DPOLL_HUMAN
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 03-AUG-2022, entry version 206.
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/";
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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 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 AlphaFoldDB; Q9UGP5; -.
DR BMRB; Q9UGP5; -.
DR SMR; Q9UGP5; -.
DR BioGRID; 118155; 70.
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; Q9UGP5; -.
DR PeptideAtlas; Q9UGP5; -.
DR PRIDE; Q9UGP5; -.
DR ProteomicsDB; 79002; -.
DR ProteomicsDB; 84253; -. [Q9UGP5-1]
DR Antibodypedia; 31295; 253 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 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; 1328151at2759; -.
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 BioGRID-ORCS; 27343; 11 hits in 1080 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 161 other tissues.
DR ExpressionAtlas; Q9UGP5; baseline and differential.
DR Genevisible; Q9UGP5; HS.
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; 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 Gene3D; 3.40.50.10190; -; 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; 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; SM00483; POLXc; 1.
DR SUPFAM; SSF47802; SSF47802; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS00522; DNA_POLYMERASE_X; 1.
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 double-
FT strand break repair by non-homologous end joining and
FT homologous recombination; no effect on 5'-deoxyribose-5-
FT phosphate lyase activity; 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 STRAND 247..250
FT /evidence="ECO:0007829|PDB:1NZP"
FT HELIX 254..269
FT /evidence="ECO:0007829|PDB:2BCQ"
FT HELIX 273..287
FT /evidence="ECO:0007829|PDB:2BCQ"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:3HW8"
FT HELIX 296..300
FT /evidence="ECO:0007829|PDB:2BCQ"
FT HELIX 307..318
FT /evidence="ECO:0007829|PDB:2BCQ"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:2BCQ"
FT HELIX 323..327
FT /evidence="ECO:0007829|PDB:2BCQ"
FT HELIX 332..339
FT /evidence="ECO:0007829|PDB:2BCQ"
FT HELIX 346..354
FT /evidence="ECO:0007829|PDB:2BCQ"
FT HELIX 360..366
FT /evidence="ECO:0007829|PDB:2BCQ"
FT HELIX 371..378
FT /evidence="ECO:0007829|PDB:2BCQ"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:2BCQ"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:2BCQ"
FT HELIX 389..404
FT /evidence="ECO:0007829|PDB:2BCQ"
FT STRAND 411..414
FT /evidence="ECO:0007829|PDB:2BCQ"
FT HELIX 416..419
FT /evidence="ECO:0007829|PDB:2BCQ"
FT STRAND 423..433
FT /evidence="ECO:0007829|PDB:2BCQ"
FT STRAND 435..438
FT /evidence="ECO:0007829|PDB:4X5V"
FT TURN 439..442
FT /evidence="ECO:0007829|PDB:2BCQ"
FT HELIX 444..453
FT /evidence="ECO:0007829|PDB:2BCQ"
FT STRAND 457..462
FT /evidence="ECO:0007829|PDB:2BCQ"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:5IIM"
FT STRAND 472..477
FT /evidence="ECO:0007829|PDB:2BCQ"
FT STRAND 480..483
FT /evidence="ECO:0007829|PDB:4XA5"
FT STRAND 487..493
FT /evidence="ECO:0007829|PDB:2BCQ"
FT HELIX 496..498
FT /evidence="ECO:0007829|PDB:2BCQ"
FT HELIX 499..507
FT /evidence="ECO:0007829|PDB:2BCQ"
FT HELIX 510..522
FT /evidence="ECO:0007829|PDB:2BCQ"
FT STRAND 525..527
FT /evidence="ECO:0007829|PDB:5IIJ"
FT STRAND 532..535
FT /evidence="ECO:0007829|PDB:2BCQ"
FT TURN 540..542
FT /evidence="ECO:0007829|PDB:4K4H"
FT STRAND 544..546
FT /evidence="ECO:0007829|PDB:2BCQ"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:2PFN"
FT HELIX 556..562
FT /evidence="ECO:0007829|PDB:2BCQ"
FT HELIX 570..573
FT /evidence="ECO:0007829|PDB:2BCQ"
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
