ID DPOLL_HUMAN Reviewed; 575 AA. AC Q9UGP5; D3DR76; Q5JQP5; Q6NUM2; Q9BTN8; Q9HA10; Q9HB35; DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 214. DE RecName: Full=DNA polymerase lambda {ECO:0000305}; DE Short=Pol Lambda {ECO:0000305}; DE EC=2.7.7.7 {ECO:0000269|PubMed:10887191, ECO:0000269|PubMed:10982892, ECO:0000269|PubMed:12809503, ECO:0000269|PubMed:14627824, ECO:0000269|PubMed:15537631, ECO:0000269|PubMed:19806195}; DE EC=4.2.99.- {ECO:0000269|PubMed:11457865, ECO:0000269|PubMed:19806195}; DE AltName: Full=DNA polymerase beta-2 {ECO:0000303|PubMed:10887191}; DE Short=Pol beta2 {ECO:0000303|PubMed:10887191}; DE AltName: Full=DNA polymerase kappa {ECO:0000303|Ref.1}; GN Name=POLL {ECO:0000312|HGNC:HGNC:9184}; 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 [MRNA] (ISOFORM 1). RC TISSUE=Placenta; RA Garcia M., Dominguez O., Saniger M.L., Garcia M.J., Martinez C., Bernad A., RA Blanco L.; RT "DNA polymerase kappa, a new mammalian meiotic polymerase."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND RP TISSUE SPECIFICITY. RC TISSUE=Lymph node; RX PubMed=10982892; DOI=10.1093/nar/28.18.3684; RA Aoufouchi S., Flatter E., Dahan A., Faili A., Bertocci B., Storck S., RA Delbos F., Cocea L., Gupta N., Weill J.-C., Reynaud C.-A.; RT "Two novel human and mouse DNA polymerases of the polX family."; RL Nucleic Acids Res. 28:3684-3693(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND RP SUBCELLULAR LOCATION. RX PubMed=10887191; DOI=10.1074/jbc.m004263200; RA Nagasawa K.I., Kitamura K., Yasui A., Nimura Y., Ikeda K., Hirai M., RA Matsukage A., Nakanishi M.; RT "Identification and characterization of human DNA polymerase beta 2, a DNA RT polymerase beta-related enzyme."; RL J. Biol. Chem. 275:31233-31238(2000). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TRP-438. RG NIEHS SNPs program; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [6] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Lung, and 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). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-575 (ISOFORM 1). RC TISSUE=Mammary gland; 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 [9] RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-312, AND ACTIVE SITE. RX PubMed=11457865; DOI=10.1074/jbc.m106336200; RA Garcia-Diaz M., Bebenek K., Kunkel T.A., Blanco L.; RT "Identification of an intrinsic 5'-deoxyribose-5-phosphate lyase activity RT in human DNA polymerase lambda: a possible role in base excision repair."; RL J. Biol. Chem. 276:34659-34663(2001). RN [10] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=12809503; DOI=10.1021/bi034198m; RA Blanca G., Shevelev I., Ramadan K., Villani G., Spadari S., Huebscher U., RA Maga G.; RT "Human DNA polymerase lambda diverged in evolution from DNA polymerase beta RT toward specific Mn(++) dependence: a kinetic and thermodynamic study."; RL Biochemistry 42:7467-7476(2003). RN [11] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-505 AND PHE-506. RX PubMed=14627824; DOI=10.1093/nar/gkg896; RA Shevelev I., Blanca G., Villani G., Ramadan K., Spadari S., Huebscher U., RA Maga G.; RT "Mutagenesis of human DNA polymerase lambda: essential roles of Tyr505 and RT Phe506 for both DNA polymerase and terminal transferase activities."; RL Nucleic Acids Res. 31:6916-6925(2003). RN [12] RP INTERACTION WITH PCNA. RX PubMed=15358682; DOI=10.1096/fj.04-2268fje; RA Maga G., Blanca G., Shevelev I., Frouin I., Ramadan K., Spadari