DPOLM_MOUSE
ID DPOLM_MOUSE Reviewed; 496 AA.
AC Q9JIW4; G5E840; Q9JJW9;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=DNA-directed DNA/RNA polymerase mu;
DE Short=Pol Mu;
DE EC=2.7.7.7;
DE AltName: Full=Terminal transferase;
GN Name=Polm; Synonyms=polmu;
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].
RX PubMed=10982892; DOI=10.1093/nar/28.18.3684;
RA Aoufouchi S., Flatter E., Dahan A., Faili A., Bertocci B., Storck S.,
RA Delbos F., Cocea L., Gupta N., Weill J.-C., Reynaud C.-A.;
RT "Two novel human and mouse DNA polymerases of the polX family.";
RL Nucleic Acids Res. 28:3684-3693(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD-1;
RX PubMed=10747040; DOI=10.1093/emboj/19.7.1731;
RA Dominguez O., Ruiz J.F., Lain de Lera T., Garcia-Diaz M., Gonzalez M.A.,
RA Kirchhoff T., Martinez-A C., Bernad A., Blanco L.;
RT "DNA polymerase mu (Pol mu), homologous to TdT, could act as a DNA mutator
RT in eukaryotic cells.";
RL EMBO J. 19:1731-1742(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=16860755; DOI=10.1016/j.immuni.2006.04.013;
RA Bertocci B., De Smet A., Weill J.C., Reynaud C.A.;
RT "Nonoverlapping functions of DNA polymerases mu, lambda, and terminal
RT deoxynucleotidyltransferase during immunoglobulin V(D)J recombination in
RT vivo.";
RL Immunity 25:31-41(2006).
RN [6]
RP FUNCTION.
RX PubMed=17483519; DOI=10.1093/nar/gkm243;
RA Capp J.P., Boudsocq F., Besnard A.G., Lopez B.S., Cazaux C., Hoffmann J.S.,
RA Canitrot Y.;
RT "Involvement of DNA polymerase mu in the repair of a specific subset of DNA
RT double-strand breaks in mammalian cells.";
RL Nucleic Acids Res. 35:3551-3560(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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 [8]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 137-496 IN COMPLEX WITH DNA,
RP MAGNESIUM-BINDING SITES, AND COFACTOR.
RX PubMed=17159995; DOI=10.1038/nsmb1180;
RA Moon A.F., Garcia-Diaz M., Bebenek K., Davis B.J., Zhong X., Ramsden D.A.,
RA Kunkel T.A., Pedersen L.C.;
RT "Structural insight into the substrate specificity of DNA Polymerase mu.";
RL Nat. Struct. Mol. Biol. 14:45-53(2007).
CC -!- FUNCTION: Gap-filling polymerase involved in repair of DNA double-
CC strand breaks by non-homologous end joining (NHEJ). Participates in
CC immunoglobulin (Ig) light chain gene rearrangement in V(D)J
CC recombination. {ECO:0000269|PubMed:16860755,
CC ECO:0000269|PubMed:17483519}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17159995};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: DPOLM has a reduced ability to distinguish dNTP and rNTP
CC as substrates, and elongates them on DNA primer strand with a similar
CC efficiency. It is able to polymerize nucleotides on RNA primer strands
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family. {ECO:0000305}.
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DR EMBL; AF176098; AAF27552.1; -; mRNA.
DR EMBL; AJ251804; CAB71154.1; -; mRNA.
DR EMBL; AL627069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466574; EDL40561.1; -; Genomic_DNA.
DR CCDS; CCDS24405.1; -.
DR RefSeq; NP_059097.2; NM_017401.2.
DR PDB; 2IHM; X-ray; 2.40 A; A/B=137-496.
DR PDB; 6GO3; X-ray; 2.20 A; A=363-394.
DR PDB; 6GO4; X-ray; 1.96 A; A=363-394.
DR PDB; 6GO5; X-ray; 2.35 A; A/B=363-394.
DR PDB; 6GO6; X-ray; 2.09 A; A=363-394.
DR PDB; 6GO7; X-ray; 2.55 A; A=363-394.
DR PDBsum; 2IHM; -.
DR PDBsum; 6GO3; -.
DR PDBsum; 6GO4; -.
DR PDBsum; 6GO5; -.
DR PDBsum; 6GO6; -.
DR PDBsum; 6GO7; -.
DR AlphaFoldDB; Q9JIW4; -.
DR SMR; Q9JIW4; -.
DR STRING; 10090.ENSMUSP00000105463; -.
DR iPTMnet; Q9JIW4; -.
DR PhosphoSitePlus; Q9JIW4; -.
DR EPD; Q9JIW4; -.
DR PaxDb; Q9JIW4; -.
DR PRIDE; Q9JIW4; -.
DR ProteomicsDB; 277596; -.
DR Antibodypedia; 13228; 145 antibodies from 31 providers.
DR DNASU; 54125; -.
DR Ensembl; ENSMUST00000020767; ENSMUSP00000020767; ENSMUSG00000020474.
DR GeneID; 54125; -.
DR KEGG; mmu:54125; -.
DR UCSC; uc007hxf.2; mouse.
DR CTD; 27434; -.
DR MGI; MGI:1860191; Polm.
DR VEuPathDB; HostDB:ENSMUSG00000020474; -.
DR eggNOG; KOG2534; Eukaryota.
DR GeneTree; ENSGT00940000158490; -.
DR HOGENOM; CLU_008698_0_1_1; -.
DR InParanoid; Q9JIW4; -.
DR OMA; WTGSQLF; -.
DR OrthoDB; 1212057at2759; -.
DR Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
DR BioGRID-ORCS; 54125; 1 hit in 107 CRISPR screens.
