R.D., Rogozin I.B., Kunkel T.A.;
RT "Low-fidelity DNA synthesis by human DNA polymerase theta.";
RL Nucleic Acids Res. 36:3847-3856(2008).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF 2540-ASP-GLU-2541.
RX PubMed=19188258; DOI=10.1093/nar/gkp035;
RA Prasad R., Longley M.J., Sharief F.S., Hou E.W., Copeland W.C.,
RA Wilson S.H.;
RT "Human DNA polymerase theta possesses 5'-dRP lyase activity and functions
RT in single-nucleotide base excision repair in vitro.";
RL Nucleic Acids Res. 37:1868-1877(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-990, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP INVOLVEMENT IN BC.
RX PubMed=20700469; DOI=10.18632/oncotarget.124;
RA Higgins G.S., Harris A.L., Prevo R., Helleday T., McKenna W.G., Buffa F.M.;
RT "Overexpression of POLQ confers a poor prognosis in early breast cancer
RT patients.";
RL Oncotarget 1:175-184(2010).
RN [9]
RP INVOLVEMENT IN BC.
RX PubMed=20624954; DOI=10.1073/pnas.0910759107;
RA Lemee F., Bergoglio V., Fernandez-Vidal A., Machado-Silva A.,
RA Pillaire M.J., Bieth A., Gentil C., Baker L., Martin A.L., Leduc C.,
RA Lam E., Magdeleine E., Filleron T., Oumouhou N., Kaina B., Seki M.,
RA Grimal F., Lacroix-Triki M., Thompson A., Roche H., Bourdon J.C.,
RA Wood R.D., Hoffmann J.S., Cazaux C.;
RT "DNA polymerase theta up-regulation is associated with poor survival in
RT breast cancer, perturbs DNA replication, and promotes genetic
RT instability.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13390-13395(2010).
RN [10]
RP FUNCTION.
RX PubMed=21050863; DOI=10.1016/j.jmb.2010.10.041;
RA Hogg M., Seki M., Wood R.D., Doublie S., Wallace S.S.;
RT "Lesion bypass activity of DNA polymerase theta (POLQ) is an intrinsic
RT property of the pol domain and depends on unique sequence inserts.";
RL J. Mol. Biol. 405:642-652(2011).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22135286; DOI=10.1093/nar/gkr1102;
RA Hogg M., Sauer-Eriksson A.E., Johansson E.;
RT "Promiscuous DNA synthesis by human DNA polymerase theta.";
RL Nucleic Acids Res. 40:2611-2622(2012).
RN [12]
RP INVOLVEMENT IN BC.
RX PubMed=25409685; DOI=10.1186/1471-2407-14-850;
RA Brandalize A.P., Schueler-Faccini L., Hoffmann J.S., Caleffi M., Cazaux C.,
RA Ashton-Prolla P.;
RT "A DNA repair variant in POLQ (c.-1060A > G) is associated to hereditary
RT breast cancer patients: a case-control study.";
RL BMC Cancer 14:850-850(2014).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF 2540-ASP-GLU-2541.
RX PubMed=24648516; DOI=10.1074/jbc.m114.556977;
RA Yoon J.H., Roy Choudhury J., Park J., Prakash S., Prakash L.;
RT "A role for DNA polymerase theta in promoting replication through oxidative
RT DNA lesion, thymine glycol, in human cells.";
RL J. Biol. Chem. 289:13177-13185(2014).
RN [14]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ORC2 AND ORC4.
RX PubMed=24989122; DOI=10.1038/ncomms5285;
RA Fernandez-Vidal A., Guitton-Sert L., Cadoret J.C., Drac M., Schwob E.,
RA Baldacci G., Cazaux C., Hoffmann J.S.;
RT "A role for DNA polymerase theta in the timing of DNA replication.";
RL Nat. Commun. 5:4285-4285(2014).
RN [15]
RP FUNCTION, INTERACTION WITH RAD51, AND SUBCELLULAR LOCATION.
