ID   DPOD3_YEAST             Reviewed;         350 AA.
AC   P47110; D6VWL4;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   04-NOV-2026, entry version 190.
DE   RecName: Full=DNA polymerase delta subunit 3;
GN   Name=POL32; OrderedLocusNames=YJR043C; ORFNames=J1626;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7668047; DOI=10.1002/yea.320110809;
RA   Huang M.-E., Chuat J.-C., Galibert F.;
RT   "Analysis of a 42.5 kb DNA sequence of chromosome X reveals three tRNA
RT   genes and 14 new open reading frames including a gene most probably
RT   belonging to the family of ubiquitin-protein ligases.";
RL   Yeast 11:775-781(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=9677405; DOI=10.1074/jbc.273.31.19747;
RA   Gerik K.J., Li X., Pautz A., Burgers P.M.;
RT   "Characterization of the two small subunits of Saccharomyces cerevisiae DNA
RT   polymerase delta.";
RL   J. Biol. Chem. 273:19747-19755(1998).
RN   [6]
RP   COMPOSITION OF THE DNA POLYMERASE DELTA COMPLEX.
RX   PubMed=11568188; DOI=10.1074/jbc.m108842200;
RA   Johansson E., Majka J., Burgers P.M.;
RT   "Structure of DNA polymerase delta from Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 276:43824-43828(2001).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-223 AND SER-230, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: DNA polymerase delta (DNA polymerase III) participates in
CC       chromosomal DNA replication. It is required during synthesis of the
CC       leading and lagging DNA strands at the replication fork and binds at/or
CC       near replication origins and moves along DNA with the replication fork.
CC       It has 3'-5' proofreading exonuclease activity that correct errors
CC       arising during DNA replication. It is also involved in DNA synthesis
CC       during DNA repair.
CC   -!- SUBUNIT: DNA polymerase delta is a heterotrimer of POL3, POL32 and
CC       HYS2. POL32 can form homodimers.
CC   -!- INTERACTION:
CC       P47110; P15873: POL30; NbExp=4; IntAct=EBI-6084, EBI-12993;
CC       P47110; P12689: REV1; NbExp=4; IntAct=EBI-6084, EBI-14951;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- MISCELLANEOUS: Present with 2410 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; L36344; AAA88745.1; -; Genomic_DNA.
DR   EMBL; Z49543; CAA89571.1; -; Genomic_DNA.
DR   EMBL; AY557918; AAS56244.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08830.1; -; Genomic_DNA.
DR   PIR; S57062; S57062.
DR   RefSeq; NP_012577.1; NM_001181701.1.
DR   PDB; 6P1H; EM; 3.20 A; C=1-350.
DR   PDB; 6V8P; EM; 4.10 A; G=1-350.
DR   PDB; 6V93; EM; 3.10 A; G=1-350.
DR   PDB; 7KC0; EM; 3.20 A; C=8-350.
DR   PDB; 7LXD; EM; 4.11 A; G=1-350.
DR   PDB; 7S0T; EM; 3.05 A; G=1-350.
DR   PDB; 8TLQ; EM; 3.53 A; G=1-350.
DR   PDB; 8TLT; EM; 2.85 A; G=1-350.
DR   AlphaFoldDB; P47110; -.
DR   EMDB; EMD-20235; -.
DR   EMDB; EMD-21108; -.
DR   EMDB; EMD-21115; -.
DR   EMDB; EMD-23570; -.
DR   EMDB; EMD-2409; -.
DR   EMDB; EMD-24793; -.
DR   EMDB; EMD-41371; -.
DR   EMDB; EMD-41372; -.
DR   SMR; P47110; -.
DR   BioGRID; 33794; 465.
DR   ComplexPortal; CPX-1091; DNA polymerase zeta complex.
DR   ComplexPortal; CPX-2101; DNA polymerase delta complex.
DR   DIP; DIP-2523N; -.
DR   ELM; P47110; -.
DR   FunCoup; P47110; 160.
DR   IntAct; P47110; 13.
DR   STRING; 4932.YJR043C; -.
DR   iPTMnet; P47110; -.
DR   PaxDb; 4932-YJR043C; -.
DR   PeptideAtlas; P47110; -.
DR   EnsemblFungi; YJR043C_mRNA; YJR043C; YJR043C.
DR   GeneID; 853500; -.