DR ChiTaRS; Polm; mouse.
DR EvolutionaryTrace; Q9JIW4; -.
DR PRO; PR:Q9JIW4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9JIW4; protein.
DR Bgee; ENSMUSG00000020474; Expressed in animal zygote and 137 other tissues.
DR ExpressionAtlas; Q9JIW4; baseline and differential.
DR Genevisible; Q9JIW4; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030183; P:B cell differentiation; IMP:MGI.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; IMP:MGI.
DR CDD; cd00141; NT_POLXc; 1.
DR Gene3D; 1.10.150.110; -; 1.
DR Gene3D; 3.30.210.10; -; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR002054; DNA-dir_DNA_pol_X.
DR InterPro; IPR027249; DNA/RNApol_mu.
DR InterPro; IPR019843; DNA_pol-X_BS.
DR InterPro; IPR010996; DNA_pol_b-like_N.
DR InterPro; IPR028207; DNA_pol_B_palm_palm.
DR InterPro; IPR018944; DNA_pol_lambd_fingers_domain.
DR InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR InterPro; IPR037160; DNA_Pol_thumb_sf.
DR InterPro; IPR022312; DNA_pol_X.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR029398; PolB_thumb.
DR InterPro; IPR001726; TdT/Mu.
DR PANTHER; PTHR11276; PTHR11276; 1.
DR Pfam; PF14792; DNA_pol_B_palm; 1.
DR Pfam; PF14791; DNA_pol_B_thumb; 1.
DR Pfam; PF10391; DNA_pol_lambd_f; 1.
DR Pfam; PF14716; HHH_8; 1.
DR PIRSF; PIRSF000817; DNA_NT; 1.
DR PIRSF; PIRSF501176; DNApol_mu; 1.
DR PRINTS; PR00869; DNAPOLX.
DR PRINTS; PR00871; DNAPOLXTDT.
DR SMART; SM00483; POLXc; 1.
DR SUPFAM; SSF47802; SSF47802; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS00522; DNA_POLYMERASE_X; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA recombination; DNA repair;
KW DNA-directed DNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..496
FT /note="DNA-directed DNA/RNA polymerase mu"
FT /id="PRO_0000218788"
FT DOMAIN 23..122
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..332
FT /note="Involved in ssDNA binding"
FT BINDING 241
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 332
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 420
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 435
FT /note="Responsible for the low discrimination between dNTP
FT and rNTP"
FT /evidence="ECO:0000250"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 18
FT /note="A -> D (in Ref. 1; AAF27552)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="A -> V (in Ref. 2; CAB71154)"
FT /evidence="ECO:0000305"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:2IHM"
FT HELIX 154..169
FT /evidence="ECO:0007829|PDB:2IHM"
FT HELIX 173..188
FT /evidence="ECO:0007829|PDB:2IHM"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:2IHM"
FT HELIX 207..219
FT /evidence="ECO:0007829|PDB:2IHM"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:2IHM"
FT HELIX 232..241
FT /evidence="ECO:0007829|PDB:2IHM"
FT HELIX 248..256
FT /evidence="ECO:0007829|PDB:2IHM"
FT HELIX 262..266
FT /evidence="ECO:0007829|PDB:2IHM"
FT HELIX 274..281
FT /evidence="ECO:0007829|PDB:2IHM"
FT HELIX 283..287
FT /evidence="ECO:0007829|PDB:2IHM"
FT HELIX 292..307
FT /evidence="ECO:0007829|PDB:2IHM"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:2IHM"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:2IHM"
FT STRAND 326..336
FT /evidence="ECO:0007829|PDB:2IHM"
FT TURN 340..345
FT /evidence="ECO:0007829|PDB:2IHM"
FT HELIX 346..356
FT /evidence="ECO:0007829|PDB:2IHM"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:6GO4"
FT HELIX 370..376
FT /evidence="ECO:0007829|PDB:6GO4"
FT HELIX 381..385
FT /evidence="ECO:0007829|PDB:6GO6"
FT STRAND 387..394
FT /evidence="ECO:0007829|PDB:6GO4"
FT STRAND 414..423
FT /evidence="ECO:0007829|PDB:2IHM"
FT HELIX 429..437
FT /evidence="ECO:0007829|PDB:2IHM"
FT HELIX 440..454
FT /evidence="ECO:0007829|PDB:2IHM"
FT HELIX 477..483
FT /evidence="ECO:0007829|PDB:2IHM"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:2IHM"
SQ SEQUENCE 496 AA; 55490 MW; D087636E30C27127 CRC64;
MLPKRRRVRA GSPHSAVASS TPPSVVRFPD VAIYLAEPRM GRSRRAFLTR LARSKGFRVL
DAYSSKVTHV VMEGTSAKEA ICWQKNMDAL PTGCPQPALL DISWFTESMA AGQPVPEEGR
HHLEVAEPRK EPPVSASMPA YACQRPSPLT HHNTLLSEAL ETLAEAAGFE ANEGRLLSFS
RAASVLKSLP CPVASLSQLH GLPYFGEHST RVIQELLEHG TCEEVKQVRC SERYQTMKLF
TQVFGVGVKT ANRWYQEGLR TLDELREQPQ RLTQQQKAGL QYYQDLSTPV RRADAEALQQ
LIEAAVRQTL PGATVTLTGG FRRGKLQGHD VDFLITHPEE GQEVGLLPKV MSCLQSQGLV
LYHQYHRSHL ADSAHNLRQR SSTMDAFERS FCILGLPQPQ QAALAGALPP CPTWKAVRVD
LVVTPSSQFP FALLGWTGSQ FFERELRRFS RQEKGLWLNS HGLFDPEQKR VFHATSEEDV
FRLLGLKYLP PEQRNA