RX PubMed=25642963; DOI=10.1038/nature14184;
RA Ceccaldi R., Liu J.C., Amunugama R., Hajdu I., Primack B., Petalcorin M.I.,
RA O'Connor K.W., Konstantinopoulos P.A., Elledge S.J., Boulton S.J.,
RA Yusufzai T., D'Andrea A.D.;
RT "Homologous-recombination-deficient tumours are dependent on Poltheta-
RT mediated repair.";
RL Nature 518:258-262(2015).
RN [16]
RP FUNCTION, SUBUNIT, AND DOMAIN.
RX PubMed=25643323; DOI=10.1038/nsmb.2961;
RA Kent T., Chandramouly G., McDevitt S.M., Ozdemir A.Y., Pomerantz R.T.;
RT "Mechanism of microhomology-mediated end-joining promoted by human DNA
RT polymerase theta.";
RL Nat. Struct. Mol. Biol. 22:230-237(2015).
CC -!- FUNCTION: DNA polymerase that promotes microhomology-mediated end-
CC joining (MMEJ), an alternative non-homologous end-joining (NHEJ)
CC machinery triggered in response to double-strand breaks in DNA
CC (PubMed:25642963, PubMed:25643323). MMEJ is an error-prone repair
CC pathway that produces deletions of sequences from the strand being
CC repaired and promotes genomic rearrangements, such as telomere fusions,
CC some of them leading to cellular transformation (PubMed:25642963,
CC PubMed:25643323). POLQ acts as an inhibitor of homology-recombination
CC repair (HR) pathway by limiting RAD51 accumulation at resected ends
CC (PubMed:25642963). POLQ-mediated MMEJ may be required to promote the
CC survival of cells with a compromised HR repair pathway, thereby
CC preventing genomic havoc by resolving unrepaired lesions (By
CC similarity). The polymerase acts by binding directly the 2 ends of
CC resected double-strand breaks, allowing microhomologous sequences in
CC the overhangs to form base pairs. It then extends each strand from the
CC base-paired region using the opposing overhang as a template. Requires
CC partially resected DNA containing 2 to 6 base pairs of microhomology to
CC perform MMEJ (PubMed:25643323). The polymerase activity is highly
CC promiscuous: unlike most polymerases, promotes extension of ssDNA and
CC partial ssDNA (pssDNA) substrates (PubMed:18503084, PubMed:21050863,
CC PubMed:22135286). Also exhibits low-fidelity DNA synthesis, translesion
CC synthesis and lyase activity, and it is implicated in interstrand-
CC cross-link repair, base excision repair and DNA end-joining
CC (PubMed:14576298, PubMed:18503084, PubMed:19188258, PubMed:24648516).
CC Involved in somatic hypermutation of immunoglobulin genes, a process
CC that requires the activity of DNA polymerases to ultimately introduce
CC mutations at both A/T and C/G base pairs (By similarity).
CC {ECO:0000250|UniProtKB:Q8CGS6, ECO:0000269|PubMed:14576298,
CC ECO:0000269|PubMed:18503084, ECO:0000269|PubMed:19188258,
CC ECO:0000269|PubMed:21050863, ECO:0000269|PubMed:22135286,
CC ECO:0000269|PubMed:24648516, ECO:0000269|PubMed:25642963,
CC ECO:0000269|PubMed:25643323}.
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;
CC Evidence={ECO:0000269|PubMed:14576298, ECO:0000269|PubMed:22135286};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.095 uM for dATP:T {ECO:0000269|PubMed:22135286};
CC KM=0.622 uM for dATP: abasic site {ECO:0000269|PubMed:22135286};
CC KM=3.08 uM for dGTP: no template {ECO:0000269|PubMed:22135286};
CC -!- SUBUNIT: Homomultimer; forms dimers and multimers (PubMed:25643323).
CC Interacts with RAD51 (PubMed:25642963). Interacts with ORC2 and ORC4
CC (PubMed:24989122). {ECO:0000269|PubMed:24989122,
CC ECO:0000269|PubMed:25642963, ECO:0000269|PubMed:25643323}.