S., RA Villani G., Huebscher U.; RT "The human DNA polymerase lambda interacts with PCNA through a domain RT important for DNA primer binding and the interaction is inhibited by RT p21/WAF1/CIP1."; RL FASEB J. 18:1743-1745(2004). RN [13] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=15537631; DOI=10.1074/jbc.m411650200; RA Maga G., Ramadan K., Locatelli G.A., Shevelev I., Spadari S., Hubscher U.; RT "DNA elongation by the human DNA polymerase lambda polymerase and terminal RT transferase activities are differentially coordinated by proliferating cell RT nuclear antigen and replication protein A."; RL J. Biol. Chem. 280:1971-1981(2005). RN [14] RP FUNCTION, CATALYTIC ACTIVITY, VARIANT TRP-438, CHARACTERIZATION OF VARIANT RP TRP-438, AND MUTAGENESIS OF ASP-427 AND ASP-429. RX PubMed=19806195; DOI=10.1371/journal.pone.0007290; RA Terrados G., Capp J.P., Canitrot Y., Garcia-Diaz M., Bebenek K., RA Kirchhoff T., Villanueva A., Boudsocq F., Bergoglio V., Cazaux C., RA Kunkel T.A., Hoffmann J.S., Blanco L.; RT "Characterization of a natural mutator variant of human DNA polymerase RT lambda which promotes chromosomal instability by compromising NHEJ."; RL PLoS ONE 4:E7290-E7290(2009). RN [15] RP FUNCTION, AND CHARACTERIZATION OF VARIANT TRP-438. RX PubMed=20693240; DOI=10.1093/carcin/bgq166; RA Capp J.P., Boudsocq F., Bergoglio V., Trouche D., Cazaux C., Blanco L., RA Hoffmann J.S., Canitrot Y.; RT "The R438W polymorphism of human DNA polymerase lambda triggers cellular RT sensitivity to camptothecin by compromising the homologous recombination RT repair pathway."; RL Carcinogenesis 31:1742-1747(2010). RN [16] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH XRCC4; PAXX AND NHEJ1. RX PubMed=30250067; DOI=10.1038/s41467-018-06127-y; RA Craxton A., Munnur D., Jukes-Jones R., Skalka G., Langlais C., Cain K., RA Malewicz M.; RT "PAXX and its paralogs synergistically direct DNA polymerase lambda RT activity in DNA repair."; RL Nat. Commun. 9:3877-3877(2018). RN [17] RP STRUCTURE BY NMR OF 241-327. RX PubMed=12911298; DOI=10.1021/bi034298s; RA DeRose E.F., Kirby T.W., Mueller G.A., Bebenek K., Garcia-Diaz M., RA Blanco L., Kunkel T.A., London R.E.; RT "Solution structure of the lyase domain of human DNA polymerase lambda."; RL Biochemistry 42:9564-9574(2003). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 245-575 IN COMPLEX WITH GAPPED RP DNA. RX PubMed=14992725; DOI=10.1016/s1097-2765(04)00061-9; RA Garcia-Diaz M., Bebenek K., Krahn J.M., Blanco L., Kunkel T.A., RA Pedersen L.C.; RT "A structural solution for the DNA polymerase lambda-dependent repair of RT DNA gaps with minimal homology."; RL Mol. Cell 13:561-572(2004). RN [19] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 242-575 IN COMPLEX WITH MANGANESE RP AND DCTP. RX PubMed=17475573; DOI=10.1016/j.dnarep.2007.03.005; RA Garcia-Diaz M., Bebenek K., Krahn J.M., Pedersen L.C., Kunkel T.A.; RT "Role of the catalytic metal during polymerization by DNA polymerase RT lambda."; RL DNA Repair 6:1333-1340(2007). CC -!