DPOD3_HUMAN
ID DPOD3_HUMAN Reviewed; 466 AA.
AC Q15054; B7ZAI6; Q32MZ9; Q32N00;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=DNA polymerase delta subunit 3;
DE AltName: Full=DNA polymerase delta subunit C {ECO:0000303|PubMed:11595739};
DE AltName: Full=DNA polymerase delta subunit p66;
DE AltName: Full=DNA polymerase delta subunit p68 {ECO:0000303|PubMed:22148433, ECO:0000303|PubMed:22801543};
GN Name=POLD3; Synonyms=KIAA0039;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S.,
RA Nagase T., Seki N., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. I. The
RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of
RT randomly sampled cDNA clones from human immature myeloid cell line KG-1.";
RL DNA Res. 1:27-35(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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 [6]
RP PROTEIN SEQUENCE OF 2-19 AND 110-123, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP FUNCTION.
RX PubMed=10219083; DOI=10.1093/nar/27.10.2108;
RA Hughes P., Tratner I., Ducoux M., Piard K., Baldacci G.;
RT "Isolation and identification of the third subunit of mammalian DNA
RT polymerase delta by PCNA-affinity chromatography of mouse FM3A cell
RT extracts.";
RL Nucleic Acids Res. 27:2108-2114(1999).
RN [8]
RP FUNCTION.
RX PubMed=10852724; DOI=10.1021/bi0000871;
RA Mo J.-Y., Liu L., Leon A., Mazloum N., Lee M.Y.W.T.;
RT "Evidence that DNA polymerase delta isolated by immunoaffinity
RT chromatography exhibits high-molecular weight characteristics and is
RT associated with the KIAA0039 protein and RPA.";
RL Biochemistry 39:7245-7254(2000).
RN [9]
RP IDENTIFICATION IN POL-DELTA COMPLEX, AND INTERACTION WITH POLD2 AND PCNA.
RX PubMed=11328591; DOI=10.1093/oxfordjournals.jbchem.a002909;
RA Shikata K., Ohta S., Yamada K., Obuse C., Yoshikawa H., Tsurimoto T.;
RT "The human homologue of fission Yeast cdc27, p66, is a component of active
RT human DNA polymerase delta.";
RL J. Biochem. 129:699-708(2001).
RN [10]
RP FUNCTION, INTERACTION WITH PCNA AND POLD1, SUBCELLULAR LOCATION, DOMAIN,
RP AND PHOSPHORYLATION.
RX PubMed=11595739; DOI=10.1074/jbc.m106990200;
RA Ducoux M., Urbach S., Baldacci G., Huebscher U., Koundrioukoff S.,
RA Christensen J., Hughes P.;
RT "Mediation of proliferating cell nuclear antigen (PCNA)-dependent DNA
RT replication through a conserved p21(Cip1)-like PCNA-binding motif present
RT in the third subunit of human DNA polymerase delta.";
RL J. Biol. Chem. 276:49258-49266(2001).
RN [11]
RP INTERACTION WITH PCNA, AND CHARACTERIZATION OF POL-DELTA2 AND POL-DELTA4
RP COMPLEXES.
RX PubMed=12403614; DOI=10.1021/bi0262707;
RA Xie B., Mazloum N., Liu L., Rahmeh A., Li H., Lee M.Y.;
RT "Reconstitution and characterization of the human DNA polymerase delta
RT four-subunit holoenzyme.";
RL Biochemistry 41:13133-13142(2002).
RN [12]
RP INTERACTION WITH POLDIP2.
RX PubMed=12522211; DOI=10.1074/jbc.m208694200;
RA Liu L., Rodriguez-Belmonte E.M., Mazloum N., Xie B., Lee M.Y.W.T.;
RT "Identification of a novel protein, PDIP38, that interacts with the p50
RT subunit of DNA polymerase delta and proliferating cell nuclear antigen.";
RL J. Biol. Chem. 278:10041-10047(2003).
RN [13]
RP UBIQUITINATION, SUMOYLATION AT LYS-258 AND LYS-433, AND MUTAGENESIS OF
RP LYS-258; LYS-325 AND LYS-433.
RX PubMed=16934752; DOI=10.1016/j.bbrc.2006.08.049;
RA Liu G., Warbrick E.;
RT "The p66 and p12 subunits of DNA polymerase delta are modified by ubiquitin
RT and ubiquitin-like proteins.";
RL Biochem. Biophys. Res. Commun. 349:360-366(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [15]
RP FUNCTION, AND INTERACTION WITH POLD2 AND PCNA.