CC -!- INTERACTION:
CC O75417-1; O75417-1: POLQ; NbExp=5; IntAct=EBI-16141065, EBI-16141065;
CC O75417-1; Q06609: RAD51; NbExp=3; IntAct=EBI-16141065, EBI-297202;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O18475}.
CC Chromosome {ECO:0000269|PubMed:25642963}. Note=Enriched in chromatin in
CC response to ultaviolet (UV) light (PubMed:25642963). Binds to chromatin
CC during early G1 (PubMed:24989122). {ECO:0000269|PubMed:24989122,
CC ECO:0000269|PubMed:25642963}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75417-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75417-2; Sequence=VSP_040747, VSP_040748;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis.
CC {ECO:0000269|PubMed:14576298}.
CC -!- DOMAIN: The loop 2 region is involved in the binding of the 2 ends of
CC resected double-strand breaks and homomultimerization.
CC {ECO:0000269|PubMed:25643323}.
CC -!- DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy
CC originating from breast epithelial tissue. Breast neoplasms can be
CC distinguished by their histologic pattern. Invasive ductal carcinoma is
CC by far the most common type. Breast cancer is etiologically and
CC genetically heterogeneous. Important genetic factors have been
CC indicated by familial occurrence and bilateral involvement. Mutations
CC at more than one locus can be involved in different families or even in
CC the same case. {ECO:0000269|PubMed:20624954,
CC ECO:0000269|PubMed:20700469, ECO:0000269|PubMed:25409685}. Note=The
CC gene represented in this entry may be involved in disease pathogenesis.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
CC -!- CAUTION: Was wrongly named DNA polymerase eta (POLH) somne authors
CC (Ref.4). This protein corresponds to DNA polymerase theta (POLQ) and
CC should not be confused with DNA polymerase eta (POLH) (AC Q9Y253).
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD05272.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF052573; AAC33565.1; -; mRNA.
DR EMBL; AY338826; AAR08421.2; -; mRNA.
DR EMBL; AC069239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF043628; AAD05272.1; ALT_FRAME; mRNA.
DR CCDS; CCDS33833.1; -. [O75417-1]
DR RefSeq; NP_955452.3; NM_199420.3. [O75417-1]
DR PDB; 4X0P; X-ray; 3.91 A; A/B/C/D=1792-2590.
DR PDB; 4X0Q; X-ray; 3.90 A; A/B=1819-2590.
DR PDB; 5A9F; X-ray; 3.20 A; A=67-894.
DR PDB; 5A9J; X-ray; 3.55 A; A/B/C/D=1-894.
DR PDB; 5AGA; X-ray; 2.90 A; A=67-894.
DR PDBsum; 4X0P; -.
DR PDBsum; 4X0Q; -.
DR PDBsum; 5A9F; -.
DR PDBsum; 5A9J; -.
DR PDBsum; 5AGA; -.
DR AlphaFoldDB; O75417; -.
DR SMR; O75417; -.
DR BioGRID; 115946; 11.
DR DIP; DIP-61500N; -.
DR IntAct; O75417; 3.
DR STRING; 9606.ENSP00000264233; -.
DR ChEMBL; CHEMBL6025; -.
DR GlyGen; O75417; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75417; -.
DR PhosphoSitePlus; O75417; -.
DR BioMuta; POLQ; -.
DR EPD; O75417; -.
DR jPOST; O75417; -.
DR MassIVE; O75417; -.
DR MaxQB; O75417; -.
DR PaxDb; O75417; -.
DR PeptideAtlas; O75417; -.
DR PRIDE; O75417; -.
DR ProteomicsDB; 49988; -. [O75417-1]
DR ProteomicsDB; 49989; -. [O75417-2]
DR Antibodypedia; 32825; 77 antibodies from 23 providers.
DR DNASU; 10721; -.
DR Ensembl; ENST00000264233.6; ENSP00000264233.5; ENSG00000051341.15. [O75417-1]
DR GeneID; 10721; -.
DR KEGG; hsa:10721; -.
DR MANE-Select; ENST00000264233.6; ENSP00000264233.5; NM_199420.4; NP_955452.3.
DR UCSC; uc003eee.5; human. [O75417-1]
DR CTD; 10721; -.
