ID   DPOLL_MOUSE             Reviewed;         573 AA.
AC   Q9QXE2; Q9CTJ1;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 171.
DE   RecName: Full=DNA polymerase lambda {ECO:0000305};
DE            Short=Pol Lambda {ECO:0000305};
DE            EC=2.7.7.7 {ECO:0000250|UniProtKB:Q9UGP5};
DE            EC=4.2.99.- {ECO:0000250|UniProtKB:Q9UGP5};
DE   AltName: Full=DNA polymerase kappa {ECO:0000303|Ref.1};
GN   Name=Poll {ECO:0000312|MGI:MGI:1889000};
GN   Synonyms=Polk {ECO:0000303|Ref.1};
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].
RC   TISSUE=Testis;
RA   Garcia M., Dominguez O., Saniger M.L., Garcia M.J., Martinez C., Bernad A.,
RA   Blanco L.;
RT   "DNA polymerase kappa, a new mammalian meiotic polymerase.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Spleen;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 262-573.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
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 that functions in several pathways of DNA
CC       repair. Involved in base excision repair (BER) responsible for repair
CC       of lesions that give rise to abasic (AP) sites in DNA. Also contributes
CC       to DNA double-strand break repair by non-homologous end joining and
CC       homologous recombination. Has both template-dependent and template-
CC       independent (terminal transferase) DNA polymerase activities. Has also
CC       a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
CC       {ECO:0000250|UniProtKB:Q9UGP5}.
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:0000250|UniProtKB:Q9UGP5};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q9UGP5};
CC   -!- SUBUNIT: Interacts with PCNA. Interacts with PAXX; promoting POLL
CC       recruitment to double-strand breaks (DSBs) and stimulation of the end-
CC       filling activity of POLL. Interacts with XRCC4; promoting POLL
CC       recruitment to double-strand breaks (DSBs) and stimulation of the end-
CC       filling activity of POLL. Interacts with NHEJ1/XLF; promoting POLL
CC       recruitment to double-strand breaks (DSBs) and stimulation of the end-
CC       filling activity of POLL. {ECO:0000250|UniProtKB:Q9UGP5}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UGP5}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-X family. {ECO:0000305}.
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DR   EMBL; AJ131889; CAB65241.1; -; mRNA.
DR   EMBL; AF176099; AAF27553.1; -; mRNA.
DR   EMBL; BC004767; AAH04767.1; -; mRNA.
DR   EMBL; AK003392; BAB22759.1; -; mRNA.
DR   CCDS; CCDS29861.1; -.
DR   RefSeq; NP_001317435.1; NM_001330506.1.
DR   RefSeq; NP_001317436.1; NM_001330507.1.
DR   RefSeq; NP_064416.1; NM_020032.3.
DR   RefSeq; XP_011245603.1; XM_011247301.2.
DR   AlphaFoldDB; Q9QXE2; -.
DR   SMR; Q9QXE2; -.
DR   BioGRID; 208108; 1.
DR   STRING; 10090.ENSMUSP00000026239; -.
DR   BindingDB; Q9QXE2; -.
DR   ChEMBL; CHEMBL3124737; -.
DR   iPTMnet; Q9QXE2; -.
DR   PhosphoSitePlus; Q9QXE2; -.
DR   EPD; Q9QXE2; -.
DR   MaxQB; Q9QXE2; -.
DR   PaxDb; 10090-ENSMUSP00000026239; -.
DR   PeptideAtlas; Q9QXE2; -.
DR   ProteomicsDB; 277390; -.
DR   Antibodypedia; 31295; 291 antibodies from 33 providers.
DR   DNASU; 56626; -.
DR   Ensembl; ENSMUST00000026239.7; ENSMUSP00000026239.7; ENSMUSG00000025218.7.
DR   GeneID; 56626; -.
DR   KEGG; mmu:56626; -.
DR   UCSC; uc008hrc.1; mouse.
DR   AGR; MGI:1889000; -.
DR   CTD; 27343; -.
DR   MGI; MGI:1889000; Poll.
DR   VEuPathDB; HostDB:ENSMUSG00000025218; -.