RX PubMed=16510448; DOI=10.1074/jbc.m600322200;
RA Li H., Xie B., Zhou Y., Rahmeh A., Trusa S., Zhang S., Gao Y., Lee E.Y.,
RA Lee M.Y.;
RT "Functional roles of p12, the fourth subunit of human DNA polymerase
RT delta.";
RL J. Biol. Chem. 281:14748-14755(2006).
RN [16]
RP IDENTIFICATION IN POL-DELTA COMPLEX.
RX PubMed=17317665; DOI=10.1074/jbc.m610356200;
RA Zhang S., Zhou Y., Trusa S., Meng X., Lee E.Y., Lee M.Y.;
RT "A novel DNA damage response: rapid degradation of the p12 subunit of dna
RT polymerase delta.";
RL J. Biol. Chem. 282:15330-15340(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; SER-407; SER-409;
RP THR-411; SER-413 AND SER-458, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [21]
RP FUNCTION, AND COMPARISON BETWEEN POL-DELTA3 AND POL-DELTA4.
RX PubMed=19074196; DOI=10.1093/nar/gkn1000;
RA Meng X., Zhou Y., Zhang S., Lee E.Y., Frick D.N., Lee M.Y.;
RT "DNA damage alters DNA polymerase delta to a form that exhibits increased
RT discrimination against modified template bases and mismatched primers.";
RL Nucleic Acids Res. 37:647-657(2009).
RN [22]
RP FUNCTION, AND IDENTIFICATION IN POL-DELTA COMPLEX.
RX PubMed=20334433; DOI=10.1021/bi100042b;
RA Meng X., Zhou Y., Lee E.Y., Lee M.Y., Frick D.N.;
RT "The p12 subunit of human polymerase delta modulates the rate and fidelity
RT of DNA synthesis.";
RL Biochemistry 49:3545-3554(2010).
RN [23]
RP FUNCTION IN NUCLEOTIDE EXCISION REPAIR, AND SUBCELLULAR LOCATION.
RX PubMed=20227374; DOI=10.1016/j.molcel.2010.02.009;
RA Ogi T., Limsirichaikul S., Overmeer R.M., Volker M., Takenaka K.,
RA Cloney R., Nakazawa Y., Niimi A., Miki Y., Jaspers N.G., Mullenders L.H.,
RA Yamashita S., Fousteri M.I., Lehmann A.R.;
RT "Three DNA polymerases, recruited by different mechanisms, carry out NER
RT repair synthesis in human cells.";
RL Mol. Cell 37:714-727(2010).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [27]
RP INTERACTION WITH PCNA, DOMAIN, PHOSPHORYLATION AT SER-458, AND MUTAGENESIS
RP OF 456-GLN--LYS-466; SER-458 AND 459-ILE--PHE-463.
RX PubMed=22148433; DOI=10.1021/bi201638e;
RA Rahmeh A.A., Zhou Y., Xie B., Li H., Lee E.Y., Lee M.Y.;
RT "Phosphorylation of the p68 subunit of Pol delta acts as a molecular switch
RT to regulate its interaction with PCNA.";
RL Biochemistry 51:416-424(2012).
RN [28]
RP SUBCELLULAR LOCATION, IDENTIFICATION IN POL-DELTA COMPLEX, IDENTIFICATION
RP IN POL-ZETA COMPLEX, AND DEVELOPMENTAL STAGE.
RX PubMed=22801543; DOI=10.4161/cc.21280;
RA Chea J., Zhang S., Zhao H., Zhang Z., Lee E.Y., Darzynkiewicz Z., Lee M.Y.;
RT "Spatiotemporal recruitment of human DNA polymerase delta to sites of UV
RT damage.";
RL Cell Cycle 11:2885-2895(2012).
RN [29]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [30]
RP FUNCTION IN OKAZAKI FRAGMENT PROCESSING.
RX PubMed=24035200; DOI=10.1016/j.dnarep.2013.08.008;
RA Lin S.H., Wang X., Zhang S., Zhang Z., Lee E.Y., Lee M.Y.;
RT "Dynamics of enzymatic interactions during short flap human Okazaki
RT fragment processing by two forms of human DNA polymerase delta.";
RL DNA Repair 12:922-935(2013).
