DPOLB_BOVIN
ID DPOLB_BOVIN Reviewed; 335 AA.
AC Q27958; Q3ZBL6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=DNA polymerase beta;
DE EC=2.7.7.7;
DE EC=4.2.99.-;
GN Name=POLB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
RC TISSUE=Testis;
RX PubMed=7590351; DOI=10.1016/0378-1119(95)00498-u;
RA Chen K.H., Wood T., He F., Narayan S., Wilson S.H.;
RT "The bovine DNA polymerase beta promoter: cloning, characterization and
RT comparison with the human core promoter.";
RL Gene 164:323-327(1995).
CC -!- FUNCTION: Repair polymerase that plays a key role in base-excision
CC repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that
CC removes the 5' sugar phosphate and also acts as a DNA polymerase that
CC adds one nucleotide to the 3' end of the arising single-nucleotide gap.
CC Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion
CC rather than in a processive fashion as for other DNA polymerases (By
CC similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. Interacts with APEX1, HUWE1/ARF-BP1, STUB1/CHIP and
CC USP47 (By similarity). Interacts with FAM168A (By similarity).
CC {ECO:0000250|UniProtKB:P06746}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Cytoplasmic in normal conditions. Translocates to the nucleus
CC following DNA damage (By similarity). {ECO:0000250}.
CC -!- PTM: Methylation by PRMT6 stimulates the polymerase activity by
CC enhancing DNA binding and processivity. {ECO:0000250}.
CC -!- PTM: Ubiquitinated at Lys-41, Lys-61 and Lys-81: monoubiquitinated by
CC HUWE1/ARF-BP1. Monoubiquitinated protein is then the target of
CC STUB1/CHIP, which catalyzes polyubiquitination from monoubiquitin,
CC leading to degradation by the proteasome. USP47 mediates the
CC deubiquitination of monoubiquitinated protein, preventing
CC polyubiquitination by STUB1/CHIP and its subsequent degradation (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family. {ECO:0000305}.
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DR EMBL; BC103229; AAI03230.1; -; mRNA.
DR EMBL; S80341; AAD14333.1; -; Genomic_DNA.
DR RefSeq; NP_001029936.1; NM_001034764.1.
DR AlphaFoldDB; Q27958; -.
DR BMRB; Q27958; -.
DR SMR; Q27958; -.
DR STRING; 9913.ENSBTAP00000000276; -.
DR PaxDb; Q27958; -.
DR PRIDE; Q27958; -.
DR Ensembl; ENSBTAT00000000276; ENSBTAP00000000276; ENSBTAG00000000225.
DR GeneID; 614688; -.
DR KEGG; bta:614688; -.
DR CTD; 5423; -.
DR VEuPathDB; HostDB:ENSBTAG00000000225; -.
DR VGNC; VGNC:33112; POLB.
DR eggNOG; KOG2534; Eukaryota.
DR GeneTree; ENSGT00940000156918; -.
DR HOGENOM; CLU_008698_1_0_1; -.
DR InParanoid; Q27958; -.
DR OMA; ITDMLME; -.
DR OrthoDB; 1328151at2759; -.
DR TreeFam; TF103002; -.
DR Proteomes; UP000009136; Chromosome 27.
DR Bgee; ENSBTAG00000000225; Expressed in spermatid and 109 other tissues.
DR ExpressionAtlas; Q27958; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:AgBase.
DR GO; GO:0016829; F:lyase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006284; P:base-excision repair; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006261; P:DNA-templated DNA replication; IDA:AgBase.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
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 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; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
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; SM00278; HhH1; 2.
DR SMART; SM00483; POLXc; 1.
DR SUPFAM; SSF47802; SSF47802; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS00522; DNA_POLYMERASE_X; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; DNA damage; DNA repair; DNA replication;
KW DNA synthesis; DNA-binding; DNA-directed DNA polymerase; Isopeptide bond;
KW Lyase; Magnesium; Metal-binding; Methylation; Nucleotidyltransferase;
KW Nucleus; Reference proteome; Sodium; Transferase; Ubl conjugation.
FT CHAIN 1..335
FT /note="DNA polymerase beta"
FT /id="PRO_0000218777"
FT REGION 183..192
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 72
FT /note="Schiff-base intermediate with DNA"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 72
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8K409"
FT MOD_RES 83
FT /note="Omega-N-methylarginine; by PRMT6"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT MOD_RES 152
FT /note="Omega-N-methylarginine; by PRMT6"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT CROSSLNK 41
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT CROSSLNK 61
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT CROSSLNK 81
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P06746"
FT CONFLICT 31
FT /note="Q -> H (in Ref. 2; AAD14333)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 38267 MW; 01FC5ED63251DB82 CRC64;
MSKRKAPQET LNGGITDMLT ELANFEKNVN QAIHKYNAYR KAASVIAKYP HKIKSGAEAK
KLPGVGTKIA EKIDEFLATG KLRKLEKIRQ DDTSSSINFL TRVSGIGPSA ARKFVDEGIK
TLEDLRKNED KLNHHQRIGL KYFEDFEKRI PREEMLQMQD IVLSEVKKVD SEYIATVCGS
FRRGAESSGD MDVLLTHPSF TSESAKQPKL LHRVVEQLQK VRFITDTLSK GETKFMGVCQ
LPSKNDEKEY PHRRIDIRLI PKDQYYCGVL YFTGSDIFNK NMRAHALEKG FTINEYTIRP
LGVTGVAGEP LPVDSEKDIF DYIQWKYREP KDRSE