- FUNCTION: DNA polymerase that functions in several pathways of DNA CC repair (PubMed:11457865, PubMed:19806195, PubMed:20693240, CC PubMed:30250067). Involved in base excision repair (BER) responsible CC for repair of lesions that give rise to abasic (AP) sites in DNA CC (PubMed:11457865, PubMed:19806195). Also contributes to DNA double- CC strand break repair by non-homologous end joining and homologous CC recombination (PubMed:19806195, PubMed:20693240, PubMed:30250067). Has CC both template-dependent and template-independent (terminal transferase) CC DNA polymerase activities (PubMed:10982892, PubMed:10887191, CC PubMed:12809503, PubMed:14627824, PubMed:15537631, PubMed:19806195). CC Has also a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity CC (PubMed:11457865, PubMed:19806195). {ECO:0000269|PubMed:10887191, CC ECO:0000269|PubMed:10982892, ECO:0000269|PubMed:11457865, CC ECO:0000269|PubMed:12809503, ECO:0000269|PubMed:14627824, CC ECO:0000269|PubMed:15537631, ECO:0000269|PubMed:19806195, CC ECO:0000269|PubMed:20693240, ECO:0000269|PubMed:30250067}. 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:0000269|PubMed:10887191, ECO:0000269|PubMed:10982892, CC ECO:0000269|PubMed:12809503, ECO:0000269|PubMed:14627824, CC ECO:0000269|PubMed:15537631, ECO:0000269|PubMed:19806195}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:17475573}; CC -!- SUBUNIT: Interacts with PCNA (PubMed:14992725). Interacts with PAXX; CC promoting POLL recruitment to double-strand breaks (DSBs) and CC stimulation of the end-filling activity of POLL (PubMed:30250067). CC Interacts with XRCC4; promoting POLL recruitment to double-strand CC breaks (DSBs) and stimulation of the end-filling activity of POLL CC (PubMed:30250067). Interacts with NHEJ1/XLF; promoting POLL recruitment CC to double-strand breaks (DSBs) and stimulation of the end-filling CC activity of POLL (PubMed:30250067). {ECO:0000269|PubMed:14992725, CC ECO:0000269|PubMed:30250067}. CC -!- INTERACTION: CC Q9UGP5-2; O95273: CCNDBP1; NbExp=3; IntAct=EBI-10320765, EBI-748961; CC Q9UGP5-2; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-10320765, EBI-11522780; CC Q9UGP5-2; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-10320765, EBI-10175124; CC Q9UGP5-2; A1L4K1: FSD2; NbExp=4; IntAct=EBI-10320765, EBI-5661036; CC Q9UGP5-2; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-10320765, EBI-5916454; CC Q9UGP5-2; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-10320765, EBI-2549423; CC Q9UGP5-2; P08779: KRT16; NbExp=3; IntAct=EBI-10320765, EBI-356410; CC Q9UGP5-2; P08727: KRT19; NbExp=3; IntAct=EBI-10320765, EBI-742756; CC Q9UGP5-2; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-10320765, EBI-3044087; CC Q9UGP5-2; Q6A162: KRT40; NbExp=3; IntAct=EBI-10320765, EBI-10171697; CC Q9UGP5-2; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-10320765, EBI-10172290; CC Q9UGP5-2; P80188: LCN2; NbExp=3; IntAct=EBI-10320765, EBI-11911016; CC Q9UGP5-2; P43365: MAGEA12; NbExp=6; IntAct=EBI-10320765, EBI-749530; CC Q9UGP5-2; P43356: MAGEA2B; NbExp=3; IntAct=EBI-10320765, EBI-5650739; CC Q9UGP5-2; Q969L2: MAL2; NbExp=3; IntAct=EBI-10320765, EBI-944295; CC Q9UGP5-2; P23508: MCC; NbExp=3; IntAct=EBI-10320765, EBI-307531; CC Q9UGP5-2; Q99750: MDFI; NbExp=3; IntAct=EBI-10320765, EBI-724076; CC Q9UGP5-2; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-10320765, EBI-79165; CC Q9UGP5-2; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-10320765, EBI-302345; CC Q9UGP5-2; O94806-2: PRKD3; NbExp=3; IntAct=EBI-10320765, EBI-13337369; CC Q9UGP5-2; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-10320765, EBI-2212028; CC Q9UGP5-2; Q12800: TFCP2; NbExp=3; IntAct=EBI-10320765, EBI-717422; CC Q9UGP5-2; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-10320765, EBI-1105213; CC Q9UGP5-2; Q9UBN6: TNFRSF10D; NbExp=3; IntAct=EBI-10320765, EBI-1044859; CC Q9UGP5-2; P36406: TRIM23; NbExp=3; IntAct=EBI-10320765, EBI-740098; CC Q9UGP5-2; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-10320765, EBI-527853; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10887191}. Chromosome CC {ECO:0000269|PubMed:30250067}. Note=Accumulates at sites of DNA damage. CC {ECO:0000269|PubMed:30250067}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UGP5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UGP5-2; Sequence=VSP_056540, VSP_056541; CC -!