DPOLL_MOUSE
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 03-AUG-2022, entry version 163.
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}; 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; Q9QXE2; -.
DR PeptideAtlas; Q9QXE2; -.
DR PRIDE; Q9QXE2; -.
DR ProteomicsDB; 277390; -.
DR Antibodypedia; 31295; 253 antibodies from 33 providers.
DR DNASU; 56626; -.
DR Ensembl; ENSMUST00000026239; ENSMUSP00000026239; ENSMUSG00000025218.
DR GeneID; 56626; -.
DR KEGG; mmu:56626; -.
DR UCSC; uc008hrc.1; mouse.
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; 1328151at2759; -.
DR PhylomeDB; Q9QXE2; -.
DR TreeFam; TF103011; -.
DR Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
DR BioGRID-ORCS; 56626; 9 hits in 106 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 187 other tissues.
DR Genevisible; Q9QXE2; MM.
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; 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; 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; 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 PRINTS; PR00869; DNAPOLX.
DR PRINTS; PR00870; DNAPOLXBETA.
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 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
