DPOLL_RAT
ID DPOLL_RAT Reviewed; 573 AA.
AC Q5RKI3;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
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};
GN Name=Poll {ECO:0000312|RGD:1308053};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC085841; AAH85841.1; -; mRNA.
DR RefSeq; NP_001014190.1; NM_001014168.1.
DR AlphaFoldDB; Q5RKI3; -.
DR SMR; Q5RKI3; -.
DR STRING; 10116.ENSRNOP00000023137; -.
DR iPTMnet; Q5RKI3; -.
DR PhosphoSitePlus; Q5RKI3; -.
DR PaxDb; Q5RKI3; -.
DR PRIDE; Q5RKI3; -.
DR Ensembl; ENSRNOT00000023137; ENSRNOP00000023137; ENSRNOG00000016748.
DR GeneID; 361767; -.
DR KEGG; rno:361767; -.
DR CTD; 27343; -.
DR RGD; 1308053; Poll.
DR eggNOG; KOG2534; Eukaryota.
DR GeneTree; ENSGT00940000158515; -.
DR HOGENOM; CLU_008698_6_1_1; -.
DR InParanoid; Q5RKI3; -.
DR OMA; KWHGASA; -.
DR OrthoDB; 1328151at2759; -.
DR PhylomeDB; Q5RKI3; -.
DR TreeFam; TF103011; -.
DR Reactome; R-RNO-5693571; Nonhomologous End-Joining (NHEJ).
DR PRO; PR:Q5RKI3; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000016748; Expressed in pancreas and 19 other tissues.
DR Genevisible; Q5RKI3; RN.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; ISS:UniProtKB.
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; ISS:UniProtKB.
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; ISO:RGD.
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_0000218786"
FT DOMAIN 35..131
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 126..235
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 126..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..212
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; 62401 MW; 5978076D6CC463B0 CRC64;
MDPQGILKAF PKRKKIHADP SSNALAKIPK REAGDARGWL SSLRAHIMPT GIGRARAELF
EKQIIQHGGQ VCSAQAPGVT HIVVDEGMDY ERALRLLRLP QLPPGAQLVK SAWLSLCLQE
KKLTDTDGFS LSSPKRSLNE PQPSKSGQDA SAPGTQGVLP RTTLSLSPPC TRAVSPPPKA
EKPPKTQTQL SSEDEASDGE GPQVSSADLQ ALISGHYPTP PGEDGGPDPA PEALGKWVCA
QPSSQKATNY NLHITEKLEV LAKAYNVQGD KWRALGYAKA INALKSFHKP VSSYQEACSI
PGVGRRMAEK VMEILESGHL RKLDHISDSV PVLELFSNIW GAGTKTAQMW YHQGFRSLED
IRGLASLTAQ QAIGLKHYDD FLDRMPREEA AEIEQMVRVS AQAFNPGLLC VACGSFRRGK
VTCGDVDVLI THPDGRSHQG IFSPLLDSLR QQGFLTDDLV SQEENGQQQK YLGVCRLPGA
GQRHRRLDII VVPYSEFACA LLYFTGSAHF NRSMRALAKT KGMSLSEHAL SAAVVRNSQG
VKVGAGQVLP TPTEKDVFKL LGLPYREPAE RDW