- TISSUE SPECIFICITY: Expressed in a number of tissues. Abundant in CC testis. {ECO:0000269|PubMed:10982892}. CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB14050.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/poll/"; 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; AJ131890; CAB65074.1; -; mRNA. DR EMBL; AF161019; AAF27541.1; -; mRNA. DR EMBL; AF283478; AAG22519.1; -; mRNA. DR EMBL; AF525924; AAM77696.1; -; Genomic_DNA. DR EMBL; AL627424; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471066; EAW49759.1; -; Genomic_DNA. DR EMBL; CH471066; EAW49760.1; -; Genomic_DNA. DR EMBL; CH471066; EAW49766.1; -; Genomic_DNA. DR EMBL; CH471066; EAW49768.1; -; Genomic_DNA. DR EMBL; BC003548; AAH03548.2; -; mRNA. DR EMBL; BC068529; AAH68529.1; -; mRNA. DR EMBL; AK022476; BAB14050.1; ALT_INIT; mRNA. DR CCDS; CCDS7513.1; -. [Q9UGP5-1] DR CCDS; CCDS76332.1; -. [Q9UGP5-2] DR RefSeq; NP_001167555.1; NM_001174084.1. [Q9UGP5-1] DR RefSeq; NP_001167556.1; NM_001174085.1. DR RefSeq; NP_001295311.1; NM_001308382.1. [Q9UGP5-2] DR RefSeq; NP_037406.1; NM_013274.3. [Q9UGP5-1] DR RefSeq; XP_006717840.1; XM_006717777.1. [Q9UGP5-2] DR RefSeq; XP_011537953.1; XM_011539651.1. [Q9UGP5-1] DR PDB; 1NZP; NMR; -; A=242-327. DR PDB; 1RZT; X-ray; 2.10 A; A/E/I/M=245-575. DR PDB; 1XSL; X-ray; 2.30 A; A/E/I/M=242-575. DR PDB; 1XSN; X-ray; 1.95 A; A=242-575. DR PDB; 1XSP; X-ray; 2.20 A; A=242-575. DR PDB; 2BCQ; X-ray; 1.65 A; A=242-575. DR PDB; 2BCR; X-ray; 1.75 A; A=242-575. DR PDB; 2BCS; X-ray; 2.20 A; A=242-575. DR PDB; 2BCU; X-ray; 2.20 A; A=242-575. DR PDB; 2BCV; X-ray; 2.00 A; A=242-575. DR PDB; 2GWS; X-ray; 2.40 A; A/E/I/M=242-575. DR PDB; 2JW5; NMR; -; A=34-135. DR PDB; 2PFN; X-ray; 1.90 A; A=242-575. DR PDB; 2PFO; X-ray; 2.00 A; A=242-575. DR PDB; 2PFP; X-ray; 2.10 A; A=242-575. DR PDB; 2PFQ; X-ray; 2.10 A; A=242-575. DR PDB; 3C5F; X-ray; 2.25 A; A/B=242-575. DR PDB; 3C5G; X-ray; 2.20 A; A/B=242-575. DR PDB; 3HW8; X-ray; 1.95 A; A=242-575. DR PDB; 3HWT; X-ray; 1.95 A; A=242-575. DR PDB; 3HX0; X-ray; 3.00 A; A/F/K/P=242-575. DR PDB; 3MDA; X-ray; 2.03 A; A=252-575. DR PDB; 3MDC; X-ray; 2.00 A; A=252-575. DR PDB; 3MGH; X-ray; 2.40 A; A/C=242-575. DR PDB; 3MGI; X-ray; 2.60 A; A=242-575. DR PDB; 3PML; X-ray; 2.60 A; A/B=242-575. DR PDB; 3PMN; X-ray; 2.20 A; A=242-575. DR PDB; 3PNC; X-ray; 2.00 A; A=242-575. DR PDB; 3UPQ; X-ray; 1.95 A; A=242-575. DR PDB; 3UQ0; X-ray; 2.14 A; A=242-575. DR PDB; 3UQ2; X-ray; 2.25 A; A=242-575. DR PDB; 4FO6; X-ray; 2.01 A; A=242-575. DR PDB; 4K4G; X-ray; 2.15 A; A/E/I/M=245-575. DR PDB; 4K4H; X-ray; 2.10 A; A/E/I/M=245-575. DR PDB; 4K4I; X-ray; 2.25 A; A/E/I/M=245-575. DR PDB; 4X5V; X-ray; 2.15 A; A=251-575. DR PDB; 4XA5; X-ray; 1.90 A; A=251-575. DR PDB; 4XQ8; X-ray; 2.80 A; A/B=242-575. DR PDB; 4XRH; X-ray; 3.00 A; A/B=242-575. DR PDB; 4XUS; X-ray; 2.40 A; A=251-575. DR PDB; 5CA7; X-ray; 2.52 A; A/B=242-575. DR PDB; 5CB1; X-ray; 3.30 A; A/B=250-575. DR PDB; 5CHG; X-ray; 2.90 A; A/B=242-575. DR PDB; 5CJ7; X-ray; 2.90 