DR DisGeNET; 10721; -.
DR GeneCards; POLQ; -.
DR HGNC; HGNC:9186; POLQ.
DR HPA; ENSG00000051341; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 114480; phenotype.
DR MIM; 604419; gene.
DR neXtProt; NX_O75417; -.
DR OpenTargets; ENSG00000051341; -.
DR PharmGKB; PA33506; -.
DR VEuPathDB; HostDB:ENSG00000051341; -.
DR eggNOG; KOG0950; Eukaryota.
DR GeneTree; ENSGT00940000158694; -.
DR HOGENOM; CLU_000818_0_1_1; -.
DR InParanoid; O75417; -.
DR OrthoDB; 179246at2759; -.
DR PhylomeDB; O75417; -.
DR TreeFam; TF105018; -.
DR PathwayCommons; O75417; -.
DR Reactome; R-HSA-5685939; HDR through MMEJ (alt-NHEJ).
DR SABIO-RK; O75417; -.
DR SignaLink; O75417; -.
DR BioGRID-ORCS; 10721; 105 hits in 1081 CRISPR screens.
DR ChiTaRS; POLQ; human.
DR GeneWiki; POLQ; -.
DR GenomeRNAi; 10721; -.
DR Pharos; O75417; Tbio.
DR PRO; PR:O75417; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O75417; protein.
DR Bgee; ENSG00000051341; Expressed in secondary oocyte and 112 other tissues.
DR Genevisible; O75417; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003684; F:damaged DNA binding; TAS:ProtInc.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IDA:UniProtKB.
DR GO; GO:0006284; P:base-excision repair; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; TAS:ProtInc.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR GO; GO:0006302; P:double-strand break repair; IDA:UniProtKB.
DR GO; GO:0097681; P:double-strand break repair via alternative nonhomologous end joining; IDA:UniProtKB.
DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; ISS:UniProtKB.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR002298; DNA_polymerase_A.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10133; PTHR10133; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR PRINTS; PR00868; DNAPOLI.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Chromosome;
KW Coiled coil; DNA damage; DNA repair; DNA-directed DNA polymerase;
KW Nucleotide-binding; Nucleotidyltransferase; Nucleus; Reference proteome;
KW Transferase.
FT CHAIN 1..2590
FT /note="DNA polymerase theta"
FT /id="PRO_0000101279"
FT DOMAIN 102..286
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 321..554
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..894
FT /note="Interaction with RAD51"
FT /evidence="ECO:0000269|PubMed:25642963"
FT REGION 1034..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1594..1622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1777..1797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2142..2177
FT /note="Loop 1"
FT /evidence="ECO:0000269|PubMed:21050863"
FT REGION 2257..2322
FT /note="Loop 2"
FT /evidence="ECO:0000269|PubMed:21050863,
FT ECO:0000269|PubMed:25643323"
FT REGION 2491..2535
FT /note="Loop 3"
FT /evidence="ECO:0000269|PubMed:21050863"
FT COILED 1655..1716
FT /evidence="ECO:0000255"
FT MOTIF 216..219
FT /note="DEAH box"
FT COMPBIAS 17..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1594..1621
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1782..1797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 115..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 990
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..828
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10395804"
FT /id="VSP_040747"
FT VAR_SEQ 829..840
FT /note="VEVILKNAVPFK -> MNSFLSFPISLC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10395804"
FT /id="VSP_040748"
FT VARIANT 1056
FT /note="P -> L (in dbSNP:rs34778629)"
FT /id="VAR_055707"
FT MUTAGEN 2540..2541
FT /note="DE->AA: Abolishes DNA polymerase activity."