RN [31]
RP POL-DELTA3 COMPLEX EXPRESSION DURING CELL CYCLE.
RX PubMed=23913683; DOI=10.1074/jbc.m113.490466;
RA Zhang S., Zhao H., Darzynkiewicz Z., Zhou P., Zhang Z., Lee E.Y., Lee M.Y.;
RT "A novel function of CRL4(Cdt2): regulation of the subunit structure of DNA
RT polymerase delta in response to DNA damage and during the S phase.";
RL J. Biol. Chem. 288:29550-29561(2013).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-277; SER-307 AND SER-458, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [33]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-258, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [34]
RP FUNCTION IN TLS, AND IDENTIFICATION IN COMPLEX WITH REV3L; MAD2L2 AND
RP POLD2.
RX PubMed=24449906; DOI=10.1073/pnas.1324001111;
RA Lee Y.S., Gregory M.T., Yang W.;
RT "Human Pol zeta purified with accessory subunits is active in translesion
RT DNA synthesis and complements Pol eta in cisplatin bypass.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:2954-2959(2014).
RN [35]
RP FUNCTION IN BIR.
RX PubMed=24310611; DOI=10.1126/science.1243211;
RA Costantino L., Sotiriou S.K., Rantala J.K., Magin S., Mladenov E.,
RA Helleday T., Haber J.E., Iliakis G., Kallioniemi O.P., Halazonetis T.D.;
RT "Break-induced replication repair of damaged forks induces genomic
RT duplications in human cells.";
RL Science 343:88-91(2014).
RN [36]
RP FUNCTION IN TLS.
RX PubMed=25628356; DOI=10.1093/nar/gkv023;
RA Hirota K., Yoshikiyo K., Guilbaud G., Tsurimoto T., Murai J., Tsuda M.,
RA Phillips L.G., Narita T., Nishihara K., Kobayashi K., Yamada K.,
RA Nakamura J., Pommier Y., Lehmann A., Sale J.E., Takeda S.;
RT "The POLD3 subunit of DNA polymerase delta can promote translesion
RT synthesis independently of DNA polymerase zeta.";
RL Nucleic Acids Res. 43:1671-1683(2015).
RN [37]
RP FUNCTION IN TLS.
RX PubMed=27185888; DOI=10.1093/nar/gkw439;
RA Hirota K., Tsuda M., Mohiuddin M., Tsurimoto T., Cohen I.S., Livneh Z.,
RA Kobayashi K., Narita T., Nishihara K., Murai J., Iwai S., Guilbaud G.,
RA Sale J.E., Takeda S.;
RT "In vivo evidence for translesion synthesis by the replicative DNA
RT polymerase delta.";
RL Nucleic Acids Res. 44:7242-7250(2016).
RN [38]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-258; LYS-261 AND LYS-433, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-144 IN COMPLEX WITH POLD2, AND
RP INTERACTION WITH POLD2.
RX PubMed=18818516; DOI=10.4161/cc.7.19.6720;
RA Baranovskiy A.G., Babayeva N.D., Liston V.G., Rogozin I.B., Koonin E.V.,
RA Pavlov Y.I., Vassylyev D.G., Tahirov T.H.;
RT "X-ray structure of the complex of regulatory subunits of human DNA
RT polymerase delta.";
RL Cell Cycle 7:3026-3036(2008).
RN [40]
RP VARIANTS VAL-194 AND LEU-195.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
CC -!- FUNCTION: Accessory component of both the DNA polymerase delta complex
CC and the DNA polymerase zeta complex (PubMed:22801543, PubMed:17317665,
CC PubMed:24449906). As a component of the trimeric and tetrameric DNA
CC polymerase delta complexes (Pol-delta3 and Pol-delta4, respectively),
CC plays a role in high fidelity genome replication, including in lagging
CC strand synthesis, and repair. Required for optimal Pol-delta activity.