A; A/B=242-575. DR PDB; 5CP2; X-ray; 2.36 A; A/B=242-575. DR PDB; 5CR0; X-ray; 2.75 A; A/B=242-575. DR PDB; 5CWR; X-ray; 2.50 A; A/B=250-575. DR PDB; 5DDM; X-ray; 2.80 A; A/B=242-575. DR PDB; 5DDY; X-ray; 3.36 A; A/C/E/G=242-575. DR PDB; 5DKW; X-ray; 2.69 A; A/B=249-575. DR PDB; 5III; X-ray; 1.80 A; A=242-575. DR PDB; 5IIJ; X-ray; 1.72 A; A=242-575. DR PDB; 5IIK; X-ray; 1.98 A; A=242-575. DR PDB; 5IIL; X-ray; 1.96 A; A=242-575. DR PDB; 5IIM; X-ray; 1.94 A; A=242-575. DR PDB; 5IIN; X-ray; 2.15 A; A=242-575. DR PDB; 5IIO; X-ray; 2.08 A; A/E/I/M=242-575. DR PDB; 5W4G; X-ray; 2.04 A; A=4-32. DR PDB; 7M07; X-ray; 1.57 A; A=234-575. DR PDB; 7M08; X-ray; 1.70 A; A=234-575. DR PDB; 7M09; X-ray; 1.65 A; A=234-575. DR PDB; 7M0A; X-ray; 1.83 A; A=234-575. DR PDB; 7M0B; X-ray; 2.00 A; A=234-575. DR PDB; 7M0C; X-ray; 2.65 A; A=234-575. DR PDB; 7M0D; X-ray; 1.80 A; A/B=234-575. DR PDB; 7M0E; X-ray; 2.25 A; A/B/C/D=232-575. DR PDB; 7M43; X-ray; 1.98 A; A=242-575. DR PDB; 7M44; X-ray; 1.90 A; A=242-575. DR PDB; 7M45; X-ray; 1.89 A; A=242-575. DR PDB; 7M46; X-ray; 1.92 A; A=242-575. DR PDB; 7M47; X-ray; 1.65 A; A=242-575. DR PDB; 7M48; X-ray; 1.93 A; A=242-575. DR PDB; 7M49; X-ray; 1.60 A; A=242-575. DR PDB; 7M4A; X-ray; 1.87 A; A=242-575. DR PDB; 7M4B; X-ray; 1.66 A; A=242-575. DR PDB; 7M4C; X-ray; 1.95 A; A=242-575. DR PDB; 7M4D; X-ray; 1.82 A; A=242-575. DR PDB; 7M4E; X-ray; 1.90 A; A=242-575. DR PDB; 7M4F; X-ray; 1.95 A; A=242-575. DR PDB; 7M4G; X-ray; 1.88 A; A=242-575. DR PDB; 7M4H; X-ray; 1.92 A; A=242-575. DR PDB; 7M4I; X-ray; 2.00 A; A=242-575. DR PDB; 7M4J; X-ray; 2.38 A; A=242-575. DR PDB; 7M4K; X-ray; 1.72 A; A=242-575. DR PDB; 7M4L; X-ray; 1.70 A; A=242-575. DR PDB; 7UN7; X-ray; 2.04 A; A=242-575. DR PDBsum; 1NZP; -. DR PDBsum; 1RZT; -. DR PDBsum; 1XSL; -. DR PDBsum; 1XSN; -. DR PDBsum; 1XSP; -. DR PDBsum; 2BCQ; -. DR PDBsum; 2BCR; -. DR PDBsum; 2BCS; -. DR PDBsum; 2BCU; -. DR PDBsum; 2BCV; -. DR PDBsum; 2GWS; -. DR PDBsum; 2JW5; -. DR PDBsum; 2PFN; -. DR PDBsum; 2PFO; -. DR PDBsum; 2PFP; -. DR PDBsum; 2PFQ; -. DR PDBsum; 3C5F; -. DR PDBsum; 3C5G; -. DR PDBsum; 3HW8; -. DR PDBsum; 3HWT; -. DR PDBsum; 3HX0; -. DR PDBsum; 3MDA; -. DR PDBsum; 3MDC; -. DR PDBsum; 3MGH; -. DR PDBsum; 3MGI; -. DR PDBsum; 3PML; -. DR PDBsum; 3PMN; -. DR PDBsum; 3PNC; -. DR PDBsum; 3UPQ; -. DR PDBsum; 3UQ0; -. DR PDBsum; 3UQ2; -. DR PDBsum; 4FO6; -. DR PDBsum; 4K4G; -. DR PDBsum; 4K4H; -. DR PDBsum; 4K4I; -. DR PDBsum; 4X5V; -. DR PDBsum; 4XA5; -. DR PDBsum; 4XQ8; -. DR PDBsum; 4XRH; -. DR PDBsum; 4XUS; -. DR PDBsum; 5CA7; -. DR PDBsum; 5CB1; -. DR PDBsum; 5CHG; -. DR PDBsum; 5CJ7; -. DR PDBsum; 5CP2; -. DR PDBsum; 5CR0; -. DR PDBsum; 5CWR; -. DR PDBsum; 5DDM; -. DR PDBsum; 5DDY; -. DR PDBsum; 5DKW; -. DR PDBsum; 5III; -. DR PDBsum; 5IIJ; -. DR PDBsum; 5IIK; -. DR PDBsum; 5IIL; -. DR PDBsum; 5IIM; -. DR PDBsum; 5IIN; -. DR PDBsum; 5IIO; -. DR PDBsum; 5W4G; -. DR PDBsum; 7M07; -. DR PDBsum; 7M08; -. DR PDBsum; 7M09; -. DR PDBsum; 7M0A; -. DR PDBsum; 7M0B; -. DR PDBsum; 7M0C; -. DR PDBsum; 7M0D; -. DR PDBsum; 7M0E; -. DR PDBsum; 7M43; -. DR PDBsum; 7M44; -. DR PDBsum; 7M45; -. DR PDBsum; 7M46; -. DR PDBsum; 7M47; -. DR PDBsum; 7M48; -. DR PDBsum; 7M49; -. DR PDBsum; 7M4A; -. DR PDBsum; 7M4B; -. DR PDBsum; 7M4C; -. DR PDBsum; 7M4D; -. DR PDBsum; 7M4E; -. DR PDBsum; 7M4F; -. DR PDBsum; 7M4G; -. DR PDBsum; 7M4H; -. DR PDBsum; 7M4I; -. DR PDBsum; 7M4J; -. DR PDBsum; 7M4K; -. DR PDBsum; 7M4L; -. DR PDBsum; 7UN7; -. DR AlphaFoldDB; Q9UGP5; -. DR