FT /evidence="ECO:0000269|PubMed:19188258,
FT ECO:0000269|PubMed:24648516"
FT CONFLICT 66
FT /note="R -> I (in Ref. 2; AAR08421)"
FT /evidence="ECO:0000305"
FT CONFLICT 982
FT /note="T -> R (in Ref. 2; AAR08421)"
FT /evidence="ECO:0000305"
FT CONFLICT 2013
FT /note="L -> F (in Ref. 4; AAD05272)"
FT /evidence="ECO:0000305"
FT CONFLICT 2513
FT /note="Q -> R (in Ref. 1; AAC33565 and 2; AAR08421)"
FT /evidence="ECO:0000305"
FT CONFLICT 2547
FT /note="A -> V (in Ref. 1; AAC33565)"
FT /evidence="ECO:0000305"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 78..85
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 94..101
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:5AGA"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 121..135
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 147..161
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 191..203
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 229..243
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 260..266
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 271..277
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 326..335
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 347..366
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 384..395
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 403..408
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 413..416
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 422..433
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 439..442
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 444..447
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 454..460
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 471..478
FT /evidence="ECO:0007829|PDB:5AGA"
FT TURN 484..486
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 490..496
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:5A9F"
FT HELIX 501..509
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 529..540
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 547..556
FT /evidence="ECO:0007829|PDB:5AGA"
FT TURN 559..562
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 581..591
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 594..598
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 607..611
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 613..620
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 625..638
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 645..647
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 648..653
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 666..674
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 678..687
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 691..698
FT /evidence="ECO:0007829|PDB:5AGA"
FT TURN 708..711
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 712..728
FT /evidence="ECO:0007829|PDB:5AGA"
FT TURN 729..731
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 734..741
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 745..768
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 772..778
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 781..787
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 791..794
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 796..798
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 804..811
