POLK_MOUSE
ID POLK_MOUSE Reviewed; 852 AA.
AC Q9QUG2; Q7TPY7;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=DNA polymerase kappa;
DE EC=2.7.7.7 {ECO:0000250|UniProtKB:Q9UBT6};
DE AltName: Full=DINB protein;
DE Short=DINP;
GN Name=Polk; Synonyms=Dinb1;
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; TISSUE=Testis;
RX PubMed=10620008; DOI=10.1046/j.1365-2443.1999.00289.x;
RA Ogi T., Kato T. Jr., Kato R., Ohmori H.;
RT "Mutation enhancement by DINB1, a mammalian homologue of the Escherichia
RT coli mutagenesis protein dinB.";
RL Genes Cells 4:607-618(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=10518552; DOI=10.1073/pnas.96.21.11922;
RA Gerlach V.L., Aravind L., Gotway G., Schultz R.A., Koonin E.V.,
RA Friedberg E.C.;
RT "Human and mouse homologs of Escherichia coli DinB (DNA polymerase IV),
RT members of the UmuC/DinB superfamily.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11922-11927(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=12432099; DOI=10.1073/pnas.222377899;
RA Ogi T., Shinkai Y., Tanaka K., Ohmori H.;
RT "Pol kappa protects mammalian cells against the lethal and mutagenic
RT effects of benzo[a]pyrene.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:15548-15553(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS GLY-544;
RP ALA-550; GLN-606; SER-692; SER-710; ALA-736 AND GLU-747.
RC STRAIN=C3H/He; TISSUE=Osteoblast;
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 [5]
RP INTERACTION WITH REV1.
RX PubMed=14657033; DOI=10.1093/emboj/cdg626;
RA Guo C., Fischhaber P.L., Luk-Paszyc M.J., Masuda Y., Zhou J., Kamiya K.,
RA Kisker C., Friedberg E.C.;
RT "Mouse Rev1 protein interacts with multiple DNA polymerases involved in
RT translesion DNA synthesis.";
RL EMBO J. 22:6621-6630(2003).
CC -!- FUNCTION: DNA polymerase specifically involved in DNA repair. Plays an
CC important role in translesion synthesis, where the normal high-fidelity
CC DNA polymerases cannot proceed and DNA synthesis stalls
CC (PubMed:12432099). Depending on the context, it inserts the correct
CC base, but causes frequent base transitions, transversions and
CC frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a
CC Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not
CC have lyase activity (By similarity). {ECO:0000250|UniProtKB:Q9UBT6,
CC ECO:0000269|PubMed:12432099}.
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:Q9UBT6};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9UBT6};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9UBT6};
CC Note=Divalent metal cations. Prefers Mg(2+), but can also use Mn(2+).
CC {ECO:0000250|UniProtKB:Q9UBT6};
CC -!- SUBUNIT: Interacts with PCNA (By similarity). Interacts with REV1
CC (PubMed:14657033). {ECO:0000250|UniProtKB:Q9UBT6,
CC ECO:0000269|PubMed:14657033}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UBT6}.
CC Note=Detected throughout the nucleus and at replication foci. Recruited
CC to DNA damage sites in response to ultraviolet irradiation: N6-
CC methyladenosine (m6A)-containing mRNAs accumulate in the vicinity of
CC DNA damage sites and their presence is required to recruit POLK.
CC {ECO:0000250|UniProtKB:Q9UBT6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9QUG2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QUG2-2; Sequence=VSP_012807, VSP_012808;
CC -!- TISSUE SPECIFICITY: Detected at low levels in heart, brain, lung,
CC liver, kidney and testis. {ECO:0000269|PubMed:10620008}.
