ID   DPOLN_MOUSE             Reviewed;         864 AA.
AC   Q7TQ07; Q3V0L3;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=DNA polymerase nu;
DE            EC=2.7.7.7;
GN   Name=Poln;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ;
RX   PubMed=12794064; DOI=10.1074/jbc.m305646200;
RA   Marini F., Kim N., Schuffert A., Wood R.D.;
RT   "POLN, a nuclear PolA family DNA polymerase homologous to the DNA cross-
RT   link sensitivity protein Mus308.";
RL   J. Biol. Chem. 278:32014-32019(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: DNA polymerase with very low fidelity that catalyzes
CC       considerable misincorporation by inserting dTTP opposite a G template,
CC       and dGTP opposite a T template. Is the least accurate of the DNA
CC       polymerase A family (i.e. POLG, POLN and POLQ). Can perform accurate
CC       translesion DNA synthesis (TLS) past a 5S-thymine glycol. Can perform
CC       efficient strand displacement past a nick or a gap and gives rise to an
CC       amount of product similar to that on non-damaged template. Has no
CC       exonuclease activity. Error-prone DNA polymerase that preferentially
CC       misincorporates dT regardless of template sequence. May play a role in
CC       TLS during interstrand cross-link (ICL) repair. May be involved in TLS
CC       when genomic replication is blocked by extremely large major groove DNA
CC       lesions. May function in the bypass of some DNA-protein and DNA-DNA
CC       cross-links. May have a role in cellular tolerance to DNA cross-linking
CC       agents. Involved in the repair of DNA cross-links and double-strand
CC       break (DSB) resistance. Participates in FANCD2-mediated repair. Forms a
CC       complex with HELQ helicase that participates in homologous
CC       recombination (HR) repair and is essential for cellular protection
CC       against DNA cross-links. {ECO:0000250|UniProtKB:Q7Z5Q5}.
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   -!- ACTIVITY REGULATION: Inhibited by ddTTP.
CC       {ECO:0000250|UniProtKB:Q7Z5Q5}.
CC   -!- SUBUNIT: Interacts with FANCD2, FANCI, PCNA, RAD51 and HELQ.
CC       {ECO:0000250|UniProtKB:Q7Z5Q5}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7Z5Q5}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7TQ07-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TQ07-2; Sequence=VSP_017616;
CC   -!- TISSUE SPECIFICITY: Expressed only in testis namely in primary
CC       spermatocytes and in round spermatids. {ECO:0000269|PubMed:12794064}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN39837.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE21491.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY135562; AAN39837.2; ALT_INIT; mRNA.
DR   EMBL; AK133063; BAE21491.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001276732.1; NM_001289803.1.
DR   RefSeq; NP_001276733.1; NM_001289804.1.
DR   RefSeq; NP_862905.1; NM_181857.4.
DR   AlphaFoldDB; Q7TQ07; -.
DR   SMR; Q7TQ07; -.
DR   BioGRID; 234863; 1.
DR   STRING; 10090.ENSMUSP00000036110; -.
DR   PhosphoSitePlus; Q7TQ07; -.
DR   jPOST; Q7TQ07; -.
DR   PaxDb; Q7TQ07; -.
DR   PRIDE; Q7TQ07; -.
DR   ProteomicsDB; 279808; -. [Q7TQ07-1]
DR   ProteomicsDB; 279809; -. [Q7TQ07-2]
DR   DNASU; 272158; -.
DR   GeneID; 272158; -.
DR   KEGG; mmu:272158; -.
DR   UCSC; uc008xbt.3; mouse. [Q7TQ07-1]
DR   UCSC; uc008xbu.3; mouse. [Q7TQ07-2]
DR   CTD; 353497; -.
DR   MGI; MGI:2675617; Poln.
DR   eggNOG; KOG0950; Eukaryota.
DR   InParanoid; Q7TQ07; -.
DR   OrthoDB; 931773at2759; -.
DR   PhylomeDB; Q7TQ07; -.
DR   TreeFam; TF337202; -.
DR   Reactome; R-MMU-6783310; Fanconi Anemia Pathway.
DR   BioGRID-ORCS; 272158; 2 hits in 105 CRISPR screens.
DR   ChiTaRS; Poln; mouse.
DR   PRO; PR:Q7TQ07; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q7TQ07; protein.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0030332; F:cyclin binding; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; ISO:MGI.
DR   GO; GO:0006261; P:DNA-templated DNA replication; ISO:MGI.
DR   GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:MGI.
DR   GO; GO:0036297; P:interstrand cross-link repair; ISO:MGI.
DR   GO; GO:0019985; P:translesion synthesis; ISO:MGI.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR040940; DNA_pol_P_Exo.
DR   InterPro; IPR002298; DNA_polymerase_A.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10133; PTHR10133; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   Pfam; PF18049; DNA_pol_P_Exo; 1.
DR   PRINTS; PR00868; DNAPOLI.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; DNA damage; DNA repair; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Nucleotidyltransferase; Nucleus;
KW   Reference proteome; Transferase.
FT   CHAIN           1..864
FT                   /note="DNA polymerase nu"
FT                   /id="PRO_0000227939"
FT   REGION          169..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..184
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         689..732
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_017616"
SQ   SEQUENCE   864 AA;  96675 MW;  37F5246FC4EEF3FD CRC64;
     MENYEACVGF DVCEIPLSAV AQKIMSAMRS GDFMDSRNEG ESTNTSKVAK KSSVHYSVLA
     EHEETQSLGT KNPESLITQT PRGSIELCPQ PSITKLTCQL SAGQVQNSIS SLGLSSYLIP
     QCDQEASVLP NMEHKRQHFL KENIGKEDKD NSSLKRKYIT CSKSSEKASK HTALEKDTDG
     TESWPNSRDT RALGERLCDV RYLGDLAKAQ LMDALKQAAA LVVTLMYKDG STQLSAKEAL
     TCTVKGIVVL LKSHVGNSTL TLPAHGGALE KDFISEDHCV YIHTEHSPFW DPKQEAHSLF
     VRNILFWTLR CKCPVVCFNA KDFVRTVLQL YGEDGSWKHV ADFVGLDPRV AAWLIDPSDT
     APSFEDLVAK HLEKSITVKP SSTFREASRN TLSQNVFMNL KILYDLTMDL CSKLKAYGLW
     QLFCTLELPL IPILAVMENH KIPVDKEEME RTSALLGARL KELEQEAHFV AGEQFLIMSN
     NQLREILFGK LKLHLLSQRK HLPRTGLQNQ LSTSEAMLNS LQDLHPLPKL ILEYRQVHKI
     KSTFIDGLLA YMKKGSISST WNQTGTVTGR LSAKHPNIQG ISKHPIKISK PWNFKGKEEE
     TVTISPRTLF VSSEGHTFLA ADFSQIELRI LAHLSGDPEL LKLFQESERD DVFSTLTSQW
     KDIPIERVTH MDREQTKKVV YSVVYGAGKE RLAACLGVTV LEATHFLERF LQKYKKIKDF
     AQTVIGQCHS AGYVTSILGR RRPLPRICAQ DQQLRAQAER QAVNFVVQGS AADLCKLAMI
     RISTAVATSP TLTARLVAQI HDELLFEVED TQVPEFAALV RRIMESLQQV QTLELQLQVP
     LKVNLSVGRS WGHLTPLQEI LGSA