DR   KEGG; sce:YJR043C; -.
DR   AGR; SGD:S000003804; -.
DR   SGD; S000003804; POL32.
DR   VEuPathDB; FungiDB:YJR043C; -.
DR   eggNOG; ENOG502QW2D; Eukaryota.
DR   HOGENOM; CLU_794694_0_0_1; -.
DR   InParanoid; P47110; -.
DR   OMA; AEMYQFY; -.
DR   OrthoDB; 4036325at2759; -.
DR   BioCyc; YEAST:G3O-31678-MONOMER; -.
DR   BioGRID-ORCS; 853500; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P47110; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P47110; protein.
DR   GO; GO:0043625; C:delta DNA polymerase complex; IPI:ComplexPortal.
DR   GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0016035; C:zeta DNA polymerase complex; IDA:SGD.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:SGD.
DR   GO; GO:0000510; F:H3-H4 histone complex chaperone activity; IDA:SGD.
DR   GO; GO:0006284; P:base-excision repair; TAS:SGD.
DR   GO; GO:0006277; P:DNA amplification; IMP:SGD.
DR   GO; GO:0006259; P:DNA metabolic process; IDA:ComplexPortal.
DR   GO; GO:0043137; P:DNA replication, removal of RNA primer; IDA:SGD.
DR   GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
DR   GO; GO:0042276; P:error-prone translesion synthesis; IDA:ComplexPortal.
DR   GO; GO:0006273; P:lagging strand elongation; TAS:SGD.
DR   GO; GO:0006272; P:leading strand elongation; TAS:SGD.
DR   GO; GO:0006289; P:nucleotide-excision repair; TAS:SGD.
DR   GO; GO:0006278; P:RNA-templated DNA biosynthetic process; IDA:SGD.
DR   DisProt; DP02847; -.
PE   1: Evidence at protein level;
KW   3D-structure; DNA replication; DNA-directed DNA polymerase;
KW   Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW   Transferase.
FT   CHAIN           1..350
FT                   /note="DNA polymerase delta subunit 3"
FT                   /id="PRO_0000186050"
FT   REGION          131..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..195
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..248
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..262
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..286
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..332
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         223
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         230
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   TURN            2..4
FT                   /evidence="ECO:0007829|PDB:8TLT"
FT   HELIX           5..10
FT                   /evidence="ECO:0007829|PDB:8TLT"
FT   HELIX           11..15
FT                   /evidence="ECO:0007829|PDB:8TLT"
FT   HELIX           22..29
FT                   /evidence="ECO:0007829|PDB:8TLT"
FT   HELIX           33..44
FT                   /evidence="ECO:0007829|PDB:8TLT"
FT   STRAND          52..60
FT                   /evidence="ECO:0007829|PDB:8TLT"
FT   TURN            61..63
FT                   /evidence="ECO:0007829|PDB:7S0T"
FT   STRAND          64..67
FT                   /evidence="ECO:0007829|PDB:8TLT"
FT   STRAND          70..72
FT                   /evidence="ECO:0007829|PDB:8TLT"
FT   HELIX           77..79
FT                   /evidence="ECO:0007829|PDB:8TLT"
FT   STRAND          80..92
FT                   /evidence="ECO:0007829|PDB:8TLT"
FT   STRAND          108..110
FT                   /evidence="ECO:0007829|PDB:8TLT"
SQ   SEQUENCE   350 AA;  40310 MW;  D0B9CC52F26E20B2 CRC64;
     MDQKASYFIN EKLFTEVKPV LFTDLIHHLK IGPSMAKKLM FDYYKQTTNA KYNCVVICCY
     KDQTIKIIHD LSNIPQQDSI IDCFIYAFNP MDSFIPYYDI IDQKDCLTIK NSYELKVSES
     SKIIERTKTL EEKSKPLVRP TARSKTTPEE TTGRKSKSKD MGLRSTALLA KMKKDRDDKE
     TSRQNELRKR KEENLQKINK QNPEREAQMK ELNNLFVEDD LDTEEVNGGS KPNSPKETDS
     NDKDKNNDDL EDLLETTAED SLMDVPKIQQ TKPSETEHSK EPKSEEEPSS FIDEDGYIVT
     KRPATSTPPR KPSPVVKRAL SSSKKQETPS SNKRLKKQGT LESFFKRKAK
//