CC -!- DOMAIN: The catalytic core consists of fingers, palm and thumb
CC subdomains, but the fingers and thumb subdomains are much smaller than
CC in high-fidelity polymerases; residues from five sequence motifs of the
CC Y-family cluster around an active site cleft that can accommodate DNA
CC and nucleotide substrates with relaxed geometric constraints, with
CC consequently higher rates of misincorporation and low processivity.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
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DR EMBL; AB027563; BAA86942.1; -; mRNA.
DR EMBL; AF163571; AAF02541.1; -; mRNA.
DR EMBL; AB040765; BAB59059.1; -; Genomic_DNA.
DR EMBL; BC052820; AAH52820.1; -; mRNA.
DR CCDS; CCDS26704.1; -. [Q9QUG2-1]
DR RefSeq; NP_036178.1; NM_012048.3. [Q9QUG2-1]
DR PDB; 2LSJ; NMR; -; B=560-582.
DR PDB; 4FJO; X-ray; 2.72 A; B=565-574.
DR PDB; 6C59; X-ray; 2.03 A; A=564-577.
DR PDB; 6C8C; X-ray; 1.50 A; A/B=564-577.
DR PDBsum; 2LSJ; -.
DR PDBsum; 4FJO; -.
DR PDBsum; 6C59; -.
DR PDBsum; 6C8C; -.
DR AlphaFoldDB; Q9QUG2; -.
DR SMR; Q9QUG2; -.
DR BioGRID; 205098; 7.
DR IntAct; Q9QUG2; 1.
DR STRING; 10090.ENSMUSP00000022172; -.
DR iPTMnet; Q9QUG2; -.
DR PhosphoSitePlus; Q9QUG2; -.
DR EPD; Q9QUG2; -.
DR MaxQB; Q9QUG2; -.
DR PaxDb; Q9QUG2; -.
DR PRIDE; Q9QUG2; -.
DR ProteomicsDB; 289361; -. [Q9QUG2-1]
DR ProteomicsDB; 289362; -. [Q9QUG2-2]
DR Antibodypedia; 12396; 341 antibodies from 31 providers.
DR DNASU; 27015; -.
DR Ensembl; ENSMUST00000022172; ENSMUSP00000022172; ENSMUSG00000021668. [Q9QUG2-1]
DR GeneID; 27015; -.
DR KEGG; mmu:27015; -.
DR UCSC; uc007rne.1; mouse. [Q9QUG2-1]
DR CTD; 51426; -.
DR MGI; MGI:1349767; Polk.
DR VEuPathDB; HostDB:ENSMUSG00000021668; -.
DR eggNOG; KOG2094; Eukaryota.
DR GeneTree; ENSGT00940000156667; -.
DR HOGENOM; CLU_012348_11_3_1; -.
DR InParanoid; Q9QUG2; -.
DR OMA; ETSWHNF; -.
DR PhylomeDB; Q9QUG2; -.
DR TreeFam; TF314387; -.
DR Reactome; R-MMU-5655862; Translesion synthesis by POLK.
DR Reactome; R-MMU-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-MMU-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-MMU-5696400; Dual Incision in GG-NER.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR BioGRID-ORCS; 27015; 4 hits in 109 CRISPR screens.
DR ChiTaRS; Polk; mouse.
DR PRO; PR:Q9QUG2; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9QUG2; protein.
DR Bgee; ENSMUSG00000021668; Expressed in spermatid and 242 other tissues.
DR ExpressionAtlas; Q9QUG2; baseline and differential.
DR Genevisible; Q9QUG2; MM.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090734; C:site of DNA damage; ISO:MGI.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IMP:MGI.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0042276; P:error-prone translesion synthesis; ISS:UniProtKB.
DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; ISO:MGI.
DR CDD; cd03586; PolY_Pol_IV_kappa; 1.
DR DisProt; DP02626; -.
DR Gene3D; 3.30.1490.100; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR HAMAP; MF_01113; DNApol_IV; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR InterPro; IPR022880; DNApol_IV.
DR InterPro; IPR006642; Rad18_UBZ4.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001126; UmuC.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
DR SMART; SM00734; ZnF_Rad18; 2.