FT /evidence="ECO:0007829|PDB:5AGA"
FT TURN 812..814
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 818..822
FT /evidence="ECO:0007829|PDB:5AGA"
FT HELIX 826..834
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 840..842
FT /evidence="ECO:0007829|PDB:5AGA"
FT STRAND 856..858
FT /evidence="ECO:0007829|PDB:5A9F"
FT HELIX 872..889
FT /evidence="ECO:0007829|PDB:5AGA"
SQ SEQUENCE 2590 AA; 289619 MW; F5550BED2DAD8013 CRC64;
MNLLRRSGKR RRSESGSDSF SGSGGDSSAS PQFLSGSVLS PPPGLGRCLK AAAAGECKPT
VPDYERDKLL LANWGLPKAV LEKYHSFGVK KMFEWQAECL LLGQVLEGKN LVYSAPTSAG
KTLVAELLIL KRVLEMRKKA LFILPFVSVA KEKKYYLQSL FQEVGIKVDG YMGSTSPSRH
FSSLDIAVCT IERANGLINR LIEENKMDLL GMVVVDELHM LGDSHRGYLL ELLLTKICYI
TRKSASCQAD LASSLSNAVQ IVGMSATLPN LELVASWLNA ELYHTDFRPV PLLESVKVGN
SIYDSSMKLV REFEPMLQVK GDEDHVVSLC YETICDNHSV LLFCPSKKWC EKLADIIARE
FYNLHHQAEG LVKPSECPPV ILEQKELLEV MDQLRRLPSG LDSVLQKTVP WGVAFHHAGL
TFEERDIIEG AFRQGLIRVL AATSTLSSGV NLPARRVIIR TPIFGGRPLD ILTYKQMVGR
AGRKGVDTVG ESILICKNSE KSKGIALLQG SLKPVRSCLQ RREGEEVTGS MIRAILEIIV
GGVASTSQDM HTYAACTFLA ASMKEGKQGI QRNQESVQLG AIEACVMWLL ENEFIQSTEA
SDGTEGKVYH PTHLGSATLS SSLSPADTLD IFADLQRAMK GFVLENDLHI LYLVTPMFED
WTTIDWYRFF CLWEKLPTSM KRVAELVGVE EGFLARCVKG KVVARTERQH RQMAIHKRFF
TSLVLLDLIS EVPLREINQK YGCNRGQIQS LQQSAAVYAG MITVFSNRLG WHNMELLLSQ
FQKRLTFGIQ RELCDLVRVS LLNAQRARVL YASGFHTVAD LARANIVEVE VILKNAVPFK
SARKAVDEEE EAVEERRNMR TIWVTGRKGL TEREAAALIV EEARMILQQD LVEMGVQWNP
CALLHSSTCS LTHSESEVKE HTFISQTKSS YKKLTSKNKS NTIFSDSYIK HSPNIVQDLN
KSREHTSSFN CNFQNGNQEH QTCSIFRARK RASLDINKEK PGASQNEGKT SDKKVVQTFS
QKTKKAPLNF NSEKMSRSFR SWKRRKHLKR SRDSSPLKDS GACRIHLQGQ TLSNPSLCED
PFTLDEKKTE FRNSGPFAKN VSLSGKEKDN KTSFPLQIKQ NCSWNITLTN DNFVEHIVTG
SQSKNVTCQA TSVVSEKGRG VAVEAEKINE VLIQNGSKNQ NVYMKHHDIH PINQYLRKQS
HEQTSTITKQ KNIIERQMPC EAVSSYINRD SNVTINCERI KLNTEENKPS HFQALGDDIS
RTVIPSEVLP SAGAFSKSEG QHENFLNISR LQEKTGTYTT NKTKNNHVSD LGLVLCDFED
SFYLDTQSEK IIQQMATENA KLGAKDTNLA AGIMQKSLVQ QNSMNSFQKE CHIPFPAEQH
PLGATKIDHL DLKTVGTMKQ SSDSHGVDIL TPESPIFHSP ILLEENGLFL KKNEVSVTDS
QLNSFLQGYQ TQETVKPVIL LIPQKRTPTG VEGECLPVPE TSLNMSDSLL FDSFSDDYLV
KEQLPDMQMK EPLPSEVTSN HFSDSLCLQE DLIKKSNVNE NQDTHQQLTC SNDESIIFSE
MDSVQMVEAL DNVDIFPVQE KNHTVVSPRA LELSDPVLDE HHQGDQDGGD QDERAEKSKL
TGTRQNHSFI WSGASFDLSP GLQRILDKVS SPLENEKLKS MTINFSSLNR KNTELNEEQE
VISNLETKQV QGISFSSNNE VKSKIEMLEN NANHDETSSL LPRKESNIVD DNGLIPPTPI
PTSASKLTFP GILETPVNPW KTNNVLQPGE SYLFGSPSDI KNHDLSPGSR NGFKDNSPIS
DTSFSLQLSQ DGLQLTPASS SSESLSIIDV ASDQNLFQTF IKEWRCKKRF SISLACEKIR
SLTSSKTATI GSRFKQASSP QEIPIRDDGF PIKGCDDTLV VGLAVCWGGR DAYYFSLQKE
QKHSEISASL VPPSLDPSLT LKDRMWYLQS CLRKESDKEC SVVIYDFIQS YKILLLSCGI
SLEQSYEDPK VACWLLDPDS QEPTLHSIVT SFLPHELPLL EGMETSQGIQ SLGLNAGSEH
SGRYRASVES ILIFNSMNQL NSLLQKENLQ DVFRKVEMPS QYCLALLELN GIGFSTAECE
SQKHIMQAKL DAIETQAYQL AGHSFSFTSS DDIAEVLFLE LKLPPNREMK NQGSKKTLGS
TRRGIDNGRK LRLGRQFSTS KDVLNKLKAL HPLPGLILEW RRITNAITKV VFPLQREKCL
NPFLGMERIY PVSQSHTATG RITFTEPNIQ NVPRDFEIKM PTLVGESPPS QAVGKGLLPM
GRGKYKKGFS VNPRCQAQME ERAADRGMPF SISMRHAFVP FPGGSILAAD YSQLELRILA
HLSHDRRLIQ VLNTGADVFR SIAAEWKMIE PESVGDDLRQ QAKQICYGII YGMGAKSLGE
QMGIKENDAA CYIDSFKSRY TGINQFMTET VKNCKRDGFV QTILGRRRYL PGIKDNNPYR
KAHAERQAIN TIVQGSAADI VKIATVNIQK QLETFHSTFK SHGHREGMLQ SDQTGLSRKR
KLQGMFCPIR GGFFILQLHD ELLYEVAEED VVQVAQIVKN EMESAVKLSV KLKVKVKIGA
SWGELKDFDV