CC Stabilizes the Pol-delta complex and plays a major role in Pol-delta
CC stimulation by PCNA (PubMed:10219083, PubMed:10852724, PubMed:11595739,
CC PubMed:16510448, PubMed:24035200). Pol-delta3 and Pol-delta4 are
CC characterized by the absence or the presence of POLD4. They exhibit
CC differences in catalytic activity. Most notably, Pol-delta3 shows
CC higher proofreading activity than Pol-delta4 (PubMed:19074196,
CC PubMed:20334433). Although both Pol-delta3 and Pol-delta4 process
CC Okazaki fragments in vitro, Pol-delta3 may also be better suited to
CC fulfill this task, exhibiting near-absence of strand displacement
CC activity compared to Pol-delta4 and stalling on encounter with the 5'-
CC blocking oligonucleotides. Pol-delta3 idling process may avoid the
CC formation of a gap, while maintaining a nick that can be readily
CC ligated (PubMed:24035200). Along with DNA polymerase kappa, DNA
CC polymerase delta carries out approximately half of nucleotide excision
CC repair (NER) synthesis following UV irradiation. In this context,
CC POLD3, along with PCNA and RFC1-replication factor C complex, is
CC required to recruit POLD1, the catalytic subunit of the polymerase
CC delta complex, to DNA damage sites (PubMed:20227374). Under conditions
CC of DNA replication stress, required for the repair of broken
CC replication forks through break-induced replication (BIR)
CC (PubMed:24310611). Involved in the translesion synthesis (TLS) of
CC templates carrying O6-methylguanine or abasic sites performed by Pol-
CC delta4, independently of DNA polymerase zeta (REV3L) or eta (POLH).
CC Facilitates abasic site bypass by DNA polymerase delta by promoting
CC extension from the nucleotide inserted opposite the lesion
CC (PubMed:19074196, PubMed:25628356, PubMed:27185888). Also involved in
CC TLS, as a component of the tetrametric DNA polymerase zeta complex.
CC Along with POLD2, dramatically increases the efficiency and
CC processivity of DNA synthesis of the DNA polymerase zeta complex
CC compared to the minimal zeta complex, consisting of only REV3L and REV7
CC (PubMed:24449906). {ECO:0000269|PubMed:10219083,
CC ECO:0000269|PubMed:10852724, ECO:0000269|PubMed:11595739,
CC ECO:0000269|PubMed:16510448, ECO:0000269|PubMed:19074196,
CC ECO:0000269|PubMed:20227374, ECO:0000269|PubMed:20334433,
CC ECO:0000269|PubMed:24035200, ECO:0000269|PubMed:24310611,
CC ECO:0000269|PubMed:24449906, ECO:0000269|PubMed:25628356,
CC ECO:0000269|PubMed:27185888}.
CC -!- SUBUNIT: Component of both the DNA polymerase delta and DNA polymerase
CC zeta complexes (PubMed:22801543, PubMed:17317665, PubMed:24449906). The
CC tetrameric DNA polymerase delta complex (Pol-delta4), which consists of
CC POLD1/p125, POLD2/p50, POLD3/p66/p68 and POLD4/p12, with POLD1 bearing
CC DNA polymerase and 3' to 5' proofreading exonuclease activities
CC (PubMed:11328591, PubMed:11595739, PubMed:17317665, PubMed:22801543).
CC Within this complex, directly interacts with POLD2 (PubMed:11328591,
CC PubMed:16510448, PubMed:18818516). Following stress caused by DNA
CC damaging agents or by replication stress, POLD4 is degraded and Pol-
CC delta4 is converted into a trimeric form of the complex (Pol-delta3),
CC which consists of POLD1, POLD2 and POLD3. Pol-delta3 is the major form
CC occurring at S phase replication sites, as well as DNA damage sites
CC (PubMed:11595739, PubMed:17317665, PubMed:22801543, PubMed:23913683).
CC Directly interacts with PCNA, as do POLD1 and POLD4; this interaction
CC stimulates Pol-delta polymerase activity (PubMed:11328591,
CC PubMed:11595739, PubMed:12403614, PubMed:16510448, PubMed:22148433).
CC POLD3 phosphorylation at Ser-458 impairs PCNA binding
CC (PubMed:22148433). Component of the DNA polymerase zeta complex (POLZ),
CC which consists of REV3L, MAD2L2, POLD2 and POLD3, with REV3L bearing
CC DNA polymerase catalytic activity (PubMed:24449906). The DNA polymerase
CC delta complex interacts with POLDIP2; this interaction is probably
CC mediated through direct binding to POLD2 (PubMed:12522211).
