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   27-MAR-2024, entry version 164.
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.ENSMUSP00000020767; -.
DR   iPTMnet; Q9JIW4; -.
DR   PhosphoSitePlus; Q9JIW4; -.
DR   EPD; Q9JIW4; -.
DR   PaxDb; 10090-ENSMUSP00000105463; -.
DR   ProteomicsDB; 277596; -.
DR   Antibodypedia; 13228; 161 antibodies from 31 providers.
DR   DNASU; 54125; -.
DR   Ensembl; ENSMUST00000020767.4; ENSMUSP00000020767.4; ENSMUSG00000020474.12.
DR   GeneID; 54125; -.
DR   KEGG; mmu:54125; -.
DR   UCSC; uc007hxf.2; mouse.
DR   AGR; MGI:1860191; -.
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; APWSQFP; -.
DR   OrthoDB; 3019669at2759; -.
DR   Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
DR   BioGRID-ORCS; 54125; 1 hit in 112 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 141 other cell types or tissues.
DR   ExpressionAtlas; Q9JIW4; baseline and differential.
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; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   Gene3D; 1.10.150.110; DNA polymerase beta, N-terminal domain-like; 1.
DR   Gene3D; 3.30.210.10; DNA polymerase, thumb domain; 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; DNA POLYMERASE TYPE-X FAMILY MEMBER; 1.
DR   PANTHER; PTHR11276:SF24; DNA-DIRECTED DNA_RNA POLYMERASE MU; 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; SSF52113; BRCT domain; 1.
DR   SUPFAM; SSF47802; DNA polymerase beta, N-terminal domain-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81585; PsbU/PolX domain-like; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS00522; DNA_POLYMERASE_X; 1.
DR   Genevisible; Q9JIW4; MM.
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
//