BMRB; Q9UGP5; -. DR SMR; Q9UGP5; -. DR BioGRID; 118155; 72. DR DIP; DIP-48999N; -. DR IntAct; Q9UGP5; 41. DR MINT; Q9UGP5; -. DR STRING; 9606.ENSP00000359181; -. DR BindingDB; Q9UGP5; -. DR ChEMBL; CHEMBL5367; -. DR GlyGen; Q9UGP5; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9UGP5; -. DR PhosphoSitePlus; Q9UGP5; -. DR BioMuta; POLL; -. DR DMDM; 17367126; -. DR EPD; Q9UGP5; -. DR jPOST; Q9UGP5; -. DR MassIVE; Q9UGP5; -. DR MaxQB; Q9UGP5; -. DR PaxDb; 9606-ENSP00000359181; -. DR PeptideAtlas; Q9UGP5; -. DR ProteomicsDB; 79002; -. DR ProteomicsDB; 84253; -. [Q9UGP5-1] DR Pumba; Q9UGP5; -. DR Antibodypedia; 31295; 291 antibodies from 33 providers. DR DNASU; 27343; -. DR Ensembl; ENST00000299206.8; ENSP00000299206.4; ENSG00000166169.17. [Q9UGP5-1] DR Ensembl; ENST00000370162.8; ENSP00000359181.3; ENSG00000166169.17. [Q9UGP5-1] DR Ensembl; ENST00000370169.5; ENSP00000359188.1; ENSG00000166169.17. [Q9UGP5-1] DR Ensembl; ENST00000628479.2; ENSP00000485885.1; ENSG00000166169.17. [Q9UGP5-2] DR GeneID; 27343; -. DR KEGG; hsa:27343; -. DR MANE-Select; ENST00000370162.8; ENSP00000359181.3; NM_001174084.2; NP_001167555.1. DR UCSC; uc001ktg.2; human. [Q9UGP5-1] DR AGR; HGNC:9184; -. DR CTD; 27343; -. DR DisGeNET; 27343; -. DR GeneCards; POLL; -. DR HGNC; HGNC:9184; POLL. DR HPA; ENSG00000166169; Low tissue specificity. DR MIM; 606343; gene. DR neXtProt; NX_Q9UGP5; -. DR OpenTargets; ENSG00000166169; -. DR PharmGKB; PA33504; -. DR VEuPathDB; HostDB:ENSG00000166169; -. DR eggNOG; KOG2534; Eukaryota. DR GeneTree; ENSGT00940000158515; -. DR InParanoid; Q9UGP5; -. DR OMA; KWHGASA; -. DR OrthoDB; 49764at2759; -. DR PhylomeDB; Q9UGP5; -. DR TreeFam; TF103011; -. DR BRENDA; 4.2.99.B1; 2681. DR PathwayCommons; Q9UGP5; -. DR Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ). DR SABIO-RK; Q9UGP5; -. DR SignaLink; Q9UGP5; -. DR SIGNOR; Q9UGP5; -. DR BioGRID-ORCS; 27343; 14 hits in 1157 CRISPR screens. DR ChiTaRS; POLL; human. DR EvolutionaryTrace; Q9UGP5; -. DR GeneWiki; DNA_polymerase_lambda; -. DR GenomeRNAi; 27343; -. DR Pharos; Q9UGP5; Tbio. DR PRO; PR:Q9UGP5; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q9UGP5; Protein. DR Bgee; ENSG00000166169; Expressed in right uterine tube and 163 other cell types or tissues. DR ExpressionAtlas; Q9UGP5; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB. DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006287; P:base-excision repair, gap-filling; IDA:UniProtKB. DR GO; GO:0071897; P:DNA biosynthetic process; IDA:UniProtKB. DR GO; GO:0006260; P:DNA replication; NAS:UniProtKB. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB. DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IDA:UniProtKB. DR GO; GO:0006289; P:nucleotide-excision repair; IDA:UniProtKB. DR GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; NAS:UniProtKB. DR CDD; cd17715; BRCT_polymerase_lambda; 1. DR CDD; cd00141; NT_POLXc; 1. DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1. DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1. DR Gene3D; 3.40.50.10190; BRCT domain; 1. DR Gene3D; 1.10.150.110; DNA polymerase beta, N-terminal domain-like; 1. DR Gene3D; 3.30.210.10; DNA polymerase, thumb domain; 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:SF44; DNA POLYMERASE LAMBDA; 1. DR PANTHER; PTHR11276; DNA POLYMERASE TYPE-X FAMILY MEMBER; 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; SSF52113; BRCT domain; 1. DR SUPFAM; SSF47802; DNA polymerase beta, N-terminal