CC {ECO:0000269|PubMed:11328591, ECO:0000269|PubMed:11595739,
CC ECO:0000269|PubMed:12403614, ECO:0000269|PubMed:12522211,
CC ECO:0000269|PubMed:16510448, ECO:0000269|PubMed:17317665,
CC ECO:0000269|PubMed:18818516, ECO:0000269|PubMed:22148433,
CC ECO:0000269|PubMed:22801543, ECO:0000269|PubMed:23913683,
CC ECO:0000269|PubMed:24449906}.
CC -!- INTERACTION:
CC Q15054; P12004: PCNA; NbExp=7; IntAct=EBI-864956, EBI-358311;
CC Q15054; P49005: POLD2; NbExp=8; IntAct=EBI-864956, EBI-372354;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9EQ28}. Nucleus
CC {ECO:0000269|PubMed:11595739, ECO:0000269|PubMed:20227374,
CC ECO:0000269|PubMed:22801543}. Note=Partially colocalizes with PCNA and
CC POLD1 at S phase replication sites (PubMed:11595739). Recruited to DNA
CC damage sites within 2 hours following UV irradiation (PubMed:20227374,
CC PubMed:22801543). {ECO:0000269|PubMed:11595739,
CC ECO:0000269|PubMed:20227374, ECO:0000269|PubMed:22801543}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q15054-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15054-2; Sequence=VSP_054150;
CC Name=3;
CC IsoId=Q15054-3; Sequence=VSP_054149;
CC -!- DEVELOPMENTAL STAGE: Expression is cell cycle-dependent, with highest
CC levels in G2/M phase and lowest in G1. {ECO:0000269|PubMed:22801543}.
CC -!- DOMAIN: The PIP-box mediates the interaction with PCNA.
CC {ECO:0000269|PubMed:11595739, ECO:0000269|PubMed:22148433}.
CC -!- PTM: Ubiquitinated, but not targeted to the proteasome
CC (PubMed:16934752). Sumoylated (PubMed:16934752, PubMed:25218447).
CC Sumoylation with SUMO3 may be predominant (PubMed:16934752).
CC {ECO:0000269|PubMed:16934752}.
CC -!- PTM: Phosphorylation at Ser-458 is catalyzed in vitro by PKA. It is
CC thought to decrease the affinity for PCNA and Pol-delta4 processivity
CC (PubMed:22148433). Can also be phosphorylated in vitro by CDK1-cyclin-A
CC complex, as well as CDK2-cyclin-A and CDK2-cyclin-E complexes. PCNA
CC interferes with CDK-cyclin phosphorylation (PubMed:11595739).
CC {ECO:0000269|PubMed:11595739, ECO:0000269|PubMed:22148433}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA05039.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
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DR EMBL; D26018; BAA05039.1; ALT_INIT; mRNA.
DR EMBL; AK316301; BAH14672.1; -; mRNA.
DR EMBL; AP001104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW74942.1; -; Genomic_DNA.
DR EMBL; BC108908; AAI08909.1; -; mRNA.
DR EMBL; BC108909; AAI08910.1; -; mRNA.
DR CCDS; CCDS8233.1; -. [Q15054-1]
DR CCDS; CCDS86228.1; -. [Q15054-2]
DR RefSeq; NP_006582.1; NM_006591.2. [Q15054-1]
DR PDB; 1U76; X-ray; 2.60 A; B/D/F=452-466.
DR PDB; 2N1G; NMR; -; B=231-246.
DR PDB; 3E0J; X-ray; 3.00 A; B/D/F/H=1-144.
DR PDB; 6S1M; EM; 4.27 A; C=2-466.
DR PDB; 6S1N; EM; 4.86 A; C=2-466.
DR PDB; 6S1O; EM; 8.10 A; C=2-466.
DR PDB; 6TNY; EM; 3.08 A; C=2-466.
DR PDB; 6TNZ; EM; 4.05 A; C=2-466.
DR PDBsum; 1U76; -.
DR PDBsum; 2N1G; -.
DR PDBsum; 3E0J; -.
DR PDBsum; 6S1M; -.
DR PDBsum; 6S1N; -.
DR PDBsum; 6S1O; -.
DR PDBsum; 6TNY; -.
DR PDBsum; 6TNZ; -.
DR AlphaFoldDB; Q15054; -.
DR SMR; Q15054; -.
DR BioGRID; 115940; 92.
DR ComplexPortal; CPX-2097; DNA polymerase delta complex.
DR ComplexPortal; CPX-994; DNA polymerase zeta complex.
DR CORUM; Q15054; -.
DR DIP; DIP-35772N; -.