DR SUPFAM; SSF100879; SSF100879; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50173; UMUC; 1.
DR PROSITE; PS51908; ZF_UBZ4; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA damage; DNA repair;
KW DNA replication; DNA synthesis; DNA-binding; DNA-directed DNA polymerase;
KW Magnesium; Metal-binding; Mutator protein; Nucleotidyltransferase; Nucleus;
KW Reference proteome; Repeat; Schiff base; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..852
FT /note="DNA polymerase kappa"
FT /id="PRO_0000173991"
FT DOMAIN 102..357
FT /note="UmuC"
FT ZN_FING 619..649
FT /note="UBZ4-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT ZN_FING 761..791
FT /note="UBZ4-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT REGION 252..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..852
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 622
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 625
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 640
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 644
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 764
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 767
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 782
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 786
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT VAR_SEQ 50..185
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012807"
FT VAR_SEQ 827..852
FT /note="GTKTKSSTLKKTKPRDPRHTLDGFFK -> RGATSPSAPPCLATMVPLMLPY
FT LPVCISVSCEQMQLELAMMSMKNISLT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012808"
FT VARIANT 544
FT /note="D -> G (in strain: C3H/He)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 550
FT /note="D -> A (in strain: C3H/He)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 606
FT /note="E -> Q (in strain: C3H/He)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 692
FT /note="L -> S (in strain: C3H/He)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 710
FT /note="R -> S (in strain: C3H/He)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 736
FT /note="E -> A (in strain: C3H/He)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 747
FT /note="D -> E (in strain: C3H/He)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT HELIX 566..573
FT /evidence="ECO:0007829|PDB:6C8C"
SQ SEQUENCE 852 AA; 96003 MW; FD8F33A6E78992F4 CRC64;
MDNTKEKDNF KDDLLLRMGL NDNKAGMEGL DKEKINKIIM EATKGSRFYG NELKKEKQVN
QRIENMMQQK AQITSQQLRK AQLQVDKFAM ELERNRNLNN TIVHVDMDAF YAAVEMRDNP
ELKDKPIAVG SMSMLATSNY HARRFGVRAA MPGFIAKRLC PQLIIVPPNF DKYRAVSKEV
KEILAEYDPN FMAMSLDEAY LNITQHLQER QDWPEDKRRY FIKMGNYLKI DTPRQEANEL
TEYERSISPL LFEDSPPDLQ PQGSPFQLNS EEQNNPQIAQ NSVVFGTSAE EVVKEIRFRI
EQKTTLTASA GIAPNTMLAK VCSDKNKPNG QYQILPSRSA VMDFIKDLPI RKVSGIGKVT
EKMLMALGIV TCTELYQQRA LLSLLFSETS WHYFLHIALG LGSTDLARDG ERKSMSVERT
FSEISKTEEQ YSLCQELCAE LAHDLQKEGL KGRTVTIKLK NVNFEVKTRA STVPAAISTA
EEIFAIAKEL LRTEVNVGSP HPLRLRLMGV RMSTFSSEDD RKHQQRSIIG FLQAGNQALS
STGDSLDKTD KTELAKPLEM SHKKSFFDKK RSERISNCQD TSRCKTAGQQ ALQILEPSQA
LKKLSESFET SENSNDCQTF ICPVCFREQE GVSLEAFNEH VDECLDGPST SENSKISCYS
HASSADIGQK EDVHPSIPLC EKRGHENGEI TLVDGVDLTG TEDRSLKAAR MDTLENNRSK
EECPDIPDKS CPISLENETI STLSRQDSVQ PCTDEVVTGR ALVCPVCNLE QETSDLTLFN
IHVDICLNKG IIQELRNSEG NSVKQPKESS RSTDRLQKAS GRTKRPGTKT KSSTLKKTKP
RDPRHTLDGF FK