domain-like; 1. DR SUPFAM; SSF81301; Nucleotidyltransferase; 1. DR SUPFAM; SSF81585; PsbU/PolX domain-like; 1. DR PROSITE; PS50172; BRCT; 1. DR PROSITE; PS00522; DNA_POLYMERASE_X; 1. DR Genevisible; Q9UGP5; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromosome; DNA damage; DNA repair; KW DNA replication; DNA synthesis; DNA-binding; DNA-directed DNA polymerase; KW Lyase; Manganese; Metal-binding; Nucleotidyltransferase; Nucleus; KW Reference proteome; Transferase. FT CHAIN 1..575 FT /note="DNA polymerase lambda" FT /id="PRO_0000218783" FT DOMAIN 36..132 FT /note="BRCT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033" FT REGION 161..205 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 265..279 FT /note="DNA-binding" FT /evidence="ECO:0000269|PubMed:14992725" FT REGION 345..348 FT /note="DNA-binding" FT /evidence="ECO:0000269|PubMed:14992725" FT REGION 420..429 FT /note="Involved in primer binding" FT /evidence="ECO:0000250" FT REGION 466..505 FT /note="DNA-binding" FT /evidence="ECO:0000269|PubMed:14992725" FT COMPBIAS 165..179 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 312 FT /note="Schiff-base intermediate with DNA" FT /evidence="ECO:0000269|PubMed:11457865" FT BINDING 386 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000269|PubMed:17475573, FT ECO:0007744|PDB:2PFP, ECO:0007744|PDB:2PFQ" FT BINDING 417..420 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000269|PubMed:17475573, FT ECO:0007744|PDB:2PFP, ECO:0007744|PDB:2PFQ" FT BINDING 426..429 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000269|PubMed:17475573, FT ECO:0007744|PDB:2PFP, ECO:0007744|PDB:2PFQ" FT BINDING 427 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:17475573, FT ECO:0007744|PDB:2PFO, ECO:0007744|PDB:2PFQ" FT BINDING 429 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:17475573, FT ECO:0007744|PDB:2PFO, ECO:0007744|PDB:2PFQ" FT BINDING 490 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:17475573, FT ECO:0007744|PDB:2PFO, ECO:0007744|PDB:2PFQ" FT BINDING 513 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000269|PubMed:17475573, FT ECO:0007744|PDB:2PFP, ECO:0007744|PDB:2PFQ" FT VAR_SEQ 1..22 FT /note="MDPRGILKAFPKRQKIHADASS -> MLMHHQKYLQRFLGGKREKKQK (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_056540" FT VAR_SEQ 23..297 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_056541" FT VARIANT 221 FT /note="T -> P (in dbSNP:rs3730463)" FT /id="VAR_020268" FT VARIANT 438 FT /note="R -> W (changed DNA polymerase activity FT characterized by decreased fidelity and unchanged FT polymerization capacity; changed function in DNA FT double-strand break repair by non-homologous end joining FT and homologous recombination; no effect on FT 5'-deoxyribose-5-phosphate lyase activity; FT dbSNP:rs3730477)" FT /evidence="ECO:0000269|PubMed:19806195, FT ECO:0000269|PubMed:20693240, ECO:0000269|Ref.4" FT /id="VAR_020269" FT MUTAGEN 312 FT /note="K->A: Reduces dRP lyase activity by over 90%." FT /evidence="ECO:0000269|PubMed:11457865" FT MUTAGEN 427 FT /note="D->A: Loss of polymerase activity; when associated FT with A-429." FT /evidence="ECO:0000269|PubMed:19806195" FT MUTAGEN 429 FT /note="D->A: Loss of polymerase activity; when associated FT with A-427." FT /evidence="ECO:0000269|PubMed:19806195" FT MUTAGEN 505 FT /note="Y->A: No effect on polymerase activity. Reduces FT terminal transferase activities." FT /evidence="ECO:0000269|PubMed:14627824" FT MUTAGEN 506 FT /note="F->G,R: Strongly reduces polymerase and terminal FT transferase activities." FT /evidence="ECO:0000269|PubMed:14627824" FT CONFLICT 138 FT /note="Y -> C (in Ref. 3; AAG22519)" FT /evidence="ECO:0000305" FT CONFLICT 298 FT /note="E -> G (in Ref. 7; AAH68529)" FT /evidence="ECO:0000305" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:2JW5" FT HELIX 41..43 FT /evidence="ECO:0007829|PDB:2JW5" FT TURN 50..52 FT /evidence="ECO:0007829|PDB:2JW5" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:2JW5" FT HELIX 60..67 FT /evidence="ECO:0007829|PDB:2JW5" FT STRAND 82..85 FT /evidence="ECO:0007829|PDB:2JW5" FT STRAND 87..89 FT /evidence="ECO:0007829|PDB:2JW5" FT HELIX 91..97 FT /evidence="ECO:0007829|PDB:2JW5" FT STRAND 108..111 FT /evidence="ECO:0007829|PDB:2JW5" FT HELIX 112..120 FT /evidence="ECO:0007829|PDB:2JW5" FT HELIX 127..129 FT /evidence="ECO:0007829|PDB:2JW5" FT HELIX 240..242 FT /evidence="ECO:0007829|PDB:7M07" FT HELIX 245..248 FT /evidence="ECO:0007829|PDB:7M07" FT HELIX 254..270 FT /evidence="ECO:0007829|PDB:7M07" FT HELIX 273..288 FT /evidence="ECO:0007829|PDB:7M07" FT STRAND 289..291 FT /evidence="ECO:0007829|PDB:7M07" FT HELIX 296..300 FT /evidence="ECO:0007829|PDB:7M07" FT HELIX 307..319 FT /evidence="ECO:0007829|PDB:7M07" FT HELIX 323..326 FT /evidence="ECO:0007829|PDB:7M07" FT HELIX 332..339 FT /evidence="ECO:0007829|PDB:7M07" FT HELIX 346..354 FT /evidence="ECO:0007829|PDB:7M07" FT HELIX 360..366 FT /evidence="ECO:0007829|PDB:7M07" FT HELIX 371..378 FT /evidence="ECO:0007829|PDB:7M07" FT HELIX 380..384 FT /evidence="ECO:0007829|PDB:7M07" FT HELIX 389..406 FT /evidence="ECO:0007829|PDB:7M07" FT STRAND 411..414 FT /evidence="ECO:0007829|PDB:7M07" FT HELIX 416..419 FT /evidence="ECO:0007829|PDB:7M07" FT STRAND 423..433 FT /evidence="ECO:0007829|PDB:7M07" FT STRAND 435..438 FT /evidence="ECO:0007829|PDB:4X5V" FT TURN 439..442 FT /evidence="ECO:0007829|PDB:7M07" FT HELIX 443..453 FT /evidence="ECO:0007829|PDB:7M07" FT STRAND 457..462 FT /evidence="ECO:0007829|PDB:7M07" FT STRAND 466..468 FT /evidence="ECO:0007829|PDB:7M07" FT STRAND 472..477 FT /evidence="ECO:0007829|PDB:7M07" FT STRAND 480..483 FT /evidence="ECO:0007829|PDB:4XA5" FT STRAND 487..493 FT /evidence="ECO:0007829|PDB:7M07" FT HELIX 496..498 FT /evidence="ECO:0007829|PDB:7M07" FT HELIX 499..507 FT /evidence="ECO:0007829|PDB:7M07" FT HELIX 510..522 FT /evidence="ECO:0007829|PDB:7M07" FT STRAND 525..527 FT /evidence="ECO:0007829|PDB:7M07" FT STRAND 532..534 FT /evidence="ECO:0007829|PDB:7M07" FT STRAND 539..542 FT /evidence="ECO:0007829|PDB:7M4H" FT STRAND 544..546 FT /evidence="ECO:0007829|PDB:7M49" FT STRAND 549..551 FT /evidence="ECO:0007829|PDB:7M47" FT HELIX 556..562 FT /evidence="ECO:0007829|PDB:7M07" FT HELIX 570..573 FT /evidence="ECO:0007829|PDB:7M07" SQ SEQUENCE 575 AA; 63482 MW; FD9196A1C94923C4 CRC64; MDPRGILKAF PKRQKIHADA SSKVLAKIPR REEGEEAEEW LSSLRAHVVR TGIGRARAEL FEKQIVQHGG QLCPAQGPGV THIVVDEGMD YERALRLLRL PQLPPGAQLV KSAWLSLCLQ ERRLVDVAGF SIFIPSRYLD HPQPSKAEQD ASIPPGTHEA LLQTALSPPP PPTRPVSPPQ KAKEAPNTQA QPISDDEASD GEETQVSAAD LEALISGHYP TSLEGDCEPS PAPAVLDKWV CAQPSSQKAT NHNLHITEKL EVLAKAYSVQ GDKWRALGYA KAINALKSFH KPVTSYQEAC SIPGIGKRMA EKIIEILESG HLRKLDHISE SVPVLELFSN IWGAGTKTAQ MWYQQGFRSL EDIRSQASLT TQQAIGLKHY SDFLERMPRE EATEIEQTVQ KAAQAFNSGL LCVACGSYRR GKATCGDVDV LITHPDGRSH RGIFSRLLDS LRQEGFLTDD LVSQEENGQQ QKYLGVCRLP GPGRRHRRLD IIVVPYSEFA CALLYFTGSA HFNRSMRALA KTKGMSLSEH ALSTAVVRNT HGCKVGPGRV LPTPTEKDVF RLLGLPYREP AERDW //