DR ELM; Q15054; -.
DR IntAct; Q15054; 15.
DR MINT; Q15054; -.
DR STRING; 9606.ENSP00000263681; -.
DR ChEMBL; CHEMBL2363042; -.
DR iPTMnet; Q15054; -.
DR PhosphoSitePlus; Q15054; -.
DR BioMuta; POLD3; -.
DR DMDM; 17375506; -.
DR EPD; Q15054; -.
DR jPOST; Q15054; -.
DR MassIVE; Q15054; -.
DR MaxQB; Q15054; -.
DR PaxDb; Q15054; -.
DR PeptideAtlas; Q15054; -.
DR PRIDE; Q15054; -.
DR ProteomicsDB; 60409; -. [Q15054-1]
DR ProteomicsDB; 61612; -.
DR ProteomicsDB; 61613; -.
DR Antibodypedia; 31076; 225 antibodies from 31 providers.
DR DNASU; 10714; -.
DR Ensembl; ENST00000263681.7; ENSP00000263681.2; ENSG00000077514.9. [Q15054-1]
DR Ensembl; ENST00000527458.5; ENSP00000432951.1; ENSG00000077514.9. [Q15054-2]
DR Ensembl; ENST00000532497.5; ENSP00000436018.1; ENSG00000077514.9. [Q15054-3]
DR GeneID; 10714; -.
DR KEGG; hsa:10714; -.
DR MANE-Select; ENST00000263681.7; ENSP00000263681.2; NM_006591.3; NP_006582.1.
DR UCSC; uc001ovf.3; human. [Q15054-1]
DR CTD; 10714; -.
DR DisGeNET; 10714; -.
DR GeneCards; POLD3; -.
DR HGNC; HGNC:20932; POLD3.
DR HPA; ENSG00000077514; Low tissue specificity.
DR MIM; 611415; gene.
DR neXtProt; NX_Q15054; -.
DR OpenTargets; ENSG00000077514; -.
DR PharmGKB; PA134868595; -.
DR VEuPathDB; HostDB:ENSG00000077514; -.
DR eggNOG; ENOG502QPSW; Eukaryota.
DR GeneTree; ENSGT01040000240530; -.
DR HOGENOM; CLU_047571_0_0_1; -.
DR InParanoid; Q15054; -.
DR OMA; GIMQSFA; -.
DR PhylomeDB; Q15054; -.
DR TreeFam; TF103006; -.
DR PathwayCommons; Q15054; -.
DR Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-HSA-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-HSA-174414; Processive synthesis on the C-strand of the telomere.
DR Reactome; R-HSA-174417; Telomere C-strand (Lagging Strand) Synthesis.
DR Reactome; R-HSA-174437; Removal of the Flap Intermediate from the C-strand.
DR Reactome; R-HSA-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR Reactome; R-HSA-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR Reactome; R-HSA-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-HSA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-HSA-5696400; Dual Incision in GG-NER.
DR Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-HSA-69091; Polymerase switching.
DR Reactome; R-HSA-69166; Removal of the Flap Intermediate.
DR Reactome; R-HSA-69183; Processive synthesis on the lagging strand.
DR SignaLink; Q15054; -.
DR SIGNOR; Q15054; -.
DR BioGRID-ORCS; 10714; 749 hits in 1057 CRISPR screens.
DR ChiTaRS; POLD3; human.
DR EvolutionaryTrace; Q15054; -.
DR GeneWiki; POLD3; -.
DR GenomeRNAi; 10714; -.
DR Pharos; Q15054; Tbio.
DR PRO; PR:Q15054; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q15054; protein.
DR Bgee; ENSG00000077514; Expressed in secondary oocyte and 193 other tissues.
DR ExpressionAtlas; Q15054; baseline and differential.
DR Genevisible; Q15054; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043625; C:delta DNA polymerase complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0016035; C:zeta DNA polymerase complex; IDA:FlyBase.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:UniProtKB.
DR GO; GO:0071897; P:DNA biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; NAS:UniProtKB.
DR GO; GO:1904161; P:DNA synthesis involved in UV-damage excision repair; IBA:GO_Central.
DR GO; GO:0006261; P:DNA-templated DNA replication; IDA:ComplexPortal.
DR GO; GO:0042276; P:error-prone translesion synthesis; IDA:ComplexPortal.
DR GO; GO:0006298; P:mismatch repair; NAS:UniProtKB.
DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IMP:UniProtKB.
DR Gene3D; 3.90.1030.20; -; 1.
DR IDEAL; IID00080; -.
DR InterPro; IPR019038; POLD3.
DR InterPro; IPR041913; POLD3_sf.
DR PANTHER; PTHR17598; PTHR17598; 1.
DR Pfam; PF09507; CDC27; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; DNA damage; DNA excision; DNA repair;
KW DNA replication; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:22223895"
FT CHAIN 2..466
FT /note="DNA polymerase delta subunit 3"
FT /id="PRO_0000186047"
FT REGION 169..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 456..463
FT /note="PIP-box"
FT /evidence="ECO:0000269|PubMed:11595739,
FT ECO:0000269|PubMed:22148433"
FT COMPBIAS 285..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..368
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:22223895"
FT MOD_RES 277
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 411
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22148433,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT CROSSLNK 258
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000269|PubMed:16934752"
FT CROSSLNK 258
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 261
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 433
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000269|PubMed:16934752"
FT CROSSLNK 433
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..106
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054149"
FT VAR_SEQ 1..39
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054150"
FT VARIANT 194
FT /note="G -> V (found in a renal cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064745"
FT VARIANT 195
FT /note="M -> L (found in a renal cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064746"
FT MUTAGEN 258
FT /note="K->R: Partially loss of sumoylation. Complete loss
FT of sumoylation; when associated with R-433."
FT /evidence="ECO:0000269|PubMed:16934752"
FT MUTAGEN 325
FT /note="K->R: No effect on sumoylation."
FT /evidence="ECO:0000269|PubMed:16934752"
FT MUTAGEN 433
FT /note="K->R: Partially loss of sumoylation. Complete loss
FT of SUMO3-sumoylation; when associated with R-285."
FT /evidence="ECO:0000269|PubMed:16934752"
FT MUTAGEN 456..466
FT /note="Missing: Complete loss of PCNA binding."
FT /evidence="ECO:0000269|PubMed:22148433"
FT MUTAGEN 458
FT /note="S->A: Partial loss of PCNA binding (60% of wild-
FT type) and strong decrease of PCNA stimulation of Pol-delta4
FT polymerase activity."
FT /evidence="ECO:0000269|PubMed:22148433"
FT MUTAGEN 459..463
FT /note="ITGFF->ATGAA: Complete loss of PCNA binding."
FT /evidence="ECO:0000269|PubMed:22148433"
FT HELIX 3..14
FT /evidence="ECO:0007829|PDB:3E0J"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:3E0J"
FT HELIX 23..30
FT /evidence="ECO:0007829|PDB:3E0J"
FT HELIX 34..52
FT /evidence="ECO:0007829|PDB:3E0J"
FT STRAND 58..81
FT /evidence="ECO:0007829|PDB:3E0J"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:3E0J"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:3E0J"
FT STRAND 93..106
FT /evidence="ECO:0007829|PDB:3E0J"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:3E0J"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:3E0J"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:3E0J"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:3E0J"
FT STRAND 238..244
FT /evidence="ECO:0007829|PDB:2N1G"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:1U76"
SQ SEQUENCE 466 AA; 51400 MW; E9625E0188725F45 CRC64;
MADQLYLENI DEFVTDQNKI VTYKWLSYTL GVHVNQAKQM LYDYVERKRK ENSGAQLHVT
YLVSGSLIQN GHSCHKVAVV REDKLEAVKS KLAVTASIHV YSIQKAMLKD SGPLFNTDYD
ILKSNLQNCS KFSAIQCAAA VPRAPAESSS SSKKFEQSHL HMSSETQANN ELTTNGHGPP
ASKQVSQQPK GIMGMFASKA AAKTQETNKE TKTEAKEVTN ASAAGNKAPG KGNMMSNFFG
KAAMNKFKVN LDSEQAVKEE KIVEQPTVSV TEPKLATPAG LKKSSKKAEP VKVLQKEKKR
GKRVALSDDE TKETENMRKK RRRIKLPESD SSEDEVFPDS PGAYEAESPS PPPPPSPPLE
PVPKTEPEPP SVKSSSGENK RKRKRVLKSK TYLDGEGCIV TEKVYESESC TDSEEELNMK
TSSVHRPPAM TVKKEPREER KGPKKGTAAL GKANRQVSIT GFFQRK
