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DNA-directed DNA/RNA polymerase mu (Pol Mu) (EC 2.7.7.7) (Terminal transferase)

 DPOLM_MOUSE             Reviewed;         496 AA.
Q9JIW4; G5E840; Q9JJW9;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 2.
10-MAY-2017, entry version 130.
RecName: Full=DNA-directed DNA/RNA polymerase mu;
Short=Pol Mu;
EC=2.7.7.7;
AltName: Full=Terminal transferase;
Name=Polm; Synonyms=polmu;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10982892; DOI=10.1093/nar/28.18.3684;
Aoufouchi S., Flatter E., Dahan A., Faili A., Bertocci B., Storck S.,
Delbos F., Cocea L., Gupta N., Weill J.-C., Reynaud C.-A.;
"Two novel human and mouse DNA polymerases of the polX family.";
Nucleic Acids Res. 28:3684-3693(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=CD-1;
PubMed=10747040; DOI=10.1093/emboj/19.7.1731;
Dominguez O., Ruiz J.F., Lain de Lera T., Garcia-Diaz M.,
Gonzalez M.A., Kirchhoff T., Martinez-A C., Bernad A., Blanco L.;
"DNA polymerase mu (Pol mu), homologous to TdT, could act as a DNA
mutator in eukaryotic cells.";
EMBO J. 19:1731-1742(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION.
PubMed=16860755; DOI=10.1016/j.immuni.2006.04.013;
Bertocci B., De Smet A., Weill J.C., Reynaud C.A.;
"Nonoverlapping functions of DNA polymerases mu, lambda, and terminal
deoxynucleotidyltransferase during immunoglobulin V(D)J recombination
in vivo.";
Immunity 25:31-41(2006).
[6]
FUNCTION.
PubMed=17483519; DOI=10.1093/nar/gkm243;
Capp J.P., Boudsocq F., Besnard A.G., Lopez B.S., Cazaux C.,
Hoffmann J.S., Canitrot Y.;
"Involvement of DNA polymerase mu in the repair of a specific subset
of DNA double-strand breaks in mammalian cells.";
Nucleic Acids Res. 35:3551-3560(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 137-496 IN COMPLEX WITH DNA,
MAGNESIUM-BINDING SITES, AND COFACTOR.
PubMed=17159995; DOI=10.1038/nsmb1180;
Moon A.F., Garcia-Diaz M., Bebenek K., Davis B.J., Zhong X.,
Ramsden D.A., Kunkel T.A., Pedersen L.C.;
"Structural insight into the substrate specificity of DNA Polymerase
mu.";
Nat. Struct. Mol. Biol. 14:45-53(2007).
-!- FUNCTION: Gap-filling polymerase involved in repair of DNA double-
strand breaks by non-homologous end joining (NHEJ). Participates
in immunoglobulin (Ig) light chain gene rearrangement in V(D)J
recombination. {ECO:0000269|PubMed:16860755,
ECO:0000269|PubMed:17483519}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1).
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:17159995};
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- MISCELLANEOUS: DPOLM has a reduced ability to distinguish dNTP and
rNTP as substrates, and elongates them on DNA primer strand with a
similar efficiency. It is able to polymerize nucleotides on RNA
primer strands (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the DNA polymerase type-X family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF176098; AAF27552.1; -; mRNA.
EMBL; AJ251804; CAB71154.1; -; mRNA.
EMBL; AL627069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466574; EDL40561.1; -; Genomic_DNA.
CCDS; CCDS24405.1; -.
RefSeq; NP_059097.2; NM_017401.2.
UniGene; Mm.260194; -.
PDB; 2IHM; X-ray; 2.40 A; A/B=137-496.
PDBsum; 2IHM; -.
ProteinModelPortal; Q9JIW4; -.
SMR; Q9JIW4; -.
STRING; 10090.ENSMUSP00000020767; -.
iPTMnet; Q9JIW4; -.
PhosphoSitePlus; Q9JIW4; -.
EPD; Q9JIW4; -.
PaxDb; Q9JIW4; -.
PRIDE; Q9JIW4; -.
Ensembl; ENSMUST00000020767; ENSMUSP00000020767; ENSMUSG00000020474.
GeneID; 54125; -.
KEGG; mmu:54125; -.
UCSC; uc007hxf.2; mouse.
CTD; 27434; -.
MGI; MGI:1860191; Polm.
eggNOG; KOG2534; Eukaryota.
eggNOG; COG1796; LUCA.
GeneTree; ENSGT00530000063002; -.
HOGENOM; HOG000263600; -.
HOVERGEN; HBG003670; -.
InParanoid; Q9JIW4; -.
KO; K03513; -.
Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
EvolutionaryTrace; Q9JIW4; -.
PRO; PR:Q9JIW4; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020474; -.
CleanEx; MM_POLM; -.
ExpressionAtlas; Q9JIW4; baseline and differential.
Genevisible; Q9JIW4; MM.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030183; P:B cell differentiation; IMP:MGI.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; IMP:MGI.
CDD; cd00027; BRCT; 1.
CDD; cd00141; NT_POLXc; 1.
Gene3D; 3.30.210.10; -; 1.
Gene3D; 3.40.50.10190; -; 1.
InterPro; IPR001357; BRCT_dom.
InterPro; IPR002054; DNA-dir_DNA_pol_X.
InterPro; IPR027249; DNA/RNApol_mu.
InterPro; IPR019843; DNA_pol-X_BS.
InterPro; IPR010996; DNA_pol_b-like_N.
InterPro; IPR028207; DNA_pol_B_palm_palm.
InterPro; IPR018944; DNA_pol_lambd_fingers_domain.
InterPro; IPR022312; DNA_pol_X.
InterPro; IPR029398; PolB_thumb.
InterPro; IPR001726; TdT/Mu.
Pfam; PF14792; DNA_pol_B_palm; 1.
Pfam; PF14791; DNA_pol_B_thumb; 1.
Pfam; PF10391; DNA_pol_lambd_f; 1.
Pfam; PF14716; HHH_8; 1.
PIRSF; PIRSF000817; DNA_NT; 1.
PIRSF; PIRSF501176; DNApol_mu; 1.
PRINTS; PR00869; DNAPOLX.
PRINTS; PR00871; DNAPOLXTDT.
SMART; SM00483; POLXc; 1.
SUPFAM; SSF47802; SSF47802; 1.
SUPFAM; SSF52113; SSF52113; 1.
PROSITE; PS50172; BRCT; 1.
PROSITE; PS00522; DNA_POLYMERASE_X; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; DNA damage; DNA recombination;
DNA repair; DNA-directed DNA polymerase; Magnesium; Metal-binding;
Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
Transferase.
CHAIN 1 496 DNA-directed DNA/RNA polymerase mu.
/FTId=PRO_0000218788.
DOMAIN 23 122 BRCT. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
REGION 323 332 Involved in ssDNA binding.
METAL 241 241 Sodium; via carbonyl oxygen.
{ECO:0000250}.
METAL 243 243 Sodium; via carbonyl oxygen.
{ECO:0000250}.
METAL 330 330 Magnesium.
METAL 332 332 Magnesium.
METAL 420 420 Magnesium. {ECO:0000250}.
SITE 435 435 Responsible for the low discrimination
between dNTP and rNTP. {ECO:0000250}.
MOD_RES 12 12 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CONFLICT 18 18 A -> D (in Ref. 1; AAF27552).
{ECO:0000305}.
CONFLICT 386 386 A -> V (in Ref. 2; CAB71154).
{ECO:0000305}.
HELIX 142 144 {ECO:0000244|PDB:2IHM}.
HELIX 154 169 {ECO:0000244|PDB:2IHM}.
HELIX 173 188 {ECO:0000244|PDB:2IHM}.
HELIX 196 199 {ECO:0000244|PDB:2IHM}.
HELIX 207 219 {ECO:0000244|PDB:2IHM}.
HELIX 223 230 {ECO:0000244|PDB:2IHM}.
HELIX 232 241 {ECO:0000244|PDB:2IHM}.
HELIX 248 256 {ECO:0000244|PDB:2IHM}.
HELIX 262 266 {ECO:0000244|PDB:2IHM}.
HELIX 274 281 {ECO:0000244|PDB:2IHM}.
HELIX 283 287 {ECO:0000244|PDB:2IHM}.
HELIX 292 307 {ECO:0000244|PDB:2IHM}.
STRAND 314 317 {ECO:0000244|PDB:2IHM}.
HELIX 319 322 {ECO:0000244|PDB:2IHM}.
STRAND 326 336 {ECO:0000244|PDB:2IHM}.
TURN 340 345 {ECO:0000244|PDB:2IHM}.
HELIX 346 356 {ECO:0000244|PDB:2IHM}.
STRAND 360 366 {ECO:0000244|PDB:2IHM}.
STRAND 389 397 {ECO:0000244|PDB:2IHM}.
STRAND 414 423 {ECO:0000244|PDB:2IHM}.
HELIX 429 437 {ECO:0000244|PDB:2IHM}.
HELIX 440 454 {ECO:0000244|PDB:2IHM}.
HELIX 477 483 {ECO:0000244|PDB:2IHM}.
HELIX 491 493 {ECO:0000244|PDB:2IHM}.
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


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