DR   eggNOG; KOG2534; Eukaryota.
DR   GeneTree; ENSGT00940000158515; -.
DR   HOGENOM; CLU_008698_6_1_1; -.
DR   InParanoid; Q9QXE2; -.
DR   OMA; KWHGASA; -.
DR   OrthoDB; 49764at2759; -.
DR   PhylomeDB; Q9QXE2; -.
DR   TreeFam; TF103011; -.
DR   Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
DR   BioGRID-ORCS; 56626; 9 hits in 111 CRISPR screens.
DR   ChiTaRS; Polk; mouse.
DR   PRO; PR:Q9QXE2; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q9QXE2; Protein.
DR   Bgee; ENSMUSG00000025218; Expressed in spermatocyte and 190 other cell types or tissues.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR   GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006287; P:base-excision repair, gap-filling; ISS:UniProtKB.
DR   GO; GO:0071897; P:DNA biosynthetic process; ISO:MGI.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR   GO; GO:0006289; P:nucleotide-excision repair; ISS:UniProtKB.
DR   CDD; cd17715; BRCT_polymerase_lambda; 1.
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; 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; IPR002008; DNA_pol_X_beta-like.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR029398; PolB_thumb.
DR   PANTHER; PTHR11276:SF44; DNA POLYMERASE LAMBDA; 1.
DR   PANTHER; PTHR11276; DNA POLYMERASE TYPE-X FAMILY MEMBER; 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   PRINTS; PR00869; DNAPOLX.
DR   PRINTS; PR00870; DNAPOLXBETA.
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; Q9QXE2; MM.
PE   2: Evidence at transcript level;
KW   DNA damage; DNA repair; DNA replication; DNA synthesis; DNA-binding;
KW   DNA-directed DNA polymerase; Lyase; Manganese; Metal-binding;
KW   Nucleotidyltransferase; Nucleus; Reference proteome; Transferase.
FT   CHAIN           1..573
FT                   /note="DNA polymerase lambda"
FT                   /id="PRO_0000218785"
FT   DOMAIN          35..131
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   REGION          126..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          214..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          263..277
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT   REGION          343..346
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT   REGION          418..427
FT                   /note="Involved in primer binding"
FT                   /evidence="ECO:0000250"
FT   REGION          464..503
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT   COMPBIAS        141..170
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        310
FT                   /note="Schiff-base intermediate with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT   BINDING         384
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT   BINDING         415..418
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT   BINDING         424..427
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT   BINDING         425
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT   BINDING         427
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT   BINDING         488
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT   BINDING         511
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGP5"
SQ   SEQUENCE   573 AA;  62943 MW;  5B2EA4D1597E06A2 CRC64;
     MDPQGIVKAF PKRKKSHADL SSKALAKIPK REVGEARGWL SSLRAHIMPA GIGRARAELF
     EKQIIHHGGQ VCSAQAPGVT HIVVDEDMDY ERALRLLRLP QLPPGAQLVK STWLSLCLQE
     GRLTDTEGFS LPMPKRSLDE PQPSKSGQDA SAPGTQRDLP RTTLSLSPPH TRAVSPPPTA
     EKPSRTQAQL SSEDETSDGE GPQVSSADLQ ALITGHYPTP PEEDGGPDPA PEALDKWVCA
     QPSSQKATNY NLHITEKLEV LAKAYSVQGD KWRALGYAKA INALKSFHKP VSSYQEACSI
     PGIGKRMAEK VMEILESGHL RKLDHISDSV PVLELFSNIW GAGTKTAQMW YHQGFRNLED
     LQSLGSLTAQ QAIGLKHYDD FLDRMPREEA AEIEQTVRIS AQAFNPGLLC VACGSYRRGK
     MTCGDVDVLI THPDGRSHRG IFSCLLDSLR QQGFLTDDLV SQEENGQQQK YLGVCRLPGP
     GKRHRRLDII VVPYCEFACA LLYFTGSAHF NRSMRALAKT KGMSLSEHAL SAAVVRNSQG
     VKVGPGQVLP TPTEKDVFKH LGLPYREPAE RDW
//